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PDBsum entry 1clv

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Top Page protein metals Protein-protein interface(s) links
Hydrolase PDB id
1clv
Jmol
Contents
Protein chains
471 a.a. *
32 a.a. *
Metals
_CL
_CA
Waters ×273
* Residue conservation analysis
HEADER    HYDROLASE                               04-MAY-99   1CLV
TITLE     YELLOW MEAL WORM ALPHA-AMYLASE IN COMPLEX WITH THE AMARANTH
TITLE    2 ALPHA-AMYLASE INHIBITOR
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROTEIN (ALPHA-AMYLASE);
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: ALPHA-1,4-GLUCAN-4-GLUCANOHYDROLASE;
COMPND   5 EC: 3.2.1.1;
COMPND   6 MOL_ID: 2;
COMPND   7 MOLECULE: PROTEIN (ALPHA-AMYLASE INHIBITOR);
COMPND   8 CHAIN: I;
COMPND   9 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: TENEBRIO MOLITOR;
SOURCE   3 ORGANISM_COMMON: YELLOW MEALWORM;
SOURCE   4 ORGANISM_TAXID: 7067;
SOURCE   5 MOL_ID: 2;
SOURCE   6 SYNTHETIC: YES;
SOURCE   7 OTHER_DETAILS: THE PROTEIN WAS CHEMICALLY SYNTHESIZED. THE
SOURCE   8 SEQUENCE OF THIS PROTEIN IS NATURALLY FOUND IN AMARANTHUS
SOURCE   9 HYPOCHONDRIACUS (PRINCE'S FEATHER).
KEYWDS    INSECT ALPHA-AMYLASE INHIBITOR, AMARANTHUS HYPOCHONDRIACUS,
KEYWDS   2 YELLOW MEAL WORM, X-RAY STRUCTURE, KNOTTIN, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    P.J.B.PEREIRA,V.LOZANOV,A.PATTHY,R.HUBER,W.BODE,S.PONGOR,
AUTHOR   2 S.STROBL
REVDAT   3   24-FEB-09 1CLV    1       VERSN
REVDAT   2   01-APR-03 1CLV    1       JRNL
REVDAT   1   03-MAY-00 1CLV    0
JRNL        AUTH   P.J.PEREIRA,V.LOZANOV,A.PATTHY,R.HUBER,W.BODE,
JRNL        AUTH 2 S.PONGOR,S.STROBL
JRNL        TITL   SPECIFIC INHIBITION OF INSECT ALPHA-AMYLASES:
JRNL        TITL 2 YELLOW MEAL WORM ALPHA-AMYLASE IN COMPLEX WITH THE
JRNL        TITL 3 AMARANTH ALPHA-AMYLASE INHIBITOR AT 2.0 A
JRNL        TITL 4 RESOLUTION.
JRNL        REF    STRUCTURE FOLD.DES.           V.   7  1079 1999
JRNL        REFN                   ISSN 0969-2126
JRNL        PMID   10508777
JRNL        DOI    10.1016/S0969-2126(99)80175-0
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.851
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.8
REMARK   3   NUMBER OF REFLECTIONS             : 31194
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.161
REMARK   3   FREE R VALUE                     : 0.190
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1663
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.03
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 988
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2577
REMARK   3   BIN FREE R VALUE                    : 0.2435
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 6.48
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 64
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3852
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 2
REMARK   3   SOLVENT ATOMS            : 273
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.01
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.007
REMARK   3   BOND ANGLES            (DEGREES) : 1.78
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.47
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.30
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1CLV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-MAY-99.
REMARK 100 THE RCSB ID CODE IS RCSB001000.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-98
REMARK 200  TEMPERATURE           (KELVIN) : 289
REMARK 200  PH                             : 5.4
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : GRAPHITE
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33598
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.4
REMARK 200  DATA REDUNDANCY                : 8.300
REMARK 200  R MERGE                    (I) : 0.13500
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.05
REMARK 200  COMPLETENESS FOR SHELL     (%) : 68.3
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.33900
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1JAE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 45.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG 1000, 12% PEG 8000, PH 5.4
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+1/3
REMARK 290       3555   -X+Y,-X,Z+2/3
REMARK 290       4555   -X,-Y,Z+1/2
REMARK 290       5555   Y,-X+Y,Z+5/6
REMARK 290       6555   X-Y,X,Z+1/6
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       21.59333
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       43.18667
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       32.39000
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       53.98333
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       10.79667
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, I
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480   M RES C SSEQI ATOMS
REMARK 480     ASP A  213   OD1   OD2
REMARK 480     GLU A  235   CG    CD    OE1   OE2
REMARK 480     ASP A  350   CB    CG    OD1   OD2
REMARK 480     ASN A  352   CB    CG    OD1   ND2
REMARK 480     GLU A  378   CG    CD    OE1   OE2
REMARK 480     GLN A  381   CD    OE1   NE2
REMARK 480     ASP A  446   CB    CG    OD1   OD2
REMARK 480     ASP A  451   CG    OD1   OD2
REMARK 480     ASP A  459   CG    OD1   OD2
REMARK 480     LYS I  511   CG    CD    CE    NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    SER A  12      142.46     73.99
REMARK 500    PHE A  31      -52.87   -135.12
REMARK 500    SER A  64     -172.50   -170.19
REMARK 500    MET A 100     -118.25   -115.87
REMARK 500    CYS A 134      163.08    172.77
REMARK 500    ASN A 137       -4.37   -146.78
REMARK 500    ILE A 224       71.96     60.91
REMARK 500    SER A 294       28.77   -140.39
REMARK 500    ASP A 390     -110.50   -145.86
REMARK 500    TRP I 505       -8.73     76.95
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A 601  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A  98   OD1
REMARK 620 2 ARG A 146   O   153.1
REMARK 620 3 ASP A 155   OD1  81.3 117.8
REMARK 620 4 ASP A 155   OD2 123.8  82.3  49.5
REMARK 620 5 HIS A 189   O    72.4  81.0 137.2 162.4
REMARK 620 6 HOH A 619   O    94.3  77.9  67.5  90.0  81.3
REMARK 620 7 HOH A 628   O   108.3  73.5 132.9  92.4  88.0 150.7
REMARK 620 8 HOH A 611   O    69.3 131.0  76.2  73.6 122.1 142.1  65.7
REMARK 620 N                    1     2     3     4     5     6     7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ACS
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CATALYTIC SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 601
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 602
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUE 1 IN THE PDB ENTRY
REMARK 999 IS A PYROGLUTAMATE (5-OXO-PROLINE)
DBREF  1CLV A    1   471  UNP    P56634   AMY_TENMO        2    471
DBREF  1CLV I  501   532  UNP    P80403   IAAI_AMAHP       1     32
SEQADV 1CLV PCA A    1  UNP  P56634    GLN     1 SEE REMARK 999
SEQRES   1 A  471  PCA LYS ASP ALA ASN PHE ALA SER GLY ARG ASN SER ILE
SEQRES   2 A  471  VAL HIS LEU PHE GLU TRP LYS TRP ASN ASP ILE ALA ASP
SEQRES   3 A  471  GLU CYS GLU ARG PHE LEU GLN PRO GLN GLY PHE GLY GLY
SEQRES   4 A  471  VAL GLN ILE SER PRO PRO ASN GLU TYR LEU VAL ALA ASP
SEQRES   5 A  471  GLY ARG PRO TRP TRP GLU ARG TYR GLN PRO VAL SER TYR
SEQRES   6 A  471  ILE ILE ASN THR ARG SER GLY ASP GLU SER ALA PHE THR
SEQRES   7 A  471  ASP MET THR ARG ARG CYS ASN ASP ALA GLY VAL ARG ILE
SEQRES   8 A  471  TYR VAL ASP ALA VAL ILE ASN HIS MET THR GLY MET ASN
SEQRES   9 A  471  GLY VAL GLY THR SER GLY SER SER ALA ASP HIS ASP GLY
SEQRES  10 A  471  MET ASN TYR PRO ALA VAL PRO TYR GLY SER GLY ASP PHE
SEQRES  11 A  471  HIS SER PRO CYS GLU VAL ASN ASN TYR GLN ASP ALA ASP
SEQRES  12 A  471  ASN VAL ARG ASN CYS GLU LEU VAL GLY LEU ARG ASP LEU
SEQRES  13 A  471  ASN GLN GLY SER ASP TYR VAL ARG GLY VAL LEU ILE ASP
SEQRES  14 A  471  TYR MET ASN HIS MET ILE ASP LEU GLY VAL ALA GLY PHE
SEQRES  15 A  471  ARG VAL ASP ALA ALA LYS HIS MET SER PRO GLY ASP LEU
SEQRES  16 A  471  SER VAL ILE PHE SER GLY LEU LYS ASN LEU ASN THR ASP
SEQRES  17 A  471  TYR GLY PHE ALA ASP GLY ALA ARG PRO PHE ILE TYR GLN
SEQRES  18 A  471  GLU VAL ILE ASP LEU GLY GLY GLU ALA ILE SER LYS ASN
SEQRES  19 A  471  GLU TYR THR GLY PHE GLY CYS VAL LEU GLU PHE GLN PHE
SEQRES  20 A  471  GLY VAL SER LEU GLY ASN ALA PHE GLN GLY GLY ASN GLN
SEQRES  21 A  471  LEU LYS ASN LEU ALA ASN TRP GLY PRO GLU TRP GLY LEU
SEQRES  22 A  471  LEU GLU GLY LEU ASP ALA VAL VAL PHE VAL ASP ASN HIS
SEQRES  23 A  471  ASP ASN GLN ARG THR GLY GLY SER GLN ILE LEU THR TYR
SEQRES  24 A  471  LYS ASN PRO LYS PRO TYR LYS MET ALA ILE ALA PHE MET
SEQRES  25 A  471  LEU ALA HIS PRO TYR GLY THR THR ARG ILE MET SER SER
SEQRES  26 A  471  PHE ASP PHE THR ASP ASN ASP GLN GLY PRO PRO GLN ASP
SEQRES  27 A  471  GLY SER GLY ASN LEU ILE SER PRO GLY ILE ASN ASP ASP
SEQRES  28 A  471  ASN THR CYS SER ASN GLY TYR VAL CYS GLU HIS ARG TRP
SEQRES  29 A  471  ARG GLN VAL TYR GLY MET VAL GLY PHE ARG ASN ALA VAL
SEQRES  30 A  471  GLU GLY THR GLN VAL GLU ASN TRP TRP SER ASN ASP ASP
SEQRES  31 A  471  ASN GLN ILE ALA PHE SER ARG GLY SER GLN GLY PHE VAL
SEQRES  32 A  471  ALA PHE THR ASN GLY GLY ASP LEU ASN GLN ASN LEU ASN
SEQRES  33 A  471  THR GLY LEU PRO ALA GLY THR TYR CYS ASP VAL ILE SER
SEQRES  34 A  471  GLY GLU LEU SER GLY GLY SER CYS THR GLY LYS SER VAL
SEQRES  35 A  471  THR VAL GLY ASP ASN GLY SER ALA ASP ILE SER LEU GLY
SEQRES  36 A  471  SER ALA GLU ASP ASP GLY VAL LEU ALA ILE HIS VAL ASN
SEQRES  37 A  471  ALA LYS LEU
SEQRES   1 I   32  CYS ILE PRO LYS TRP ASN ARG CYS GLY PRO LYS MET ASP
SEQRES   2 I   32  GLY VAL PRO CYS CYS GLU PRO TYR THR CYS THR SER ASP
SEQRES   3 I   32  TYR TYR GLY ASN CYS SER
MODRES 1CLV PCA A    1  GLU  PYROGLUTAMIC ACID
HET    PCA  A   1       8
HET     CA  A 601       1
HET     CL  A 602       1
HETNAM     PCA PYROGLUTAMIC ACID
HETNAM      CA CALCIUM ION
HETNAM      CL CHLORIDE ION
FORMUL   1  PCA    C5 H7 N O3
FORMUL   3   CA    CA 2+
FORMUL   4   CL    CL 1-
FORMUL   5  HOH   *273(H2 O)
HELIX    1   1 TRP A   21  ARG A   30  1                                  10
HELIX    2   2 TRP A   56  TYR A   60  5                                   5
HELIX    3   3 GLU A   74  ASP A   86  1                                  13
HELIX    4   4 SER A  127  ASP A  129  5                                   3
HELIX    5   5 ALA A  142  ASN A  147  1                                   6
HELIX    6   6 ASP A  161  ASP A  176  1                                  16
HELIX    7   7 ALA A  187  HIS A  189  5                                   3
HELIX    8   8 PRO A  192  GLY A  201  1                                  10
HELIX    9   9 THR A  207  TYR A  209  5                                   3
HELIX   10  10 LYS A  233  GLU A  235  5                                   3
HELIX   11  11 PHE A  245  GLN A  256  1                                  12
HELIX   12  12 LEU A  261  ASN A  266  5                                   6
HELIX   13  13 PRO A  269  TRP A  271  5                                   3
HELIX   14  14 GLY A  276  ASP A  278  5                                   3
HELIX   15  15 TYR A  299  ALA A  314  5                                  16
HELIX   16  16 GLU A  361  ARG A  363  5                                   3
HELIX   17  17 ARG A  365  ALA A  376  1                                  12
HELIX   18  18 VAL A  467  ALA A  469  5                                   3
HELIX   19  19 PRO I  510  ASP I  513  1                                   4
SHEET    1   A 7 ARG A 321  SER A 324  0
SHEET    2   A 7 ILE A  13  LEU A  16  1  N  ILE A  13   O  ILE A 322
SHEET    3   A 7 GLY A  39  GLN A  41  1  N  GLY A  39   O  VAL A  14
SHEET    4   A 7 ARG A  90  ALA A  95  1  N  ARG A  90   O  VAL A  40
SHEET    5   A 7 GLY A 181  VAL A 184  1  N  GLY A 181   O  VAL A  93
SHEET    6   A 7 PHE A 218  GLU A 222  1  N  PHE A 218   O  PHE A 182
SHEET    7   A 7 CYS A 241  LEU A 243  1  N  CYS A 241   O  GLN A 221
SHEET    1   B 3 GLN A 392  ARG A 397  0
SHEET    2   B 3 GLY A 401  THR A 406 -1  N  PHE A 405   O  ILE A 393
SHEET    3   B 3 VAL A 462  HIS A 466 -1  N  ILE A 465   O  PHE A 402
SHEET    1   C 2 LEU A 411  ASN A 416  0
SHEET    2   C 2 SER A 449  LEU A 454 -1  N  LEU A 454   O  LEU A 411
SHEET    1   D 2 GLY A 422  CYS A 425  0
SHEET    2   D 2 SER A 441  VAL A 444 -1  N  VAL A 444   O  GLY A 422
SSBOND   1 CYS A   28    CYS A   84                          1555   1555  2.03
SSBOND   2 CYS A  134    CYS A  148                          1555   1555  2.04
SSBOND   3 CYS A  354    CYS A  360                          1555   1555  2.03
SSBOND   4 CYS A  425    CYS A  437                          1555   1555  2.03
SSBOND   5 CYS I  501    CYS I  518                          1555   1555  2.03
SSBOND   6 CYS I  508    CYS I  523                          1555   1555  2.03
SSBOND   7 CYS I  517    CYS I  531                          1555   1555  2.03
LINK         OD1 ASN A  98                CA    CA A 601     1555   1555  2.44
LINK         O   ARG A 146                CA    CA A 601     1555   1555  2.32
LINK         OD1 ASP A 155                CA    CA A 601     1555   1555  2.74
LINK         OD2 ASP A 155                CA    CA A 601     1555   1555  2.47
LINK         O   HIS A 189                CA    CA A 601     1555   1555  2.37
LINK        CA    CA A 601                 O   HOH A 619     1555   1555  2.54
LINK        CA    CA A 601                 O   HOH A 628     1555   1555  2.47
LINK        CA    CA A 601                 O   HOH A 611     1555   1555  2.58
LINK         C   PCA A   1                 N   LYS A   2     1555   1555  1.33
CISPEP   1 VAL A  123    PRO A  124          0        -6.37
CISPEP   2 GLU I  519    PRO I  520          0        -5.50
SITE     1 ACS  3 ASP A 185  GLU A 222  ASP A 287
SITE     1 AC1  7 ASN A  98  ARG A 146  ASP A 155  HIS A 189
SITE     2 AC1  7 HOH A 611  HOH A 619  HOH A 628
SITE     1 AC2  3 ARG A 183  LEU A 243  ARG A 321
CRYST1  119.250  119.250   64.780  90.00  90.00 120.00 P 61          6
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.008386  0.004841  0.000000        0.00000
SCALE2      0.000000  0.009683  0.000000        0.00000
SCALE3      0.000000  0.000000  0.015437        0.00000
      
PROCHECK
Go to PROCHECK summary
 References