spacer
spacer

PDBsum entry 1cpu

Go to PDB code: 
Top Page protein ligands metals links
Hydrolase PDB id
1cpu
Jmol
Contents
Protein chain
496 a.a. *
Ligands
GLC-AGL
GLC-GLC
NAG
HMC
Metals
_CA
_CL
Waters ×261
* Residue conservation analysis
HEADER    HYDROLASE                               07-JUN-99   1CPU
TITLE     SUBSITE MAPPING OF THE ACTIVE SITE OF HUMAN PANCREATIC ALPHA-AMYLASE
TITLE    2 USING SUBSTRATES, THE PHARMACOLOGICAL INHIBITOR ACARBOSE, AND AN
TITLE    3 ACTIVE SITE VARIANT
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROTEIN (ALPHA-AMYLASE);
COMPND   3 CHAIN: A;
COMPND   4 EC: 3.2.1.1;
COMPND   5 ENGINEERED: YES;
COMPND   6 OTHER_DETAILS: MODIFIED ACARBOSE BOUND AT ACTIVE SITE
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 ORGAN: PANCREAS;
SOURCE   6 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4922
KEYWDS    AMYLASE, ACARBOSE, GLYCOSYLATION, MUTAGENESIS, DIABETES, CATALYSIS,
KEYWDS   2 PANCREATIC, ENZYME, HUMAN, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    G.D.BRAYER,G.SIDHU,R.MAURUS,E.H.RYDBERG,C.BRAUN,Y.WANG,N.T.NGUYEN,
AUTHOR   2 C.M.OVERALL,S.G.WITHERS
REVDAT   5   13-JUL-11 1CPU    1       VERSN
REVDAT   4   24-FEB-09 1CPU    1       VERSN
REVDAT   3   05-AUG-03 1CPU    1       JRNL   REMARK
REVDAT   2   24-APR-00 1CPU    1       SEQADV
REVDAT   1   14-JUN-99 1CPU    0
JRNL        AUTH   G.D.BRAYER,G.SIDHU,R.MAURUS,E.H.RYDBERG,C.BRAUN,Y.WANG,
JRNL        AUTH 2 N.T.NGUYEN,C.M.OVERALL,S.G.WITHERS
JRNL        TITL   SUBSITE MAPPING OF THE HUMAN PANCREATIC ALPHA-AMYLASE ACTIVE
JRNL        TITL 2 SITE THROUGH STRUCTURAL, KINETIC, AND MUTAGENESIS
JRNL        TITL 3 TECHNIQUES.
JRNL        REF    BIOCHEMISTRY                  V.  39  4778 2000
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   10769135
JRNL        DOI    10.1021/BI9921182
REMARK   2
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR
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)) : 0.000
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             : 35710
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.170
REMARK   3   FREE R VALUE                     : NULL
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL
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           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
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            : 3945
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 71
REMARK   3   SOLVENT ATOMS            : 261
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
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) : 0.008
REMARK   3   BOND ANGLES            (DEGREES) : 1.23
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
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 1CPU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JUN-99.
REMARK 100 THE RCSB ID CODE IS RCSB001160.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 298
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : NULL
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : NULL
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33610
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.8
REMARK 200  DATA REDUNDANCY                : 4.700
REMARK 200  R MERGE                    (I) : 0.03600
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) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 42.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
REMARK 290       4555   X+1/2,-Y+1/2,-Z
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 -1.000000  0.000000  0.000000       26.45500
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       65.88500
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.45000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       65.88500
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.45500
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       34.45000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PCA A   1    OE
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500    GLU A 484   CB    GLU A 484   CG     -0.123
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    LEU A  26   CA  -  CB  -  CG  ANGL. DEV. =  14.2 DEGREES
REMARK 500    CYS A 115   CA  -  CB  -  SG  ANGL. DEV. =  10.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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    TYR A  31      -52.34   -141.20
REMARK 500    MET A 102     -151.27   -109.33
REMARK 500    THR A 114       -9.25    -57.98
REMARK 500    CYS A 115       59.24   -164.84
REMARK 500    VAL A 129      -60.13    -91.08
REMARK 500    ASP A 317       52.82   -101.16
REMARK 500    SER A 414     -109.31   -127.07
REMARK 500    ASP A 433       34.13    -91.13
REMARK 500    PRO A 486       39.68    -72.15
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 498  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG A 158   O
REMARK 620 2 HOH A 544   O   122.4
REMARK 620 3 ASP A 167   OD2  75.3  74.2
REMARK 620 4 ASP A 167   OD1 115.3  78.4  50.7
REMARK 620 5 ASN A 100   OD1 158.3  71.9 126.2  82.1
REMARK 620 6 HOH A 565   O    74.6  59.3  92.4 131.2 104.4
REMARK 620 7 HIS A 201   O    81.1 121.8 156.3 143.6  77.3  83.4
REMARK 620 8 HOH A 510   O    75.8 150.9  91.3  73.0  98.7 148.2  80.8
REMARK 620 N                    1     2     3     4     5     6     7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AGL A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 497
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 498
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 499
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HMC A 503
DBREF  1CPU A    1   496  UNP    P04746   AMYP_HUMAN      16    511
SEQADV 1CPU PCA A    1  UNP  P04746    GLN    16 SEE REMARK 999
SEQRES   1 A  496  PCA TYR SER PRO ASN THR GLN GLN GLY ARG THR SER ILE
SEQRES   2 A  496  VAL HIS LEU PHE GLU TRP ARG TRP VAL ASP ILE ALA LEU
SEQRES   3 A  496  GLU CYS GLU ARG TYR LEU ALA PRO LYS GLY PHE GLY GLY
SEQRES   4 A  496  VAL GLN VAL SER PRO PRO ASN GLU ASN VAL ALA ILE TYR
SEQRES   5 A  496  ASN PRO PHE ARG PRO TRP TRP GLU ARG TYR GLN PRO VAL
SEQRES   6 A  496  SER TYR LYS LEU CYS THR ARG SER GLY ASN GLU ASP GLU
SEQRES   7 A  496  PHE ARG ASN MET VAL THR ARG CYS ASN ASN VAL GLY VAL
SEQRES   8 A  496  ARG ILE TYR VAL ASP ALA VAL ILE ASN HIS MET CYS GLY
SEQRES   9 A  496  ASN ALA VAL SER ALA GLY THR SER SER THR CYS GLY SER
SEQRES  10 A  496  TYR PHE ASN PRO GLY SER ARG ASP PHE PRO ALA VAL PRO
SEQRES  11 A  496  TYR SER GLY TRP ASP PHE ASN ASP GLY LYS CYS LYS THR
SEQRES  12 A  496  GLY SER GLY ASP ILE GLU ASN TYR ASN ASP ALA THR GLN
SEQRES  13 A  496  VAL ARG ASP CYS ARG LEU THR GLY LEU LEU ASP LEU ALA
SEQRES  14 A  496  LEU GLU LYS ASP TYR VAL ARG SER LYS ILE ALA GLU TYR
SEQRES  15 A  496  MET ASN HIS LEU ILE ASP ILE GLY VAL ALA GLY PHE ARG
SEQRES  16 A  496  LEU ASP ALA SER LYS HIS MET TRP PRO GLY ASP ILE LYS
SEQRES  17 A  496  ALA ILE LEU ASP LYS LEU HIS ASN LEU ASN SER ASN TRP
SEQRES  18 A  496  PHE PRO ALA GLY SER LYS PRO PHE ILE TYR GLN GLU VAL
SEQRES  19 A  496  ILE ASP LEU GLY GLY GLU PRO ILE LYS SER SER ASP TYR
SEQRES  20 A  496  PHE GLY ASN GLY ARG VAL THR GLU PHE LYS TYR GLY ALA
SEQRES  21 A  496  LYS LEU GLY THR VAL ILE ARG LYS TRP ASN GLY GLU LYS
SEQRES  22 A  496  MET SER TYR LEU LYS ASN TRP GLY GLU GLY TRP GLY PHE
SEQRES  23 A  496  VAL PRO SER ASP ARG ALA LEU VAL PHE VAL ASP ASN HIS
SEQRES  24 A  496  ASP ASN GLN ARG GLY HIS GLY ALA GLY GLY ALA SER ILE
SEQRES  25 A  496  LEU THR PHE TRP ASP ALA ARG LEU TYR LYS MET ALA VAL
SEQRES  26 A  496  GLY PHE MET LEU ALA HIS PRO TYR GLY PHE THR ARG VAL
SEQRES  27 A  496  MET SER SER TYR ARG TRP PRO ARG GLN PHE GLN ASN GLY
SEQRES  28 A  496  ASN ASP VAL ASN ASP TRP VAL GLY PRO PRO ASN ASN ASN
SEQRES  29 A  496  GLY VAL ILE LYS GLU VAL THR ILE ASN PRO ASP THR THR
SEQRES  30 A  496  CYS GLY ASN ASP TRP VAL CYS GLU HIS ARG TRP ARG GLN
SEQRES  31 A  496  ILE ARG ASN MET VAL ILE PHE ARG ASN VAL VAL ASP GLY
SEQRES  32 A  496  GLN PRO PHE THR ASN TRP TYR ASP ASN GLY SER ASN GLN
SEQRES  33 A  496  VAL ALA PHE GLY ARG GLY ASN ARG GLY PHE ILE VAL PHE
SEQRES  34 A  496  ASN ASN ASP ASP TRP SER PHE SER LEU THR LEU GLN THR
SEQRES  35 A  496  GLY LEU PRO ALA GLY THR TYR CYS ASP VAL ILE SER GLY
SEQRES  36 A  496  ASP LYS ILE ASN GLY ASN CYS THR GLY ILE LYS ILE TYR
SEQRES  37 A  496  VAL SER ASP ASP GLY LYS ALA HIS PHE SER ILE SER ASN
SEQRES  38 A  496  SER ALA GLU ASP PRO PHE ILE ALA ILE HIS ALA GLU SER
SEQRES  39 A  496  LYS LEU
MODRES 1CPU ASN A  461  ASN  GLYCOSYLATION SITE
MODRES 1CPU PCA A    1  GLU  PYROGLUTAMIC ACID
HET    PCA  A   1       7
HET    GLC  A 501      12
HET    AGL  A 502      10
HET    GLC  A 504      11
HET    GLC  A 505      11
HET    NAG  A 497      14
HET     CA  A 498       1
HET     CL  A 499       1
HET    HMC  A 503      11
HETNAM     PCA PYROGLUTAMIC ACID
HETNAM     GLC ALPHA-D-GLUCOSE
HETNAM     AGL 4,6-DIDEOXY-4-AMINO-ALPHA-D-GLUCOSE
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM      CA CALCIUM ION
HETNAM      CL CHLORIDE ION
HETNAM     HMC 5-HYDROXYMETHYL-CHONDURITOL
FORMUL   1  PCA    C5 H7 N O3
FORMUL   2  GLC    3(C6 H12 O6)
FORMUL   2  AGL    C6 H13 N O4
FORMUL   4  NAG    C8 H15 N O6
FORMUL   5   CA    CA 2+
FORMUL   6   CL    CL 1-
FORMUL   7  HMC    C7 H12 O5
FORMUL   8  HOH   *261(H2 O)
HELIX    1   1 TRP A   21  ARG A   30  1                                  10
HELIX    2   2 TRP A   58  TYR A   62  5                                   5
HELIX    3   3 GLU A   76  VAL A   89  1                                  14
HELIX    4   4 GLY A  133  ASP A  135  5                                   3
HELIX    5   5 ALA A  154  ASP A  159  1                                   6
HELIX    6   6 LEU A  162  GLY A  164  5                                   3
HELIX    7   7 ASP A  173  ILE A  189  1                                  17
HELIX    8   8 SER A  199  HIS A  201  5                                   3
HELIX    9   9 PRO A  204  LYS A  213  1                                  10
HELIX   10  10 SER A  244  TYR A  247  5                                   4
HELIX   11  11 PHE A  256  ILE A  266  1                                  11
HELIX   12  12 TRP A  269  GLY A  271  5                                   3
HELIX   13  13 MET A  274  ASN A  279  5                                   6
HELIX   14  14 GLU A  282  TRP A  284  5                                   3
HELIX   15  15 SER A  289  ARG A  291  5                                   3
HELIX   16  16 ASN A  301  ARG A  303  5                                   3
HELIX   17  17 GLY A  309  SER A  311  5                                   3
HELIX   18  18 PHE A  315  ALA A  330  5                                  16
HELIX   19  19 GLU A  385  ARG A  387  5                                   3
HELIX   20  20 ARG A  389  VAL A  400  1                                  12
HELIX   21  21 ALA A  492  SER A  494  5                                   3
SHEET    1   A 6 THR A 336  SER A 340  0
SHEET    2   A 6 SER A  12  LEU A  16  1  N  ILE A  13   O  THR A 336
SHEET    3   A 6 GLY A  39  VAL A  42  1  N  GLY A  39   O  VAL A  14
SHEET    4   A 6 ARG A  92  ALA A  97  1  N  ARG A  92   O  VAL A  40
SHEET    5   A 6 GLY A 193  LEU A 196  1  N  GLY A 193   O  VAL A  95
SHEET    6   A 6 PHE A 229  GLN A 232  1  N  PHE A 229   O  PHE A 194
SHEET    1   B 3 GLN A 416  ARG A 421  0
SHEET    2   B 3 GLY A 425  ASN A 430 -1  N  PHE A 429   O  VAL A 417
SHEET    3   B 3 PHE A 487  HIS A 491 -1  N  ILE A 490   O  PHE A 426
SHEET    1   C 2 PHE A 436  GLN A 441  0
SHEET    2   C 2 LYS A 474  ILE A 479 -1  N  ILE A 479   O  PHE A 436
SHEET    1   D 2 GLY A 447  CYS A 450  0
SHEET    2   D 2 LYS A 466  VAL A 469 -1  N  VAL A 469   O  GLY A 447
SSBOND   1 CYS A   28    CYS A   86                          1555   1555  2.03
SSBOND   2 CYS A   70    CYS A  115                          1555   1555  2.03
SSBOND   3 CYS A  141    CYS A  160                          1555   1555  2.03
SSBOND   4 CYS A  378    CYS A  384                          1555   1555  2.03
SSBOND   5 CYS A  450    CYS A  462                          1555   1555  2.03
LINK         O4  GLC A 501                 C1  AGL A 502     1555   1555  1.41
LINK         O4  GLC A 504                 C1  GLC A 505     1555   1555  1.44
LINK         O4  HMC A 503                 C1  GLC A 504     1555   1555  1.41
LINK         C1  HMC A 503                 N4  AGL A 502     1555   1555  1.52
LINK         ND2 ASN A 461                 C1  NAG A 497     1555   1555  1.45
LINK         C   PCA A   1                 N   TYR A   2     1555   1555  1.35
LINK        CA    CA A 498                 O   ARG A 158     1555   1555  2.46
LINK        CA    CA A 498                 O   HOH A 544     1555   1555  2.74
LINK        CA    CA A 498                 OD2 ASP A 167     1555   1555  2.56
LINK        CA    CA A 498                 OD1 ASP A 167     1555   1555  2.58
LINK        CA    CA A 498                 OD1 ASN A 100     1555   1555  2.48
LINK        CA    CA A 498                 O   HOH A 565     1555   1555  2.79
LINK        CA    CA A 498                 O   HIS A 201     1555   1555  2.51
LINK        CA    CA A 498                 O   HOH A 510     1555   1555  2.63
CISPEP   1 ASN A   53    PRO A   54          0        -0.07
CISPEP   2 VAL A  129    PRO A  130          0        -0.26
SITE     1 AC1  5 TYR A 151  LYS A 200  ILE A 235  GLU A 240
SITE     2 AC1  5 AGL A 502
SITE     1 AC2  8 ALA A 198  HIS A 201  GLU A 233  ASP A 300
SITE     2 AC2  8 HIS A 305  GLC A 501  HMC A 503  GLC A 504
SITE     1 AC3  8 TRP A  58  TRP A  59  TYR A  62  GLN A  63
SITE     2 AC3  8 HIS A 305  AGL A 502  HMC A 503  GLC A 505
SITE     1 AC4  7 GLN A  63  GLY A 104  THR A 163  ASP A 433
SITE     2 AC4  7 GLC A 504  HOH A 568  HOH A 711
SITE     1 AC5  6 LYS A 140  ARG A 176  TRP A 203  ASP A 206
SITE     2 AC5  6 ASN A 459  ASN A 461
SITE     1 AC6  7 ASN A 100  ARG A 158  ASP A 167  HIS A 201
SITE     2 AC6  7 HOH A 510  HOH A 544  HOH A 565
SITE     1 AC7  3 ARG A 195  ASN A 298  ARG A 337
SITE     1 AC8 11 TRP A  58  TYR A  62  HIS A 101  LEU A 162
SITE     2 AC8 11 ARG A 195  ASP A 197  GLU A 233  HIS A 299
SITE     3 AC8 11 ASP A 300  AGL A 502  GLC A 504
CRYST1   52.910   68.900  131.770  90.00  90.00  90.00 P 21 21 21    4
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      0.018900  0.000000  0.000000        0.00000
SCALE2      0.000000  0.014514  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007589        0.00000
      
PROCHECK
Go to PROCHECK summary
 References