Dictionary of Protein Secondary Structure:
Pattern Recognition of Hydrogen-Bondedand
Geometrical Features
WOLFGANG KABSCH and CHRISTIAN SANDER, Biophysics
Department, Max Planck Institute of Medical Research, 6900
Heidelberg, Federal Republic of Germany
Synopsis
For a successful analysis of the relation between amino acid sequence and protein structure,
an unambiguous and physically meaningful definition of secondary structure is essential. We
have developed a set of simple and physically motivated criteria for secondary structure,
programmed as a pattern-recognition process of hydrogen-bonded and geometrical features
extracted from x-ray coordinates. Cooperative secondary structure is recognized as repeats
of the elementary hydrogen-bonding patterns “turn” and “bridge.” Repeating turns are
“helices,” repeating bridges are “ladders,” connected ladders are “sheets.” Geometric
structure is defined in terms of the concepts torsion and curvature of differential geometry.
Local chain “chirality” is the torsional handedness of four consecutive Ca positions and is
positive for right-handed helices and negative for ideal twisted @-sheets. Curved pieces are
defined as “bends.” Solvent “exposure” is given as the number of water molecules in possible
contact with a residue. The end result is a compilation of the primary structure, including
SS bonds, secondary structure, and solvent exposure of 62 different globular proteins. Th e
presentation is in linear form: strip graphs for an overall view and strip tables for the details
of each of 10,925 residues. The dictionary is also available in computer-readable form for
protein structure prediction work.
INTRODUCTION
Background
a-Helices and pleated @-sheetswere predicted in 1951 by Linus Pauling
and Robert Corey’ on the basis of hydrogen-bonding and cooperativity
criteria. They were seen later, and beautifully, in the first structures shown
in atomic detail by x-ray crystallography. Since then, the number of known
protein structures has risen to over 100 and comprehensive analysis of
secondary structure requires a computerized compilation of structure assignments, especially in the context of structure prediction methods.
Existing compilations have various shortcomings. The crystallographers’
assignments of secondary structure in the Brookhaven Protein Data Bank2
are often subjective and sometimes incomplete. Objective algorithms exist,
e.g., for defining turn^^-^ (reviewed in Refs. 7, 8), P-sheets? and solvent
accessibility,1° but only Levitt and Greerll have published an extensive
compilation of automatic assignments of helices and sheets. Their apBiopolymers, Vol. 22,2577-2637 (1983)
0 1983 John Wiley & Sons, Inc.
CCC 0006-3525/83/122577-61$07.10
2578
KABSCH AND SANDER
proach has the advantage of giving assignments when only backbone Ca
coordinates are known; the price paid is loss of accuracy when all-atom
coordinates are known. Solvent exposure has been published for no more
than a few proteins, and chirality only on microfiche.12 We are thus motivated to make available an accurate?exhaustive, and up-to-date compilation.
The Main Ideas
Our goal is to approximate the intuitive notion of secondary structure
by an objective algorithm. An algorithm for extracting structural features
from the atomic coordinates is obviously a pattern-recognition process.
The elementary patterns on which this process is based should be as simple
as possible yet capable of discriminating among the main types of secondary
structure. To discriminate whether a pattern is present or not in a continuum of‘possible atomic configurations, continuous decision parameters
must be fixed. Using backbone p,+ angles or Ca positions requires the
adjustment of several parameters, e.g., four angles for a rectangle in the p,$
plane for each type of secondary structure. In contrast, the presence or
absence of an H bond can be characterized by a single decision parameter,
a cutoff in the bond energy. Therefore, we base our secondary structure
recognition algorithm mainly on H-bonding patterns: “n-turns” with an
H-bond between the CO of residue i and the NH of residue i n , where n
= 3,4,5, and “bridges” with H bonds between residues not near each other
in sequence. These two types of pattern essentially exhaust all backbone-backbone H bonds. Repeating 4-turns define a-helices, and repeating bridges define 0-structure, in good agreement with intuitive assignments. All other occurrences of the basic patterns provide an interesting survey of 3lo-helices, rhelices, single turns, and single &bridges.
The results are presented in short form as strip maps of secondary
structure (Fig. A l ) , and in long form, together with the amino acid sequence
as an easy-to-use dictionary (Table AIII). The computer program DSSP
(Define Secondary Structure of Proteins) written in standard PASCAL will
be available from the Protein Data Bank, Chemistry Dept., Brookhaven
National Laboratory, Upton, N.Y. 11973. Publication of an update of this
compilation is planned as more protein structures are solved.
+
DEFINITIONS
The definitions of H-bonded features form a hierarchy: first H bonds
are defined; based on them, turns and bridges; and, based on them, a-helices
and @-ladders,including common imperfections such as helical kinks and
@-bulges. Features defined geometrically are bends, chirality, SS bonds,
and solvent exposure. Each structural feature is defined independently
of the others and structural overlaps are resolved by defining a secondary
structure summary that assigns a single state to each residue. For brevity
we express the pattern definitions in the form of equations. For example,
DICTIONARY OF PROTEIN SECONDARY STRUCTURE 2579
I
:40 -
120 -
e
0-c
h°F;\
100 -
40
20
‘\‘\
‘\
\ \
\
\
I
\
\
0
2.5
3.0
3.5
4.0
5.0
4.5
5.5
Fig. 1. H bond between peptide units is described here by the dominant electrostatic part
E (see text) of the H-bond energy, drawn in contours of constant E a t 0.5 kcal/mol intervals
as a function of the distance, d , and the alignment angle 0. Dotted lines, E positive or zero;
broken lines, E negative. An ideal H bond has d = 2.9 A, 19 = 0, and E = -3.0 kcal/mol. We
assume an H bond for E up to - 0.5 kcal/mol (solid line). Thus, misalignment of up to 63”
is allowed a t the ideal length; an N - 0 distance of up to d = 5.2 8, is allowed for perfect alignment. This definition of H bonds is particularly simple and physically meaningful. It is more
general than the historical definition of hydrogen “bond” and could be called polar interaction.
“Hbond(ij)=: [E < -0.5kcal/mole]” means: there is an H bond (ij)if
E is less than -0.5 kcal/mol.
Hydrogen-Bonded Structure
Hydrogen Bonds
Hydrogen bonds in proteins have little wave-function overlap and are
well described by an electrostatic m0de1.l~ We calculate the electrostatic
interaction energy between two H-bonding groups by placing partial
charges on the C,O (+q1, - q1) and N,H (-q2,
q 2 ) atoms, i.e.,
+
E
= qlq2(1/r(0N)
+ l/r(CH) - l/r(OH) - l/r(CN))*f
with q1 = 0.42e and q 2 = 0.20e, e being the unit electron charge and r(AB)
the interatomic distance from A to B. In chemical units, r is in angstroms,
the dimensional factor f = 332, and E is in kcal/mol. A good H bond has
about -3 kcal/mol binding energy. We choose a generous cutoff to allow
for bifurcated H bonds and errors in coordinates and assign an H bond
between C=O of residue i and N-H of residue j if E is less than the cutoff,
i.e., “Hbond(ij)=: [E < -0.5kcal/mole].”
Figure 1illustrates the relation of this one-parameter definition to the
2580
KABSCH AND SANDER
’>’
’3‘
‘3’
3-turn
no t a t i o n
’<‘
residues
H-bond
4-turn
notation
residues
H-bond
5-turn
notation
residues
H-bond
p a r a l l e l bridge
not a t ion
residues
H-bonds
( \ and / , or .)
residues
notation
a n t i p a r a l l e l bridge
notation
residues
H-bonds
( ! o r .)
residues
notation
bend
-
notation
re s f due s
d i r e c t i o n change
more t h a n 70
degrees
chirality
f o u r C(a1pha) atoms
define t h e dihedral
angle alpha
Fig. 2. Elementary patterns used in structure definition
DICTIONARY OF PROTEIN SECONDARY STRUCTURE
2581
more complicated description of H bonds in terms of one distance and one
angle. There is no generally correct H-bond definition, as there is no sharp
border between the quantum-mechanical (wave-function overlap dominates a t short distances) and electrostatic (electrostatic interaction dominates a t larger distances) regimes and no discontinuity of the interaction
energy as a function of distance or alignment. Thus, any H-bond definition
is empirically tailored to a particular purpose. Our definition, well tested
by trial and error, reflects a compromise suitable for the purpose of secondary structure definition. The cutoff chosen, which allows for an N - 0
distance up to 2.2 A larger than the optimal value a t perfect alignment or
a misalignment of maximally 60” is similar to the tolerances used by Levitt
and Greerl’ (1.8 A excess and 60’) and was found to be sufficient to average
over coordinate errors without leading to spurious secondary structure
assignments. Were it not for historical reasons, we would use the term
“polar interaction” rather than “hydrogen bond.”
Elementary H-Bond Pattern: n-Turn
The basic turn pattern (Fig. 2) is a single H bond of type (i,i + n). We
assign an n-turn a t residue i if there is an H bond from CO(i) to NH(Z + n ) ,
i.e., “n-turn(i)=: Hbond(i,i n), n = 3,4,5.”
When the pattern is found, the ends of the H bond are indicated by using
“)” a t i and “(” a t i 4-n in line %TURN, 4-TURN, or 5-TURN of Table AIII;
the residues bracketed by the H bond are noted “3,” “4,” or “5” unless they
are also the end points of other H bonds. Coincidence of “ ) ” and “(” a t
one residue is indicated by “X.” In line SUMMARY of Table AIII, residues
bracketed by the hydrogen bond of an n- turn are marked “T,”unless they
are part of an n-helix (defined below).
+
Elementary H-Bond Pattern: Bridge
Two nonoverlapping stretches of three residues each, i - 1,i,i + 1 and
j - l j j 1, form either a parallel or antiparallel bridge, depending on
which of two basic patterns (Fig. 2) is matched. We assign a bridge between
residues i and j if there are two H bonds characteristic of P-structure; in
particular,
+
Parallel Bridge(i,j)=:
Antiparallel Bridge(i,j) =:
[Hbond(i - 1,j) and HbondCj,i
[HbondG - 1,i) and Hbond(i,j
+ I)]or
+ I)]
[Hbond(i,j) and HbondCj,i)]or
[Hbond(i - 1,j + 1)and Hbondfi - 1,i + l)]
Parallel bridges are marked at i and j by lower-case letters, antiparallel ones
by upper-case letters.
KABSCH AND SANDER
2582
Cooperative H-Bond Pattern: Helices
A minimal helix is defined by two consecutive n-turns. For example,
a 4-helix, of minimal length 4 from residues i to i 3, requires 4-turns at
residues i - 1and i ,
+
4-helix(i,i
+ 3)=:
[4-turn(i - 1)and 4-turn(i)]
+
+
i.e., an H bond (i - 1,i +3) and an H bond (i,i 4). Note that nothing is
required about the H-bond state of residues i 1and i 2. Similarly, two
consecutive turns are required and a 3-helix of minimal length 3 from residue i to i + 2 and a 5-helix of minimal length 5 from residue i to i 5:
+
+
3-helix(i,i
5-helix(i,i
+ a)=:
+ 5)=:
[3-turn(i - 1)and 3-turn(i)]
[5-turn(i - 1)and 5-turn(i)]
Longer helices are defined as overlaps of minimal helices. Conventionally,
these structures are called a-helix, 3,10-helix,and 7r-helix. In Table AIII,
a 3-helix can be recognized by the pattern ) ) 3 ( (, a 4-helix by ) )44( (, and
a 5-helix by ) ) 555 ( (. In the line SUMMARY, the residues bracketed by H
bonds are labeled G, H, I, e.g.,
5-TURN
4-TURN
3-TURN
SUMMARY
) )555( (
))44((
))3((
GGG
HHHH
11111
These helices are one residue shorter at each end than they would be according to rule 6.3 of IUPAC-IUB.14 Examples of a 3-helix and a 5-helix
are shown in Fig. 3.
Couperatiue H-Bond Patterns: /%Ladders and /3-Sheets
We coin the term “ladder” and define
ladder=: set of one or more consecutive bridges of identical type
sheet=: set of one or more ladders connected by shared residues
Ladders are given letter names, where a,b,c, . . . is for parallel, A,B,C . . .
for antiparallel arrangement. Along the sequence, the first ladder is named
“a” or “A,” the second “b” or “B,” etc. Sheets are also given letter names
A,B,C . . . When the alphabet is exhausted, names restart at “a” or “A.”
In Table AIII, each residue is labeled in line SHEET by the sheet name and
in lines BRIDGE by the names of the ladders in which it participates (at most
two, one on each side). In line SUMMARY, residues in single bridges (ladders of length 1)are marked “3,”
all other ladder residues “E” (extended).
Thus, continuous stretches of “E” are /%strands. The P-sheet notation
is illustrated in Fig. 4.
Secondary Structure Irregularities
Long helices can deviate from regularity in that not all possible H bonds
DICTIONARY OF PROTEIN SECONDARY STRUCTURE
2583
(b)
Fig. 3. Stereoviews of secondary structure: (a) 3-helix (3lo-helix) and (b) 5-helix (*-helix).
(a) 3-Helix Gly232-Lys237 from triose phosphate isomerase (ITIM). In Table AIII, it appears
as the H-bond pattern
S-TURN
SUMMARY
SEQUENCE
3-Helices are not uncommon, but have only two or three weak H bonds with E about -1
kcal/mol and the C=O direction tilted away from the helix axis typically by 30". (b) 5-Helix
Gly181-Lys188 from alcohol dehydrogenase (4ADH), a t the C-terminal end of a 4-helix. In
Table AIII, it appears as the H-bond pattern
.!-TURN
SEQUENCE
5-Helices are extremely rare; the longest one, shown here, has three H bonds. All stereoviews
are by PLUTO (Sam Motherwell, unpublished). In Figs. 3 and 5, the larger atoms are backbone
atoms with 1/4 their hard-sphere radius (C-, 0.47; C of CO, 0.44; 0,0.35; N, 0.41 A) and in Fig.
4 with twice these values; side-chain atoms are small, with 0.20-A radius.
KABSCH AND SANDER
2584
(b)
Fig. 4. Stereoviews of secondary structure: (a) antiparallel and parallel P-sheets with two
ladders (three strands) each. (a) Two connected antiparallel P-ladders from trypsin (IPTN).
The three participating strands are Va116(31)-Ser20(37), Ile46(63)-Gly51(69), and
Glue62(80)-Ala67(85), where the first number is the sequential residue number from Table
A111 and the number in parentheses the authors’ residue identifier. The corresponding Hbond notation (Table AIII) is
................. CCC.. .............. C C C C ........... . C C C C . . ..
................................... NNNN... ..................
................. KKK ............... K K K . . ............NNNN.. ..
.............. VSLNS.. ............ IQVRLG.. ........ E Q F I S A ..
SHEET..
BRIDGEZ..
BRIDGE1
SEQUENCE
The middle strand participates in two ladders. Both ladders belong to sheet C. (b) Two
connected parallel P-ladders, Arg172(189)-Gly177(194), Thrl96(213)-Ile200(217),
Asp266(283)-Ala271(288) from glutathione reductase (BGRS). The corresponding H-bond
notation (Table AIII) is
.................EEEE ................ E E E ............. E E E E ....
............ 1 1 I ...........................................
................ k k k k ................ I 1 I ............. k k k k .....
.......... . R S V I V G . . ............ T S L M I . . ......... DCLLWA ...
SHEET
BRIDGEZ.....
BRIDGE1
SEQUENCE..
The first strand has two ladder partners. The three strands are part of sheet E.
DICTIONARY OF PROTEIN SECONDARY STRUCTURE
2585
are formed. This possibility is implicit in the above helix definition, e.g.,
two overlapping minimal helices offset by two or three residues are joined
into one helix:
+
=
=
))44( (
))44((
) ) 4 )x ( 4( (
HHHHHHH
)) ) )x( ( ( (
+
irregular
=
=
perfect
))44((
) )44((
) ) 4 4 ~ x 44( (
irregular
HHHHHHHH
> > ) > X X ( ( ( ( perfect
even though the third and/or fourth H bond is missing, compared to a
perfect seven- or eight-residue helix. Such imperfections are often associated with a kink in the helix, e.g., due to a proline residue.
For 6-structure, we define explicitly: a bulge-linked ladder consists of
two (perfect) ladders or bridges of the same type connected by at most one
extra residue on one strand and at most four extra residues on the other
strand. This definition follows Richardson's* observation of 6-bulges, a
frequent lattice fault in ,&sheets, but. includes more general bulges than
her main types. In naming ladders, a bulge-linked ladder is treated as one
ladder (lines BRIDGE). In line SUMMARY, all residues in bulge-linked
ladders are marked "E," including the extra residues.
Geometrical Structure
Bend
Bends are regions with high curvature. We quantify chain curvature
at the central residue i of five residues as the angle between the backbone
direction of the first three and the last three residues. This definition of
curvature is identical to that of Rose and Seltzer5 but slightly different from
that of Rackovsky and Scheraga.I5 For a bend at i, we require a curvature
of a t least 70". The cutoff value was chosen by visual inspection of threedimensional traces. With C" the position vector of C", we define
Bend(i) =: [angle ( ( C W - Ca(i - 2)),(C"(i
+ 2) - C"(i))) > 70"]
and assign "S" for a bend at residue i.
Chirality
We define chirality at each residue (except at the ends of the chain) as
(Fig. 2)
a(i) = dihedral angle(C"(i - l),C"(i),C"(i
"+"
+ l),C"(i + 2))
but report only the sign of a in Table AIII:
if 0" < a < 180" and "-"
if -180" < a < 0". Note that most helices have positive, most twisted
,&ladders negative, chirality. We have found only one left-handed helix,
in thermolysin. This rare specimen is shown in Fig. 5.
2586
KABSCH AND SANDER
Fig. 5. Stereoviews of secondary structure: illustration of chirality. This short left-handed
a-helix, Gln225-Val230 from thermolysin (2TLN)is the only one known to us. In Table A111
(note that chirality is entered a t the second residue of each quartet) it appears as:
_--
CHIRALITY
4-TURN
SUMMARY
SEQUENCE
))44( (
HHHH
QDNGGV
SS Bonds
SS bonds, i.e., covalent links between the S Y atoms of two Cys residues,
are taken directly from the Data Bank SSBOND records, as they can be
considered part of the amino acid sequence (primary structure). For the
coordinate data sets used here, an S-S distance of less than 3.0 8, can also
serve as a definition. The SS bonds are given names a,b,c . . . , and the
participating residues noted by this name in the line SEQUENCE in Table
AIII. Thus, Cys appears in the amino sequence either as C or as a lowercase letter.
Chain Breaks
Chain breaks are assumed if the peptide bond length (distance C’-N)
exceeds 2.5 A. They are labeled “!” and counted as a break residue. Thus,
“!” may reflect the absence of a chemical peptide bond, missing density in
the crystallography map, or coordinate errors. The residues for which there
are coordinates in the data set are numbered sequentially, including break
residues. The resulting residue numbers often agree with the authors’
except for proteins numbered according to sequence homology or those with
missing density or chain breaks. In any case, inspection of the amino acid
sequence in Table A111 always allows unambiguous identification of a
residue.
DICTIONARY OF PROTEIN SECONDARY STRUCTURE 2587
Structure Summary
To make contact with the usual notation of secondary structure and to
facilitate comparison with intuitive assignments, we summarize secondary
structure in a single line (SUMMARY in Table AIII). Structural overlaps
are eliminated in this line by giving priority to H,B,E,G,I,T,S in this order,
i.e., when several symbols coincide, the first one in this list is written. For
example, a helix is also a series of bends, but the state helix is given higher
priority. Pieces of 3- or 5-helix, reduced to less than minimal size due to
overlaps, are labeled “T.” A blank, by implication, means a piece of low
curvature not in H-bonded structure.
Static Solvent Exposure
Physically, we are interested in the number of water molecules in direct
contact with the protein or with a particular part of the protein.
Geometrically, a very useful representation of a monomolecular layer
of water is the surface described by all possible positions of a water molecule
in touching contact with protein atoms. That was the idea of Lee and
Richards’lo water sphere rolling around the protein surface. Note that the
surface associated with holes in the protein interior is very small, e.g., a hole
that accommodates just one water molecule has zero area. For most of the
protein exterior, however, the surface is proportional to the number of water
molecules in the first hydration shell.
Mathematically, one calculates the surface by integrating a step function
f over all points x on the surface of a sphere of radius r(atom) r(water)
around atom i. f = 1if a water sphere centered a t x (by definition in contact with atom i ) does not intersect with any other protein atom; otherwise,
f = 0.
Algorithmically, we integrate by summing over a polyhedron made of
20,80,320, or more approximately equal triangles. The integration points
are the triangle centers, the weights are the triangle area. The polyhedron
is generated starting from an icosahedron; a recursive procedure then divides each triangle into four by connecting the midpoints of the sides and
projects the three new vertices onto the surface of the sphere, ready for the
next level of recursion. The final polyhedron is reminiscent of the shells
of certain viruses and of Buckminster Fuller’s architecture of geodesic
domes. Hence, we call the algorithm “geodesic sphere integration.” It
is similar to the algorithm of Shrake and RupleyI6and conceptually simpler
than z-layer integration.
With 320 integration points, the surface area of a residue is accurate to
within 1Az;with 80 points, to within 4 A2. For myoglobin, the numerical
values agree with those of Lee and Richards,lo using their parameters. The
numbers given here are based on slightly different values of atomic radii:
1.40 for 0,1.65 for N, 1.87 for Ca,1.76 for C of CO in the backbone, 1.80 for
+
KABSCH A N D SANDER
2588
all side-chain atoms,17 and 1.40 for a water molecule following observed
water-protein distances (Ref. 18 as cited in Ref. 19).
In Table AIII, we report the average number, W ,of water molecules in
contact with each residue. W can be estimated from the surface area by
W=
Area
=-Area
V(water molecule)2/3 10
since the surface is proportional to the volume of the monolayer, which,
in turn, is proportional to the average number of molecules in the monolayer. For a water molecule volume of 30 A3 and area in A2, the conversion
factor is 9.65 N 10. Note that solvent exposure differs for a monomer and
a dimer: here, it is calculated in the presence of all monomers in the data
set (Table AI) but omitting HETATOMs (substrates, ligands, heme, etc.).
The sum over all residues is the total solvent exposure of the protein.
RESULTS AND DISCUSSION
Choice of Proteins
Of the more than 100 coordinate data sets in the Protein Data Bank,2
about 75 have complete backbone coordinates and a known amino acid
sequence. When two protein data sets had more than a 50% sequence
homology, i.e., identical amino acids in equivalent positions, the one with
higher resolution, better refinement, or more secondary structure was
chosen as representative, e.g., the first one was chosen of these pairs: serine
proteinase lSGA=lSGB by 61%;lactate dehydrogenases 4LHD=lLDX
by 63%; carbonic anhydrase lCAC=lCAB by 60%; chymotrypsin
2GCH=2CHA by 98%. Both were chosen of the following pairs: sulfhydry1 proteinases actinidin/papain 2ACT=8PAP by 47%; immunoglobulins
lFAB=lREI by 47%; cytochrome c550/c2 155C=lC2C by 43%; chymotrypsin/trypsin 2GHA=lPTN by 42%; elastase/trypsin lEST=lPTN by
38%; acid protease/penicillopepsin lAPR=lAPP by 43%;a l p subunit of
hemoglobin 2MHB(a)=2MHB(P) by 44%. The final 62 data sets thus
cover essentially all known different protein structures, except those not
deposited with the protein data bank (Table AI).
H-Bonded Structure
Backbone-backbone H bonds can be simply classified by the number
of residues they bracket or, in our notation, by n of (i,i n ) = (CO(i),NH(i
n ) ) . Let us discuss the structural role of H bonds for each n.
H bonds n = 0 and n = 1are sterically disallowed. A hydrogen bond (i,i
2) can be formed between two consecutive peptide units for certain 4,$
values of residue i 1. This local conformation is known as C7 and leads
to an extended strand roughly similar to a P-strand if it repeats. When
it occurs as part of a tight turn, that turn is sometimes called a y-turn.
+
+
+
+
DICTIONARY OF PROTEIN SECONDARY STRUCTURE
2589
30
30K
ia
5
10
15
25
20
10
5
Length of &leltx
10
15
Ladders per sheet
lb)
30
5
10
15
20
25
Length of p-Ladder lparollell
Hydrogen Bond Type
:L
Length of R-Ladder tontiporallel I
Fig. 6. The common feature of the size distribution of secondary structure segments is the
gradual fall-off: larger sizes are less probable than smaller ones. Note that we give (b,c) the
length of 8-ladders (strand pairs) rather than the length of 6-strands. A strand is often longer
than the ladders in which it participates, since sheets tend to be trapezoidal rather than rectangular in shape. The number of bulge-linked ladders per sheet (d) is given as an indication
of the width of the sheet. The width of a ladder is about 5 p\. In an ideal sheet, center strands
take part in two ladders, edge strands in one: the number of ladders is equal to the number
of strands minus one. In general, however, one strand can participate in more than one ladder
on each side and the width of the sheet less than the number of ladders times 5 A. Note:
sheets consisting of a single bridge are not included in the histogram of ladders per sheet. (e)
Number of H-bonds of type (CO(i),NH(i n ) ) . Due to the nature of L-amino acids, positive
n are heavily favored. The dominant peak a t n = 4 represents a-helices and 4-turns. We
find that H bonds (i,i 2) and (i,i 3) are surprisingly common, though generally weak.
+
+
+
Using our H bond definition, we find that many P-strands have, in addition
to the main interstrand H bonds, minor (i,i 2) intrastrand H bonds [see
peak in Fig. 6(e)]. These reflect part of the electrostatic stabilization of
extended conformations due to the polar interaction of the C - 0 and N-H
groups of adjacent peptide units, first shown by Flory’s group20to be essential in stabilizing the C7 conformation in solution. We speculate that
P-strands originate as extended C7 strands as the protein folds up. Outside
of @strands, we typically find one or two weak ( E < -1.0 kcal/mol) (i,i
2) H bonds per 100 residues, but most of them are neither repeating nor
part of a tight turn.
+
+
KABSCH AND SANDER
2590
H bonds with n
=
+3,+4,+5 are reported as turns or helices. Most (i,i
+ n ) hydrogen bonds for n > 5 or n < -5 are part of a bridge or ladder.
Interestingly, H bonds (i,i - a), (i,i - 3) . . . (i,i 5) are also rare. There
-
is steric hindrance, e g , in an (i,i - 4) helix between the backbone oxygen
and the first side-chain atom CB.
3-Helices are more frequent than previously believed, although they are
usually short and have mediocre hydrogen bonds. a-Helices are rarely
entirely pure: numerous H bonds in them are bifurcated, i.e., (i,i 4) and
(i,i 3) or sometimes (i,i + 5). The ends of a-helices often are overwound,
ending in a 3-turn or 3-helix, or underwound, ending in a 5-turn. Some
of these cases were already noted and generalized by Schellman21 and
Richardson.8 We even find a few 5-helices (r-helices)-see Fig. 3.
Tabulation of the relative number of H bonds in Table A1 may be useful
in calibrating spectroscopic determination (CD, laser Raman) of the percentage of secondary structure (e.g., by the algorithm of Provencher and
Gloeckner22). In particular, we suggest that the distinction between parallel and antiparallel & ~ t r u c t u r e in
~ ~the
* ~reference
~
spectra will improve
the overall accuracy of these experiments.
+
+
Accuracy of H-Bond and Secondary Structure Assignments
At best, secondary structure assignments can only be as accurate as the
coordinates on which they are based. In using this dictionary, it is therefore
very important to be aware of the state of resolution and refinement of each
structure indicated in Table AI. The coordinate data sets range from refined structures at better than 1.5-A resolution, where individual side chains
can clearly be seen, to unrefined structures a t a resolution just sufficient
to trace the protein chain. As a test, we compare our assignments with
those of the crystallographers and of Levitt and Greerl' for three proteins
of 1.5,2.5, and 3.0 A resolution (Table I).
For the higher-resolution structure of trypsin inhibitor (3PTI),
Deisenhofer and Steigemann25assign an H bond when the N - 0 distance
d is no greater than 3.1 A and list 18 backbone-backbone H bonds. Of
these, we find all except Tyr35(CO)-AlalG(NH),which has d = 3.1; instead,
we have Gly36(CO)-Ala16(NH),which has E = -2.2. In addition, we assign 11others, due to the rather generous energy cutoff in our definition.
One, Tyr35(CO)-Ile18(NH) is quite strong, with E = -2.0, consistent with
the slow hydrogen-exchange rate of 2.6 X lop5min-' measured by nmr.26
Three others of type (i,i 3), with E = -1.3, -1.7, -0.9, form the wellknowns 3-helix Asp3-Leu6. One (i,i 5) H bond, Asn24(CO)-Leu29(NH),
is part of the &hairpin. Six are of type (i,i 2), characteristic of the C7
configuration: five weak ones and one stronger one ( E = -1.8) in a y-turn
at Asn43. The additional H bonds assigned by us lead to identification
of two unambiguous segments of secondary structure not cited by the authors but also assigned by Levitt and Greer.ll
For the medium-resolution structure of cytochrome c550, Timkovich
and DickersonZ7use a conservative interpretation of hydrogen bonds and
+
+
+
DICTIONARY OF PROTEIN SECONDARY STRUCTURE 2591
TABLE I
Comparison of Secondary Structure Assignments for Three Proteins of Higher, Medium,
and Lower Resolution
Structurea
3PTI
G1
El
E2
E3
H1
155C
H1
G1
El
E2
E3
H1
H2
H3
H4
H5
2ADK
H1
El
H2
E2
H3
H4
H5
E3
H6
E4
Hi
H8
H9
E.5
HI0
Original
Authors
(AU)
Levitt
& Greer
(LG)
This Work
-h
16-25
28-36
-b
47-56
2-7
14-25
28-37
43-46
47-55
?-6
18-24
29-35
45-45
48-55
4-16''
6-12
11-13
19-20
(KS)
6-11
11-13
56-63
73-79
107-118
17-23h
26-3 1
33-39
40-44h
55-65
7 1-80
81-9Ob
106-118
56-64
73-80
107-117
1-8
10-14
23-30
35-38
41-48
53-62
69-84
90-94
100- 107
114-1 I8
I 23- 133
144-158
160-164
169-1 73
179-194
1-7
8-15
21-31
34-38
39-49
52-61
68-83
88-95
100-109
113-120
12 1- 136"
141-1<57']
159-166
169-175
179-192
2-7
10-14
23-31
35-38
39-48
52-62
69-83
90-93
101-108
114-118
122-132
143-157
160-167h
170-1 7 3
179-193
-
-
35-37
-
Clearly 310; LG have
N
@-Bridge,2 H bonds
4-Turn 13-16
Overlaps with H1
AU have 2 H bonds; KS, 4
Discontinuity a t Asp28-He29
AU have 2 H bonds; KS have 4
KS have 3-Turn
Pro a t 82,84; possible helix
<?-Helixends in 3-turn
N o (i,i + 4) H bond a t Asp 141
Two weak H bonds a t 167,168
a H = n-helix, G = 31,)-helix,E = @-strand. 3PTI = pancreatic trypsin inhibitor, 1.5-A
resolution, Diamond real-space refinement (Re!. 25). 155C = cytochrome c550,2.5-A
resolution, Diamond model building to guide coordinates, assignments derived from the H-bonding
diagram of Ref'. 27. 2ADK = adenylate kinase, :LO-.& resolution, unrefined (Ref. 28).
Serious discrepancy (segment missing or boundary different by three or more residues).
give a minimal set of 41 backbone-backbone H bonds. We assign all of
these, except Alall5(CO)-Glnll9(NH),a t the end of an a-helix; instead,
we see the helix end with the (i,i 3) H bond Alall5(CO)-Aspll8(NH>.
We assign an additional 24 H bonds, of which 7 are the secondary partners
of a bifurcated H bond, which is common in helices, and 8 others are marginal, with E > -1.0 kcal/mol. Of the remaining 9, four are of type (i,i +
+
2592
KABSCH AND SANDER
2) in approximate y-turns a t Glu2, Gly40, Lys 53, and Lys88; two are (i,i
4) H bonds at the end of a-helices; two are (i,i - 3) and (i,i - 6) in the
loop region Gln22-Asp28; and one is involved in forming the heme pocket
by a tertiary contact between Thr80(CO) at a helix end and MetlOS(NH)
in an extended strand. All of these have a meaningful structural interpretation. The resulting secondary structure assignments are consistent
with the authors’ H-bond list, except for the additional short parallel bulged
&strand pair, 19-20135-37, which is due to two additional weak H bonds.
Levitt and Greer” assign considerably more secondary structure (Table
I), including a much longer parallel 0-sheet 17-23/33-39 (probably too
long), a 0-strand 26-31 (roughly antiparallel to 17-23), a helix 40-44 (we
assign a 3-turn), and a longer helix 81-90 (which has only two of the seven
possible H bonds but looks very much like a helix in a C* chain tracing and
therefore may be seen to be a helix a t higher resolution).
For the unrefined, lower-resolution structure of adenylate kinase
( 2ADK28),all secondary structure assignments (ours, the original authors’,28
and Levitt and Greer’s’l) are similar. Other lower-resolution coordinate
data sets show more discrepancies, depending on the quality of the H
bonds.
This detailed comparison shows that our H-bond energy cutoff, chosen
out of necessity to allow for coordinate errors in lower-resolution data,
typically leads to 50% more H bonds than conservative assignments in
higher-resolution data (example, 3PTI). All these have a physical meaning
in terms of electrostatic interaction energy and nearly all have an interpretation in terms of canonical secondary structure; and, most importantly,
the increased number of H bonds does not give rise to spurious secondary
structure assignments.
H-bond assignments become less certain for some lower-resolution data.
For example, in the data sets lAPR, 3PGM, and lABP, Richardson8 sees
a number of 0-strands, which, in Table AIII, do appear as uncurved (non“S”) strands but with relatively few H-bonded bridges between them. A t
least for lAPR, only partially refined at 2.5-A resolution with tentative
amino acid sequence, one may expect that more H bonds will form in the
,f3-sheetson further refinement.
We conclude that our criteria for H-bonded secondary structure are
relatively strict, in spite of a generous cutoff in the H-bonding energy. For
higher-resolution data sets, our assignments are more accurate than those
of Levitt and Greer,l’ and for lower-resolution data, they are conservative
compared with both Levitt and Greer’s program and Richardon’s8 visual
processing.
+
Secondary Structure Size
What is the extent of secondary structure cooperativity? Are there any
preferred lengths of secondary structure segments? The length distributions [Fig. 6(a-c)] fall off almost monotonically with increasing length up
DICTIONARY OF PROTEIN SECONDARY STRUCTURE 2593
to a maximum segment length of about 30 A, with parallel &ladders slightly
shorter. There appear to be no statistically significant peaks, either for
an integral number of helical repeats or for typical domain sizes, with the
possible exception of four-residue parallel @-ladderscharacteristic of the
al@lafolding unit and, perhaps, 13- and 18-residue a-helices. We speculate that protein folding, although cooperative, follows random polymer
statistics approximately in that long segments are statistically less likely
than short ones. The apparent maximum size of 30 A perhaps reflects the
maximum size of globular domains.
OUTLOOK
The structure of influenza virus h e m a g g l ~ t i n i nwith
, ~ ~ its 50-residue
helix, shows that our data base certainly does not exhaust all possible
variations in protein architecture. In spite of this limitation, this compilation will be used in the ongoing development of protein structure prediction methods.
APPENDIX DICTIONARY OF PROTEIN SECONDARY
STRUCTURE
Notes to Table A1
Proteins are ordered by function and can be found in the strip tables (Table AIII) and strip
maps (Fig. AI) by their running number. Yo a-helix, YOP-antiparallel, YO&parallel = number
of H bonds per 100 residues of type 4-turn, parallel and antiparallel bridge; these percentages
can be compared with results from spectroscopy (CD, Raman, ir). Exposure = estimated
number of water molecules in contact with protein surface (first hydration shell); it can also
be read as the static exposed surface area in units of 10 A?. Exposure is calculated for the
entire data set and then divided by the multiplicity of sequence-unique molecules, e.g., the
data set lINS has two copies each of the insulin A- and B-chain (multiplicity 2). Exposure
given is that of the A- and B-chain in the tetramer. Number of residues is also for the sequence-unique molecule. Crystallographic resolution (A) and refinement give some indication
of the quality of the coordinates; both are taken from the Data Bank without further checking.
In case of doubt, consult the original papers. Refinement code: D1 = Diamond model
building to guide coordinates (Ref. 30); D2 = Diamond real-space refinement (Ref. 31); HK
= Hendrickson-Konnert (Ref. 32); DO = Dodson, Isaacs, and Rollett (Ref. 33); J L = Jack
and Levitt (Ref. 34); DS = Deisenhofer and Steigemann (Ref. 25); DF = difference Fourier;
DC = difference Fourier with constraints; FD = difference Fourier and D1; LS = least squares;
R L = restrained least squares; CL = constrained least squares; S D = steepest descent; LL
= energy minimization of Levitt and Lifson (Ref. 35); H H = D2 and Hermans’ REFINE2 and
HK; DD = DS and D2; DL = D F and LS; DJ = D2 and JL; AD = Agarwal least squares (Ref.
36) and DO; DH = D2 and HK; DE = D2 and LL; MD = energy minimization of McQueen
and D O CS = constrained difference Fourier of Chambers and Stroud (Ref. 37); RE = real
space and energy minimization; CC = constrained crystallographic refinement; CD = D2 and
CORELS (Ref. 38).
KABSCH AND SANDER
2594
TABLE A1
List of 62 Different Globular Proteins
...........
.
..
..
.
.
..
.
..
XBA
%BP
.
..
.
..
I A L P H A H E L I C A L AND 4-TURN HYDROGEN BONDS
I B E T A ANTIPARALLEL
HYDROGEN BONDS
% BETA
PARALLEL
HYDROGEN BONDS
WATER E X P O S U R E
X U L T I P L I C I T Y OF D A T A S E T
N U 3 B E R O F RESIDUES
RESOLUTION
. . . . ... . . . . . . . . . . . . . .
.................
.. . . . ... . . .... . . ..
.. . .. . . .. . .. . ..
REFINEHENT
.
LEN
RES RF
I08
306
1.9 D F
2.4 - -
I ) lCPV CALCIUM-BINDING P4RV4LBUXIN B
2) 1ABP L-ARABIUOSE-BINDING P R O T E I X
transfer
I3
2
690
85
2.0 DF
?)
election Lrd"SP0rt
7
566
15
19
85
ZAH
EXPO
M
PROTEIN I D E N T I F I E R , N A X E
hlnding proceins
38
4
31
eleccio"
1
7
57
34
23
23
38
9
0
30
0
6
0
0
2
2
0
2
9
0
0
2
665
620
642
3
781
0
0
482
316
623
715
376
0
18
0
I
I7
I7
21
610
1423
7
10
2
I'iIP O X I D I Z E D H I G H P O T E N T I A L I R O N PROTEIN (HIPIPI.
CY T V C H R O N E
CYTOCHROXE
CYTOCHROlE
CYTOCHROXE
CYTOCHRUXE
CYTOCHROXE
FERREDOXIN (PEPTOCOCCUS AEROGENES)
FERREDOXIN (SPIRULINA PLATENSIS)
F L A V O D O X I N IOKIDILED)
RUBREDOXIN
A211
R IN
~.
PLASTOCYANI
103
I03
112
I34
a2
54
98
I38
54
125
99
645
513
~
hormones
0
343
36
0
354
29
2
51
0
301
hydrolase, phospharlde acyl
37
7
0
712
123
hydrolases, 0-glycolsyl
164
7
0
918
38
2
665
129
8
24
hydrolaser, phosphoric d i e i t e r
142
20
3
842
I9
2
709
124
28
I4
hydrolJses, protelnases
9 1209
303
23
5
3
1333
324
3
I3
323
6
1272
32
7
316
27
9
6 1266
1093
236
31
I
6
821
198
37
3
3
929
223
7
31
I
145
131
34
2
6
275
5
I2 I 0 5 8
23
240
35
0 LO89
4
923
218
21
19
1
968
212
I5
I
19
44
38
29
0
0
12
immunoglobulins
I
1
34
37
2
5
2101
492
5
12211
428
1.4 RL
3.0 R E
1.5 D L
1.7
AD
16) IPPT AVIAN P A N C R E A T I C P O L Y P E P T I D E
17) ICCN G L U C A G O N ( P H 6-7)
18) L l N S INSULIN (A AND B CHAIN)
19) IBPZ P H O S P H O L I P A S E A2
2.6 C L
2.5 CD
2d) I L Z M L Y S O Z Y X E (BACTERIOPHAGE T4)
21) 7 L Y Z L Y S O Z Y M E (HEN EGG W H I C E , TRICLINIC)
(6 - 2.0 S D
22) IS35 STAPHYLOCOCCAL NUCLEASE (COMPLEX)
23) I R X S RIBONUCLE4SE-S
--
2.0
2.5
2.8
2.3
1.9
2.8
HK
D2
D2
HH
1.5
02
LS
D1
24) LCPA C A R B O X Y P E P T I D A S E A
2 5 ) LAPR ACID P R O T E A S E (RHIZOPUS CHINENSIS)
2 6 ) I A P P ACID P R O T E I N A S E (PENICILLOPEPSIN. FUNGUS)
27) 2 T L N T I I E R X O L Y S I N
28) 2GCH G A M X A CHYXOTRYPSIN A
29) M L P ALPHA L Y T I C P R J T E A S E
30) lPTN BETA-TRYPSIN ( N A T I V E AT P H 8 )
311 I S G A P R O T E I N A S E A FROM S T R E P T O M Y C E S G K I S E U S (SGPAI
3 2 ) iiaT SUHTILISIH BPN'
3 3 ) i E s r TOSYLkELAST4SE
34) 2 A C T ACTINIDIN
35) 8 Y A P Y A P A I N
2.0 - 2.0 C C
3 6 ) IFAR L A X B D A IXMUHOGLOBULIN F A B
?7) I R E 1 BENCE-JONES IXMUNOGLORVLIN (VARIABLE P O R T I O N )
2.8
2.5
2.5
1.7
2.8
DL
DI
FU
--
2
107
2 3 1)
246
2 . 8 HK
2
2.5 DO
3 8 ) 3PGY PdOSPl{OCLYCERATE H U T A S E ( D E - P I l O S P ! l O )
39) I T I M T R l O i E P H O S P H A T E I S U X E K A S E
237
2.4 Y D
40) 3CNA CONC.\UAVALIX A
IEOlerdSeS
23
2
1326
15
I
35
Iecrio (agglutinin)
2
n
15
1125
Lyasc, carbon-oxygen
1271
5
4
23
oxidoreduc~a~es
15
I2
13
937
10 1505
22
I1
I1
9 I639
I7
27
22
6
I2
7
7
I
33
I
oxygen r r o r r g e
65
0
0
256
1753
2356
686
842
2.5
I53
2.0 0 2
48)
136
DS
DD
2.0 DL
2.0 D 2
491 IECD
so I 2:IHB
5 1 ) lLHB
52) IHBL
297
I68
I53
46
proteina5c
I3
I4
13
23
17
12
2.9
2.4
2.0
2.0
2.0
DI
DJ
DZ
_-
HK
1.4
2.0
1.5
HK
2
2
0
351
632
412
6
(FERRIC
IRON
- METXYOCLOBIN)
5 3 1 ICRN CR.438111
1.9 DJ
2.6 D O
1.9 02
5 4 ) IOVl O V O M U C O I D T H I R D DOXAIN
5 5 ) 2SSI STREPTOXYCES SUBTILISIN
56) 3 P T I T R Y P S I N INRIBITOR
I7
0
29
2.8 _ _
2.0 H K
1 . 4 HK
57) I C T X A L P H A C O B R A T O X I N
58) IXLT MELITTIN
591 iNXB NEUROTOXIW B (PROBABLY IDENTICAL TO ERABUTOXIN B
0
0
0
511
406
71
26
62
I0
222
2
10
1251
1456
194
293
2.5 DI
7
652
114
1.8
3.0
INHIBITOR
._
6 9 1 2ADK ADENYLATE KINASE
6 1 ) IRHD RHODANESE
0
2
LransPOCr
7
33
20
MYOCLOBIN
HEXOGLOBIN (ERYTHROCRUORIN DEOXY)
HEMOGLOBIN ( H O R S E , AQUO M E T )
HEXOGLOBIV(HEP)-CYANIDE V (SEA LAYPREY)
L E G H E M O G L O B I N (ACETATE,MET) (YELLOW LUPII)
56
107
58
trB"SferaSe5
47
INBV
inhibitors
L 0 X l " S
3
71
0
IDFR
IGPU
4ADli
6LDH
2GRS
2S0D
162
333
374
329
661
IS1
DO
6 2 1 > P A 8 P R E A L B U X I N (HUMAW PLASMA)
DICTIONARY OF PROTEIN SECONDARY STRUCTURE 2595
TABLE A11
Structure Notation Used in Table AIII
First line: running number 1-62, data set identifier (3PTI,4LDH . . .), protein name,
[function], {sourcel
One-character name of P-sheet (“A,” “B,” “C” . . .) in which residue i
SHEET.. .
participates.
One-character name of P-ladders in which residue i participates,
H H I D G E ~. . .
“A,” “B,” “C” . . . = antiparallel,
HRIDGE1 . . .
“a,” “b,” “c” . . . = parallel.
Ladders are named sequentially from N- to C-terminus.
A 8-strand can be part of two ladders, one to each side, so there are
two lines for the possible ladder partners. Each ladder name appears
twice, once for each participating strand. Partner strands can thus be
easily identified by identical letters. The sheet topology can he
reconstructed by starting from a P-strand and tracing all partners and
their partners.
CHIRALITY
or “-”
Chirality a t residue i is the sign of the dihedral angle defined by CC1
i - 1 to i 2. Thus, a right-handed a-helix has “+,” an ideal twisted
P-strand “-.”
“S” = five-residue bend centered a t residue i.
HEN11 . .
Hydrogen-bonding pattern for turns and helices:
5-TURN.. ,
“ ) ” = backbone CO of‘thisresidue makes H bond (i,i + n )
4-’I‘URN
“ ( ” = backbone NH of this residue makes H bond ( i - n,i)
:j-‘rURN
“X” = both CO and N H make H bond
“3,” “4,” “5” = residues bracketed by H bond
SUMMARY. ..
Structure summary:
“H” = +helix (a-helix)
“B” = residue in isolated P-bridge
“E” - extended strand. participates in 8-ladder
“G” = %helix (3lo-heIix)
“I” = 5-helix (?r-helix)
“T” = H-bonded turn
“S” = bend
In case of structural overlaps. priority is given to the structure first in
this list.
EXPOSURE.
Solvent exposure is the estimated number of water molecules in
contact with residue i. The scale is 0-9; ‘ I * ” = more than 9 water
molecules, Exposure can he read as solvated surface area in units of
“+”
+
.
..
10 A?.
SEQUENCE
Amino acid sequence in one letter code:
“b,??i C c I f , . . are Cys residues labeled by their SS-bond name. “!”
chain break (peptide bond length exceeds 2,s A), Residues
including chain breaks are numbered sequentially within the
coordinate data set, irrespective of the residue identifier given there.
Thus, the tot,al number of residues is equal to the total number of
print positions minu8
the
number of.chain hreak8,
..
.. . . . .~
.
.
-
.
SUIMARY..
....
SHEET..
BRIDGEZ..
BRIDGEI..
CHIRALITY
BEND..
5-TURN..
4-TURN...
3-TURN..
..
...
.
....
..
3136288.
EFTALVKA
3<>33<
HHHHHHH
>5555<
>XXX<<<<
SSSSSS
++++++
sssss ssss sss s ssssssssss ss
> 5555<
> > > > x < <<<
>> >>xxxxx<<<<
ss
>>
>>
++++++++++ -++-----++
s ssssssssss sss
...
...
SWMARY..
SHEET..
BRIDGE?.
BRIDGE1..
CHIRALITY
BEND.....
5-TURN..
4-TURN..
3-TURN..
>33<
++++++++++ +++++++-+- -+++----++
s ssssssssss ssssssss
sss
>55>5<55<
> >>>xxxxxxx xxxxx<<<<
DDD
ee
dd4
>4>>x
>>3<<
>xxxxxxxx< <<<
> 5 5 55<
sssssss ssssssssss sss
sss
-+++-+++++ ++++++++++ +-+--+++--
sss
>5555<
> > >>xxxxxxx< <<<
d
D
>33<
B SS
STT
"29188018 48299'2.55
YDMKVIAWD WVNAKGKPM
3<
H
++++++++++ +++++++--ssssss ssssssssss ss s s
----+-+-++
e e
D D
ss
>3><3<
>>3<<
> 33< >>3<<
SS
B S HHHHHHHHHH HHHHHHHHT
S R EEE
SSGGGHH HHHHHHHHHH HHS SSS E E
SSSSSH HHHHHHHHHH HH S S E
* 9 2 1 1 0 1 0 0 0 7*108*017~3 08*21**963 8 6 * 4 0 1 0 1 # @ 119*3610*4 1 0 4 0 0 1 8 2 1 7 89216**33* *292*45695 1 0 8 * 1 0 6 6 1 2 **2**18400
DTVPLVMMM TKIGERCGOE LYKEMQKRCW DVKESAWAI TANELDTARR RTTCSMDALK AAGPPEKQIY QVPTKSNDIP GAFDAANSML VQHPEVKHWL
SS
++---+---+
C
C
>3
TTHHHHHHHH
06402550*6
GSAIVAMRG
4 > > x > x x x < < <<
-t-+---+-+--+-+---
b
B
33<
>3
TT SSEEEHH
*96838808*
SDGDGKIGW
3<
>33x
HHHHHHHHT
12*901*701
ETKTPLMGO
ssssssssss s
++++++++++
ss
>xxxx<<<<
M A
>>>
ss ss
1CPV
M A
++++++++++ +-+-+-+-++
ss sssssssss
...............................
>4<<< >444 <
>>>
>>><<<
> 3 3 < > 3 3< > > 3 < <
3xx3<<>33<> 3 3 <
>3
HHHHH HHTT TTS H HHHHHHHHHH SS SEEEH HHHHTSSTTT STT
HHHHHHHT S SS
HH
26403*81*6 745392.518 580225*854 g 6 0 4 4 2 2 4 7 1 1*9*63804* * 2 1 9 6 0 8 7 5 3 49.1748443
I A A A L E A C M ADSPNHMPP AKVCLTSKSA DDVKKAFAII DQDKSGPIEE DELKLPLWP KAMRALTDG
xxxx<<<<
ssssssss s ss
+++++++++- +++--+++++ ++-++++--+ ++++++++++ -+-+-+---+
A M
A M
PARVALBUHIN B [CALCIUM B I N D I N G PROTEINS] (CARP: CYPRINLE CARPIO)
lABP L-ARABINOSE-BINDING PROTEIN (BACTERIAL: ESCHERICHIA COLI).....................................................lABP
SHEET.. ,
AAA
A M
B
BRIDGEZ..
BRIDGE1..
aaa
aaa
b
CHIRALITY
+-+---+-- --+-++++++ ++++++++++ -+----+--+
+-++++++++ +++++-+--- --+--+-+++
BEND..
ssssssss ssssssssss sss
sssssssss ssssss
s ss
5-TURN..
4-TURN..
> 4 > > < > x x>xxxxx<<< <
>>>>xx<xx x><<<<
>
3-TURN..
> 3 3 < > 3 3< > 3 3 <
>33x3 3<>>3<<
SUIMARY..
EEE
SSTTHHHH HHHHHHHHHH S S S
EEE
SHHHHHHHH HHHHHT
B S SS
EXPOSURE.
"65100002
65*2401*10 5740S402** 631.16.540
492**11910 6 7 0 3 9 5 5 1 9 0 00000563*3
1 SEQUENCE. ENLKLGFLVK OPEEPWPOTE WKFADMGKU L Q E V I K I A V PDGEWLNAI CSLAASGAKC PVICTPDPKL
EXPOSURE.
1 0 1 SEQUENCE..
2)
EXPOSURE.
101 SEQUENCE.
1)
lCPV CALCIUM-BINDING
SHEET..
BRIDGE2..
BRIDGE1..
CHIRALITY
+-----+++
BEND.....
SS S SSS
5-TURN..
4-TURN..
>>>>
3-TURN..
>33<
SUUMARY..
TT S HHH
EXPOS ORE.
4 4 5 9 3 8 47 4
1 SEQUENCE. LSAGVLNDAD
..
TABLE A111
Strip Tables of Secondary Structure Assignment for 62 Different Proteins in the Notation of Table A11
3s ez
dIHK""
nsua
a d H i a x I u YSIZLIY~,LSH M ~ B W O L V ~D D V D ~ M M 3~3~d H a a i m ~ ~ M Y A H ' I I ~ M S Y S N N H X ~ IOB-JWAXAV
*L9091bLE+ .28r.E..9S
L f r L E L r Z l S ZKZS.9ZL.8
E9rE.rIL.b KS109.8200 ZBE.BL~E+I 09rESbr.8*
LLHHHHHH a IL.+LHHHHHS
LL D ~ W U a a a a v n a ~3 3 a u 3 3 LL HHHH 38
>>> x<<<
>>E<<
>E>XE<XEE< >EEX>C<XEE <
>EE<
> E E < > > E <<
3333 DD a a a a a s ~XUHHHHH
L..91
>>EXX E < <
{snMnvJ
soe
Y Y
:MMI+I
ILMWSNYML
53
W V Y VVY vee el3
N O M L J ~ ~ (I a a z r a r x o )
aaa
se
(P
' ~ s ~ a n ~K a s
.
.....
'3MflSOdXa
--mvuYns
'' ' N W J - E
' * 'NWL-P
* 'NlmL-S
aN3e
ALX1VMIH3
"KaMIME
'zaxme
vv
. * * * La3HS
3 ~ 1 1 ~ 3 0 3~s e3z
>P bP<
>>>><<<< >>>><<<<
>>>b<<<
>bP><PP <
> >bP<<
> SSSS<
sss ss
ss ssssssss
sssssss
ss sssssss ss ssssss
sss
sss ss ssss
+++ ++-----+++ ++++++++-- --++++++++ -+++++++++ --+-++++++ ++---+---++--+-++++ ++++----ww
5 3
eeee 888 ea3 a 3
We
aa a
vw v
. . . . . . . . . . . . . . . . . . . . . . . . . . I . . . . . .
--++-++---
33 3
S<
3
>
+++---+---
(dIdIH)
>>E <XE E <
>bbX<bb<
NOML33131
--++-+++-+
w
'M3dSNVMJ
+++--++-++
33 3
vw v
ssssssssss ssss
D
33
++++++++++ ++++++----
s
++---++--
+++-
ss
Y331DY
.8EZSS
LL LL
>EE<
>P
>s5
>>>>xx<< X < t b <
++++-+++-+ --+-*++++-
3 3
sss
++++++++-+ ---+++++--
ssss ssssssssss
--++---+-+
+--++t++++
PP
+++++-+-+-
ssssssssss sssssss
M A l L n S S Y A 3 H h C d S d l 7 S D A d 3 J V O W S 7 3 S A V M D N I 3 1 3 I I O Y W J 31)33LVW33 lALSUNY9AI
V89029K0SS 0 0 S Z 0 0 0 0 0 0 0L0025.6.8
0 1 6 b 0 2 2 0 1 0 00000SEE1Z t.LL0K8000 2 0 1 2 0 1 1 0 0 0
HHHWHHHHHH H L L U
33
S S S S S HHHHLLLSSO 3
U S
SSSHHHHHHH H L U S S S 33
>EE<
> E E < > E EXE E <
>>E<X>E< < > E E <
>xxxx<xx<> < X P < b <
(NIP&OMd Yfld'lllS-NOMI
+-- -++---++--
e
w v
.....
'33N31103S K0Z
'3MnSOdXa
* 'AMVWiUlS
' 'NMnL-t
' ' 'NMflL-b
* ' 'NYnJ-S
aN3e
ALI'lVMIH3
* 'K3XIIME
....
ON3 e
ALI1VMIHJ
* * K 3WIL1E
"Z8MIME
L33HS
...NWJ-S
.....
' * 'NWL-E
'* 'NWL-b
....
3W1& S Y 3 M 3 N A N I 1 Y C d d l d 3 3 Y Ma(LLVDVVaV O W & X V 3 H O 3 3 d d l N M V Y VAM3SYLVaO N A M 1 V I V L Y N (IYVAYNVdVS
'33NanOaS K
66.65 0bbZ006ZK0 BL8.19.20E
1 6 r 9 V 9 6 E r L 9C99KbPKSB ..ESE9r6SS
662*2+.098 915E8.09EE .61KZ9rESr
'aMnSOdX3
e LL e ~ 1 3 3 a .+LsLaaa 3ss usu B ~ U E D D ~ DDD sss H HHHSSDDDSS e LHHHHHH LL BJL
*-AMVUUIIS
>EE< > t E <
>EEXEE<
> E t XE t < > E C X>E <<> > E < <
>>E<<
> E E < >EE<
"'NWL-E
>> P b < <
>>>><<<<
* * 'NMRL-C
>5ss5<
* * 'NWL-S
s
ss
sssss
ss sss s
ss sss
sss sss s ss sssssss
ssssss ss sss
.***. aNae
ALI1VMIH3
3
a
w
ee
88 3
a
w
* 'K3MIME
"23MIME
E
V
u a ~ s
N 1 3 U U d NOMI 1 V I L N 3 J O d H D I H a B Z I a I X 0 d I H 1
(E
3
(YnSONIA U I I I L V W M H 3 )
~ 3 1 3 JNCY
3 ~
w6ZL.rZV.6
13333JLJSSS
>>E<XEE<
>DXD<C<
55<
ssssssssss
++++++*+ti
33
.
.
KYR
S
93.
<
S
t
TABLE AIII (continued)
..
..
.
..
SUMMARY..
>55>5<5
XX<<X<44<
>4>>X>X
>33x>3<<
>33<
HMHHHTTTS
STTTTHHHH
*'13*718*2
'698605608
NDNLKVIEKA BBZKANDAAL
SSSSSSSSS
+
HH
20'
ATS
<<<
S
156B
ttttt++tt- tttt-++-tSSSSSSS
S SSSSSSSSS
+tttt+ttt+
sss ssssssssss
>>>> x x x x x x x x x ~
t----t-ttt
... . . .... ..... ,... ........lCYT
4-,
OR 5-TURN..
..S-BEND.. ..
>4<<<
> > > > x x x < < < x> 4 4 < <
3<<
>33<
HHH HHHHHHHHHH
HHHHS 8 S H H H H H H H H H HHHHSTT
329.924927 8.21682298 0 * * 3 0 9 7 2 ' 5 * 5 * 1 1 * * * 4 5 3 9 2 0 1 1 3 1 7 9
ANKSKGIWN NDTLMEYLEN PKKYIPGTKH IFAGIKKKGE RQDLVAYLKS
SSSSS
+ttt-t--+-
A
HEART: THUNNUS ALALUNGA]
A
>5555<
>444<
> > > > x xxxxxxxxxx xxxxx<<<< > > > > x x x x < xx x > < < x x 4 4 <
> > 3 x x 3<<
>33<
>>> <<<
> 3 3 < >33< >> 3<< >33<
>33<
HHHHHHHHHG GCS TTTTT
SSTTHHHH H H H H H H H H H H HHHHHHHHT SHHHHHHHHH H H H H H H H H H H
8'19618'60
4*270'*2'*
77*'2'61*8
0 2 9 4 2 2 ' 0 6 6 603'31**59
4 * * 0 3 6 3 2 8 * 1782'564'.
VKMRAAALNA QKATPPKLED NSQPMKDFRH GFDILVEGID DALKLANEGK VKEAQAAAEQ LKTTRNAYHQ
5<
XXXXXX<<<<
.., ...HIALPHA-HELIX.. . E=BETA-STRAND.. ..B=BETA-BRIDGE.. ..GD3-HELIX.. ..1-5-HELIX.. ..T=3-,
.
.
........................
tt+tttttt- t-tttttttt ttt+tttttt t+---ttttt ttttttttt+ tttttttttt tttttt+-tt tttttttt+t ttt+tttttt
SSSSSSSSS S S S S S S S S S S S S S
SSSSS
S S S S S S SSSSSSSSSS S S S S S S S S S S S S S S S S S S S S S S S S S S S S S
( O X I D I Z E D ) [ELECTRON TRANSPORT1 {ESCHERICIA C O L I ) . . . . . . . . . . . . . . . . . . . . .
1CYT CYTCCHROME C ( O X I D I Z E D ) [ELECTRON TRANSWRTI (ALBACORE TUNA
A
SHEET..
BRIDGE2..
A
BRIDGEl..
CHIRALITY
-ttt++ttt +ttt+t+--t -tt--t-t--tttt++--t tt-+t----t
BEND.....
SSSSSSSS SSSSSSS
SSS
SS
SS SSS S S SS
S
5-TURN..
> 5555<
>>>>XXXXX (<<X444<
>>
4-TURN...
>33<
>33<
>33x33<>3 3<>33< >>
3-TURN.
SUMMARY..
H H H H H H H H HHHTTTT
STT
SS
TT TTSBT T TT
H
8'65'0**21
8'923'5321
* * 8 2 * 8 9 9 1 2 2 3 9 3 2 4 6 5 ' 8 0*0*84'43*
EXPOSURE.
GDVAKGKKTF VQKCAWHTV ENGGKHKVGP NLWGLFGRKT GQAEGYSYTD
1 SEQUENCE.
SHEET..
BRIDGEI..
BRIDGE1..
CHIRALITY
BEND.....
5-TURN..
4-TURN.. ,
3-TURN..
SUMMARY..
EXPOSURE.
1 0 1 SEQUENCE.
6)
SHEET.. ,
BRIDGE2..
BRIDGE1..
CHIRALITY
BEND.....
5-TURN..
4-TURN...
)-TURN..
SUMMARY..
EXPOSURE.
1 0 1 SEQUENCE.
.
.
.
..
1 5 6 8 CYTOCHRWE 8 5 6 2
5)
SHEET..
BRIDGE2..
BRIDGE1..
ttttttttt
CHIRALITY
BEND.....
SSSSSSSS
5-TURN..
>>>>XXXXX
4-TURN...
3-TURN..
>>><<<
SUMMARY..
HHHHHHHH
EXPOSURE.
*64'716'43
1 SEQUENCE. ADLEDDMQTL
..
..
.
....
.
..
....
..
..
.
....
.
aa
B
-+-++-t--+
s s
sss
B
sss ss
t--++----+
a a
sss
ss
--++---+++
s
ssss
>5
>>>>X
++----++++
sssss ssss s
sssssssss ssssssssss
s
s
155C
++++++++-- -++++++++- -++++++++- +-++---+++
.............................................
t----+++++
sss ss ss ss
+++---++-+
ss
TS SS
S
HHHH
6 2 5 8 8 * 2 * 1 * 568'2''921
KSCDPKAKSK MWKLTKDDE
3<
<
sssssss ssssssssss ss
+++++++--- -+-+++++++ ++-+*+++++ +--------+
s sss ssss
lC2C
>33x33<
xxxx<<<<
S SS S
> 3 3<
++
ss s
ST T
9.27'44222
02112*31*'
6795678478 4146
FKHCKNQADV VAFLAQDDPD AXXXXXXXXX XXXX
S HHHH HHHHHHHS
s ss s
<x<4><44<
> > > > x x x<<<<
> > > > x x < < << > 4 4 > < 4 4 <
>><<x33<
>33<>33<
> > 3 < <>33< > 3 3 <
HHTTTTTTEE
S S S SS
SSEEE S S TTS TT SS SS
HHHHH HHHH S
SHHHHHHHH SSTTTTTTTS
S
S
5 1' 9 4 7 8 6 2 3 0 7 2 * * 2 7 6 4 * 82'9122261
1 1 3 6 8 0 1 6 6 * 8 5 * 3 1 4 1 2 6 8 0 1 * * 6 9 9 1 1 2 5 7 6 2 1 5 8 4 3 4 6 0 9 5 1 1 3 8 7 3 '9'51'3'4'
EPNKCKACHM IQAPOCTDIK CGKTCPNLYC WCRKIASEE CFKYCEGILE VAEKNPDLW TEANLIEYW DPKPLVKKMT DDKCAKTKMT
++++++++-ssssssss
s ssss ssssssss
>>>>X
s s ss
-++++-+--+
[ELECTRON TRANSPORT] (PARACOCCUS DENITRIFICANSI..
AA
A A
--++++++++ +++++++-++ -------+-+
---
sss
> 4 44<
> > > > < x << 4 < > 4 4 4
>33< >33<
>33x33<>3 3<>33<
> 33<
>33<>3
STT
TTS
TT TT BT T TTS
T TTS SSSS
B SHHHHHH TTSSSTTTTT
**7364**12 1 2 4 2 1 3 ' 6 4 1 1 1 6 * * 6 8 4 2 * 1 3 6 4 3 * 6 * 5 2 5 2 5 9 8 2 1 3 5 3 2 * 9 0 8 4 1 1 6 *
DWGANKVCP NLFCWENTA AHKDNYAYSE SYTEMKAKCL WTEANIAAY VKNPKAFVLE
sssssss
x<4><44<
><<x33<
HTTTBTTB
2* * 2 9 6 6 2 1 2
SKKCLACHTF
sss
...................................
-++--+-t--
a
RHOWSPIRILLUM RUBRUM).
B
,++++++--+
a
C2 [ELECTRON TRANSPORT] (BACTERIAL:
A A
B
55><555<
XXXX<XX<4< <
>33<>33<
HHHHHHHHHH
95184073'6
'3
IENVIAYLKT LK
SSSSSSSSSS
155C CYTCCHROME C 550
SHEET..
BRIDCE2..
BRIDCEl..
++++++
CHIRALITY
BEND..
ssssss
5-TURN..
>5555<
4-TURN..
>>>>X<
3-TURN..
>
SUMMARY..
SHHHHH
EXPOSURE. '*3726'0**
1 SEQUENCE. NECDAAKCEK
SHEET..
BRIDGE2..
BRIDGE1..
CHIRALITY
BEND..
5-TURN..
4-TURN..
3-TURN..
SUMMARY..
EXPOSURE.
101 SEQUENCE.
8)
.
...
+++++++-++
1C2C FERRICYTOCHRQYE
SHEET..
BRIDGE2..
BRIDCEI..
CHIRALITY
-++++++++
BEND..
SSSSSSSS
5-TURN..
>5555<
4-TURN..
>>>>XXX<<
3-TURN..
>>
SUMMARY..
THHHHHHHH
EXPOSURE.
'6'23286'1
1 SEQUENCE. ECDAAACEKV
SHEET..
BRIDGE2..
BRIDCE1..
CHIRALITY
BEND.....
)-TURN..
4-TURN..
3-TURN.
SUMMARY..
EXPOSURE.
101 SEQUENCE.
7)
z
P
x
8
co
c.l
CIN3E=S""NWL-S
....
<
s
E
ssssss
E
<
sssssss s s
<<
>>E<<
s
ss ss
>EE<
>PIP<
sss
t+-+--+++-
s
sss
a
.....
-*.-
m ~ n n b a s1:
....
.'.** a N 3 E
AJI'IYHIH3
* '1 3 1 M I Y E
"133aIYE
L33HS
JXdI
' ' 'NMflL-5
"'NWL-E
* * 'NWL-P
"AYVWWIS
'3MnSOdX3
S
immv
rPV2669TS2 L99rrr6rI1:
s
+++++--+-
s s
LS U S L 5
E < > E E < >E E <
sss
+-++-+-+-+
s ss
LL 333LL
tEX>EX<E<
>PVP<
ss ssss
S
vv
-+-++++++- +--++----
VV
>>E<X CE< >EE<
>PPP<
>>>>X<<<<
>s s s s <
-++--+++++
"AYVWWIIS
.....
(6
(01
* ' 'NYflL-E
* "WL-P
* ' 'NWL-S
aNae
ALIlVMIH3
**I~~CIIIE
"Z33aIYE
* ' . .L33HS
XalT
3TSZ
L33HS
....
I S 5 3 3WoYH3JLA3
-+++++++-
sss sss s ssssssss
(03ZIaIXO)
'33N3nO3S I
'3WSOdX3
**Aiivwwns
"'NYflL-E
"'NMflL-0
* ' *NYflL-S
*.*.* a N 3E
ALIlVUIH3
"133cIIME
"za3aIYa
[ L Y O d S N V Y L N O Y L 3 3 1 3 1 NIXOC13MM3d
E
----+-++++
0
a
>>>>x x<<<<
>EEXEE<
ss s ssss ssss
'33NBflbPS
'3YflSOdX3
(SIS N I J V l d Y N I l f l Y I d S 1 [ L Y O d SNQYZ N O Y J 3 3 ' 1 3 1 NIXO(13YLIBd
>>>P<
ss ssss
ssssssssss
-+++++++++ +++-+-++++ ++++---+-+
> >>>xxxxx<<< <
Q
[LYOdSNYML N O Y L 3 3 1 3 1
T
X I L ~ N I ~ a~ aVi
[LYOdSNVYL N O Y L 3 3 1 3 1
VVVV
meee
s sssss s sss
---+-+++++
+--+++----
~ J L E 333 3 3 3 s LLLU
>EE<
>EE<
>PtV<
>PPP
ss
>fE<
s sss
EE<
s
++++-++-+- +++-++-+-+ +--+-+-+++
sss
+++--++++- +++++++--+ ---+-++--+
s
ssssss
--+--++++-
SVNOWOan3Sd)
(17
I\arDsaIrDr V I ' I ~ V W ~ N
OJDSMMIXW
*a3~3nb~
I s
Trd9r600r 101L00rLBD ZeSZEZ00LV '3YflSOdX3
3 3 LLHHHHH HHHHHHHHHH sss 33333
**Iuvwwns
>EE<
* ' 'NYflL-f
>>>>xx XXXXXXX<<< <
* * 'NYflJ-P
* * 'NWL-5
>SSSS<
aN3E
sssssss ssssssssss sss
-+-+-+++++
++++++++++ +-+-+-+-ALIlVYIH3
epee
"I33aIYE
qWqq
"233aIYE
WWV
L3PHS
( a 3 Z I a I X O ) N I X O a O A Y l d NXdE
(7.7
YO ' - P ' - E ~ L ~ ~ ~ ~ X I 1 3 H ~ ~ ~ I ~ ~ ~ ~ ~ X I l 3 H - E ~ 3 " 3 3 a I ~ ~ ~ " L 3 E ~ ~ ' ' ' ~ ~ N Y l L L S - V J 3 E - 3 ' ~ ' ' X I ~ ~ ~ -wwwns
YHdlV~H~~~~''''
a d a u w w 3 a D M D A S D ~ V A XX ~ S I X L S I1dadas33'1
~ ~
~ h a a ~ w s 3 3 - 1n I a 3 N i i a a I t u a s A N I m
>EEXE ><E
>>>> x x < < < <
s ss sss ssssssss
sss
-+++++++++
++++++++-- -+--++--+-
>5sss<
LBLrIBrBrZ rZS0000006 V S 6 0 r 6 E B r r 0199086rZI SPr9LZ1000 0 0 0 r E ~ 9 1 r r EBVr9TEPPr
HHHHHHHS s ~ ~ 3 3 3 3 3 3 3 3LL LLLHHH HHHHHLLL
s 9~~33
xxxx<<<<
ssssssss s ss
++++++++-++-+-++---
>
33333
d
d qqq qq
aaaa pp
33
333
N ~ d E " . . . . .VVVVVWY
. . . " . . . . . . . . . . . . . . . . . . . . . . . . . . . E. . . . .E. . .QVV
, . . .VQV
(dW WflIaIlLLSO'I3)
LL
>EE<
sss ss ss
---+-+
++--+++---
x i 3 3 a b ~x I~L 3 a s w . v A ~ J M A D V ~ Ibaaaidsoas b a I m s u m v a s 3 ~ 3 w 3s ; i d i a i D w a V v a ' I I A L a a o
L S E E r r 6 E rrrS9L9260 Z Z E B T E Z B r r 6r0tr9SV69 Z r V r V L 5 5 1 0 TBYZESI9.L
6 1 V 8 S r P L r r 9EISrrSrSr
sss ss
LLS
s
s sss
s
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LJSSSSS L L S
SS S S
S
' L
>E E <
>E
3XdI
Q Q
.......................V V
(S3N33013V S n 3 3 J 3 0 J d 3 d )
+- +++-+-++++
s
r r 9 8 IBP96EYrPT ZZ96629rPL ZSS6eSrBTe L6Ze69IPZL SrE9rSZ9EL
S3 3 S S HHHH H
ALL
0 SSS E
LL 33
>E E <
>
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a 3 d N d Q W d X S V 3 S3XI3SaW I V A I S S O I I N A d 3 3 d X 3 V 3 5 V I J S a N I A A Q
.........................................................
xadI...."........".,..............
>E<<
>>>>xxxxxx <<<<
LHHHHHHHHH HHH
V
V
sss
X b S l A M X Y l J d Y 3 C K l S A V N d d Y d I d 3 M S O S 3 N X I Y O Y 1 3 V 3 V3Vb3V91YV A C U A V d 3 A W U I I Q H 3 V A 3 3 X N X d ' I A 3 d 0 3
-9 8 E I Z 8 0 0 Z 9 0 2 ~ 6 1 1 6 P - 6 5 ; 8erC699rEZ 6928r02r56 IPrr8lrZrPB IBrZ02188r BrSZZS89ZE LrrZ08rILr
HHHHHHHHHH HLJ LLHHHH HHHH sss sss LDWJ JHHHHHHH
>
ssssssssss sss s
++++++++++ +++--+---Q
3 1 5 ~ . . " . . . , . . " . . . . . . . . . . . . . . . . . . . . . . . . . .( V S O N 1 3 n Y 3 V
..
eeee
S
SSS
+---+-'--+-
dd
SSSSSSSSS SSSSSS
++++++++++ ++++++
>5555<
XX<<<<
> > > > x x x xxx<<<<
>>3<<
>>3<<
>>3<<
HHHHHTT EE S E E E E S S GGGHHHHHH HHHHHHT
186.01.9
* 6 0 8 7 6 3 1 7 3 43*2261*87 09*29*'018
ERMNGYGCW VETPLIVQNE PDEAEQDCIE F G K K I A N I
SSSSSSS
+++++-+---
AAM
AA
--
................
......
.2RXN
..
..
...
.
SUMMARY..
>444<
ccc
-+-
SS
.E=BETA-STRAND..
.
EEEE
S T T T T T T S E E EEEE
'89'140808
264128'040
5863.
EGEQYMPFCT P P G H S A L R K G T L T L K
>3><3<
.HIALPHA-HELIX..
.....
..
.
SS
++----+--+
--+++++++sss ssss
BB BBBB
FF FF
DDDD
BBBB
FFFF
..BIBETA-BRIDGE.. ..G-3-HELIX.. .. 1 - 5 - H E L I X . . ..T-3-,
4-,
OR 5-TURN..
.SEEEND..
.
..
1 A Z U A Z U R I N [ E L E C T R O N T R A N S P O R T , C O P P E R B I N D I N G ] (PSEUDOMONAS AERUGINOSA)..........................................lAZU
BBB
AMAAA A
c BBBB
B
C
AAAAAA
SHEET..
AAAA
BBBBBB
E
BRIDGE2..
E
G
B BBBBB
aaaa
ccc
aaa a
G DDDD
BRIDCE~.
CHIRALITY
-+----+-+
--+++----++-+-----+
--+-+--+++---+-+--t
++++++++++ ++--++--+- ----+++++- --+--++-+--+--+++-BEND..
sss
s ss
ssss
s s sss s
s ssssssssss sss sss ss ss ss s
ss
sss
5-TURN. + .
>5555<
>5555<
4-TURN..
>444 <
> 4 44x>>>xxxx < < < x > 4 4 < <
3-TURN..
>33<
> 3 3x33<
>33<
> 33<
>33<
B T T E EEEEESSS
E E E E SSS
S S S E E E S S S S E E E E E E E SS TTT S B E E E E T TTTHHHHHHH HHH HHHHSS S S TT SB
SUMMARY..
41629759.7
3 0 8 8 8 8 8 8 2 6 9 5 3 9 1 0 3 8 6 8 8 8 2 2 7 * * 4 4 1 9**296351' 0 8 1 8 0 3 7 8 8 4 51*1836"1*
*3*09074*5 8274*61*8* **5**13040
EXPOSURE.
S M I Q G N D Q M B N T N A I T W K S C K Q F T W L S H P G N L P K N V MGHNWVLSTA A D n Q G W T D G MASGLDKDYL K P D D S R V I A H T K L I G S G E K D S V T P D V S K L K
1 SEQUENCE.
..
....
.
..
2RXN R U B R E D O X I N ( O X I D I Z E D , F E ( I I 1 ) ) [ E L E C T R O N T R A N S P O R T ] ( C L O S T R I D I U M P A T E U R I A N u n ) . .
SHEET..
AAA
AA
B
B
AA A
BRIDGE2..
BBB
c BB B
C
AA
BRIDGE1..
AA
----+t--++
+-+--++--+ tt--++---t +-+--+++-CHIRALITY
-----+t-+
sss
sss
sss 5 s s sss ss
s 5 s sss
BEND..
5-TURN..
4-TURN.. ,
>444<
>444<
> 4 44<
>4 44<
3-TURN..
>33<
> 3 3 t >> 3 < < > 3 3 < > > 3 < < > 3 3 <
>>3<<
SUMMARY..
EEETTT
E E T T T G GGS TT G GGS T T B T TT BGGGEE E
EXPOSURE.
* * * 4 4 0 7 R 6 5 5 7 0 4 8 * * 1 2 6 '951'95331
* * 0 8 * * 2 6 0 5 * 5 4 5 3 3 * 8 2 * 83"
1 S E Q U E N C E , MKKYTCTVCG Y I Y B P Z R G B P BBGVBPGTBF K B I P B B W V C P LCGYCKBZFZ Z V Z Z
SHEET..
BRIDGE2..
BRIDGEl..
CHIRALITY
BEND.....
5-TURN..
4-TURN..
3-TURN..
SUMMARY..
EXPOSURE.
101 SEQUENCE.
141
13)
..
.
SHEET..
BRIDGE2..
BRIDGE1..
CHIRALITY
BEND.....
5-TURN..
4-TURN..
3-TURN..
SUMMARY..
EXPOSURE.
101 SEQUENCE.
Y
..
..............
-
<x<<4<
>>3<<
HHHTTS
8*9******
DFVQWIMNT
tt+t+tt
SSSSSS
SUS S C R O F A )
SUMMARY........H=ALPHA-HELIX....E~BETA-STRAND..~~B~BETA-BRIDGE....G-J-HELIX....I=5-HELIX....T~3
.
...
..............................................
................................
-,4-,
OR 5-TURN....S=BEND....
..........................................................
IHORMONEI (PIG P A N C R E A S :
1 I N S I N S U L I N ( A AND B C H A I N ) [HORMONEI I P I G : SUS S C R C F A I
SHEET..
A
B
A
BBB
BRIDGEZ..
ccc
A
B
A
B
BRIDGEI..
CHIRALITY
++t+tt--- --t+ttttt
---++-- t++t+++t++ +++----++BEND.. ,
SSSSSSS
SSSSSSS
s ssssssssss ssss
5-TURN..
(-TURN...
>>>>X<<<<
>>44<<
> >>>xxxxx<<<<
3-TURN..
>>><<<
>> 3<<
>>3<<
SUMMARY..
HHHHHHHS B HHHHGGGB
B
T HHHHHHHHHH HGGG E E E
EXPOSURE.
6 1 2 5 7 0 5 ' 7 8 825'709'72
*0'**9'143
3'805106'4
1 2 * * 0 0 8 1 7 3 **
SEQUENCE.
G I V E Q a b T S I a S L Y Q L E N Y c N I F V N Q H L b G S H L V E A L Y L V c G E R G F F Y T P KA
..
.
.
..
1 G C N GLUCAGON ( P H 6
P H 7 FORM)
SHEET..
BRIDGE2.
BRIDGEl.,
CHIRALITY
++-+++tt+ ++t+t++ttt
BEND.....
S S SSSS SSSSSSSSSS
5-TURN..
4-TURN.. ,
> > 4 4 x <4>X4>XX>X
3-TURN..
>>3<x 3>x3<<
SUMMARY..
S S HHHH TTTHHHHHHH
EXPOSURE.
t*+4'**8**
9++7*B"5.
SEQUENCE.
HSQGTFTSDY SKYLDSRRAQ
..
....
..
1 P P T A V I A N P A N C R E A T I C P O L Y P E P T I D E [HORMONE] [ T U R K E Y P A N C R E A S : M E L E A G R I S G A L L O P A V O ) .
SHEET..
BRIDGEZ..
BRIDGE1..
CHIRALITY
--------t
t--tttt+tt tttt+ttt++ +-tt
BEND..
s ss SSSSSSS ssssssssss sss
5-TURN..
> 5 555<
4-TURN..
>>>>xxxx xxxxxxxx<< <<
3-TURN..
> 3 3<>33<
> 33<
SUMMARY..
T T S HHHHHHH HHHHHHHHHH H T T
EXPOSURE.
*6**3**63* * 2 7 * * 6 6 9 * 4 *8*69*6932 99'"'
SEQUENCE.
G P S Q P T Y P G D O A P M D L I R F YDNLQQYLNV VTRHRY
..
....
.1INS
lGCN
lPPT
l P C Y PLASTOCYANIN [ELECTRON TRANSPORT, C O P P E R B I N D I N G ] ( P O P L A R LEAVES: POPULUS NIGRA VARIANT I T A L I C A )
lPCY
SHEET,.
AAAA
AA E B B B
AAAAA A
C B B
C
AA AAA
BBB B B B
BBBBEB
BB
ccccc
F F F FFF
FFFFFF
BRIDGEZ..
BRIDGEl..
aaaa
BB ddd d
aaa a
G E E
G
CC CCC
EE
dddd
CHIRALITY
---t--t-+ -+--+t+t-t --+t-----+-+-++--I--ttt--tt- -tt++---++ --tt-tt--- t--tt-t--- t---+t++t- t+t---BEND..
ss ss s ssss
ss
ss
ssss ss sssss ss
sss
s s
SSSSSS s
5-TURN..
> 5 5 5 5<
4-TURN..
>>44<<
3-TURN..
>33<
>33<
>33< >33< >>3<< >33 <
>33<
>>3<x33 <
SUMMARY..
EEEES TT
S E E S S E E E E T T E E E E E E S S B E E TTSS T T
HHHHS T T
B S T T E E EEE S EEE E E E GGGTTT T E E E E E E
EXPOSURE.
6 9 0 5 0 0 2 * * 4 6 6 3 0 6 5 5 ' 2 7 0 6 6 5 8 9 0 3 0 6 0 3 2 4 7 5 0 0 0 1 1 5 * * 5 2 2 * 9 3 829'1224''
871*5'4765
*14089*3*0 3050474997 48715038'
SEQUENCE.
IDVLLGADDG S L A F V P S F S S I S P G E K I M K N N A G F P H N I V F D E D S I P S G V D A S K I S M S E E D L L N A K G E T F EVALSNKGEY S F Y C S P H Q G A GMVGKVTVN
TABLE A111 (continued)
Q)
E3
TZ
Y
U
Z
x
>
Lo
0
..
..
.
.
.
B
+
S S
----+-+---
XXXX<<<<
>>3<<
> > 3 x < 3 < > >3 < <
HHHHHHHTS
GGGBT G GG
8 0 8 4 4 1 4 ' 4 8 9 5 4 + 4 6 * 3 9 7 **6
NAAIdFSKVP YNKEHKNLDK KNb
SSSSS
++++++++-- --++++---+
SSSSSSSSS
A
..
.
.
SUMMARY..
++++++++++ ++++++++++ -+++++++++ --++++++++
XXX<<<X>44
3<<
>>3<
HHHHHH H H H
00136636*4
NMVFWGFTC
SSSS SSSSSSSSSS SSSSSSSSSS SSSSSSS
S
5555<
4<< >444<
> > > 4 < < x > > > x x < x xx > < < < <
X<3< > 3 3 <
>33<
>3><3<
>33<
HHTT TTTS SSSTTSHHHH HSHHHHHHHH HHHHHSS S
508.725542
'37.209581
19'**5'801
8583'3.17.
LQQKRWDEAA VNLAKSRWYN OTPNRAKRVL TTFRXTWDA
1*.*
YKNL
SS
SS
4-,
OR 5-TURN..
S-BEND..
..
..
4 > x x > x x < < x x>>xxx<<<<> 4 4 > x > > < < < <>>>>xxxxx
3x33< > 3 3 <
> 3 3 x > 3 < x 3 3 x > 3 < x 3 3 < >33< >>
H H H H H H H H H H HHHHHHHHHT STTTHHHHHH S H H H H H H H H
*309*119*4 17414'809'
3**0'504'2
1572381001
DEAEKLFNQD VDAAVRGILH NAKLKPWDS LDAVRRCALI
..E=BETA-STRAND.. ..B=BETA-BRIDGE.. ..Ga3-HELIX.. ..I-5-HELIX.. ..T=3-,
<< >>>4XX<
X33<
>>3
HTT HHHHHH
01639881'4
VAGFTNSLRM
>
. .....lLZM
SSSSSSSSSS SSSSSSSSSS SSSSSSSSSS S SSSSSSSS
+++++--+++ ++++++++++ ++-+++++++ +++++-++++ ++++++++++ ++++-+-+++ +-
SSSSSS SSS S S S SSSSSS SSS
.H=ALPHA-HELIX..
.....
.
>> >>xxxxxxxx
>33<
EEEE TT
H HHHHHHHHHH
0546007007
*0844*'277
E I q S S E N N A fEAFIgNeDR
<
++++++++++
ss s ssssssssss
-----++--+
cccc
BBBB
........ ....................................
,
lLZM LYSOZYME [O-GLYCOLSYL HYDROLASE] [BACTERIOPHAGE T 4 ) .
ABAA
AAAA
AA A
B
SHEET..
BRIDGES..
BBB
BRIDGE1..
ACAA
AA A
88 B
C
CHIRALITY
-++++++++
+-+-+-+--+ ----+-+-++ +++++++++- +-+--++--+
BEND.....
SSSSSSSS S
SS
SSS
SSS
S S SS SSSSSSSSSS SS
SS
S
5-TURN..
> > 5 5 5 <<
4-TURNe..
>>44<X44 4 <
>444 <
> >4>xx><<<<
>>
3-TURN..
>>3<<
> 33<
>33<
>33< > 3
SUMMARY..
SHHHHSTT T EEEEEE TTS EEEETT EEEES S S S HHHHHHHHHT TS TTB H
EXPOSURE.
8 6 3 6 9 0 6 ' 5 2 424*7*25*4 * * 4 9 3 0 1 0 1 2 3812.4'68'
3 0 3 7 6 8 3 ' 5 5 6*'1*0726*
1 SEQUENCE. MNIFEMLRID EGLRLKIYKD TEGYYTIGIG HLLTKSPSLN AAKSELDKAI GRNCNGVITK
..
.
SHEET..
BRIDGE2..
BRIDGE1..
CHIRALITY
BEND.....
5-TURN..
4-TURN...
)-TURN...
SUMMARY..
EXPOSURE.
1 0 1 SEQUENCE.
20)
--++-----+
1 B P 2 PHOSPHOLIPASE A2 [PHOSPHATIDE ACYL-HYDROUSE] [ C W PANCREAS: 80s TAURUS)......................................lBP2
SHEET..
A
A
BBBB
BRIDGE2..
B
BRIUGEl..
A
A
cccc
CHIRALITY
+++++++++ +++++--+++ ++++--+++++++++++++ +++++++-++ +++-+--+++ -+-+--+--+
BEND.....
SSSSSSSS SS SS SSS SSSS S S S S S S
SS S S S S S S S S S S S S S S S S S S S S SS S S S S
SSS
sss
5-TURN..
>55 55<
>5555<
> > >>xxxxxxxx x x < < < < >>> 4 < < < > 4 4 4 <
4-TURN...
> > > > X X X X X < <<<
> > 4 4 << > 4 4 4 <
3-TURN..
>33<>33< >33<
>>3<<
>33< >33<
>33
EEEETT
S S SSH H H H H H H H H H H HHHHHTT H H HHHTT TTT
SUMMARY..
H H H H H H H H H H H TT H H H HTTTBTTTBS S
0'066667'8
0'*9*580*9
0 0 ' 8 1 4 7 2 4 7 32'90**4*4
EXPOSURE.
1 * * 0 2 4 2 0 1 7 1339*1'0**
6 2 7 6 0 0 0 3 0 3 '5383'352'
1 SEQUENCE. ALWQFNGMIK aKIPSSEPLL DFNNYGbYcG LGGSGTPWD LDRdcQTHDN eYKQAKKLDS fKVLMNPYT NNYSYSaSNN
SHEET..
BRIDGE2..
BRIDGEl..
CHIRALITY
BEND.....
)-TURN..
4-TURN...
3-TURN..
SUMMARY..
EXPOSURE.
1 0 1 SEQUENCE.
19)
w
t
9
a3
0
or
TABLE A111 (continued)
>5555<
> > > ><<<<
< >>><<<
> 3 3 < > >3 < < > 3 3 <
SSSGGGGSHH HHHHTTTS G GGSSTT
* 7 * 1 0 5 5 1 7 1 2***0*97*1 '364'72.9
DGDGMNAWVA WRNRbKGTDV Q A W I R G a R L
<
ssssss
ttttt-t-tt tttttt-
sss s ssss ssssssss
-t--ttt-+t
---
ss
sss
3<
> 3 3 < > > > < <<
THHHHHHHHH HHHHTT GGG G
34'989'125
787'9'4444
5'
HEPHLRKSEA QAKKEKLNIW SE
>>>>xxxxxx x < < < <
>5555<
ttttt+tt+t +ttt---+++
s ssssssssss sssss
tt---tt+tt
>33<>3
HHHHHTTS E E
TT T
4 2 0 8 8 * 0 1 8 9 01'3**4146
EALVRWLAK VAYWKPNNT
>5555<
>X<<<<
>33x33<
ssssssss
ttttt-tt--
H H
8 8
SUMMARY
........H=ALPHA-HELIX....E~BETA-STRAND....B-BETA-BRIDGE....G~3-HELIX....I~S-HELIX....T~3
....
..
SHEET..
BRIDGE2..
BRIDGE1..
CHIRALITY
BEND..
5-TURN..
4-TURN..
3-TURN..
SUMMARY..
EXPOSURE.
SEQUENCE.
..
..
....
- , 4 -,
3<
>33
HHHHHHHHHH
1 0 9 0 0 5 '1 1 3
SVNdAKKIVS
>xxxxxx<<<
ssssssssss
+++++t+t+t
GG
OR 5-TURN....S=BENDe...
>33<
EEEETTEEHH
082075'218
YIYADGKMVN
>>>
-----+--++
sss ss
GG
EEEE
..........AAAA
......AAlSNS
lSNS STAPHYLOCOCCAL NUCLEASE ICWPLEX) [PHOSPHORIC DIESTER ( D N A ) HYDROLASE] (STAPHYLOCOCCUS AUREUS)
SHEET..
A AAAA A
AAAAA
AAAAAA 80
AAAAA
A
AAA
BRIDGE2..
ccccc
ddd
EEEEE
F E
AAA
F
ddd
BRXDGEI..
A AABB B
B BB
CCCCC
HH
+++-+---+--+--+--+
++-+----++------+----++-+--+
--++++++++ ++++++++-+ -------++t--+-t--+CHIRALITY
ssss
ss s
ss
ss
ss ssss s ssssssss ssssssss s
ss
sss
s
BEND..
5-TURN..
>>>>xxx xxxx<<<<
4-TURN..
3-TURN..
> 3 3<
>33<
>33< > 3 3 <
>33x33<
>33<
SSSS
E EEEEEEE ST TEEEEE S S EEEEEETTEE
S S STTS S TTHHHHHH HHHHHHHT S
EEEEE SS
B TTS EEE
SUMMARY..
* * 7 + + + 4 * 6 4 '1'39'2718
0 1 1 7 8 7 4 * 6 * ' 5 3 8 3 1 1 1 0 3 0153*****3 "6'887'836
519'219'2'
'1 4 8 13 0 * 2 9 * 9 2 + * 4 7 0 3 0
EXPOSURE.
ATSTKKLHKE PATLIKAIDG DTVKLMYKGQ PMWRLLLVD TPETKHPKKG VEKYGPEASA FTKKMVENAK KIEVEPNKGQ RTDKYGRGLA
SEQUENCE.
..
....
..
SHEET..
BRIDGE2..
BRIDCE1..
CHIRALITY
BEND..
5-TURN..
4-TURN..
3-TURN..
SUMMARY..
EXPOSURE.
SEQUENCE,
..
...
.
7LYZ LYSOZYME (TRICLINIC CRYSTAL FORM) [O-GLYCOLSYL HYDROLASE] (HEN EGG WHITE: GALLUS GALLUS)......................7LYZ
SHEET....
A
B
B
A
CC
CC
CC
DD
DD
DD
BRIDGE2..
A
B
B
A
ee
ee
CC
CC
DD
BRIDGE1..
ttt-t-t+-+ ++-++-t--+ +tt+-t-ttt
t+++t+ ++++-tt-t- -t--+ttt+t tttt---+-t +-----t-t- ----t----t
CHIRALITY
sss
s sss ss s s ss s sssssss ss
ssssss ssssss sss ss ssssss ssssssss s s
sss
BEND..
5-TURN..
>5555<
>5555<
>5555<>5 555<
>>>
4-TURN..
> > > 4 x x x ><<<<
>>>>xx xx<<<<
>444< > 4 44<
> 3 3<
> 3 3 < > 3 3 < >> > x < < <
>3
>33<>3>x 3<<>>3<<
> 3 3<
3-TURN..
EETTTTEET TTTEE SS T T
TT EEG GGGGSSS HH
B H H H H H H HHHHTT TTB TTB THHHHH HHHHHTSSBT T EE SSS
SUMMARY..
8 2 2 0 0 0 1 0 3 0 6'38746'19
65'672*470
8304669152
' 6 5 4 0 0 2 0 0 0 0 0 5 6 5 2 9 3 5 0 *287'7*720
EXPOSURE.
9'1473.803
108'6506'7
SEQUENCE. KVFGRaELAA AMKRHGLDNY RGYSLGNWVb AAWESNFNT QATNRNTDGS TDYGILQINS RWWcNDGRTP GSRNLdNIPc SALLSSDITA
..
..
.
sss
B B B B B
EEE EEEE
6.38660306 8*5*9*3126 3 3 2 4 8
TQANKH I IVA c EGNPYVPVH F DASV
+--
F F F F F
++-+-+-++-
EEEEE E E E E E SSS
-+-+---+--
AAAAA BBBB B
FFFF F
CCCCC EEE
CCC
..............................
EEEEEEE TT
>33 <>33<
BTTB EEE
31138*6889 2*'7'241*5
SITDaRETGS SKYPNbAYKT
ss
BRIDGE.?.
..
.
.
SS
>33<>33<
>>>d<YYdA<
S
ss s
ssssssss
-++++-+--+
>h44<
>33<
>>3<< > 3
ss s
GGGSSSSST
T TT S
* 6 5 9 3 3 8 0 5 1 7*8*3*5381 0 0 8 3 8 0 8 0 1 6
ENRLWRKTRS VTSSSLaVGV OANRNWDAGF
........... <
> 5 5 5 5<
S S S SSSSSSSS S SS
TSEEEEES S SHHHHHHHHH
6108000080 0 0 0 0 1 2 4 0 7 9
SMDIFLEIVT NPNGFAFTNS
<
.A<
+++++++++- ++++++--+- ++-+-+-+--
3<
>33
TSSSSBS TT
5'61339737
GKAGASSSPa
+-++++++++ +++++++++- ---+-++-+ssss sssssssss sssss
s
ss
> > 4 > x x > x x xx<<<<
> 3 3 <>33x33< > 33<
A A AAAAA
eeeee
d d ddd
f
G
A
OR S-TURN....S-BEND....
x33<
STTB SSTT SHHHHHHHH HHHHH EEE EEEEE SS E
374220**22 2160071807 41**36518R 0 0 0 0 8 0 7 3 2 2
SETYHGKYAN SEVEVRSIW FVKNHGNFM FLSIHSYSQL
sssss s ss sss
i
C
+-++--+-++ -++---+-++
i
C
SUMMARY........H~ALPHA-HELIX....E-BETA-STRAND....B-BETA-BRIDGE....G~3-HELIX....I~5-HELIX....T-3-,4-,
.
+------+++
EBB
CCCCC
AAAAA
SICPA
ICPA CARBOXYPEPTIDASE A (C-TERMINAL A M I N O ACID HYDRCLASE] ( C W PANCREAS: BOS TAURUS)
SHEET..
AAAAA AA
AAAAAA A
A AAAA
B
B
BB B
d dddd
BRIDGEl..
AAAAA AA
AAMAA A
c cccc
h
h
CHIRALITY
-+++-+++- ---+++++++ ++++++++++ ++---+---+-+------+--+------++++++-++ ++++++++++ ++++++++++ +-++++++++
BEND.....
SSS
SS
SSSSSSS SSSSSSSSSS S
sss
s ss
ssss
ssssssss ssssssssss s ssssssss
5-TURN..
4-TLBN..
>>>>YY!iY
Y Y X < < < 0 4 4 A<
>>>>xxxxx x x < x x < 4 x < 4 4 x > > > x < x < <
. .-...............................
3-TURN..
>33<
> 33<
>33 <
> 33<
> 3 3 x33<
>33<
>33x33
SUMMARY..
STT
SS
HHHHHHH HHHHHHSSTT TEEEEEEEE TTS E E E E E E E S SS E EEEE SSTT THHHHHHHH HHHHHHHHBT TBHHHHHHHT
EXPOSURE. *30**38355 4351*803*0 695837748' 3076**22*1 * * 2 8 3 0 4 8 0 5 0 2 5 3 5 f 8 5 4 0 R000880003 0 4 8 0 0 1 0 0 1 4 8014018286 '594035067
1 SEQUENCE. RSTNTFNYAT YHTLDEIYDF MDLLVAQHPE LVSKLQIGRS YEGRPIYVLK FSTGGSNRPA IWIDLGIHSR WITQATGVW FAKKFTENYG QNPSFTAILD
...
....
..
SHEET..
BRIDGES..
BRIDGE1..
CHIRALITY
BEND.....
5-TURN..
4-TURN...
. . . . . .
3-TURN...
SUMMARY..
EXPOSURE.
1 0 1 SEQUENCE.
24)
G
.lRNS
AM
+-+++----+
G
BBBBB
+---+---++
ss
C
AAAAAAA
CCCCCCC
.............................. C
lRNS RIBONUCLEASE-S [PHOSPHORIC DIESTER ( R N A ) HYDROLASE] ( C W PANCREAS: 80s TAURUS).
AAAAA
BBB B
B
BBB
A
SHEET..
A
BBBBB
EEE
C
BRIDGEZ..
a
DDD D
D
DDD
BRIDGE1..
a
CHIRALITY
--+++++++ +++--+-+
---+++++ +++-+-++-- ---+----+-+++++++++ --+---+-+++----+--BEND.....
SSSSSSS SS
SS
sssss ssssssssss
s
s sssssssss ss
sss ss
ss
>5555<
5-TURN..
> > > > X X X < <<<
> > > > x x <<<<
>>>4<<<
>444<
4-TURN..
>33<
> > > x < <<
>33<
3-TURN..
HHHHHHH HHB
SS
H H H H H HHHTTSSSSS
SEEEEE S HHHHHGGGG SEEEEETTTE E E E E E SS E
SUMMARY..
EXPOSURE.
'584348688 3114667*6* kl"45801.3
8876580*9* 2 4 9 5 2 1 8 8 2 5 376987588' 4*9470**69 '48456'761
1 SEQUENCE. KETAAAWER QHMDSSTSAA 1 SSSNYaNW MKSRNLTKDR bKPVNTPVHE SLADVQAVCS QKNVAdKNGQ TMYQSYSM
SHEET....
BRIDGE2..
BRIDGEl..
CHIRALITY
BEND..
5-TURN..
4-TURN..
3-TURN..
SUMMARY..
EXPOSURE.
101 SEQUENCE.
23)
0
UI
Q,
N
..
..
..
..
1APR ACID
SHEET..
BRIDGEZ..
BRIDGE1..
CHIRALITY
BEND.....
5-TURN..
4-TURN..
3-TURN...
SUMMARY..
EXPOSURE.
1 SEQUENCE.
ss
ssssssssss sss
--++++++++ ++++++++++ +-------+-
>>>>xxx xxxxx<<<<
--++----+ssss
AB
sss
E E
--+--+-+--EE
SSSSS
-++++----+
> 5 5 5 5<
+-+++++++- +++++-----
s ssssssss s s
SU~MARY
+--+-+-++-
s ssssss
sssssssss ssssssssss
-+++++++++ ++++++++++
----++-+-+
ss
s
----++--++
9
E
>
>
+++-+++--sss ss
H
+--+--+-+-
ss
---+--++-+
IIH
sss
J
H
lAPR
+----+---+
J
...................................................
F
GGF
H
+++-+----ss ss ss
(RHIZOPUS CHINENSIS).
BBB
B DD E
ccc
B
D ff g
>>44<<
> > > > x x < < <<
>>>>xxx xxxxxxxxxx
<
>33<
>>><< <
>33< >>3<<
>33<
S H H H H H H H H T S EEEEE
S SSSSTT
GGGHHHHHH HHHHHHHHHH
SSS
EEE EHHHHS
0 0 0 0 0 2 0 2 7 8 6 1 6 0 0 0 0 0 0 0 31'5*+14*1
43*4053005 0024002200
9 8 * 4 1 8 2 * 9 0 285857'610
SLYGTSYKYG S I I T T I Y Q A S GGSIWSYNQ CIKYSFWEL RDTGRYGFLL PASQIIFTAQ EIWLGVLTIM
S
eeeee
GGG
AAAAA
---++++-+-
SSSSSSSS
SS
++-+-++---
S SS S SSSSS
----++--+-
>
>
+++++++-++ -+-++--++SSSSSSSSSS
SSS
--++-+---+
sss
KKK
K
H
-+----++++----+---5s
ssss s
L
J
ssss
++----+---
LL
..
00
-,4-,
OR 5-TURN....S=BEND..
>4>x<4<<
>444<
>33<
>3<<
>33<
>33<
SSSS
EE
SS
TTSB S
B
SSEEE S SS S SSSSS
HHHHHHHSSS SSS
EE E TTT EEE
S TT EEEEE SSSSSSSS
37'2591726 21'1701078
4 0 1 5 1 2 1 0 4 9 1 2 4 4 6 2 4 6 3 1 0 0 2 0 0 0 0 1 4 9 7 3 1 5 2 * * 1 7 0 1 0 4 1 0 6 8 6 8 8 1 * * 3 0 0 0 0 4 0 0 2 3 * * 8 5 1 3 0 2132'5*'43
GGPQIQLAQR LGGGGFPGDN DGLLGLGFDT LSITPQSSTN AFDQVSAWK VIQPWVVYL AASNISDGDF THFGWIDNKY GGTLLNTNID AGEGYWALNV
S S
SS
ffI I
-------++-
I1 I
KK K
BBB
D
ccc
DDG G
I11
444<
>33<
> 33<
33<
TT
B TTSS B B E E SSS EE
EEESS
B EE BS
SS SS SS
B TTT SS
B
SS
EEB
BSSS B
''0489273'
5'04512090
4 0 1 2 ' 5 6 7 1 5 0 1 1 1 0 2 2 0 1 1 1 1 0 8 6 8 1 ' 5 5 0 0 * 8 6 2 8 7 1 5 4'80*66*75
9**175584* 2 6 1 5 1 5 0 1 1 4 1 0 6 1 2 6 1 7 0 5
GVGTVPMTDY GNDVEYYGQV TIGTFGKSFN LNFMGSSNL WVGSVQaQAS GaKGGRDKFN PSDGSWKAT GYDASIGYGD GSASGVLGYD TVQVGGIDVT
S
-+-------
A
PROTEASE [HYDROLASE: PROTEINASE]
A
AB C C
CC
X<<<<
>>3<<
HHHHT
7604**042
EHTVNNIGY
SSSS
++++
>33<
>>3<
EEES SS
TTHHHHHH HHHHHHHHTT
00102044** 61948'5869 00*502630*
LLYPYGYTTQ SIPDKTELNQ VAKSAVAALK
t--++++-+S SS
SSSSS
fff f
fff
GG
AAA A
AAA
........H~ALPHA-HELIX....E~BETA-STRAND....B~BETA-BRIDGE....G~3-HELIX....I=5-HELIX....T~3
.
..
SHEET..
BRIDGE2..
BRIDGE1..
CHIRALITY
BEND.....
5-TURN..
4-TURN..
3-TURN..
SUMMARY..
EXPOSURE.
101 SEQUENCE.
25)
....
..
SHEET..
BRIDGE2..
BRIDGE1..
CHIRALITY
BEND..
5-TURN..
4-TURN..
3-TURN..
SUMMARY..
EXPOSURE.
3 0 1 SEQUENCE.
..
..
.
SHEET..
BRIDGEZ..
BRIDGEl..
CHIRALITY
BEND.....
5-TURN..
4-TURN..
3-TURN..
SUMMARY.,
EXPOSURE.
2 0 1 SEQUENCE.
TABLE A111 (continued)
0,
tQ
Q,
0
..
..
.
..
....
..
BRIDGEZ..
SHEET..
3-TURN..
SUMMARY..
EXPOSURE.
1 SEQUENCE.
QQ
MM
--+-+---++
+-+--+--++
+++-++++-+ ----+-+++s
s ssss
ss sssss ss
ssss
> 5555<
LL
P
00
s
sss
----+--+--
s
s ss
R
---+++++--
0
0
N
ssss
--++++++--
sss
R
---+--+---
N
ssss
PQQ
-+-+-+----
LMM
>77<
--TL
PJ
+++++++---
s sss
---+--+++-
;;j
c ccc
N
sss
+--+-----+
C
CCCC
a
s ssssssssss s
++---+---+
BBBBB
DDDD
A
+++++++-+-
00 PPPP P PP
M MMMM MM I
PPP
P
...,.......,.......lAPP
c cccccccc c cc ccc c
ss s
s
BBBBB
DDDD
BBBBB
----+-++--
ssssss
R
-+++------
E
ssss
E EEE
+---+++-+-
B BBB
xxx
S
s wwwww
G GGGG
+---------
F
SUnMARY........H-ALPHA-HELIX....E~BETA-STRAND....B=BETA-BRIDGE....G~3-HELIX....I~S-HELIX..~~T~3-,4-,
OR 5-TURN....S=BEND....
EEEE S E E H H H H H TT S E E E E s GGG
BSSS
H H H H H T T T ~ S S E E E E E ss s E E E E E S
GGGBSS E E E E GGGTS B E E E E E E
410000848' '812000874 5 7 9 5 3 8 7 9 3 5 9241887'84 020*194240
1 0 1 0 0 7 * 1 3 4 8 3 7 ' 4 7 8 1 1 0 1 0 0 0 0 2 2 9 5 2 3 1 * * * 7 5 5 0 0 03486.615.
AVQAAQQISA WQQDTNNDG LLGLAFSSIN TVQPQSQPTF FDTVKSSLAQ PLFAVALKHQ QPGWDPGF I DSSKYTGSLT YTGVDNSNF WSFNVDSYTA
ss s ssss s s
11 00
---+++--+
PPP
cccc cc
MM
N
M MMMM
PENICILLIUM JANTHINELLUM]
D
cc
c cccc
>33 <
>33<
>33<
>33<
HTTS B H H HH EEEEEEE EEEE TTS E EEEEEEEEEE EETTEEEEEE
0 3 1 2 0 1 4 1 4 0 4026078'50
4 9 5 3 5 3 0 7 0 . 7 8 2 * * 5 * 7 6 8 882'6**515
QSGHSWNPS ATGKELSGYT WSISYGDGSS ASGNVFTDSV TVCGVTAHGQ
>33<
(FUNGUS:
>33<
>33<
E E E BSSS H H H
B EEEEEEE TTS EEEE EEETTEEEEE EEESS
'472618062 2781710206 0302768060 2020110000 00048877*3
AASGVATNTP TANDEEYITP VTIGCTTLNL NFDTGSADLW VFSTELPASQ
PENICILLOPEPSIN [HYDROIASE: PROTEINASE]
CCCC CCC CCCCC CCC
CC C D
HHH HHH
jjj
1 1
GG
I HHHHH H
KK K q
BB
HHHHTTB
EEETTTEEE
0 0 0 0 0 1 4 1 0 0 0 0 2 5 ' 7 1 0 5 0 854'
CDQFLKQQYV VFDRDNGIRL APVA
>444<
sss
>>44<<
-+-+-+---+
M
KKK
NNN
sssssss
NNN
T
-++++++---
KKK
P
>3 3<
>>3x<3<
>33<
SSS B
SSSSBEE
BSSS B
SSSS
SSSS
B S TTS
S EE
T TSSSEE S S TTTGGGTTS
SSSS
301150**1* 0714800354 ***9314001 0 0 4 9 6 6 8 0 2 0
5 1 0 5 0 6 * 5 * 0 2 6 * 2 ' 0 1 0 1 1 4 4 3 4 0 4 8 2 7 . 1 0 3 2 8 1 6 6 1 8 3897.73218 6155'4773.
TGATADSTYL GAIF QAILDT GTSLLI LPDE AAVGNLVGF A GAQDAALGCF VIAbTSAGF K S IPWSIYSAI F EIITALGNA EDDSGbTSGI GASSLCEAIL
ssss
+++--++-++
l A P P A C I D PROTEINASE,
A BBBBBCC
SHEET..
BRIDGE2..
BRIDCE1..
a BBBBBGG
BRIDGE1..
CHIRALITY
BEND..
5-TURN..
4-TURN..
)-TURN..
SUMMARY..
EXPOSURE.
1 0 1 SEQUENCE.
26)
....
..
SHEET..
BRIDCEZ.,
BRIDGE1..
CHIRALITY
BEND..
5-TURN..
4-TURN..
?-TURN..
. ....
SUMMARY..
EXPOSURE.
3 0 1 SEQUENCE.
..
....
..
SHEET..
BRIDGE2..
BRIDGEl..
CHIRALITY
BEND..
5-TURN..
4-TURN..
3-TURN..
SUMMARY..
EXPOSURE.
2 0 1 SEQUENCE.
s
Q,
t3
h
M
ul
..
HHHH
ss s
>5555<
-+-----++sss
BBBB
FF
EEEE
-
CR
IE
4><<4<
3x>3<<
HHHTTB E E E ETTTTEEEE B B
8 0 0 1 1 0 0 0 0 0 33*7170080 5 4 8
IFLKSQYWF OSDGPQLGFA PQA
sssss
+++++-+---
F F
C CCC C
I BBB B
>>>>xx<<<<
>>> <<<
HHHH FFF
BBBB
AA uuu
> 4 4 4<
> 5 5 5 5<
..
..
SWMARY..
I 1
B B B
C
sss
sss
5s
s
>>
DD
ss
>555 5<
>>> >xxxxxxxxx xxxxxxx<<< <
ssss ssssssssss ssssssssss
s ss
t+ttt++++t ++++tt+t+- t--+-+--tt
KK
f
..SIBEND.. ..
sss ss ss
+t--++-+++
J
C
STTTTS
E
88244*4228
LSYDGNNAAI
>5555<
--+-+----ssssss
B
..EsBETA-STRAND.. ..B=BETA-BRIDGE.. ..G-3-HELIX.. ..1-5-HELIX.. ..T=3-,
4-,
OR 5-TURN..
33<>33<
HHHHHHHHHH HTT
SSHH HHHHHHHHHH H H H H H H H H H H TSS SEES SSB SS SS
0 1 1 0 0 1 0 0 0 7 *4121998*6 1 8 8 8 0 8 8 8 8 0 1 8 8 0 1 8 8 3 9 4 * 4 * 4 3 3 3 8 0 3 587277**64
AHELTWVTD YTAGLIYCHE SGAINEAISD IPGTLVEFYA NKNPDWEIGE DWTPCISGD
> > > > x xxxxxxxx<< <<
> 5 555<
sss ssss ssssssssss sss
>>3<<
>
EEEEEE'ITT
E E SSSE E E E
SSSB
GGG H H H H
* 8 8 0 1 3 4 * 3 6 5 7 8 6 3 7 3 8 1 0 0883195'61 4 2 8 8 0 8 8 0 1 0
RSSVHYSQGY NNAFWNGSEH WGDGDGQTF IPLSGGIDW
>444<
s sss
---++---+-
BB
I1
h h h
J
t-t---t+-- ------tt-- --ttt-tt++ +++ttt+t++ t-----++-t
.H-ALPHA-HELIX..
.....
....
..
BBBB B
hh h
ffff
s
ttt
-+--+---+--+
V
FFF
33<
>>> <<<
>33 <
>3
TTEEEEE GG GGEEEEETTT TEEEESEEE
S SSEEE H
6 7 4 8 0 6 8 6 0 8 38331922.8 8 2 8 1 0 8 0 1 3 1 * 6 8 5 8 0 2 0 8 0
SGYTATVPGS LINYGPSGNG STaLGGIQSN SGIGFLIFGO
ss
B BBB
++---++--+
-----++--ss ss
sss s
s
H HHH
GGGGG
YYYYY
GGGGG
2222
w YYYYY
+-++++--++ -----+----+------++
HHHH
AA
s ssss
2222
+t-+++---+
ssssssss 5s ss
--+++t+++t
S
---++-+--+
ss ss
FF F
V
uu u
F FF
t tt
> 5 555<
> 4 44<
33<
>33<
> 3 3<
>33 <
>
TTEEE
E E E TT SSEE E H H H H H H H H TT SSEEEET TTTEEEE TT S
EEEEE
3*791*4260 1 8 2 8 3 2 4 3 0 3 0 5 9 8 0 0 6 6 8 1 952*52**4* * 3 5 1 5 0 8 7 6 * 3 * 2 2 8 8 2 0 2 1
GSQSGDGFSG IADTGTTLLL LDDSWSQYY SQVSGAQQDSNAGGYWDaS SSVPDFSVSI
ss
xxx
++------+-
GGG
ZTLN THERMOLYSIN [HYDROLASE: NEUTRAL METALLO-PROTEINASE] (BACILLUS THERMOPROTEOLYTICUS)............................ZTLN
AAAAAA A
AAAA AAA
AA B
BB BBB
BB AA
AA
SHEET..
BRIDGEZ..
bb
C
DD
ff fff
BRIDOEl..
AAAAAA A
AAAA A M
C E
E GG
GG DD
bb
+--+-+-+--+-+-+--+--+-+---+
-+++----------+-+-+
-----+-+-+
-++-++++++ ++++++++++ +++++++-+CHIRALITY
BEND..
sss
sss
ssss
s s s s
sss
sssssss ssssssssss ssssssss
5-TURN..
>5555<
4-TURN..
> 4 4 4 < > 4 4 > < > > x >x < x < < 4 <
3-TURN..
>33<
>33<
>>3x<3<
>33<
SVPIMARY..
E E E E E E E S S S E E E E E E E SSSEE B SSTT E E E E E TT S S S E E EESSS EE SGGGTTT SSTTTTTHHH HHHHTTTS
EXPOSURE.
400*4**558 106853'082 0320'**8*6
9.48749138 *83'55*3*8
6 3 5 3 2 5 2 6 9 2 9875'92118 0888'18018 1 3 1 8 7 * 7 2 * 3
1 SEQUENCE. ITGTSTVGVG RGVLGOQRNI NTTYSTYYYL QDNTRGDGIF TYDAKYRML PGSLWADAON QFFASYDAPA M A H Y Y A G V T YDYYKNVHNR
SHEET..
BRIDGEZ..
BRIDGEl..
CHIRALITY
BEND.,
5-TURN..
4-TURN..
3-TURN..
SVPIMARY..
EXPOSURE.
1 0 1 SEQUENCE.
27)
..
.
..
....
....
SHEET..
BRIDGEZ..
BRIDGE1..
CHIRALITY
BEND..
5-TURN..
4-TURN..
3-TURN..
SUMMARY..
EXPOSURE.
3 8 1 S EQUENC E
..
.....
..
SHEET..
BRIDGEZ..
BRIDGE1..
CHIRALITY
BEND..
5-TURN.
4-TURN..
3-TURN..
SUMMARY..
EXPOSURE.
281 SEQUENCE.
TABLE A111 (continued)
N
Q,
P
l3
0
03
..
..
s
ssss
-+--+-+++-
ss sss ss
++-++---++
++++++++++
+++++-4-+-
ssssssss ssssssssss ssssss
s
LL
-+-------+
ss
EE
>33< > 3
HHHHHHHHHH
'204809508
QEVASVKQAP
><3<
HHHT
80020'
DAVGVK
> 5555<
>>>xxxxxxx <<<<
ssssssssss sss
++++++++++ ++-+
..
....
..
SUWUARY..
SS
B
---+-+--+
ss s
ss
-+-----
NNNNO
++-+-----+
sss
0000
ss
+-----++--
CCCC
nn
P
P
++-++-++-sss s
..2GCH
CC
00
D
A
GGGGG
F
.
sss
..
C
BBB
HHH
+--+--+---
B BBBBB
H HHHHH
EE
4-,
OR 5-TURN..
.S=BEND..
>33x33<
>33<
TTTSGGG T TEEEEE SS B TT TT E EEEEETTEEE
***63*'18'
1 0 1 0 8 0 3 6 3 2 1 2 1 7 1 0 2 0 0 0 080'7'5221
KKYWGTKIKD AMIdAGASGV SseMGDSGGP LVCKKNGAWT
> > 4 4 x <44<
3 < < > > 3 < < > 3 3<
ss ss
---+++++--
A
BBBBB
> 5555<
> 444<
>33<
>33<
EEES S TT SSS EEEEE E E E E E TT B TTTTBS EE
5'44'0*'57
8'55338010
0002223464 '*5'64*0*:
WAGEPDOCS SSEKIOKLKI AKWKNSRYN SLTINNDITL
--++++-++s s ss
KKK
,
............... D
...............
ccccc
+-----++++
+++--++--4
+--++++-+ssss sssssss s s
ss
888 BBBB
DDD DDD
88
F
TAURUS)
NNN
ccc
..E*BETA-STRAND.. ..B-BETA-BRIDGE.. ..G-3-HELIX.. ..I - ) - H E L I X . . ..T-3-,
> 33<
++----++-+
ss
ss
D DDDDD
EE
B BBBBB
>33<
>>
TT
TT E EEEEESS S
SS EEE EEEB
HHHH
8 6 8 7 6 5 1 8 7 7 '583102415 5.5'356559
080000846' '0929'1381
5840253'60
LKLSTAASFS @TVSAVsLF5 ASDDFMGTT cVT'NiWGLTR Y I TPDRLQQA SLPLLSNTW
EEESS
ss
C
B
+++-------
.H-ALPHA-HELIX..
.....
.
..
SS
---+----+-
CCC
000
UU
++++++++++ +++++--++-
ssssssssss ssssss ss
> 5555<
>5555<
> >>>xxxxxxx x<<<< >
44>X4>XX4< <<
33x33<
>33<
>33< >33<
TTTHHHHHHH HTTT TT
HHHHHHHHHH HHHHTT TT
'688908370 04'9167'14
0 5 9 0 3 4 1 8 4 9 80456839*1
DKLGKIFYRA LTQYLTPTSN FSQLRAAAVQ SATDLYGSTS
ss
++++++++++ ++-+--++--
s ssssssssss ssss
> 5 5 55<
>5555<
> > 4 4 x < 4 4 < > > > > x x x xx<<<<
>
>>3< <
>>3<<
>>><<< >> 3 < <
>
SEESS GGG TT
SGGG
SSSHHHHT TTTTHHHHHH HHHHHT EES SS EE
S
0 5 3 0 0 4 8 0 5 * 77222369''
7'34.59108
5 4 1 0 0 0 0 0 2 0 86001813*2 '758174239
SLRSUSDPAK YGDPDHYSKR YTGTQDNGGV HINSGIINKA AYLISQGGTH YGVSWGIGR
----++++++
EE
LL
DD
RK
2GCH G M U A CHYUOTRYPSIN A [HYDROLASE: SERINE PRoTEINASEl ( C W PANCREAS: BOS
SHEET..
A 88
ccccc
c cccc c c cccc
c
BRIDGEZ..
KKKK
L L L unun
N
BRIDGEI..
A 88
JJJJJ
J JJJJ
LLL
K
CHIRALITY
+--+----+++-----++
+++++----+-+-++------++--+-++----++-BEND..
ss
sss
ss ssss
ss
ssss
sss
sss
5-TURN..
(-TURN..
3-TURN..
>33<
> 3 3 <>33<
> 33<
>33<
> >3<< >33<
SUUMARY..
SS
SET E E TT SSTTEEEEE TT E E E E E E EEETTEEEE GGG
TTSE
EXPOSURE.
48.854'29'
32*28*0472 8 1 0 0 1 0 0 0 2 4 *'5*141000 0 2 4 9 6 i 0 0 0 0 1 6 2 5 2 7 9 7 2 3
1 SEQUENCE.
aGVPAIQPVL SVNGEEAVPG SWFUQVSLQD KTGFHFbGGS LINENWVVTA AHBGVTTSDV
SHEET..
BRIDGE2..
BRIDGEl..
CHIRALITY
BEND.....
5-TURN..
4-TURN..
3-TURN..
SWUARY..
EXPOSURE.
1 0 1 SEQUENCE.
28)
....
..
SHEET..
BRIDGE2..
BRlDGE1..
CHIRALITY
BEND..
5-TURN..
4-TURN..
3-TURN..
SWUARY..
EXPOSURE.
301 SEQUENCE.
..
...
..
SHEET..
BRIDGE2..
BRIDGE1..
CHIRALITY
BEND..
5-TURN.. a
4-TURN..
3-TURN..
SUWUARY..
EXPOSURE.
201 SEQUENCE.
N
(0
0
Q,
or
..
...
..
S
CC
sss
s
--+-+----+
NNN
CCCC
MMMM
j
CC
MU
-+-+-----+
MM
E
R
H-ALPHA-HELIX.
D
E
LLL
-++--+--++ ++-++----+
sss
ss s ss
ss
+----++-+-
-+--->55 55<
sssssss s
---+++++++
BS
FF
PP PPP
NN N
>33<
>33<
ETTEEEE B
TT
58'7'140.1
3973675370
NGSSFVTVRG STEAAVGAAV
ss
ss sss
s
+++++-----
00000
MMMM
+----+-+++
sss
ss
lPTN
...........ccccc
............
---++--++-
N N N N O 00 00
+++-++-+-+ +--+---+-S
s sssss s
ccccc cc cc
...E-BETA-STRAND ....B~BETA-BRIDGE....G~3-HELIX....I-5-HELIX....T=3
-,4-,
OR 5-TURN....S-BEND....
>444 <
>33<
> > 3 <<
>33<
>33<
>33<
SSEEEEEEEE ETTEEEE GG G SS EEEE S SSTTS S
EEEEEEEE EE TT TTT TT EEEEE SS
SSS
7 * 4 3 1 0 0 0 0 2 5 4 7 1 0 0 0 0 0 7 0 * 5 * 6 1 5 0 5 0 1 1 2 3 3 * 7 * * 5 5 3 3 8 2 4 2 7 6 4 452'7678'7
3420000040 *851887*70
GYHFbGGSLI NSWWSAAH bYRSGIQVRL GEDNINVVEG NEQFISASKS IVHPSYNSNT LNNDIMLIKL KSAASLNSRV
SS
+-++-+--+-
NNNN
KKK
MMMM
cccc
L
LL
J JJJJ
8) [HYDROLASE: SERINE PROTEINASE] ( C W PANCREAS: 80s TAURUS)
c ccccc c cccc
BBBB
cc ccc
+--+++-+--
ssssss ss sss
R
----+-+-++
CCC C C
PPP P P
00
D
q
AAAA
--+----+++
A
B
........., , ,..... . .lALP
>444<
> > 4 > x < 4 <<
3<
>33<
>>3<<
>33<
TTSBSS SS GGG E E EEESHHHHHH HT E E
T B EEEEE E
7 0 6 0 1 0 0 0 0 1 3367**0207 6383**5401 1080*302** 24172395
AGQAQGVMSG GNVQSNGNNC GIPASQRSSL FERLQPILSQ YGLSLVTG
q
-+-+---+-+
s s
3x33<
>3
T TT EEE T
102000003*
GDSGGSWITS
CCC
00
LL
++++--+--+
ssss
>3
EEEETTTEEE E EEEEEEE EE SSSEEEE EEEE S BT
004020010*
0081.55455 6 2 4 8 5 3 7 ' 4 7 1*6'*360*2
bRSGRTTGYQ bGTITAKNVT ANYAEGAVRG LTQGNACMGR
>444<
sss s
--+-++--+-
C CC C
M MM M
+--++-++--
KKK K
.......
.
..
.....
...
CCC C
KKKK
LL
CCCC
IPTN BETA-TRYPSIN (NATIVE AT PH
A BB
ccccc
SHEET....
BRIDGE2..
KKK
BRIDGEl..
A BB
JJJJJ
CHIRALITY
++------+ +-++----+BEND...,.
S
SS SSSS
S
5-TURN..
4-TURN..
3-TURN..
>33 0 3 3 <
SUMMARY..
BS EE TT SSTTEEEEES
EXPOSURE.
0153.82364
9132100023
1 SEQUENCE. IVGGYTaGAN TVPYQVSLNS
SUMMARY.
30)
ssssssss sssss
--++++++++ +++++
G
> 4 4 > x > > x xxx<<<<
3<>33<
>>3<<
T TTSEEEE EEGGGTHHHH H H H H H H
7 0 3 4 8 3 0 1 0 0 0 50 3 6 0 5'1 0 ** 138 8
TeSTSTPGW ARVTALVNWV QQTLAAN
GGGG
B B B B SB
I 1 I1
---++---+s s sss
>3
EEEEEEE T
0 0 0 0 1 0 5 3 2'
LVGIVSWGSS
++--+-++-+
I11 I
H HH
B BBB B
lALP ALPHA LYTIC PROTEASE [HYDROLASE: SERINE PROTEINASE] (MYXOBACTER495: LYSOBACTER ENZYMOGENES)
SHEET..
A BBB B
BBB
BBBB BBB BB
BBBS BB BBB BBB
C BBSBBB
AAA
BRIDGE2..
DD D
FF
G GG
HHHH
I11 111
111111
BBB
BRIDGE1..
a CCC
CCC
EEEE E E E E
DDD H H HH
j
GGG
a
CHIRALITY
-+-++-----++-+----+----+-t- -+--+++--+
+----+-+-+
-----+--++
--++-..---++----+--+
BEND..
ss
sssss
sss
ssss s s
ssss
s s
sss
5-TURN..
4-TURN..
3-TURN..
>33<
>33<
> 3 3<
>33<
SUMMARY..
BT EEE ESSSSEEE
EEEETTEEE EE SSSS T T EEEETTEE EEEEEEEE S S EEEEEE SSS
EEE
EXPOSURE.
6'02817702
1 8 * 7 8 8 0 0 0 0 0105'89640
0 0 0 0 0 4 2 0 9 6 ' 0 5 8 6 1 8 8 6 8 0 0 6 1 4 3 9 6 2 4 3 4 0 4 0 2 0 3 2 6 993'443.03
1 SEQUENCE. ANIVGGIEYS INNASLaSVG FSVTRGATKG FVTAGHaGTV NATARIGGAV VGTFAARVFP GNDRAWVSLT SAaTLLPRVA
SHEET....
BRIDGE2..
BRIDGE1..
CHIRALITY
BEND.
5-TURN..
4-TURN.
3-TURN..
SUMMARY..
EXPOSURE.
1 0 1 SEQUENCE.
2 9)
..
....
SHEET....
BRIDGE2..
BRIDGE1..
CHIRALITY
SEND..
5-TURN..
4-TURN..
3-TURN..
SUMMARY..
EXPOSURE.
2 0 1 SEQUENCE.
TABLE AIII (continued)
z
M
U
Z
2
0
N
..
B
.
-++----++-
ss
BBBBBB
EE
DDDDDD
+--+-++-+s
sss
--+-----+ss
ssssss ssss
ss
+-+++--++-
> > > > x < << x 4 4 4 <
----++++++
BBBBB BB
DDDDD D
BB
F
s ssss
-++--+-+++
F
G GGG
B BBB
.
..
.
....
ss
s
---+++++--
A
A
ssss
P
D
ssss s
+-+----+-+
BB BB B B
HH H H
c I I I I
----+-++--
EE
B BBB
H HHH
++++++++++
t
> > > > x x x x <<<<
ss ssssssssss s
3<
>>> <<<
> 3 3<
TB EEEEEGG GGHHHHHHHH H H
870 0 0006 0 2 7 1 3950**14 8 89
NKPGWTKVC NYVSWIKQTI ASN
S
++------++
1111
P GGGG
D BBBBB
>>3<<
ss
1x1
H HH
--++----+s
s
9
HH
cc cccc
ss ss
+--+++++--
1
C
EE
00
+---+-+-+sss
E EEE
00
N NN
ss sss
P
F
+-+-+--++-
K KK
1
C CC
I11
KKK
CCC
+---+---++
P
F
BB
cc
'
>5555<
>x<4<<
x33x33<
HHHHHTT EE
9029655093
EALSAYGATV L
+++++-+-ss ssssss
>444 <
>>4
>33x33<
>33<
>33
EEEEEEEEE E E E E E GGG EEEEEEEES
TT BT E EEETTEE
EEEESSBTTT B EEE HH
1 5 8 * 1 5 0 6 1 9 * 28 2 * 6 3 * 9 1 7 0 ' 3 0 1 7 8 7 1 1 1 8 * 0 0 2 0 0 0 0 0 2 5 3 3 0 0 0 0 1 1 2 5 9 6 6 1 * * 2 3 5 0 3 0 0 3 0 5
GLRSGSVTGL NATVNYGSSG IVYGMIQTNV CAQPGDSGGS LFAGSTALGL TSGGSGNCRT GGT'ITYQPVT
s s
+---t-++--
H HH
---+--++-+
C CC
EEEEEC C
MMMMMH H
ss
NNN
MMMMM
-----+-++-
+-+----++
LLL
sss
lSGA
EEEEE
DDD
>33 <
EE S S S EEE
TT EEEEE S S S
0447'7776'
08724*2*96 2817000251
WLYNGSYQD ITTAGNAFVG QAVQRSGSTT
sss
---+-+----
LL
DD
... .................................
>33<
>33< >33<
>33<
>33x33<
>33<
>3
B SS
TT EEEEEE S
SSS
S S EEEEE EB
H H H H H H HSTTT TTE EEES TTSS B TT TT E EEETTEEEEE EEE SSSSBT
351851'763 8664'14000
0 0 0 2 * 6 * 5 +6 ' 2 7 3 0 4 0 1 * 0 4 1 2 5 9 9 2 0 9 8 1 0 9 9 9 2 4 8 3 1 2 0 0 0 7 7 * 1 4 ' 1 1 1 * 2 0 2 0 0 0 010'490100
115375118'
ASISLPTScA SAGTWLISG WGNTKSSGTS YPDVLKaLKA PIffiNSSeKS AYFCQITSNM FeAGYLQGGK DSfQCDSGGP WdSGKLQGI VSWGSGfAQK
ss
c
------+---
,
lSGA PROTEINASE A ISGPA)
.
. [HYDROLASE: SERINE PROTEINASEl ISTREPTWYCES GRISEUS)
i 'BBB B
c BBBB B D
SHEET..
AA
AA
BB BB BBBBBB
FFF F
FFF F
BRIDGE2..
C C
DDDD
L
a
DDDD
E E
BRIDGE1..
AA
AA
BB BB BBBB
CHIRALITY
-++-+++-- +-+-----+---+-+--+-+++++--++ -+----++++
+++-+-----+-+++--+BEND.....
SSS
SS S
sss
ssssss s
ss
sss
sssss ss
5-TURN..
4-TURN..
>>44<<
3-TURN..
>33<
>33<
>33<
SUMMARY..
SSSEE SS S EE
EE EETTEEEEEE HHHHSS S BTTEEEEE
SBS EEEE ESSTTS SE
EXPOSURE.
4 0 0 0 5 5 0 4 5 7 9 5 * 1 0 0 0 1 1 1 42'6422008
0040068349 1 6 2 1 7 7 9 1 5 3 478202000* 18'9832528
1 SEQUENCE. IAGGEAITTG GSRCSLGFNV SVNGVAHALT AGHCTNISAS WSIGTRTGTS FPNNDYGIIR HSNPAAANGR
SHEET....
BRIDCEZ..
BRIffiEl..
CHIRALITY
BEND..
5-TURN..
4-TURN..
3-TURN.. ,
SUMMARY..
EXPOSURE.
1 0 1 SEQUENCE.
31)
.
..
SHEET..
BRIDGEZ..
BRIffiE1..
CHIRALITY
BEND.....
5-TURN..
4-TURN..
)-TURN..,
SUMMARY..
EXPOSURE
2 0 1 SEQUENCE.
..
.
.
...
SHEET....
BRIDGE2..
BRIDGEl..
CHIRALITY
BEND..
5-TURN..
4-TURN..
3-TURN..
SUMMARY..
EXPOSURE.
101 SEQUENCE.
or
E
n
A
5
x
53a
<
z
ss
Y
I
s
x xx
1 1 1 I 1111 I I 111111
TI 11 x nx
rrrrr
33 33 3 3333 3 3333 33 333333
:SY3UWYd D I d ) [ 3 S V N I Z & O M d 3 N I U 3 S : 3 S \ n O W A H 1
"K3MIYE
8 8 4'
* *zaxaIw
* * * . L33HS
88 Y
3SYLSM3-1XSOL
LS31
ss
v
3
we
PSPP
YWY
9 99q
YY
s s
PPPP
VYYY
[ 3 S Q N I 3 L O k ! d 3 N I U 3 S :3SV7OtlCIAH1
BE
'*
JaaHs
'NMIIL-S
.....
aNae
ALI1YYIH3
L33HS
(EE
1
*-I~MIME
-*'..
'zma1~8
'AMVWwnS
'33N3003S
'3MnSOdX3
' ' 'NMnL-C
"'NMIIJ-P
*
'*
'NMnL-S
.....
"K3XIME
A L I I Y aMNI 3HE3
JBSK
"Z3MIUE
....
LaaHs
(ZE
' 3 3 N B n O 3 S T01
'3MnSOdX3
"AUYWWIIS
"'NUnJ-E
"'NMnJ-C
'***
"23!XIME
"13MIM8
* * . * * (IN38
ALIlWIH3
* * 'NMIIL-E
* ' 'NWJ-P
* 'NYnL-S
' 3 3 N W l O 3 S KBZ
dlLSO1ShM
EE008K9EQB ' 3 M n S O d X 3
~~ ~3 3 3 3 3 s3~ **mvwwns
P<
aaaaa
11111
+---+-+-++
ss s
1 S S U A O J N J M N d H Y S 1 1 1 Y Y YDYAHdSYWS L D N A V 3 A X N 3
KESS06828I *6ECEZ0000 000K000001 006r9K9.rE
HHHHHHHH s LJSHHHHHHH HHHHHHHHHH H 3 3 3 3 3
XCEXEC< > EE<>EEXEE< >EEXEE<>E E<
P>XX><<<<
> > P > X X > X xxxxx<xx<r < <
>PV
>SSSS<
s
3
++++++++-- -+--++-+-+---++++++ +++++++-+rr
n ww
ssssss ssssssss
+---+-++++
a
P PPP
YY Y W
>ssss<
sssssss sssssss
aaaaa
11111
++++++++-- ++++++++++ ++++++++++ +-+---+-+-
>>>>xx xxxxx<<<<
ssss ssssssss s ssssssssss ssssssssss s
+---+--+++
sssss s s
OYYVO A N I 1 3 X D A A I S ( I D l P L J L N ( I
r00P6 Bt010rKP65 6 r E P . L E P r Z
HHHH H E JLHHH H s ESLLH
>EE<>E E <
>>E<
> > P I <<
>>
4
I
\I
ss ss
++++--++-+ --+--+----
ssss ssss
-+-----++-
>PCt<
sss s
+++ +---+---++
>>>I<
<<
NNNN NWWW W
o
rrrrr
1111
muww
NNNNN
33x3
L33333
s ~ I . . . . . . . . . . . . . . . . . .3333
. . . . .3333
. . . . .3. . . . . . . . {YaOMSS
.a
SnS
sss
-++---+-+-
x
3
aa
V M a 7 3 d M S S d S V M O N S S a A Y M Y I A S d A x M A 3 A L S S S X S 3 3 N D Y Y Y M A A 3 S Y A Q X MYYX'IYYSD S d D D l S W N I A a W N N Y I Y M 3 1 D N I I M S A O D S
000f096000 09rlSwSBLS 0 0 0 0 0 1 0 E ~ Z S009KKZE+* 9r8KrLKBT0 BQBKE+6EBr 900S80P6SZ 8rTSE00000 91rLLC0990 06ElSS9r9C
SE
3333 S LLHHHHHH H H H H H H H 33
S 33 3 3 3 L H H H H H H H H H H H H H
SL LS
333 LL
SLL E LL 333333SJL.5 LLLE
>EE<
>EE< > E E <
m x Ec<
x E<
>>E< <
>EEX>E<<
>EE<
>>>>XXX XXXX<<<< >
ss
3
-+--+++-+3
VVYWY
aaa
333
q
Y
3333
Y W
>EE<
3535
> >E<<
>EE<
>E E X E C <
>EE<
>EE<
> EEXEE<
>>>P < X X > P < < <
> > > P < < X > >><<<<
> ssss< >ss ss<
sssss
ss ++++++++-+
ssssssssss +-++-+-++ss
ss +---+----+ s +-++-----+
s ss
ss ---+-+++-+
ss s +-+++++++ssssssss s +++++---sssss
--+-+--+-+
YVYQ
Sn1113YE A l E V 8 0 M d )
aNdE N I S I l I L E f l S
3 Y a D 7 A X A Y A 1 Y S S d Y A D l A 3 I S N N ' l Y Y A J 3 Y A H J 3 H S N a Q O d N d J 3 S d A WSYDDYAX1a d H S S Q I D S C I I A Y A X A N S D W D O S H l Y d Q X I O S A D A d A S O Y
P E E Z Z S E I Z ~ L069E00000 0009T.L0ZB
SB.EBZP090
PL008C6LLr
3333
L L LL
833 3333 JJ S LLLHHHHHJH H H H H H
>EE<
s ss
---++++--w e e ee
YY
(SN313Vd3Il61101AWV
Pr60V0000P 0 Z Z E Z 0 0 0 Z l 1966rK0101 0 0 0 0 0 0 S E S 6 266KS.SrrK
JLL33 3333 33 JLSS
SSSSS
HHH HHHHHHHSSS
SS
JL
PPP<
rr
ss
--+--++-+5553
88 YYVY
~EsK"........"".*'".......
..
..
------++-ss
--++-+---+
ss
Q
F
-+--+-++-s ssss
BBBB B
ODD D
CCC
D BBBB
DDDD
ss
0 88
--+-----+-
Q
F
>
ss ss ss
S
H
S
H
>> >>xxx<<<<
++++++++
sssss ssssssss
-----+++++
BBBBB
HHHH
FFFF
++--------
33< > 3 3 <
>>3<<
>>3<<
EEEEEEEE B TTBSSBTTB EEEEEGGGSH HHHHHHHHT
1 0 1 0 0 1 0 3 2 1 ** 1 0 5 4 8 * 5 0 0 0 0 0 3 0 0 5 1 2 84R7.12899
AVHGVTSFVS RLGdNVTRKP TWTRVSAYI SWINNVIASN
-++--+----
>
R
R
+--++-++--
G
B B BBB B G
HHH H
GG GG
..
..
.
SUMMARY.
ssssssssss s
>4<<<
> >>>xxxx<<<<
>33<
>33<
HHHH
B
EEEE TT HHHHHHHHHH S EEEEE
7 4 4* 6 **0 6 1 8559'18.67
1*2014103* 2000010215
ALQDQKYVTI DTYENVPYNN EWALQTAVTY QPVSVALMA
ss
+++++++++- ---+-+-+++
ccccc
AAAAA
D
CCC
----+--+-+
ss
> 5 5 5 5<
88
GG
ssss
>444<
ss
+-+-+----+
>>
s
.2ACT
sss
---+-+----
I
B
H
A
4-,
H ee
GGGGG
AAAAA
OR 5-TURN..
SIBEND..
..
..
4<
33<
TTEEEEE
*020404187
EGYURILRNV
--+--++---+-----++ss sssss ss
AAAAAA A
GGGG G
FFFFFF F
3<<
H H H H H H H H H H T B BTTTS
SS
H
33006284.2 4 0 0 0 2 3 9 6 1 7 573973'489
TDGFQFIIND GGINTEENYP YTAClDGDbDV
>>xxxxx<<<<
AAAAA AAA AA
FF FFF FF
CCCCC AA
+-+--+--+-
L J
+++++++++- -----+++-ssssssssss s
E C
...............................
>44
>33<
>33<
>33< >
SHHHHH S S EE
SS
EEEEEEEEE EETTEEEEEE E SB TTSTB
3.489'2793
4292.43984
9 1 1 0 1 0 0 B 0 0 7.87652080
111766.226
GDAFKQYASG IFTGRGTAV DHAIVIVGYG TEGGVDYWIV KNSWDTWGE
>>>4<<<
-++++++-+- -+--+--+-+
ssssss ss
ss
ee
AA
BBBBBB
GGGGGG
3 3 < > > 3 < < > 33 <
>33x33<
>33<
TTTTGGGS T TEEEE S S S SB TT TT EEEEEETTEE
* 7 6 3 2 * 5 0 7 9 3 2 2 0 0 2 1 7 2 9 9 0 0 1 * 1 0 3 0 0 001064'7*'
SSYWGSTVKN SMVCAGGOGV RSGd QGDSGC PLHb LVNGQY
5555<
.......HIALPHA-HELIX.. ..EmBETA-STRAND.. ..B-BETA-BRIDGE.. ..G=3-HELIX.. ..I-5-HELIX.. ..T=3-,
....
..
BBBB
-------++-
L
++++-++--ssss
AAAA
E
A
A
BBBB
FFFF
EE
+--+-++-++ +---+++++sss s s
sss s
ss ss
++---++--+
ssssss sss
----+++++-
EE
88
>>44<<
>33<
>33<
>33<
>33x
S
BTTB
TT
TT EEEE ES BSSTT
B SB EEEE
EE HHHHTS
' 70 9 66 8 9 09 6 1 6 5 1 * 6 5 4 * 4 7 6 ' 2 5 8 6 0 0 0 0 0 2 6 * 5 * 4 * 7 1 * 2 1 3 3 0 8 0 2125.76845
QSVTLNSYVQ LGVLPRAGT I LANNS PbYIT GWGLTRTNGQ LAQTLQQAYL PTVDYAIC S S
>33<
----+-+++s
sss
E
P
E
P
2ACT ACTINIDIN [HYDROLASE: SULFHYDRYL PROTEINASE] (KIWIFRUIT: ACTINIDIA CHINENSIS].
SHEET..
AA
B
C
D
D
BRIDGE2..
BRIDGEI..
AA
I
J
K
K
CHIRALITY
-+++-++++-++++++++ ++++++++++ +-+-+---++ ++++++++-- ++-++-+--+
BEND.....
S
SSSS S
ss
sssss ssssssssss sss
s ssssss
s s sss
s
5-TURN..
> 5 5 5 5<
> 5 5 55<
>5555<
4-TURN..
>>>>xxx xxxxxxxxx< <<<
> > >>x<<<<
>>
3-TURN..
>>><< <
> 3 3< > 3 3 <
> 3 3 < > > 3 < < >>
SUMMARY..
S EEGGGG T
B T TS H H H H H H H H H H H H H H H H HHS
8 H HHHHHH BT TB GGG
H
EXPOSURE. * 6* * 2 24* * 5 4822.23515 * 1 3 0 2 0 0 1 0 0 0 1 0 0 0 0 1 1 6 7 6 7 4 6 7 5 4 0 0 0 0 0 0 0 2 2 1 * 6 * *0*03*23*1
1 SEQUENCE. LPSYVDWRSA GAWDIKSQG EaGGCWAFSA IATVEGINKI TSGSLISLSE Q E L I BG RT Q NTRGaDGGYI
SHEET..
BRI.DGE2..
BRIXEI..
CHIRALITY
BEND..
5-TURN..
4-TURN..
3-TURN..
SUMUARY..
EXPOSURE.
101 SEQUENCE.
34)
....
..
SHEET..
BRIDGE2..
BRIDGE1..
CHIRALITY
BEND..
5-TURN..
4-TURN..
3-TURN..
SUUUARY..
EXPOSURE.
2 0 1 SEQUENCE.
..
.
...
SHEET..
BRIDGE2..
BRIDGE1..
CHIRALITY
BEND..
5-TURN.. ,
4-TURN..
3-TURN.. ,
SURUARY..
EXPOSURE.
1 0 1 SEQUENCE.
E
w
N
3
M
f3
z
0
c3
..
..
..
..
CHIRALITY
BEND.....
5-TURN.
4-TURN..
3-TURN..
SUMMARY..
EXPOSURE.
1 SEQUENCE.
...
BRIDGEl..
++--------
SSSS S
> 5 5 5 5<
ss
SSSSSS
A AAA
>>>> x x x x < < < <
X<3<
GTTS EEEE
0013412403 '5
GLYTSSFYPV KN
S SS
AAAA
D
BBBB
+++-+-+---
<
ee
AA
s
SSSSSS
sss
sss
-+--+-++-+
s s
ss
--+----++-
AA AAA AA
FF F
CC CCC AA
I
H
ssss
--+++--+-+
5
s
ssss
-+--+++++-
.BPAP
>444<
ee
AAAAA
GGGGG
----+-----
ss ss sssss
-----+--++
F FF
G GGGG
A AAAA
ss ss ss
++-+-+--+-
>>44<
>33
HHHHHHHS B BSSSS
S S
HHHH
005202**00 194'606491
86**150*'9
ALQLVAQYGI HYRNTYPYEG VQRYbRSREK
xxxx<<<<
sss ssssssss
+++++++++- -++++--+++ ++++++----
............................
C B
OR 5-TURN....S=BEND....
33<
>>3
TTT SSSEE
S
S
EE EEEEEE SSE EEEE SS SS STTTSEEEEE
SS S S G G
0**2'3372'
2'42'*5921
0000010565 0102016398 216'028807 45'777'018
FQLYRGGIFV GPcGNKVDHA VAAVGYGPNY I LIKNSWGTG WGENGYIRIK RGTGNSYGVC
> 444<
+-+-+++-++ ++++-+--+s ss sss sss
c cccc
A AAAA
D
>33<
>
S SB S E EEE S S HHH HHHHHHHS E EEEE S SS
3'951'8925
'*1*5*7552 12'1028210
670202871'7
GPYAAKTDGV RQVQPYNQSA LLYSIANQPV SVVLQAAGKD
<
I
B BBB
+--++--------++-+++
++++++---S S
S
ss sss ssssssss
C
H
>555 5<
<<<
>> > > x < < < <
>>>>
>33< >33<
HH
B H HHHHHH TTT TSTT
HHH
*85*636000 0000031**0 '04'3281'8
RTGNLNQYSE O E L L W D R R S YGaNGGYRJS
ssssssssss ss
+-++++++++ ++++++++++ +-+-----++
> > > > x x x xxxxxxxxx<
>33 <
>33<
>33<
S EESTTT T
SS
HHHHHH HHHHHHHHHH
*7**134*** 3022932714 *030210100 0100000155
IPEYVDWRQK GAVTPVKNQS SaGSCWAFSA W T I E G I I K I
S
-+-+-+++-
AA
(HYDROLASE: SULFHYDRYL PROTEINASE] (PAPAYA FRUIT LATEX: CARICA PAPAYA].
AA
B
>33X>3X<3<
T T GGGTTS S EEEE
5521 100004 8005034*
GGAGTCGIAT MPSYPVKY
TABLE A111 (continued)
SUMMARY........H=ALPHA-HELIX....E=BETA-STRAND....B=BETA-BRIDGE....~=3-HELIX....I=5-HELIX....T~3-,4-,
..
SHEET..
BRIDGE2..
BRIDGEl..
CHIRALITY
BEND.....
5-TURN..
4-TURN..
3-TURN...
SUMMARY..
EXPDSURE.
201 SEQUENCE.
..
.
BBBB
D
AAAA
++---+
SS SSSSSS S
+-----++++
EPAP PAPAIN
SHEET..
BRIDGE?.
SHEET..
BRIDGE2..
BRIDGEl..
CHIRALITY
BEND.....
5-TURN..
4-TURN...
)-TURN...
SUMMARY..
EXPOSURE.
101 SEQUENCE,
35)
.
SHEET..
BRIDGE2..
BRIDGE1..
CHIRALITY
BEND.....
5-TURN..
4-TURN..
3-TURN...
SUMMARY..
EXPOSURE.
201 SEQUENCE.
..
..
.
-------+++
sss
ss
JJJ
++++------
CCC
---++--+++
sss sss
EEEE EEEE
PPPP P
0 0000
ssssss
----+----+
TTTTTTT
GGGGGGG
w
ss s
ss
G GGFF
vwrr
---+-+----
GG
---+------
+--+
B BBBBB
G GGGGG
BBB
GG
sss
ddd
---- +- ---- ++----
BB BBBBBBB
GG GGGGGG
E EEEEE
sss
DDDD DD
DDDD
NNNN
sss
-+--+-----
LLL LL
NNNN NN
----+---++
----++---s s s
s
I1 11111
CCC CCCCC
KK
JJJ
-+-+-+--+-
KK
CC
H
w
J
Y
--------++
I
x
s
ss ssss
--++-+-++-
GGG
EEEE
EEEE E
G
KKKK
,... .
A
J
+++-++----
ssss s ss
cccc
++-------+
s s s
zzzzz 2
Y x w
----+++-+-
JJJJJI J H
sss
----+-+---
BB
JJ
Z
BB
A
22227,
---------+
JJ J J J J J
sss
>33<
>33<
>>3<<
ETTS EEE S SSTTSEEEE
SSSS EEEE E S GGG E
3 4 ' 5 4 7 5 4 1 7 91*'4374B5 6 * * * 6 7 0 2 0 * 0 4 6 1 6 8 8 0 3 0
FYHGTSDTDT PLRSRVTMLV NTSKNQFSLR LSSVTAADTA
uuu
QQQ Q
V
ss sss s
uuu
QQQQ
PPPP P
-+-+------+-++----+
++++++---- --+-++--++ -+-+-++++s s
sss
s sssss
ssss
s sss s
-,4-,
OR 5-TURN....S=BEND....
>33<
>33<
>33<
>
EEEEEEE S S S
EEEEE EEEE SS B
B B S
SS STTS
EEEEEEEEBS S EEEETTT S TT B
EE SSS EE EEEEE SSS
3 0 1 0 0 3 1 7 * 3 3 3 1 8 5 2 1 9 1 3 40285'6'59
2 2 5 2 3 3 0 1 2 3 2 ' 4 3 8 9 6 3 1 2 1 0 0 0 0 0 3 0 3 0 8 4 2 8 2 4 1 3 * 6 85*'33*623
30'37.5648
1002093888
WYdARDLIA GCIDWGQSS LVTVSSASTK GPSVFPLAPS SKSTSGGTAA LGeLVKDYFP EPVTVSWNSG ALTSGVHTFP AVLQSSGLYS LSSVVTVPSS
---+--+--+
GGGGGGG
W W
TTTTTTT
BBBBB
>33<
>33<
>33<
EETTEEEEEE S STT EE EEEEEEETTE E E E E E E E E E E
* 8 6 5 4 0 2 0 1 0 538'4'1211
0101004'41 1010420'84
KSGSSATLAI TGLQAEDEAD YYaQSYDRSL RVFGGGTKLT
GG GGG G
>444 <
>33<
> 3 3c
E E SS
E E E E E S E E TTS E E E E EEEESS TTT EEEEEEE T T
EEEEEE
8347*'4*0*
7'2.372714
2*58*40403 041562934. 250000224+ 8'31610810
TVAPTECSI X VQLEQSGFGL VRPSWLSLT d T V S G S V S N DYYTWVRQPP GRGLEWIGYV
SS
r r
F F
+-+--+--++ --++---+-s
sss
00000
NN
++-+++
EEEEE
DD
D
M
cccccc
AAAAAA
___ss+++---- +-+-++++-s ss s
AA
CC
x4<4<
><3<
>33<
>33<
TTTT EEEE E E E SSS
EEEEE SSSB
TTEEE
E E STT E E E EEEEE S S S
S EEEE EESSS EEEE
7 * 8 * 7 1 1 1 0 0 0 0 2 5 0 5 1 3 7 3 '331618'79
4 * * 1 2 5 6 3 * 4 5 5 7 8 ' 3 4 4 1 0 0 0 1 0 6 5 7 7 9 f * * 6 6 * 2 4 1 0 4 041'8485'6
LQANKATLVb LISDFYFGAV TVAWKADSSP VKAGVETTTP SKQSNNKYAA SSYLSLTPEQ WKSHKSYSbQ VTHEGSTVEK
sss
-+----++--
M
LLLLL
1111 I11
HHH
-+++-+-++-
DDDDD
cccc ccc
++-+------
sss ssss
>4>4
>3
ES
E EE
TTT
17'39.3616
0221451'78
VLRQPKAAPS VTLFPPSSEE
S
-++-------
H HH
SUMMARY........H=ALPHA-HELIX....E=BETA-STRAND....B=BETA-BRIDGE....G=3-HELIX....I=5-HELIX....T=3
.
....
SHEET....
BRIDGE2..
BRIDGEl..
CHIRALITY
BEND..
5-TURN..
4-TURN.. .
3-TURN..
SUMMARY..
EXPOSURE.
3 0 1 SEQUENCE.
..
.
SHEET..,.
BRIDGE2..
BRIDGE1..
CHIRALITY
BEND.....
5-TURN..
4-TURN..
3-TURN..
SUMMARY.,
EXPOSURE.
2 0 1 SEQUENCE.
..
.
c cc
B
d
lFAB LAMBDA IMMUNOGLOBULIN FAB (NEW1 lHUMAN).......................................................................lFAB
SHEET..
A
BB BB
AA AAA
BBBBBB
BB
AAAA
BRIDGE2..
BB EBB
FF
BRIDGE1..
A
dd dd
A
EEEEEE
FF
CCCC
CHIRALITY
-+-+--+-+--++----+-+--+-+++ -+------+-++------+-+-+++--BEND..,..
S
S
sss
sssss ss
ssss
ss ss
5-TURN..
>5555<
4-TURN..
3-TURN..
>33<
>33x33 c
SS SSEEEE
S B S E E E E TTS EE EEE TTTTT SS EEEEEE SSSS E E
SUMMARY..
6*+5**2676
EXPOSURE.
9 3 * 1 * 2 3 * 7 2 7 0 2 7 7 8 ' 1 7 8 5 0 5 2 5 ' 6 0 8 3 5 6 7 6 1 5 0 0 5 1 886908'43.
XSVLTQPPSV SGAPGQRVTI SaTGSSSNIG AGNHVKWYQQ LPCTAPKLLI FHNNARFSVS
1 SEQUENCE.
SHEET....
BRIDGE2..
BRIDGE1..
CHIRALITY
BEND.....
5-TURN..
4-TURN..
3-TURN..
SUMMARY..
EXPOSURE.
1 0 1 SEQUENCE.
361
v1
M
SHEET..
..
38)
sss
>5555<
..
....
..
---+---
DDD DDD
-+-++-+---
C C CC
KKK KKK
S
++-------s
3<
>3
T EEEEEE T
870008325'
KYLNWYQQTP
..
....
c ccccc
sss
>>>>
XXXXXXKX<<
<<
> 5 5 55<
s
sss
-+++------
dd d
++++++++++ -++++----+
AAA
I
s
.3PGM
>
>>>
SSSS
++++--++++
s
...........................
s sss ssssssssss ss
-----+-+++
ccc
ssss
++-+------
SSSS
B
*061301010 474834328'
E D I A T Y Y a Q Q YQSLPYTFGQ
GG S E E E E E E
3<<
s
1REI
B
1181.36986
S E E E E E S HHH HHHHHHHHHH HT
S
EE ESSS
S S SSHH
HHHHHS
1110062521 3 5 0 0 8 2 1 2 * * 1'5**4957*
1371140041 8321845391
LLKEKGVNVL W Y T S K L S R A I Q T A N I A L E R ADRLWIPVNR SWRLNERHYG DLWKDKAQT
xx<<<<
>555<<
ssssss
s
SACCHARWYCES C E R E V I S I A E I
AAAAA
ddd
++++-+---+
(YEAST:
HH I
EEEEEE
+++-------
s s
>4 44<
3<
>33<>3 31
>33<
>>
T S E E E E E T T T E E T T T T E E E E E E T T E EEEEESS G
8'31.00854
078638815. 5061739269 0403073068
C K A P K L L I Y E ASNLOAGVPS R F S G S G S G T D Y T F T I S S L Q P
s s
ss
B BBBBB
-----+---+
CCCCCC
GG
++--+---++
A AAAAA
AAAAAA
BB
....................................................
BBBBBB
+----++-+++----+--+
s ss
ss ss
ss
3PGM PHOSPHOCLYCERATE MUTASE (DE-PHOSPHO)
[ISWERASE]
SHEET....
AA B
BRIDGE2..
BB
BRIDGE1..
a
f
CHIRALITY
+--+-----+++++-+++ -+-+----++
++++++++++
BEND..
sssssss
ss
ss ssssssssss
5-TURN..
> 5555<
>
4-TURN..
>>44<<
>>> >xxxxxxxxx
>33<
>33<
3-TURN..
SUMMARY..
TT
HH HHHHHHHHHH
EE B
SSHHHHS
1 1 3 4 3 9 1 2 5 * 0'*601900*
EXPOSURE.
5400014104 07525'8552
1 SEQUENCE.
PRLVLVRHGQ SEWNERNLFT G W W V K L S A K GQQEAARAGE
EEEEE
0090*5*
GTKLQIT
.... ----..
BBBBB
HH
dddd
>3
EEEEESS T
040918*908
ITaQASQDII
ss
-----+-+--
VARIABLE PORTION ( R E 1 1 (HUMAN).
AAAAA
BBBBBB
88 B B
BBBB
FFF
GG
AAAA
EEEEEE
FF F
33<
>>3<<
T T S S S EEE EEEGGGTEEE E E E
S
* 3 9 * * 8 2 4 0 3 0 6 0 * 2 3 * 3 * 4 '1391.688.
S L G T Q T Y I e N VNHKPSNTKV D K K V E P K S c
SSS
++++------
KKK KKK
DDD DDD
l R E I BENCE-JONES IMMUNOGLOBULIN
SHEET....
AAAA B 888
AA
BRIDGEZ..
BB
BRIDGE1..
AAAA d ddd
CHIRALITY
-----+-++
-+--++---BEND..
s s
ss
5-TURN..
4-TURN..
>33<
3-TURN..
SUMMARY..
E E E E S E EEE T T E E
EXPOSURE.
*0*1606467 3814857115
D I Q M T Q S P S S LSASVGDRVT
1 SEQUENCE.
SHEET..
BRIDGE2..
BRIDGEl..
CHIRALITY
BEND..
5-TURN..
4-TURN..
3-TURN..
SUMMARY..
EXPOSURE.
1 0 1 SEQUENCE.
37)
....
..
BRIDGEl..
CHIRALITY
BEND.,
5-TURN..
4-TURN,.
3-TURN..
SUMMARY..
EXPOSURE.
4 0 1 SEQUENCE.
BRIDGEZ..
TABLE AIII (continued)
to
03
+
03
..
..
.
....
...
..
A
A
E
88
ss
-+--+-+-++
s
E
s s
----- t t +
A
SSSSSS
SSSSSSSSS
AAAAAAA
fffffff
ee
sssssss ssss sss
+--+++++++ +++--++--+
s
ssss
s ss
-+-++---++
++++-+-+--
ss ssssss
+++-++++++
ssssss
ss
++++++++++ ++++--++++
ssss ssssssssss sssss ssss
> > > > xxxxxxxxxxx x x < < < x > > > <
-+----++++
ssss sss
----++++-+
OR 5-TURN....S=BEND....
3<
>33<
>33<
>>3<<
HHHH H H H H H H H H H H HHHHH H H H H
TTEE EEEEEGGGSS SSS
HHHHHTTHHH H H H H H H H H H H H H
0 0 0 1 1 1 3 2 8 9 6 5 * * 2 4 3 + 7 1 3 9 1 0 9 ' 0 3 3 4 0'9*45*720
* 9 5 * 8 4 6 2 9 * 2 0 4 * 2 0 * 2 0 2 '41'728618
OEREAGITEK VVFQETKAIA DNVKDWSKW LAYEPVWAIG TGKTATPQQA QEVHEKLRGW LKTHVSDAVA
>><<<<>>>> xxxxxxxxx< <<<
>5555<
ff fffff
4 499
AA AAAAA
++++-+++++ ++++++++++ ++---+++--
s ssssss sss ssssssssss ss
xxxxxx<<<<
>5555<
>>
<< > > > > X X X X X X X < < < <
>3
>33<
EEEEEEE H
H
H H H H H H HHHHHHHTT
55246.3807 0 0 3 3 0 1 9 6 6 1 1 0 1 0 0 0 1 0 9 4
FGESDELIGQ KVAHALAEGL GVIACIGEKL
5<
S
ss
+++-t-----
--+---+--+
(CHICKEN BREAST MUSCLE: CALLUS GALLUS) l T I M
AAA M A
C
AA Ah
ee
c c c ddd
J
dd d
THHHHHHHHH SS SSSSSS
1 1 0 3 0 1 2 4 ' 1 9537.7625'
NSLRGLVKHL EGlSDADIAK
3<
>>>>xxx<<<<
++++++++++ -+--++++++
s ssssssssss ss ssssss
>5555<
>555
>>> >x<<<<
>>>>X<<
> 4 > > x > x x <<<<
>33 <
>33<
>33<
>33<
HHHHHHHHH
S
H H HHHHHT EE EE H H H H H H
..................
.S
. EEEE
~ _ _ _E TTHHHHH HHHS TTEEE EEE S S S S BS SS
1*20*71362 * 9 6 8 * 3 7 1 1 0 0 0 0 2 1 0 0 1 3 0 5 * 8 1 6 9 9 0 2 0 0 1 1 2 0 1 6 5 7 * 2 5 5 0 1 2 1 0 0 4 01'7231630 10001213'6
GELIHTLDGA KLSADTEW C GAPS I YLDF A RQKLDAKIGV AAQNC YKVPK GAFTGE IS PA M I KD I GAAWV ILGHSERRHV
sssssssss
+++++++++-
-+--++++++ +++++++-+- ----+----+
---------
AAAA A
ccc ,
aaaa a
[D-GLYCERALDEHYDE-3-PHOSPHATE-KETOL-ISOMASE]
>444<
>33<
>33<
BSS EE
TTT
S B S T T
**24301011 1416**4*47 *969725**6
LN I PPGT I LV F ELDENLKPS KPS Y Y L DPEA
sss
+---++----
f
B
~
ss
>>555<<
x<<<x>44<<
>>3<<
>3
HHHHTHHHH SS EEE
T
33**412*51 8 9 3 0 8 1 0 0 2 1
YWQDVIAKLV GKTSMIAAHG
AAA
ccc
a
++++++++++ +-+---+-+-
SUMMARY........H=ALPHA-HELIX....E=BETA-STRAND....B=BETA-BRIDGE....G~3-HELIX....I=5-HELIX....T=3-~4-,
.
++t+++++++
ssssssssss sssssssss
5555< > 5 5 5 5<
> 44>x>4xxx>
4 < < < > > > 4 < <<
>3><3<
>>3<<
>33<
>33<
SSSSS
SSTTTTS _.
S S S ~.
SS
TTTHHHHHHH
-.....
HHHT SHHHH HSTTSSS S
3*39*71**2 *9*413*211 2 4 8 1 5 9 2 2 6 4
~ * + * i * * * s * 1 6 6 9 3 * + 6 4 a 3739;;;;93
LKWGEEWN TYRRSFDVPP P P I 3 A S S P F S QWCDEKYKYV DPNVLPETES LALVIDRLLP
+++++-++++ +++--++t-- ----++-++- +-+-+++++- -+++--+--sssss
sssssss ss s ss
ssss sssss sssssss s
l T I M TRIOSE PHOSPHATE ISOMERASE
SHEET..
AAAAA
B
BRIDGE2..
bbbb
BRIDGE1..
aaaaa
I
CHIRALITY
--++--++++
s ssss
BEND..
5-TURN..
>>>>X
4-TURN.
3-TURN..
SUMMARY.
EEEEE
B
HHHH
EXPOSURE.
* 9 9 9 3 0 0 0 0 1 13042'8'41
1 SEQUENCE. APRKFFVGGN WKMNGKRKSL
SHEET..
BRIDGE2..
BRIDGE1..
CHIRALITY
BEND.....
5-TURN...
(-TURN...
3-TURN..
SUMMARY..
EXPOSURE.
1 0 1 SEQUENCE.
39)
.
SHEET..
BRIDGE2..
BRIDGE*.
CHIRALITY
BEND..
5-TURN..
(-TURN..
3-TURN..
SUMMARY..
EXPOSURE.
2 0 1 SEQUENCE.
..
.
....
.
..
...
SHEET..
BRIffiE2..
BRIDGE1..
CHIRALITY
,
BEND.,
5-TURN..
4-TURN..
)-TURN..
SUMMARY..
EXPOSURE.
101 SEQUENCE.
0
0
z4
..
t-tttttttt t-ttt----t
SSSSSSSS SSSS
AAAA
h
bbbb
> 4 > > x > < < <<
> 3 3x33<
HHSEEEE S
TTHHHHHH TSTT EEEE
8 8 0 2 0 0 1 1 2 8 045451'701 62'5100028
VQSRIIYGGS VTGGNCKELA SQHDMGFLV
<<<
tt-----t-SSS
S
h
qgqq
AAAA
> 4 4 4 < >>>> <<<<
>>><<x33< >33<
SGGGGSTHHH HHHT
26207.7502 *0151**
GGASLKPEFV D I I N A K H
ttttt-+ttt ttttt
ssssssssss ssss
TABLE A111 (continued)
.
....
..
sss
s
s ss
ss
-t--tt-tt-
NN
BB
JJ
s
-t---t-t--
s sss
BB
NN
EEEEE
sss
ss
t-t---tt--
00
CC
ss
t-t--t---t
A AAAAA
FFFFF
E EEEE
ss s
tt-ttttttt
--tt----tt
G GGGGGGGG
BB BBBBBBBB
M M MMMMM K
DDD
ss
-+-+--++--
sss s
tt--t
>4 44<
--+++-++-ss sss
SS S S S T TTS S
SSSS
E EEEEE S S
1*5**10100 0 0 0 2 0 2 8 * 2 9 41'4858930 0 1 0 7 9 6 7
SPDS HPADGI AFF I S N I D S S I PSGSTCRLL GLF PDAN
ssss
-+-+-----+
A AAAAA
A AAAAA
OR 5-TURN....SeBEND....
5,
cn
8
2
5,
ssss ss
>444<
>33<
E E E E E E TTS
EEEEEE
TTTS SEEE EEEEEE S S S
12261518.4 '729138'27
2**4169*04 10000002*8
LSAWSYPNA DATSVSYDVD LNDVLPEWVR VGLSASTGLY
w
3.
x
cn
t-t---ttt-
OOD DD
tttt--tt--
>444 <
>33<
>33<
EES E E EEEEE TTT
EEEEEEE S
S
SSE EEEES E E S SSSEE S
SSS
S S E EEEEESS E E
TT S E E E E E E E E E E
8*0R**3'61 4 7 7 4 4 1 8 1 4 7 * 1 2 0 3 0 0 * 5 6 * * 4 7 2 5 1 8 0 2 0 1 0 6 3 . 4 6 2 3 5 6 4 * 6 4 7 3 1 2 3 * 0 3 1 1 0 6 0 *
8 0 1 0 0 0 5 3 1 3 1 2 1 9 0 7 2 2 . 6 **6975'3*4
KETNTILSWS FTSKLKSNST HQTDALHFMF NQFSKDQKDL ILOGDATTGT DGNLELTRVS SNGSPEGSSV GRALFYAPW IWESSAATVS FEATFAFLIK
S
t---t--tt-
F FFFF
LLLLLLL
t--t-tt--t
A AAAA
BBBBBBB
111111
---t---t--
sss
SUMMARY........H~ALPHA-HELIX....E=BETA-STRAND....B=BETA-BRIDGEI...G=~-HELIX....I=~-HELIX....T~~-,~-,
SHEET..
BRIDGE?.
BRIDGE1..
CHIRALITY
BEND..
5-TURN..
4-TURN..
3-TURN..
SUMMARY..
EXPOSURE.
2 0 1 SEQUENCE.
.
....
..
..
.
.
.. ..
tt--ttt-t-
BB BBBBB
MM MMMMM
LL LLLLL
t--t--t-tt
BB
K
JJ
sss
++--+--++-
11111
HHHHH
..BBBBBB
........, , ...BBBBBB
. .... ,... . ... ...CCA
....AAAAAA
.... ,.3CNA
3CNA CONCANAvALIN A [LECTIN, AGGLUTININ] (JACK BEAN: CANAVALIA ENSIFORMIS]
B
AAA
BBBB BBBBB
AAAAAAA
AAAAAA
SHEET....
H H HHH
I
BBBBBB
ccc
BRIDGEZ..
ccc
GGGG GGGGG
AAAAAA
BBBBBB
BRIDGEl..
CHIRALITY
--+-+----+
+-ttt+-t-- t-+-+----+ -+--+-------++-----tt--t+-+BEND.,
s
sss ss
ss
sss
ss sss ss
5-TURN..
>5555<
4-TURN..
>444<
>33<
>33<
3-TURN..
SUMMARY..
EEEEEEE S TTTT
S S EEEEEES SSS SSEEE
TT EEEE EEEEETTT E
EXPOSURE.
* 5 4 1 0 0 1 0 0 0 6 5 4 1 9 ' 2 5 1 3 9 8 4 0 1 0 0 0 2 ' 21'29'62'1
* 5 7 7 3 * 8 0 5 0 807174'*9*
ADTIVAVELD TYPNTDIGDP SYPHICIDIK SVRSKKTAKW NMQDGKXTA HIIYNSVDKA
1 SEQUENCE.
SHEET..
BRIDGE2..
BRIDGE1..
CHIRALITY
BEND..
5-TURN..
4-TIIRN..
. ..
. . . ..
3-TURN..
SUMMARY..
EXPOSURE.
1 0 1 SEQUENCE.
40)
.
..
SHEET..
BRIDGEZ..
BRIDGE1..
CHIRALITY
BEND.....
5-TURN..
4-TURN..
3-TURN..
SUMMARY..
EXPOSURE.
2 0 1 SEQUENCE.
..
.
.
.
<
>
S
ssss
--+--+-+++
+---+-+-+ssss
BB
NN
-
MM
BB
...
>4>x<4<<
33x>3<x>>< x<3<
>3><3 <
H H H H H H H G G G GTTSSSS EE E
TTTT S S
E E E E SSSS
9 2 1 4 * 1 0 * 5 1 *6071*5*81 *28*692'51
52.2860212
4004013705
PGLQKVVDVL DSXKTKGKSA DFTNFDPRGL LPESLDYWTY PGSLTTPPLL
BB
MM
L
--+-+---+-
sssss
-+++--++++
DD D
BB B
++++++++++ ++++-++---
sssssssss ss ssss
3<
T S B
S
EE
6'7'2'0358
8144468*'4 * 3 8 1 2 9
GEPEELMMN WRPAOPLKNR QIKASF
0
C
33x33<
>
TTSTTSEEEE EEEEEEES
3**9500001 0011'53873
VQQPDGLAVL GIFLKVGSAK
++++--+--+ +-++--++++ ------+++sssss ssss ss s s s
-----+++++
0
C
>>44<
>>3<< >33x
EGGGSSHHHH
13'76665'0
NTKYGDFGKA
s s
-----+----
kkkk
1111 1111
jjjj j
BBBB BBBBBBB
-++---++++ ++-+++---sssssssss ssssss
>>4>x< 4<<
>>3<< > 3
S EEEEE SS E E E E H H H H H HHTT BSS T
5 0 1 3 0 0 1 0 * 7 4 2 5 6 4 4 ' 1 2 8 814.83552'
ECVTWIVLKE PISVSSEQVL KFRKLNFDGE
S
ss
kkkk
jjjjj
++--++--+-
BBBB
BBBBB
NN L
>33<
SSEETTB
SEEEEEEEE
0001136'*8 5 0 1 0 0 1 1 1 0 2
GSQHTVDKKK YAAELHLVHW
S
-------+--
BBBBBBBB B
11111111
HHHHHHHH H
-+++-++-++ -+----+--+
s ssss
ss ss
>33 <
>33<
S EEEE
S SSSSEEEETT SS EEEEEE EEEE SSTT
5 0 0 3 0 5 0 7 4 9 '68111'222
2.53051431 2 1 1 1 0 4 * 8 6 5
HAFNVEFDDS EDKAVLKGGP LDGTYRLIQF HFHWGSLDGE
s
+-------++
[HUMAN ERYTHRDCYTESl...................lCAC
BBBB
BBBB
BBB BB BBBB
FFF
GG
H H H HH HHHH
E EE
cccc
GG F F F
. ......H=ALPHA-HELIX.. .,E=BETA-STRAND.. ..B=BETA-BRIDGE.. ..G=3-HELIX.. ..I = 5 - H E L I X a . .
....
..
.T=3-, 4-,
OR 5-TURN..
..S=BEND.. ..
1DFR DIHYDROFOLATE REDUCTASE [OXIDOREDUCTASE: NADPH/DONR, DIHYDROFOLATE/ACCPTRl
(BACTERIAL: LACTOBACILLUS CASE11 ,
lDFR
SHEET....
AAAAAAA
A B
AAA
AAA
A
AAA
bbbbbbb
eee
f
eee
BRIDGE2..
BRIDGE1..
aa
C
C I
aaa
ddd
f
aa
CHIRALITY
--+-----+-+---+---+++++++++ ++++++---+ --++++++-+ -+--++----+-+-++-+- ++--+-+-++ ++++++++-+ ++---++--+
BEND..
ss s s ssss s s sssssss sssssss
ssssssss sss sss
ss
sss s ss sssssssss s
s s
5-TURN..
4-TURN..
>>>>XXKX X<<<<
>>4><<4<
>>> > x < < < <
>>
3-TURN..
>33 <
> > 3 << > 3 3 <
>>3<<
> 33<
>33<
>>
SS
TTB
S HH HHHHHTTSS S E E E S H
EEEEEEETT B SBSSSS S S H H H H H H H HHHHTTSEEE
HHHHTTSS SSS SSSEEE
SUMMARY..
EXPOSURE.
32082121"
2 1 3 1 5 * 5 9 8 0 2 ' 0 6 5 2 9 * 4 4 ' 6 5 0 4 5 2 0 0 2 Bl''30755f
**435*4400 041*9**3*1 '524548956 327581**3* '7'2002821
TAFLWAONRN GLIGKDGHLP WHLPDDLHYF RAOTVGKIMV VGRRTYESFP KRPLPERTNV VLTHQEDYQA CGAWVHDVA AVFAYAKQHL DQELVIAGGA
1 SEQUENCE.
SUMMARY.
42)
SHEET..
BRIDGE2..
BRIDGEl.,
CHIRALITY
BEND..
5-TURN..
4-TURN..
3-TURN..
SUMMARY..
EXPOSURE.
2 0 1 SEQUENCE.
..
....
..
..
.
B
A
SS SSS
+++----+--
AA
0
aa
lCAC CARBONIC ANHYDRASE FORM C [CARBON-OXYGEN LYASE, CARBONATE DEHYDRATASE]
SHEET.,
AA
BBBB
BBBB
BRIDGEZ..
EEE
BRIDGEl..
aa
cccc
DDD
+-+-+++-+ ++++-+++++ +-++-+---+ -+++--++++ ------++++ -----+-+-+
CHIRALITY
BEND.....
SSSSSSS SS SSS SS S SS SS
SSSS
S S
ss
s
5-TURN..
4-TURN.. ,
>444<
> 3 3 < > > 3 < x 3 3 < > > > < <<
>33 <
>33 <
3-TURN.,
SUMMARY..
SSTTSSG GG TTS GGG G SS SS EE TTTS
TT S E E E E TT
EEEE S
EXPOSURE.
* 5 1 4 3 * * 4 0 3 * 5 1 * * * 7 9 7 1 * 3 ' * 0 0 0 1 5 1 85*917'3**
4.734561''
2666.03171
HWGYGKHDGP EWHKDFPIA KGERQSPWI DTHTAKYDPS LKPLSVSYDQ ATSLRILNDG
1 SEQUENCE.
SHEET.. ,
BRIDGE2..
BRIDGEl.,
CHIRALITY
BEND.....
5-TURN..
4-TURN..
3-TURN..
SUMMARY..
EXPOSURE.
1 0 1 SEQUENCE.
41)
..
1<<
>??<
__
>>XX<<<<
ss
s
--+-++---+
s s s
-++-+--+++
--
>
.??
<.
> 4 4 4<
+-----+-++
++--+----ssss s
HHHHHHHTS SFEEEEEESS
SB
S S EEE EEEE SSTT T EEEEEEE
* 2 0 8 5 2 8 * 8 1 6 3 1 2 0 0 6 0 7 1 68'387.22'
2R9.929986 7**3*5*6*3 2 2 0 2 2 2 3 4 * * **
QIFTAFKDDV DTLLVTRLAG SFEGDTKMIP LNWDDFTKVS SRTVEDTNPA LTHTYEVWQK KA
S
++++++++++ +-------+-
SSSSSSSSS
A AAA A AA
GGGGGGG
H H HHHH
A A AAAA
HHHHHH
I
B
bbbbbbb
AAAAAAA
GGGGGGG
..
....
.
.
. ..
SUMMARY..
DDDDD
s
s
ss
-+---+----
>
ss
ss
----+++-++
P
E
>>>XXXXXXX
++++++++++
ssssssssss sssss
ss
s
<<<<
>5555<
...
+++-++++++ ---+-----+
a a a
F F F
s
++++-+---+
sss ss
E
.
1
ssss
000
..
DDD
..
--++-+--+a aa
F FF
3x33<
T TT BSSS
**42240276
DWRGGRGAAQ
P
----+--+++
s s
sss
3<
>33<
>33 <
>3
HHHHHHRHHH HHHH B
EEEEE
TT
SB
T
1 1 0 0 1 1 1 5 1 1 4**2*14'1*
138610148* 243120536.
NCLAPVAKVL HENFEIVEGL MTTVHAVTAT QXTVDGPSAK
--------++
DDDDD
LLLL
kkkkk
4-,
OR 5-TURN..
.S-BEND..
..
>33<
>33<
>3><3<
>33 <
>33< >
EEEEE HH HHHHHHSSSS SSS EEEEE S S EEE EEEE TT
HHHHHHHHHH HHHTTTTTSE EEE S
TT
SSS S S E EESSTT EEE
5 ' 3 9 1 6 4 5 8 2 '0889216'8
6 6 ' 3 8 2 6 8 6 5 3 6 5 3 0 0 0 3 8 4 1 3 0 9 0 5 * * 2 3 2.913321'7
31'3'2.342
3319'**493 92637.8110 1 1 0 * 5 4 2 * 8 8
NIIPSSTGAA KAVGKVIPEL DGKLTGMAFR VPTPDVSVVD LTVRLGKECS YDDIKAAHKT ASEGPLQGFL G Y T E D D W S S W I G D N R S S I FDAKAGIQLS
-+-++-----
N NNNN
J
LLL L
DDD DDDD
kkkkk
MMMMM
s
3><3< >33<
>3
TTTTS TT SEEEE H H H
13***16*+4 6 8 0 0 8 0 3 4 1 0
VNLEKYSKDM TWSNASCTT
DDDDD
++++-----4
ssssssssss sss
++++++-+++
>>> >xx<<<<
---+---+++
MMMMM
D
J
++-+++-+++ ++-----+++ ++++++++++ +++----+-S SSS SS S
sss ssssssssss s s s s
>>5 55<<
4<
> > > > <xxx>xxx<x x < 4 < <
AAAA
f
eeee
......H=ALPHA-HELIX, ...E=BETA-STRAND.. ..B=BETA-BRIDGE.. ..G-3-HELIX.. ..I=S-HELIX.. ..T=3-,
..
....
SHEET..
BRIDGE2..
BRIDGEl..
CHIRALITY
BEND..
5-TURN..
4-TURN.,
3-TURN..
SUMMARY..
EXPOSURE.
2 0 1 SEQUENCE.
..
.
-++--+--+-
f
A
SSSSSSSSSS S S
SS
SSS
SS
>5555<
>>><XXX4<<<
>44
>>>X<<<
>
H H H H H H H H H H S SEEEEES
SSS B TT
4*803205*2 21*3001226 1.74331011
IEKASAHFKG GAKKWISAP SADAPMFVCG
+++++++++- +-+-+--+--
AAAAA
eeee
dddd
lGPD D-GYCERALDEHYDE-3-PHOSPHATE DEHYDRCGENASE [OXIDOREDUCTASE: ALDEHYDE/DONR,NAD/ACCPTR] (LDBSTER: HIMARUS AMERICAlGPD
AAAA
AA
B
E
CCCC
CCCC CCC AA
A AAA
SHEET..
BRIDGE?.
bb
cc
I11
d ddd
BRIDGEl..
aaa a
bb
G
G
HHHH
H H H H I11 c c
a aaa
CHIRALITY
+---+-+-+ ++++++++++ +--+-+---+
+++--+++++ +++++-++-- --+--+-++- +-----+-+---+-+-+++ -++++-+++- --++-++++BEND..
s s s s ssssssssss sss
sss s s s s s s s s s sss
s
s ss sss
s s s s s s sss s
ss s
5-TURN..
> 5 5 5 5< > 5 5 5 > x 5 55<<
> 5 555<
>5555<
4-TURN..
> > > > x x x x < < <<
> > > > x xx < < < < > 4 4 4 <
>444 < >444<
>
3-TURN..
> 3 >x3<<
>33<
> 3 3< > 3 3 <
>33 < >33<
E E TTS H H H H H H R H H BTTTB
S EEEET TEEEETTEEE E E SSTTT S TTTT E EEE S S S
SUMMARY..
EEEE TTT H H H H H H H H H H TTT
EXPOSURE.
5 5 1 0 1 1 2 1 3 5 3 0 1 1 0 1 4 0 1 4 * 5 3 5 7 5 2 0 0 1 23.247'412
6 0 1 5 9 0 3 2 6 4 82'6.2'9'.
81131.59'1
533*6**09* 0 3 0 8 * 7 3 1 6 1 080155'541
1 SEQUENCE. SKIGIDGFGR IGRLVLRAAL SCGAQWAVN DPF IALEYMV YRFKYDSTHG W K G E V K M E D GALVVDGKKI TVFNEMKPEN IWSKAGAEY IVESTGVFTT
SHEET..
BRIDGE2..
BRIDGE1..
CHIRALITY
BEND.....
5-TURN..
4-TURN...
3-TURN.. a
SUMMARY..
EXPOSURE.
101 SEQUENCE.
43)
.
SHEET..
BRIDCE2..
BRIDGE1..
CHIRALITY
BEND.....
5-TURN..
4-TURN...
?-TURN...
.
.. . ..
SUMMARY..
EXPOSURE.
1 0 1 SEQUENCE.
TABLE A111 (continued)
tQ
0
p\3
6,
.
..
>33<
H H H H H H H H H H HT
8 3 1 1 9 6 0 3 ' 3 28.
I DLLKHMQKV DSA
>>>><xx<>xx>xxxxxx<< <<
>55 55<
ssssssss ssssssssss s
++++++++++ ++++++++++ +
33<
>>3xx3<<
TTEEEEE
HHHHHHHHH
85'1711831 0123120310
KTF VKWSWY DNEF GYS QRV
ss
+++-t-+---
DDDDD
000
NNNNN
..
....
..
..
.
SUMMARY..
ss ssss
s sss
s
ssss
s sssss ssssss s
PP P
P PP
n n nn
sss
ss
>5555<
>>>55<c<
++-+++++++ ++++++----
sssss ssssssssss sssssss
-++--+++,+
s
s
0000
4949
G FFFF
+++++++-+- --+---++-+
ssssss s ssssssssss
--+++-+--+
FF F
FF FF
-+-+-+++++ ++++-+-+--
++--++-+-s ss
ss
sss
--+--+-++-
s
s
+++--++---
rrr r
444 4
ss
33<
TT EEEE
'612008011
WSTCAVFGL
FFF F
t--+++----
sssssssss ss sss
-+++++++++
5
G
ss
++-----+-+
nnnn
0000
FFFF
>5555<
>K<<<<
-,4-,
OR 5-TURN....S=BEND....
>5555<
>>>>xxx<<<< > 4 4 4 <
>>>>xxxxxx x < < < <
>>>
>444< >> 4>x<4<<
> 3 3<>33<
>33<
>>3<<
>33<
> 3 3<>33x33<
EE E E S G G G H H HHHHHT S E E E TTTSSS H HHHHHHTTTS BSEEEE S
H H H H H H H H H TB TTT E E E E
TT
SHHHHHHHHH HHHHS
3 1 4 0 0 0 0 0 2 0 0 ' 6 4 1 4 5 7 8 0 01379**5*6 60'*120774
1 2 4 * * 8 * 9 6 1 7'104*62*4
0 0 4 2 0 0 0 2 8 1 9 5 ' 1 0 3 3 0 8 2 003'5'0300
332836'5.'
GGVGLSVIMG CKAAGAARII GVDINKDKFA KAKEVGATEC VNPQDYKKPI QEVLTEMSNG GWFSFEVIG RLDTMVTALS CCQEAYGVSV IVGVPPDSQN
ssssssssss sssss
-+++++++++ +++---+---
ss
>444<
>>>>xxxx<<<<
444<
>>3<<
> 3 3 x > > x<<<
> 3 3<
>
33<
SS TTTGG GGGTHHHHHH HHHHTTT
TTT SBSEE EEEGGGEEE
1 3 0 1 0 0 0 3 5 0 00323100*0 867041'780 0 0 0 1 1 0 0 2 0 2 0005811*18
LGTSlTSQYT VWEISVAKI DAASPLEKVC LIGCGFSTGY GSAVKVAKVT
ssss
-+-+++-++ss
B GG GGG
+--+++----
EEE
MMM
A CC CCC
DDf
+--+------
s
++--++++-+ --++---+++
ss
...... ..4ADH
(HORSE LIVER: EQUUS CABALLUS).
B
D
CC CC
CEE E
I
f
H H HH
IMM M
E
K
> > > > X <<<<
>
>33<
>33<
>>3<<
EEE H H H H HHHTTSS
SSB
B
E E E E E TT
S
TT B E E E S S
SSS
4 0 0 0 0 1 ' 5 0 1 3015244.14 5 2 0 1 0 0 0 0 0 0 0 6 1 3 2 3 2 * 5 1 * 6 0 * 7 6 2 5 0 0 0 0 2 0 1 2 4 6 * 2
VATGICRSDD HWSGTLVTP LPVIAGHEAA GIVESIGEGV TTVRPGDKVI PLFTPWGKC
>5555<
AA B
444<
>
>
>33<
>33<
>33<
TTTSSTT
S S SSSS
S TTS
SE EETTEE B
*32*8"229
09'2268'3'
031*756128 10+7*71510
RVCKHPEGNF CLKNDLSMPR GTMQDGTSRF TCRGKPIHW
sssssss
+--+-+--++
+++-++-+--
NAD/ACCPTR]
ssss sssssss
------++++
CHOH/DONR,
DDD
K
JJJ
......H=ALPHA-HELIX....E=BETA-STRAND....B=BETA-BRIDGE....G=3-HELIX....I=5-HELIX....T13
CHIRALITY
BEND..
5-TURN..
4-TURN..
3-TURN..
SUMMARY.
EXPOSURE.
2 0 1 SEQUENCE.
....
BRIDGE1..
SHEET..
BRIDGE2..
..
...
....
++++-++++- -++-++--+-
A AA
DD
C C
4ADH APO-LIVER ALCOHOL DEHYDRWENASE IOXIDOREDUCTASE:
SHEET..
AAAA AAAB
AAAAAAA
CCCCC
BRIDGEZ.,
B
cc
HHHH
BRIDGE1..
AAAA AAAE
AAAAAAA
GGGGG
-++---+-+ ---++-++---+--------++-----+
CHIRALITY
BEND..
sss
ssss
ss
5-TURN..
4-TURN..
3-TURN..
>33<
>33<
SUMMARY..
SSS EEEE EEEB STTS
EEEEEEE
TTEEEEE
EXPOSURE.
*'54*81'09
00008*'**9
1 4 7 5 9 0 5 1 3 5 1'4'100060
1 SEQUENCE. STAGKVIKCK AAVLWEEKKP FSIEEVEVAP PKAHEVRIKM
SHEET..
BRIDGEZ..
BRIDGE1..
CHIRALITY
BEND..
5-TURN..
4-TURN..
3-TURN..
SUMMARY.
EXPOSURE.
101 SEQUENCE.
44)
..
....
SHEET.. ,
BRIDGE2..
BRIDGE1..
CHIRALITY
BEND..
5-TURN..
4-TURN..
3-TURN..
SUMMARY..
EXPOSURE.
3 0 1 SEQUENCE.
N
w*
M
cn
..
>555
>>44<<
>>3<X33
THHHHT
5*896*46*6
LSMNPMLLLS
rrrr
..
.
..
.
..
.
..
..
S S S S S SSSSSSSSSS S S S S S S S S S
AA
e
dd
SSS
>
E
3
E
1
>>xxxxxx<< <<
KKK
PPF
SS S S S S S S S S S S SSSS
SSSS SSS
SSSS SSSSSSSSSS
SS
++++-+++-+ --++++++++ ++++++++++ +---++++++ ++++++++++ +-+-+---+-
SSSSS
C
C
BB
FF
sssss
+--+++--+-
HHH
CCC
ss
+-+-+-+---
G
CCC
HHH
sss
M
G
-+-+------
F FFG
L
K KKM
s
L
F
444<
-,4-,
OR S-TURN....S=BEND...,
> > 5 55<<
>5 555<
>>4<<<
>44>x4 4<<
> > 4 4 <<
> > > > x x<x<x>x><<<<
>33< > 3 3 <
>>><<<
>33<>33 <
>33< >>3<<
> 33<
>33x33<
>33<
H H H H HHHHTHHHHH HTT EEE
EEE TTSTT
SS EEE
E EEBTTB SB
TTT BTTB HHHHH
S S SSSGGGGTHH HHTSTTSHHH HBS
60262**68* '*6*51*420
* 1 0 0 6 0 0 3 8 0 2'98696118 81106'7551 " 6 4 1 0 0 0 8 1 0 1835'014'3
3 6 1 0 7 5 6 * * 8 2 4 8 * 6 5 4 2 * * 9*947*23'6
WSGMWNALKE LHPELGTNKD KQDWKKLHKD VVDSAYEVIK LKGYTSWAIG LSVADLAETI MKNWRVHPV SMVKDFYGI KDNVFLSLPC VLNDHGISNI
SSS
++++-+-+--
D
1
I
FF
e
++++++++++ +++++++-+- -+++-+-+++ +-++++---ssssssss sssssssss
SSSS
ssssss
BB
A
>5555<
>4>>X4X< < > < 4 > < 4 4 < > 4 4 4 <
>
>33<
>33<
>33<
> > 3 <<
>33<
HHHHHHHHHH H
TTS B
TTTTHHHHH TTTTTTTTT
TTTS E E BSSSTT E E
0 2 0 0 3 0 0 3 9 2 2 6 1 7 ' 7 4 0 0 8 1 0 0 2 2 1 1 4 7 0 7*310"*75
'386030580 0262'40118
DVLTYVAWKL SGLPMHRIIG SGCNLDSARF RYLMGERLGV HSCSGVGWVI GQHGDSVPSV
sss
++++++++++ -+--++++--
ss s ssssssssss s
>5555<
> > > 4 x x x>xx<xx<4x x>>x<<<<
>>
> 33<
>33x33 <
SS
H H H H H H H H H H H H H H H H H H H H H H TT
EE S S H
+ * 5 8 4 * 6 * 1 1 3 9 0 0 8 7 8 7 ' 1 06583'387'
0800822'31
QEGESRLNLV QRNVNIFKFI IPNIVKHSPD C I I L W S N P V
D
[DOGFISH MUSCLE: SQUALUS ACANTHIUSILDH
AAAAA
AAAA
dd
ccccc
bbbb
+-+-++++++ ++++++++++ +-t-+++--- +-++++++-+ ---+++---s ssssss ssssssss s ss s
ssssss s s
> > > > x x <x x x 4 < < <
>37<
> > 3 < < > 1 > x 7 <<
>>7<<
E s HHHHHH HHHHHHTTGCGS S E E E E E SSSGCG s s E E E E
SUMMARY........H=ALPHA-HELIX....E~BETA-STRAND....B~BETA-BRIffiE....G~3-HELIX....I=5-HELIX...~T~3
.
.
SHEET..
BRIDGEZ..
BRIDGEl.,
CHIRALITY
BEND.....
5-TURN..
4-TURN...
3-TURN..
SUMMARY..
EXPOSURE.
2 0 1 SEQUENCE.
++++++++++ +-++-+---ss
>5 555<
> > >>xxxxxx<< <<
ss ssssssssss ss
NAD/ACCPTRl
> 3 3x33<
S E E E E E S H H H H H H H H H H H HTT S E E E E
6 1 0 0 0 0 0 1 6 3 3 8 2 1 0 0 8 1 0 1 * ' 7 1 0 6 1 0 8 1 0 2 * 9 9 + 9 1 ' 4 43'*37*25'
*4'1882421 *927303417 00001442*6
NKITWGCDA VGMADAISVL MKDLADEVAL MVMEDKLKG EMMDLQHGSL F LHTAKIVSG KDYSVSAGSK LVVITAGARQ
s
+----+-+++
ENZYME M4 [OXIDDREDUCTASE: CHOH/DONA,
AAAAA
AAAA A
bbbb
cccc c
aaaaa
aaaa a
-++--+++++ ++++++++++ ++++++++++ ----++-+++
SS
___
JJJ
--
11
.
. 111
DD DDD
T EEEE SGG G H H H H H H H HHHHHHTS
TTTEEEEE ETTTHHHHHH HHHTS
EE EEE
4 3 7 6 8 5 4 6 1 0 1 2 3 0 5 * 1 0 4 * 1 0 5 5 3 8 5 * * 1 5 0 7 2 0 3 4 5 9 3 50**04*009 538'5'1328
0057
GRWKGAIFG GPKSKDSVPK LVADFMAKKF ALDPLITHVL PFEKINEGFD LLRSGESIRT ILTF
<
5<
D
1 111 1
D DDD
+--+++++++ ++++++-++- +++++++-+- -+++++++++ ++++-+-+-sss s SSSSSSS ssssssss
sss
ss sssss sssss
> > 4 > x x > x xxx<<<<
>444<
> > > > x x x <<<<
> > 3 <<
>33<
>33<
>33<
> 3 > < 3 < > 3 3x33<
+--+-+-+--
ssssss s
-+--+++++-
FFFF
4LDH LACTATE DEHYDROGENASE, APO
SHEET..
BRIDGEZ..
BRIDGEl..
CHIRALITY
-++++++-- -+++--+--+
BEND.....
SSSSSS
S
s
5-TURN..
>5555<
4-TURN..
>>44<<
3-TURN..
>>3<<
>33<
SUMMARY..
THHHHS
TT
s
EXPOSURE.
* 8 * * 9 * * 9 6 * '*9*****2'
1 SEQUENCE.
ATLKDKLIGH LATSQEPRSY
SHEET..
BRIDGEZ..
BRIDGE 1.
CHIRALITY
BEND.....
5-TURN..
4-TURN..
3-TURN..
SUMMARY..
EXPOSURE.
1 0 1 SEQUENCE.
45)
.
. ..
SHEET..
BRIDGEZ..
BRIDGE1..
CHIRALITY
BEND..
5-TURN..
4-TURN..
3-TURN...
SUMMARY..
EXPOSURE.
3 0 1 SEQUENCE.
TABLE A111 (continued)
E.3
E.3
h3
Q,
..
>33x3
HHHH
6'4*29**16
VKMKLKPNEE
>>4>x
s
3<>33<
>33<
HHHHHHHHHH HHH
S
*785*01962 7*28*2*49
QQLQKSATTLWDIQKDLKF
x>xxxxxxxx <<<<
++++++++++ +++++-+
ssss ssssssssss ss
------++++
..
....
..
..
>5555<
SSSS
s
ssss s
sss
ss
EE
ss
++++++++++ +++-++---ssssssssss sssss
S
s
+--++---++
NNN NNN
sss
-+-------+
FFFFFF
0000
NNNNNN
+-+------ssss
ss ssssssssss sss
jj
EEEE
kkkk
-----+---+
ss
000 0
FFF F
+-----++++
-++++-+--s
s . s s s sss
11
DD
P
G
sss
P
-+-+--+--+
G
> >>>xxxxx<<<<
s
OR 5-TURN....S=BEND....
>5555<
>444<
>33<> 33<
>33<
> 3 3<
>33 <
>33 0 3 3 <
>33<
SSSSS TTS H H H H H H H H H H HTTSS EET TEEEEEEETT SSS E E E E E E
SSSS
E E E E SS E E E E S E E S TT S TTTTT B TTS B
S
* 6 8 3 8 1 * * 4 8 54816181*2 386532922' 5 0 9 1 + 9 8 8 * * 4.33613143
57*6**6**8
3 9 2 * 9 5 2 1 0 1 29555172'.
141**351*8 6**248647*
RHDNVLRSFD SMISTNCTEE LENAGVEVLK FSQVKEVKKT LSGLEVSMVT AVFGRLPVMT MIPDMCLLW AIGRVPNTKD LSLNKLGIQT D D K G H I I M E
sssss
+-+-++++--
FFF FFF
EE
mm
ss
> 5 555<
44<<
>> >>xxxxxx<< <<
3x>3<<
>33<
HHHTT S S
SSEEEE SH H H H H H H H H H H HTT
EEE
4282*5**61 3200021248 5 0 8 l l l l B R 3 1 2 4 1 9 0 0 1 0 0
DGFFQLEELP GRSVIVGAGY IAVEMAGILS ALGSKTSLMI
++++++++++ +-+-----+-
EEE
mrn
111
111
kkkk
EEEE
+++++++--- ++---+-+-+
s sssss ss
>>
ii
__
-+++++---+
sss sss ss
+------+++
11
b
+-+---++++
DD
M A
ddd
>33<
>33<
>33 < >33< >3
HHHTTEEEEE S
B S S S S S B STT B
SSEEE
EE
STT SSS TT E E H
09'391961'
2*12117*9* 51081.6854
5885000150 183392**9* 4 7 1 0 9 7 2 6 3 1
LTKSHIEIIR GHAAFTSDPK PTIEVSGKKY TAPHILIATG GMPSTPHESQ IPGASLGITS
<<<<
+--+--+---
H
C
SUMMARY........H=ALPHA-HELIX....E=BETA-STRAND....B~BETA-BRIffiE....G=3-HELIX....I~5-HELIX....T~3-,4-r
...
..
SHEET..
BRIDGE2..
BRIDGEl..
CHIRALITY
BEND.. ,
5-TURN..
4-TURN..
3-TURN..
SUMMARY..
EXPOSURE.
2 8 1 SEQUENCE.
..
....
..
--+---+-+-
G
ccccc
+++-+----+
C
AAAAA
C
H
G
+-++++++++ ++++-+----
2GRS GLUTATHIONE REDUCTASE IOXIWREDUCTASE: GSSG/ACCPTR, NADPH/DONR, FLAVOENZYMEI (HUMAN ERYTHRCCYTE)..............ZGRS
SHEET..
AA
B
AA AAA
B
BRIDGEZ..
b
cc ccc
BRIDGE1..
aa
f
aa
f
CHIRALITY
+--++--+-+-+--+--+ ++++++++++ ++++++++++ ++-++++-+- --+----+++ ++++++++++ ++++++++++
BEND..
s
s sssssssss sssss
ss ss s ssssssssss ssssssssss ssss
ss
ss ssssssssss ssssssssss
5-TURN..
>5555<
> 4 > > < > x x >x < < < <
> > > > < < < x > > > x xxxxxxxxxx< <<<
>>> >xxxxxxxxx xxxxxxxxxx
4-TURN..
3-TURN..
>>3<<
>3><3 <
> 3 3<
>>3<<
>33<
SUMMARY..
S EES BTTnHHHHH HHHHTT E E EEESS TBHH HHHHSHHHHH H H H H H H H H H H HHSS GGGS
H H HHHHHHHHHH H H H H H H H H H H
EXPOSURE. * 5 5 3 7 0 0 0 0 1 0 1 3 1 0 1 1 0 0 5 702*960*80 0836**2826 2 8 2 4 2 5 3 0 3 7 4028304.23 *5*6045*7* **8*5*7*1* 732**05391 7'23698'86
1 SEQUENCE. VASYDYLVIG GGSGGLASAR RAAELGARAA WSHKLGGT aVNVCaVPKK WNTAVHSE FMHDHAWGF PSCEGFFNWR V I K E K R D A Y V SRLNAIYQ"
SHEET..
BRIDGE2..
BRIDGEl..
CHIRALITY
BEND..
5-TURN..
4-TURN..
3-TURN..
SUMMARY..
EXPOSURE.
1 0 1 SEQUENCE.
46)
....
..
SHEET..
BRIDGEZ..
BRIDGE1..
CHIRALITY
BEND..
5-TURN..
4-TURN..
3-TURN..
SUMMARY..
EXPOSURE.
301 SEQUENCE.
w
to
Q,
E3
m
2
..
....
..
..
SSSS
E
SSSSSS
++-++-+--+
AA A
dd d
sss
--++-++-+-
HH HHHHH
TT TTTTT
U RRRRR
....
..
.
U
H
>5555<
++++++++++ +++++----+
s ss sssssss ssssss
xxxx<<<<
D
D
s
> 3 3 < > 33<
s
.,..
ssss ssss sss
s s ssssss
+++---++++ +++--++++- -+--+---++
Q QQ
HH HHHHHH
+++-+-+--ss sss ss
S
H
s
--+---+-++
++--+++---+++-+--+ss
sssssss s
E
BB
+++-----+
I I111
B B B B B AA
S
EEEEEEEBTT TBEEEEEEES
0 1 0 4 1 5 1 9 * 7 052*1*3*0*
DLGNVTADKN C V A I V D I V D P
<
JDDDDDDD
>44 4<
FFFFJ
-++-++--++ +-----+++++-+++---+
ss ss ss
ss s
F
H
.2SOD
.
___.
~
~
BBBBC
CAAAAAAA
.....,...........
B
BOS TAURUS1
( C c W ERYTHROCYTE:
B
8~335sa:g:
PTSSEELVTL R
>>><<<
s SSSCGCCSS
79:6*7*5**
ADfDNTVAIH
HHHHTS
7<>77<
>4<<<
t-+++++++
>33<
>3>X3X<3<
>17c
>?7
TT SS
EEETTEEEEE EEEES SEE EEEEEES
TTGCGTT s B s s
43'6'40385
3 6 0 3 3 2 * + 3 8 1 0 0 0 0 6 6 3 0 3 7 7 ' 3 2 8 2 8 2 7 00476*6*10 0 5 * 5 * 8 1 0 0 0
EAKGDTVVVT G S I T G L T E G D HGFHVHQFGD N T W a T S A G P H F N P L S K K H G GPRDEERHVG
ss
--+++--+--
sss
++------+----+++--+ ++++--+++sss
ss
ss ss sssss s
BBBBB
11111
GGGG
ss
H HHHH
R RRRR
s sssssssss
> 4 44<
>33<
SS S T TTTTS S
EEEEEE EE
S BSSSTTB TTSEEEEESS
683293'820
10310000** 71571*649* *047404037 6301110021
L I S L S G E Y S I I G R W I W H E R PDDLGRGGNE E S T R T G N A G S R L A a G V I G I A K
s sssss
k
k
++-t-+++-+
QQQ
----+-+---
SUPEROXIDE/ACCPTRl
B B BBBBBB
GGCG
FF FF F H
-+--+---++
[OXIDOREDUCTASE:
AAA AAAAA AAAA
DDDD DUD
CCCCC C C C C
ccc
SSS
+++++----+
s ssssss
> > 4 4 x x > > x x<<<<
>>
> 3><3<
>>3<< > 3
>33<
E E E E E E F T T T T E E E E E E E E S T T H H H H H H H H HHHHTTTB H
e73a**s:i:
a ~ i a a ~ 8 8 *s*8 i : a ~ e a 7~4 8~3 . 2 e . 5 3
VMWMVCANKE E K W G I H M O G LCCDEMLOCF AVAVKMGATK
>555 5 <
+---+---+-
SSSSSSS
HHHHHHH
TTTTTTT
>33<
SSB S S S S E E E STTSSS
S
HHH
> >_
,
\>Y
((<(
....
> 33<
> > 3 <<
E
E E E SS E E E E E HHHH HHHS S S S E E E E E E E E GG C S S SS
HHHHHHHS
TT
SSS
6005411*** * * 2 9 3 7 7 7 4 4 4 4 4 0 4 1 4 1 1 0 0 2 0 2 3 1 5 * 9 0 4 * * 4 3 * * 4 3 '
52748381'6 0880*6*180
KLAHRLFEYK E D S K L D Y N N I P T V V F S H P P I GTVGLTEDEA I H K Y G I E N V K T Y S T S F T P M Y HAVTKRKTKC
SSSSSSSSS SSSSSSSS
-+++++++++ +++++++-+- +++---+++-
>>>4xxx>xx
>33<>33<
HHHHHHHHH
524274'101 0824023.46 4 3 9 1 1 5 2 0 0 7
F Q N T N V K C I Y AVGDVCGKAL L T P V A I A A G R
SS
-+--+-+++-
E
A
ZSOD C U , ZN S U P E R O X I D E D I S M U T A S E
AAAAAB
AAAAAA
SHEET..
cccccc
BB
BRIDGEZ..
AAAAA
AAAME
BRIDGEl..
+-+++----+
++----++CHIRALITY
S
sss
BEND..
5-TURN..
4-TURN..
3-TURN..
S E E E E E B sss E E E E E E
SUMMARY..
EXPOSURE.
89600040*1 '4*1*04060
1 SEQUENCE.
ATKAVCVLKG D C P V Q G T I H P
SHEET..
BRIDGEZ..
BRIDGEl..
CHIRALITY
BEND..
5-TURN..
4-TURN..
3-TURN..
SUMMARY.
EXPOSURE.
1 0 1 SEQUENCE.
47)
....
..
SHEET....
BRIDGEZ..
BRIDCEI..
CHIRALITY
BEND..
5-TURN..
4-TURN..
3-TURN..
SUMMARY..
EXPOSURE,
4 0 1 SEQUENCE.
..
.
SHEET....
BRIDGE2..
BRIDGE1..
CHIRALITY
BEND.....
5-TURN..
4-TURN..
3-TURN..
SUMMARY..
EXPOSURE.
381 SEQUENCE.
TABLE A111 (continued)
~
.
N
03
N
A
~
.
..
..
.
.
.........................................
>>>XXXXXXX
33< > 3 3 X 3
HHHHHHHHHH
4'42634091
IKYLEFISEA
ss sssssss ssssssssss ssssssssss
>5555 <
XXXXX<<<X4 4 4 < > > > > x x x xxxxxxxxxx xxxxxx<<<<
>33<
3<
>33< >33<
H H H H H H H H T TTTSHHHHHH H H H H H H H H H H HHHHHHHHHT
119189892' 78848'1730 0 6 9 0 0 + 2 2 3 * 6 0 1 6 2 1 * * 6 7 '8'
IIHVLHSRHP GNFGADACGA MNKALELFRK D I A A K Y K E L G YW
SSSSSSSSSS SSSSSSSS S
++++++++++ ++++++++++ +++-++++++ ++++++++++ ++++++++-+ +
..
....
..
SUMMARY..
> 4 4 > x > > xxxxxxxxxx xx<<<<
>>><<<
>33<
H H H H H H H H H H HS GGGGHHH H H H H H H H H H H H H H H H
65003710'8 *3'1571981 02201'6214 4 0 6 9 5 5
RAGFVSYMKA HTDFAGAEAA WGATLDTFFG MIFSRCI
xxxxxxxx<< <<
ssssssssss ss ssssss ssssssssss ssss
++++++++++ +-++++++++ ++++++++++ ++++
.... .H~ALPHA-HELIX....E=BETA-STRAND....B~BETA-BRIDGE....G~3-HELIX....I=5-HELIX....T-3-,4-,
..
....
5<
sssssss
>>>>xxxx
t--+++++++
OR 5-TURN....S=BEND....
3x<3<
>>3< <
HTTT HHHH HHHHHHHGGG T HHHHHHH
5428'8'620
8832755'"
4367'21754
GELPNIEADV NTFVASHKPR GVTHDQLNNP
+-++++++++ +++++++++ss s ssss ssssssssss
>555
<< > > > > xxxxx<<<<
lECD
xx<<<<
.............................
l E C D HEMOGLOBIN (ERYTHROCRUORIN, DEOXY) [OXYGEN TRANSPORT] (CHIRONOMOUS THUMMI THUMMI)
SHEET.. ,
BRIDGE2..
BRIDGE1..
CHIRALITY
-++++++++ ++++++++++ ++++++++++ -++++++-++ +++--+++++ +-++++++++ ++++++++++
BEND..
ssssssss ssssssss s ssssssssss ssssss ss ssss sssss ssssssssss ssssssssss
5-TURN..
(-TURN..
>>>>xxxxx x < x < < 4 < > > >>xxxxx<<<x > 4 4 < < > 4 4 4< > > 4 4 < < >>>>xxxxxxxxxxxxx<<
>33<
>>3<x33<
> 3 3 x > 3 < x 3 3 x33<>33<>3 3<
>>
3-TURN..
SUMMARY..
H H H H H H H H HHHHTTTT H H H H H H H H H H H HHHHTT TT TTTS HHHHT TSHHHHHHHH HHHHHHHHHH
859'82'818
8 6 7 5 0 * 7 5 0 8 '514724'11
EXPOSURE.
768'526507 611'+1*861 31114100'5 295226.5'9
1 SEQUENCE. LSADQISTVQ ASFDKVKGDP WILYAVFKA DPSIMAWTQ FAGWLESIK GTAPFETHAN RIVGFFSKII
.
.
SHEET..
BRIffiE2..
BRIDGE1..
CHIRALITY
BEND..
5-TURN..
4-TURN..
)-TURN..
SUMMARY..
EXPOSURE.
1 0 1 SEQUENCE.
49)
--+++++++ ++++++++++
-
METWYOGLOBIN) (SPERM WHALE)
lMBN
l M B N MYOGLOBIN [OXYGEN STORAGE] (FERRIC I R O N
SHEET..
BRIDGEZ..
BRIffiEl.,
++++++++++ +++++-++++ ++-+++++++ -++++++-++ ++++++++++ +++++++--+ ++++++++++ ++++++-+-CHIRALITY
sssssss sssssss
sssssss ss ssssssssss ssssssssss
BEND.....
SSSSSSS SSSSSSSSSS ssssssssss sssss ssss ss sssss
>5555<
>>555<<
5-TURN..
4-TURN...
> > > > X X X X X X X X < < < < > >>>xxxxxxx x x < < < x > > 4 << < > > 4 4 < < > > > > < < < x >>xxxxxxxxx
>
xxx<<<<
>>4>xx>xx
>
>
>33<
>>3x<3 <>33<
> > 3 < x 33X33X33<
3-TURN..
>3>x3<<
SUMMARY..
H H H H H H H HHHHHHHTTS H H H H H H H H H H H H H H H H H H H HT HHHHT
SHHHHHH HH H H H H H H H H H H HHHHHHTTTT
H H H H H H H H HHHHHTT
EXPOSURE.
*15*551*50 5'81650997 3 2 1 0 0 2 6 1 1 1 * 1 1 * 5 5 8 8 1 2 * 8 6 + * 8 8 + 1 + 68791*83*6 0 7 * 3 0 5 * 4 0 8 418310'882 '8'781'748
74508'9'25
1 SEQUENCE. VLSEGEWQLV LHWAKVEAD V A G H G Q D I L I RLFKSHPETL EWDRFKHLK TEAEMKASED LKKHGVTVLT A L G A I L K K K G HHEAELKPLA QSHATKHKIP
SHEET..
BRIDGE2..
BRIDGE1..
CHIRALITY
BEND.....
5-TURN..
4-TURN...
3-TURN...
SUMMARY..
EXPOSURE.
1 0 1 SEQUENCE.
48)
v1
to
to
Q,
M
I/,
.
...
.
4-TURN...
3-TURN..
SUMMARY..
EXPOSURE.
1 SEQUENCE.
5-111111..
..........
..
..
.
< < X 4 4 4 < > > >> X X X X X X X X X
>33<
H H TTT HH HHHHHHHHHH
1 63 4 ' 6 1 5 2 4 2 1 1 0 1 2 7 0 1 6
VHLPNDFTPA VHASLDWLS
XXX<<<X444 <
>>>>X
>3><3<
HHHHHHTTTT
HHHH
2227221679 *09*255*45
SVSTVLTSKY RIVQLSGEEK
SS SSSSSSSSSS SSSSSSS S
~
>
. > > 5 5 < <.
>>XXXXXXXX XXXX<<<<
>>3xx
H H H H H H H H H H HHHHHHHTTG
*896706*30 9310900*81
KVKAHGKKVL HSFGEGVHHL
SSSSSSSSSS SSSSSSSS
XXXX<<<<
>>>>XXXXXX
>>3<<
HHHHHHHTT
HHHHHHHHH
5406521**2 74**001200
AAVLALWDKV NEEEVGGEAL
XXX<<<<
>33< >>>x
HHHHHHSGGG
00102036*1
GRLLWYFWT
.........................
.......
,
>>>4<<<>>
xx<xx3<<
>33<>33<
SSHHHHHT H
GGGGGGG
5*74*'3591 '8 6 5 3 8 5 5 2 "
QRFFDSFGDL S NPGAVMGN P
SSSSSSSSS SSSSSSSSSS SSS SSSSS SSSSSSSSSS SSSSSS
>>555<<
> > 4 4 < X > > >X X < < < <
>>>>xxxxx xxxxxxx<<< < > > > > x x xxxxxxxxxx x < < < <
3<<
>>3<<
> >3<<
GGHHHHSHHH HHHHHTTS
THHHHHHHH HHHHHHHHHH GGGS H H H H H H H H H H H H H H H HHHHSS
* 9 1 * 4 5 0 2 7 5 8.8528'7'2
'4'2282362
1 0 0 0 0 0 0 6 7 4 1 * * 0 5 2 * 2 0 1 1 0 1 9 1 0 4 1 0 1 *023**5*
DNLKGTFAAL SELHCDKLHV DPENFRLLGN VLWVLARW GWFTPELQA SYQKWAGVA N A L A H K Y H
S SSSSSSSS SSSSSSSS
<
< 4 < > > 4 4 < x >>>xxx<<<<
>>>>xx
3x33< > 3 3 <
>>><<<
TTTT HHHHT HHHHHHHHHT S
THHHHH
6 8 2 '91 8 4 2 1 7*419750** 7.186822.2
GHLDDLPCAL SDLSNLHAHK LRVDPVNF K L
++++++++++ ++++++++++ ++++++++++ +++++++-+- -+++++++++ +++++++++- +++--+++++ ++++++++++ ++++++
XXXXXXXXX<
>33<
HHHHHHHHHH
4220110010
LSHCLLSTLA
SSSSSSSSSS SS SSS
>3
T HHHHHHHH HHHHHHHHHH
71871'6609 *309316702
CSAQVKAHGK XVCDALTLAV
> > > > x x x x x xxxxxxx<x<
3<
---++++ +++++++++- -+++++++++ ++++++++++ ++++++-+++ +-++++++-+
ssss sssssssss
sssssssss sssssss s s sss ss
ssssssss s
<<x33< > 3
H H H H H GCGG GG TTS ST
0116138*0* *73**4855*
RMFLGFPTTK TYFPHFDLSH
>>>xx
XX<<<<
++++++++++ +++++++-++ ++++++++++ +++++++++
>>>>XXXX XXXX<<<< > >>>XXXXXXX
>33<>>3<<
H H H H H H H HHHHHHHGGG H H H H H H H H H H
* 3 6 8 6 3 5 9 5 0 *4 1 2 9 * 0 4 8 8 1 1 * 1 0 1 4 0 0 6
VLSAADKTNV XAAWSXIICGH AGEYGAEALE
SUMMARY..
.H-ALPHA-HELIX..
.....
....
..
..
..E-BETA-STRAND.. ..B-BETA-BRIDGE. ...G=3-HELIX.. ..I-5-HELIX.. ..T=3-,
4-,
OR 5-TURN..
SxBEND..
..
..
lLHB HEMOGLOBIN(MET)-CYANIDE V [OXYGEN TRANSPORT] [SEA LAMPREY: PETRWYZON MARINUS].
lLHB
SHEET..
BRIDGEZ..
BRIDGE1..
CHIRALITY
--++-------++++++++ ++++++++++ ++++++++++ ++++++++++ +-+++++++- ++++++-+++ ++++++++++ +++++++++- -+++++++++
BEND..
SSS
ssssssss sssssssss ssssssssss ssss SSSSS s sss s s ssssss sss ssssssssss ssssssssss s
sss
5-TURN..
> 5 5 55<
4-TURN..
> > 4 > x x > < x < < > x > 4 < < x 4 >>x>xxxxxx x < < < < > 4 4 4 <
> 4 4 4 < > > > > xxxxxxxxxx xxxx<<<<
>>>>
>3>x>x<<<
3-TURN..
>33<
> 3 3 < > 3 3 x 3 > < 3<
> 3 3 < > 3 3x>3x<3<
>33<
>> 3 < x 3 3 <
>33<
SSS
H H H H H H H H HTTHHHHHTT THHHHHHHHH H H H H TTTTT T GCCTT S SSTTTS H H H H H H H H H H H H H HHHHHHHSSS STTGGGHHH
SUMMARY..
EXPOSURE.
*3 4 2* 6 * 379 2788436'1'
732663.997
' 7 2 0 1 7 1 6 2 6 1 0 6 7 2 8 4 0 3 * 4 4 9 * 1 * 7 3 * 7 5*70**1780 8 * 4 0 4 * 3 1 9 3 1 4 9 1 2 6 2 1 * * 6 * * 2 3 9 3 * * 5
1 SEQUENCE. PIVDTGSVAP LSAAEKTKIR SAWAPWSDY ETSGWILVK PFTSTPAAEE FFPWKGLTT ADELKKSADV RWHAERIIDA VDDAVASMDD TEKMSSMKDL
.
.
SHEET..
BRIDGE2..
BRIDGE1..
CHIRALITY
BEND.....
5-TURN..
(-TURN...
3-TURN..
SUMMARY..
EXPOSURE.
2 0 1 SEQUENCE.
511
.............................................
2MHB H E M O G L O B I N ( A Q U O MET) [OXYGEN TRANSPORT] (HORSE: EQUUS CABALLUS)
.2MHB
SHEET..
BRIDGEZ..
BRIDGE1..
CHIRALITY
--+++++++ +++++++-++ ++++++++++ +++++-++++ +++++--+-+ t - + + + + + + + + ++++++++++ ++++++++++ ++++++++++ ----++++++
BEND.....
SSSSSSS SSSSSSS S SSSSSSSSSS SSSSS SSSS SS SSS SS S SSSSSSSS SSSSSSSSSS SSSS SSSSS SSSSSSSSSS S
SSSSSS
SHEET..
BRIDGE?.
BRIDGEl..
CHIRALITY
BEND.....
5-TURN..
4-TURN...
3-TURN.
SUMMARY..
EXPOSURE.
1 0 1 SEQUENCE.
50)
TABLE A111 (continued)
Q)
N
N
03
..
BRIDGEI..
SHEET..
BRIDGEZ..
..
.
.
..
>>4>XX>XXX
x<3<
THHHHHHHHH
654'285818
NIPRHTHRPF
---
.H=ALPHA-HELIX..
..., .
....
..
E-BETA-STRAND..
..
33<
<<
HT
*4*
DAA
.C=3-HELIX..
.
I-5-HELIX..
..
.T=3-,
.
4-,
CRAMBE ABYSSINICA).....................................lCRN
>>3<<
CGG
58'778
PGDYAN
sss
-+tt
.B=BETA-BRIDGE..
.
+----+-+--
SEED:
<<< >>>> XXXXXXXXXX XXXXXXXX<<
>>3<<
>
HHHHHHHHHH HHCCC HHH HHHHHHHHHH HHHHHHHHHH
4*882'809*
114"54*61
3 4 8 0 3 5 8 2 6 8 119225'41'
K E A I L R T I K E V V G A M S E E L NSAWTIAYDE L A I V I K K E M D
SSS SSSSSSSSSS SSSSSSSSSS S
+
.................
lHBL
>555
>>>> xxxxxx<<<<
.S=BEND..
.
..
>33
HSS
HHH HHHHHHHHHT
8682578762 99305555"
T C W A S D A T L KNLCSVHVSK
<<
5<
OR 5-TURN..
>555
444X444<
> > > > xxxxxxxxxx xxxxxxxx<<
x<<x>3<x33 <
>33<
SS H H H HHHHHHHHHH HHHHHHHHHH
HHHHHH GCC CCC CCC T T
3103.83981
5.65628'3'
3 * 2 3 * * 4 * * 8 47782'4844
14'114826'
I L V L E I A P A A KDLFSFLKCT SEWQNNPEL QAHACRWKL W E A A I Q L E V
>
>>>x
<XX<4<<
+ttt+ttttt +ttttt-ttt ttttttt+tt ttt+tt+ttt
XXXXXXXXX<
LUPINUS LUTEUS L ) .
ttttt+++4+
t t t + t + - 4 t +t t t - t t t - 4 t - - - - t + - + t t t t t t + t t t t t t t t + t t t + + t- t - - - t - + t + t t t t t t t + t SSSSSSSSS SSSSSS SSS SSS SSS SS
SS SSS SSSSSSSSSS SSSSSSSSSS SSS
SSS SSSSSSSSSS
(YELLOW L U P I N ROOT NODUI.ES:
l C R N CRAMBIN [PLANT SEED PROTEIN] ( A B Y S S I N I A N CAEIBACE
SHEET....
AA
AA
BRIDGE2..
BRIDGE1..
AA
AA
CHIRALITY
+-t+++
+ t + + t + + + ---+++++t++
BEND..
SSSSSS sssssssss
ssssssss s
sss
5-TURN..
>5555 <
4-TURN..
>>>>x xxxx<<<<
>>>>xx<<< <
3-TURN..
>3><3<
>33<
SUMMARY..
EE SSHHHH HHHHHHHTTT
HHHHHHHH S EE SSS
EXPOSURE.
8 2 8 8 5 5 * * 1 6 6819*29'*5
4876*81'*2
41583.48'5
T T a b P S I V A R SNFNVCRLPG T P E A I C A T Y T C b I I I P C A T a
1 SEQUENCE.
SUMMARY..
53)
<
>>><<<
>>>>XXXXX X<<<<
[OXYGEN T R A N S W R T ]
SSSSSSS SSSSSSSSSS SS SS
>44>X>>X
>>3X<3<
T CCCHHHH
535'863734
CVADAWPW
5<
t--ttttttt
XXX<<<<
HHHHHH S
SHHHHHHHH HHHHCCC
221.62378'
2 1 2 4 8 1 1 7 3 2 1421'55'
V I A M V A A C D AGPEKLLRMI C I L L R S A Y
<
++++++
-t+ttt+++t
tt+tt--+-+ - t + t + + t t t t
SSSSSSSSS SSSSSS
S
SSSSSSSSS SSSSSS
>>>>XXX
>>3<< > 3 3
HHHHHTTT
CCCHHHHHH
83*71****2
62'5182385
SCKHAKSFEV DPEYFKVLAA
XX<<X<44<
5555<
SSSSSSSS
+++++-+---
I H B L LECHEMOGLOBIN (ACETATE,MET)
SHEET..
BRIDGE2..
BRIDGEI..
CHIRALITY
-+-t+tt44 4tttt4ttt+
BEND.....
S SSSSSS SSSSSSSSSS
5-TURN..
4-TURN...
>>>>XXX XXXXXX<<<<
3-TURN..
>33<
>>3
SIRIMARY..
T T HHHHHH HHHHHHHHHT
EXPOSURE.
2.56'61156
89703'7088
CALTESQAAL VKSSWEEFNA
1 SEOUENCE.
CHIRALITY
BEND.....
5-TURN...
4-TURN...
3-TURN...
SUMMARY..
EXPOSURE.
1 8 1 SEQUENCE.
52)
.
.
SHEET..
BRIDGE2..
BRIDCE1..
CHIRALITY
BEND.....
5-TURN..
4-TURN...
3-TURN..
SUMMARY..
EXPOSURE.
1 8 1 SEQUENCE.
to
0-2
to
4
r
0
Y
..
..
..
....
..
3 P TI TRYPSIN INHIBITOR [PROTEINASE INHIBITOR] [CCW PANCREAS: 80s
SHEET..
AAA AAAA
A A AAAAA
A
BRIDGE2..
B
BRIDGE1..
AAA AAAA
A A AAAAA
B
CHIRALITY
-++++---- --+-+-+-+----++-+--+----++--+++-+-+++
BEND..
SSSSS
S
sssss
sss ss sssss
5-TURN..
>5555<
4-TURN..
>444<
>>>>
3-TURN..
>>><<<
>33<
S
EEE EEEETTTTEE EEEEE S S S
SS BSSHHH
SUPIMARY..
GGGGS
EXPOSURE.
'5.40'5'59
7295'5'6'5
72145'5482
88272842'5
''822'33.8
1 SEQUENCE. RPDPaLEPPY TGWKARIIR WYNAKAGW QTFWGGbRA RRNNPKSAED
TSSSS
2'11055
GSSYFM
4<
SSSS
-++++
HHHHHS
07.5024.
cMRTaGGA
xx<<<<
ssssss
+++++-
TAURUS)....................................
SUPIMARY...~~...H~ALPHA-HELIX....E~BETA-STRAND....B~BETA-BRIDGE....G~3-HELIX....I~5-HELIX....T-3
56)
.
....
-,4-,
CCCCCC
-+--++++--
E g
>>>><X<<
sssssssss
---++++++-
OR 5-TURN....S-BEND....
.......3 P TI
33<
>33<
TTEEEEEE
BSBHHHHHHT
*5**4*2*67 0 6 1 8 3 6 0 7 2 0
WKRVSYERV FSNEbEMNAH
sss
.2SSI
lOV0
.............
....................................................
AAAAAA
B D
2S S I STREPTOMYCES SUBTILISIN INHIBITOR [PROTEINASE INHIBITOR].
AAAAAA B
AAAACC
cc
D B AAAAAA
SHEET.. ,
BRIDGE2..
BBBB
E CCCCCC
BRIDGE1..
AAAAA
D
BBBBFF
FF
g D AAAAA
CHIRALITY
--+++---+ -+-+-+++-- +------+++-++-+-+++ +++++++++- -+-+++---- -+----+-+-----++--BEND..
s sssss
s
s s S S S S s ssssssssss s ss s
ss
s s
5-TURN..
> 5 5 5 5<
4-TURN..
>> >>xxxxx<<< <
3-TURN..
>33<
>33<
>>><< < > 3 3 <
>
SUMMARY..
EEEEEE B SSTTS
SEEEEEE S S EESSTTH H H H H H H H H H H TS STTS
SS
B B EEEEEE
EXPOSURE.
' 4 8 2 4 2 5 1 3 0 0'0936'936
* * 8 5 2 5 1 5 2 4 '376491'42
47017717.3
6 2 6 1 9 6 2 + + 5 *f9'49*7*9
1110208223
1 SEQUENCE. YAPSALVLTV GKGVSATTAA PERAVTLTaA PGPSGTHPAA GSAaADLAAV GGDLNALTRG EDVMbPMVYD PVLLTWGW
.
....
..
....
..
l O V 0 OVOMUCOID THIRD D O M A I N [PROTEINASE INHIBITOR, KAZAL] (JAPANESE QUAIL: COTURNIX COTURNIX JAPONICA)
SHEET..
AAA
BBB
B B
B 88
BRIDGE2..
ccc
BRIDGE1..
aaa
BB
B B
c cc
CHIRALITY
+----++++ +--+---+-+ -----+-+----+++++++ +++--+++-+ --+BEND..
s
ss
sss
sssssssss sssssss
ss
5-TURN..
>5555<
4-TURN..
> > > > x x x x <<<<
3-TURN..
>33 <
>33<
>>3x<3<
SUMMARY..
EEE TT
SS
EEETTS E ESSHHHHHHH HHHTTTS E EEES
EXPOSURE.
'96971582'
258'837.9'
*300055'*6
5 5 1 8 0 6 0 0 2 2 12'374'171
779348
1 SEQUENCE. tAAVSVDaSE YPKPAbPKDY RPVCGSDNKT YSNKbNFaNA WGSNGTLTL NHFGKC
SHEET..
BRIDGE2..
BRIDGE1..
CHIRALITY
BEND..
5-TURN..
(-TURN...
3-TURN..
SUMMARY,.
EXPOSURE.
1 0 1 SEQUENCE.
55)
54)
TABLE A111 (continued)
A P I S MELLIFERA)
+-+---+-++
SUMMARY.
.......HFALPHA-HELIX....E=BETA-STRAND....BIBETA-BRIDGE.
.
...GL~-HELIX....I-~-HELIX....T-~
-,4-,
sss ss s
a aaa
A A M
c ccc
.2ADR
........
lNXB
.........
.1MLT
...S-BEND.
ss
>
SSSS
H H H T T T S E EEES SSSS
77*4**2*00 1 1 2 4 2 1 * * 7 '
VAKWTSKGF LIDGYPREVK
<<x<44<
>33c
+++++++--- ---++++-++
OR 5-TURN.
2ADK A D E N Y L A T E K I N A S E I A T P - A M P P H O S P H M R A N S F E R A S E ] ( P O R C I N E M U S C L E : S U S S C R W A ] . . . . . . . . . . . . . . . . . . . . . . . . . .
SHEET.,
A AAM
MAA
bbbb
BRIDGE2..
BRIDGE1..
a aaa
cccc
CHIRALITY
++++++--+ --++--++-+ ++++++++++
++++++++-- -+++++++++ ++-+----++ ++++++++++
BEND.....
SSSSSS
sss ssssssssss ss
ss sssssssss
sssssssss ssss
ss ssssssssss
5-TURN..
> 5 5 55<
>5555 <
4-TURN...
>>>><<<<
> 4 > > x > x x x < <<<
> > > >xxxx<<<< >>>>xxxxx<<<<
>>> >xxxxxxxxx
3-TURN.,
>33 <
>33 <
SUMMARY..
HHHHHHS E E E E E SSTT TTHHHHHHHH H T E E E E H H HHHHHHHHS
HHHHHHHHH H H S S
HH HHHHHHHHHH
EXPOSURE.
9***2**240
1 0 3 2 1 1 4 2 4 2 '3651.926.
'543362488 923.429974
3940*883*2 5**6**554* 131812*921
SEQUENCE.
M E E K L K K S K I I F W G G F G S G K G T W E K I V Q KYGYCHLSTG D L L R A E V S S G S A R G K H L S E I MEKGQLVPLE T V L M L R D A M
..
..........................
...........................................
l N X B N E U R O T O X I N B ( P R O B A B L Y = E R A B U T O X I N 8) ( S E A S N A K E : L A T I C A U D A S E H I F A S C I A T A )
SHEET..
AAA
AAA
BBBBBBB B BBBBBBB B
BBBB
cccc
BRIDGE2..
BRIDGEl..
AAA
AAA
BBBBBBB B BBBBBBB B
cccc
CHIRALITY
+-++---+-+------++
++-----+-+
-+------+-------++++---+--++
BEND..
sss s
ss
ss
ss
ss
sss
5-TURN..
4-TURN..
3-TURN..
>33<
>33 <
>33<
> 3 > < 3<
SUMMARY..
E E E STT S E E E TT
E E E E E E E E T T E E E E E E E ES
SS
E E E E STTT T
EXPOSURE.
B 6 0 2 5 1 8 5 9 * **69**17*8 7 6 2 0 3 4 3 9 8 7 6**3*21721 4 0 6 5 * 6 * * 6 5 * 4 7 5 4 * 6 9 3 3 0.
SEQUENCE.
R I a F N Q H S S Q PQTTKTbSPG E S S a Y H K Q W S D F R G T I I E R G b G c P T V K P G I K L S C d E S E V d NN
..
....
..
.
.
.
..
l M L T M E L I T T I N [ H E M O L Y T I C P O L Y P E P T I D E ] ( H O N E Y B E E VENOM:
SHEET..
BRIDGEZ..
BRIDGE1..
+++++++++ ++++++++++ ++++
CHIRALITY
BEND.....
SSSSSSSS SSSSSSSSSS SSSS
5-TURN..
4-TURN...
>>>>XXX<X< <>X>>XXXXX XX<<<<
3-TURN..
>33<
SUMMARY..
HHHHHHHHH TTHHHHHHHH HHHHH
9.3 671 **58 '4 387 72 7'3 a*****
EXPOSURE.
SEQUENCE
G I G A V L K V L T T G L P A L I SW I KRKR QQ
....
..
l C T X A L P H A C O B R A T O X I N (COBRA: NAJA NAJA SIAMENSIS).................................................................lCTX
SHEET. +.
A AMAA
AAAM
AAAAA
BRIDGE2..
BBBBB
BRIDGEl..
A AAAA
BBBBB
AAAAA
CHIRALITY
--t-++--+ -++-++-t--+---+-ttt ++------++-+----+-+
+-+----+-+
+++----+BEND..
sssss
sss
sss sss
ss
s s
s s s sss
5-TURN..
(-TURN,.
>> 4 4 < <
3-TURN..
>33<
>33x 33<
> 3 3<
>33<
SUMMARY..
sssss
T T S E E E E E E T T H HHH E E E E E
SS
S S EEEEE
T T S STT
5*0253***9 5 5 9 5 7 . 1 ' 2 8
3240977**1 9 * * 4 4 * 5 6 0 0 345*83*7** 6 5 5 4 * 3 3 9 9 9 * 3 0 7 * 4 9 * 8 *
EXPOSURE.
SEQUENCE.
I R a F I T P D I T S K D b P N G H V a YTKTWCDAFC S X R G K R M L G bAA,TdPTVKT G M I Q d e S T D N e N P F P T R K R P
N
CD
Ga
N
E
4
Z
2
v
M
rn
..
S
d ddd
A AAA
.. ........ .... . .
>3<x33<
>33<
>33 <
HHTTTT
H H H H H H H H HHHHHHHTTH HHHHHHHS E E E E
S HH HHHHHHHAHH
*94'*46*8*
86**52***4 "636'31980
1 2 * 2 7 * * 3 6 5 7'2'4'699.
7347524943
KRGETSGRVD DNEETIKKRL ETYYKATEPV IAFYEXRGIV RKVNAEGSW DVFSQVCTHL
......
>33<
HHH
*+2*
DTLK
-+++++++++ +++++-++-+ ++++++++++ ++++++++++ ++++++-+++ ---+++--++ ++++++++++ ++
sssssssss ssssss
ssssssss ssssssssss ssssssss
s ss ssssssssss s s
>5555<
>5555<
> 5.5.5.
5_
<
>>>>xxxxx<< x < 4 4 <
>>>>xxxxxx x x x < < x < > >x > x x < < < <
>>> >xxxxxxxxx <<<<
>>>XX<<<<
>33<
>
SEEEEE
HHHHHHHHH
HHHHHHHHS
4 0 5 2 0 6 * 8 2 0 8 2 5 2 8 5 6 3 7 1 2**316*'1*
Q C E E F E R K I G QPTLLLYVDA GPETnTKRLL
SSSSSSSSS
+++++++-++ --+-----+-
AAAAA
dddd
bbbb
..
..
....
..
..
....
SHEET..
BRIDGE2..
BRIDGEI..
CHIRALITY
BEND..
5-TURN..
4-TURN..
3-TURN..
SUMMARY..
EXPOSURE.
2 8 1 SEQUENCE.
..
....
..
-+--+---+-
DDDD
il
hhhh
---+---+++ +--+++++++ ++-++--+-sss
sssssss sss s
DD
99
C
F
---++--+-s ssssss s ss ss
+--++++-++
ss
>5555<
ss s
hhhh
JJ
2 2
DDDD
++++++++++ ++-++++---
E
S
>3>X3<X33<
>>3<<
ETTTHHHHHH HS GGGSB S S
810083204* *167*2353* 5 * *
YDCSWFEWFH RAPPEWVSQ G KG
ss ssssss ss ssss s
> > > > x < <<<
K
-+--++++++ +--+++-+-+
4 4
-J J_
??
sss ssssssssss ssss
> 5555<
>>>>xxxx <<<<
>3><3<
> 33< > 3 3 <
++++-+--++ ----++---+
ssssss ssssss
----++++++
L
F
> > 4 > x x > x<<<<
>33<
>3><3<>33<
>33< >>3<< >33 <
B TT EE
TTTTB TTS B HHHHHH HHHHTT TT S EEEE SSS STTHHHHHHH HHHT TT EE
1 8 3 0 * 6 1 5 2 8 2 2 9 7 0 1 4 ' 9 8 5 2 5 3 8 * 8 0 * 5 4 0 * 8 8 * 1 6 4 + ' 6 8 0 0 0 8 2 4 8 0180080000 1 5 4 5 1 1 8 8 8 8
SGH IRGSVNM P F M W LTENG F EKS PE ELRA MFEAKKVDLT KPLIAXRKG VTACHIALAA YLCGKPDVAI
sssss sss
-++++--+-+
L
il
K
+---++--+-
F
DD
E
>5555<
>>> >xx<<<<
>>>4c<<
>4>>x4xx <4<<
>33<
>33<
>>3x<3<
>33<
>33x33<
EEEETTHH HHHHHHT
STTS SSHHH HHHHHHHT
B
TTS EE TTHHHHH H H H SEEEE S HHHHHT s'.17*5*737
ss ss
2 * 5 0 1 6 1 0 0 0 8 0 0 1 0 3 0 0 5 1 ' 3 0 0 0 1 4 8 0 2 8 2 0 8 * 8 5 5 7 6 4 9 * * 2 * 4 * 8 4 * 1 * 1 9 7 6 * 7 1 3353'506'1
5 * 7 * * 4 5 2 0 0 012'25471'
DDLCSFYAPR VWWnFRWGH RTVSVLNGGF RNWLKEGHPV TSEPSRPEPA IFKATLNRSL LKTYEQVLEN LESKRFQLVD SRASRYLGT QPEPDAVGLD
>5555<
+++++-+---
ss s ssssss
-+-+++++++ +++++++-+- +++---+--+
ssss sssss ssssssss
>>>> xxxx<<<<
AAAA
ddd
aa
-+----++++
l R H D RHODANESE [THIOSULFATE-CYANIDE SULFURTRANSFERASE] (CCW LIVER: BOS TAURUS)
,
,
.......I). l R H D
SHEET..
AA
A
AAA B B
c
BB
AAAA
BRIDGE2..
ccc
ddd
b
b
ee
BRIDCE1..
aa
F
ee
ccc
CHIRALITY
++---++-- -+++++++++ -+++-++--+ -++++--++- -+++++++++ ---+-----+
+++--++-+++++++-+-- ++---++--+
BEND..
sssssssss s sss
sss ssssssss ss
s ssss s sss s
ssss ssssssss sss
5-TURN..
>55 55x5555<
4-TURN..
>>>>xxxx<<<<
>444 <>>>4x<<4<
> > > > xx<x<<4<
3-TURN..
> 3 3 x 3 3<
>33<
>33<
> 3 3< > 3 3 <
> 33<>>3<< > 33<
SUMMARY..
E E H H H H H H H H H HT BTTTEEE EE
TTT
HHHHHTTS B TT EE T TSSS TTSSS S
H H H H HHHHGGGS
TTSEEEE
EXPOSURE. * * * + 7 5 * 1 5 1 51'801*13*
75'51'4141
0 1 0 1 6 3 4 ' 9 9 7*1'*729**
0 0 3 4 0 2 3 0 5 1 9'077'83'4
5 2 2 2 2 7 ' 7 3 8 1'50882084 6 * 0 2 0 0 8 1 0 2
1 SEQUENCE. VHQVLYRALV STKWLAESVR AGKVGFGLRV LDASWYSPGT REARKEYLER HVPGASFFDI EECRDKASPY EWLPSEAGF ADYVGSLGIS NDTHWWNG
SHEET..
BRIDGE2..
BRIDGEl..
CHIRALITY
BEND..
5-TURN..
4-TURN..
3-TURN..
SUMMARY,.
EXPDSURE.
181 SEQUENCE.
61)
....
SHEET..
BRIDCE2..
BRIDCEl..
CHIRALITY
BEND..
5-TURN..
4-TURN...
)-TURN...
SUMMARY,.
EXPOSURE.
1 0 1 SEQUENCE.
TABLE A111 (continued)
0
0
E3
03
BRIDCE2..
SHEET....
....
..
--
>33<
EEETTEEEEE EEE
7843*7866e 799'
LLSPYSYSTT AVVT
SS
-+-+++--+-
DDDDD DDD
AAAAA hAA
SUMMARY........H~ALPHA-HELIX....E~BETA-STRAND....B~BETA-BRIDCE....G~3-HELIX....I~5-HELIX....T~3-,4-r
..
.
aa
AAA
DDD
2PAB PREALBUMIN [THYROXIN, RETINQL TRANSPORT] (HUMAN PLASMA).....r......................,.......................,..2PAB
SHEET....
AAAAAAA
AA
B BBBBBB
BBB BBBB
AA
BBB BBBB
BRIDGEZ..
BB cc
FFFFF
GGG GGGG
BRIDGEI..
aaaaaaa
CC
E EEEEEE
EEE EEEE
BB
F FFFF
CHIRALITY
++------+
+-+---++--------+-+
---+--+---+-+-+++--++++-+------++++++
BEND..
s ssss s
sss s
sss
s
ssss ss
ssss
5-TURN..
> 5 555<
>
> 4 44<
r444i
>>>>xx
4-TURN..
j-TURN..
>33<
>33<
>33<
>
SUMMARY..
EEEEEEET TTTEE S E EEEEEE TTS SEEEEEEEE
TTSEE S
TTTS SEEE EEEE HHHHH
B"'16'160
3050515630
EXPOSURE. 6284888785 8.74486'81
0704761"'*
99'*4282*8
5'68418822
1 SEQUENCE. CPLMVKVLDA VRGSPAINVA V H W R K A A D D TWEPFASGKT SESGELHGLT TEEQFVEGIY KVEIDTKSYW
BRIDGEI..
CHIRALITY
BEND.....
5-TURN..
4-TURN..
3-TURN..
SUMMARY..
EXPOSURE.
101 SEQUENCE.
62)
aaaaa
-___-___--
OR 5-TURN....S-BEND....
>3<<
HHHT
S S EEEEEEE S SS
EEEEE
'"77693'5'
789274783. *3'2'34040
KALGISPFHE HAEVVFTAND SGPRRYTIAA
::::
5555<
++-+--+-----+--+++
ssss
s s
s ss
AAAAA
DDDDD
BBBBBBB
CGGGGGG
i
3
0
m
0
1
1
,
1
1
1
,
:..........W(II,,,:..H~IWII.M
.............llmllllll
1
I
I
1
I
1
~
1
1
1
1
~
................................
1
......UwyMYwH...-., .......
1
1
1
~
................
20 0
~
I
1
~
1
1
~
,1
I
~
l
300
1
11-14)
l
~
I
Fig. A l . Strip maps of secondary structure and solvent exposure for 62 proteins. Top line dots: residues with more than three contacting water molecules.
Vertical bars: short, 3-helix; medium, 4-helix (a-helix);long, 5-helix. Dots above baseline: residue has antiparallel /3-bridge partnerb). Dots below baseline:
P-strand has parallel /3-bridge partner(s). The four-letter code is the Protein Data Bank data set identifier (Table AI).
I
.....................................................................
..................................................................................................
1 FXC
....................................
..::..........w( .....:......:......... .....::...
1FDX
L
1
.............................................................
................................................................
.......:..................... :...w.......................... IIUIHHIHH..
..IIIHWI(R.........................
...........................................................
.................................................
. . I H H ...........
~
l m l..............
w ............ymrmw......
156B
......
....
........:.......w
..................................
.........................................................
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DICTIONARY OF PROTEIN SECONDARY STRUCTURE
2633
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DICTIONARY OF PROTEIN SECONDARY STRUCTURE 2637
For reasons of space it is impossible to cite the tremendous amount of work by the crystallographers on which this paper is based; references for each structure are in the Protein
Data Bank. C. Oefner provided computer graphics software. The Deutsche Forschungsgemeinschaft gave financial support to the project “Protein Structure Theory.”
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Received December 22,1982
Accepted May 12,1983