spacer
spacer

PDBsum entry 1kgx

Go to PDB code: 
Top Page protein ligands metals links
Hydrolase PDB id
1kgx
Jmol
Contents
Protein chain
496 a.a. *
Ligands
NAG
Metals
_CA
Waters ×261
* Residue conservation analysis
HEADER    HYDROLASE                               28-NOV-01   1KGX
TITLE     THREE DIMENSIONAL STRUCTURE ANALYSIS OF THE R195Q VARIANT OF HUMAN
TITLE    2 PANCREATIC ALPHA AMYLASE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ALPHA-AMYLASE, PANCREATIC;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: 1,4-ALPHA-D-GLUCAN GLUCANOHYDROLASE, PANCREATIC ALPHA-
COMPND   5 AMYLASE, PA;
COMPND   6 EC: 3.2.1.1;
COMPND   7 ENGINEERED: YES;
COMPND   8 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 4922
KEYWDS    ALPHA-AMYLASE, CHLORIDE BINDING, PICHIA PASTORIS, MUTAGENESIS,
KEYWDS   2 CATALYSIS, PANCREATIC, ENZYME, HUMAN, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.NUMAO,R.MAURUS,G.SIDHU,Y.WANG,C.M.OVERALL,G.D.BRAYER,S.G.WITHERS
REVDAT   3   13-JUL-11 1KGX    1       VERSN
REVDAT   2   24-FEB-09 1KGX    1       VERSN
REVDAT   1   16-JAN-02 1KGX    0
JRNL        AUTH   S.NUMAO,R.MAURUS,G.SIDHU,Y.WANG,C.M.OVERALL,G.D.BRAYER,
JRNL        AUTH 2 S.G.WITHERS
JRNL        TITL   PROBING THE ROLE OF THE CHLORIDE ION IN THE MECHANISM OF
JRNL        TITL 2 HUMAN PANCREATIC ALPHA-AMYLASE.
JRNL        REF    BIOCHEMISTRY                  V.  41   215 2002
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   11772019
JRNL        DOI    10.1021/BI0115636
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) : 10.00
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)   (%) : 88.0
REMARK   3   NUMBER OF REFLECTIONS             : 31572
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) : 0.197
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            : 3944
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 15
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) : 22.60
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) : 0.22
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) : NULL
REMARK   3   BOND ANGLES            (DEGREES) : NULL
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 1KGX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-DEC-01.
REMARK 100 THE RCSB ID CODE IS RCSB014946.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 09-JUL-99
REMARK 200  TEMPERATURE           (KELVIN) : 298
REMARK 200  PH                             : NULL
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 RU300
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : OSMIC MIRRORS
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IIC
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32187
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.0
REMARK 200  DATA REDUNDANCY                : 3.300
REMARK 200  R MERGE                    (I) : 0.06500
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 16.4000
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) : 2.07
REMARK 200  COMPLETENESS FOR SHELL     (%) : 73.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.60
REMARK 200  R MERGE FOR SHELL          (I) : 0.09300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 10.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: PDB ENTRY 1BSI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 43.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, HANGING DROP,
REMARK 280  TEMPERATURE 298K
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       26.54050
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       65.91350
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.51350
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       65.91350
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.54050
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       34.51350
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 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      -55.37   -143.29
REMARK 500    MET A 102     -146.38   -111.45
REMARK 500    ASN A 137       50.92   -102.75
REMARK 500    ASP A 317       50.65   -105.24
REMARK 500    ALA A 318      -62.00    -29.15
REMARK 500    GLN A 349      -75.81    -88.20
REMARK 500    ASN A 350       55.04   -112.56
REMARK 500    THR A 376       -5.04     80.02
REMARK 500    ASP A 381        2.92     84.70
REMARK 500    SER A 414     -110.61   -131.23
REMARK 500    ASN A 481        0.28    -63.72
REMARK 500    PRO A 486       25.77    -65.26
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 HOH A 502   O
REMARK 620 2 ASP A 167   OD2  86.1
REMARK 620 3 HOH A 510   O   146.3 101.2
REMARK 620 4 ASN A 100   OD1  99.1 129.9 100.9
REMARK 620 5 HIS A 201   O    82.0 155.8  78.3  73.1
REMARK 620 6 ASP A 167   OD1  72.0  50.5 137.0  83.6 141.7
REMARK 620 7 ARG A 158   O    78.7  75.5  71.6 154.5  81.5 118.9
REMARK 620 N                    1     2     3     4     5     6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 497
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 498
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BS1   RELATED DB: PDB
REMARK 900 HUMAN PANCREATIC ALPHA-AMYLASE FROM PICHIA PASTORIS,
REMARK 900 GLYCOSYLATED PROTEIN
REMARK 900 RELATED ID: 1KB3   RELATED DB: PDB
REMARK 900 THREE DIMENSIONAL STRUCTURE ANALYSIS OF THE R195A VARIANT
REMARK 900 OF HUMAN PANCREATIC ALPHA AMYLASE
REMARK 900 RELATED ID: 1KGU   RELATED DB: PDB
REMARK 900 THREE DIMENSIONAL STRUCTURE ANALYSIS OF THE R337A VARIANT
REMARK 900 OF HUMAN PANCREATIC ALPHA-AMYLASE
REMARK 900 RELATED ID: 1KGW   RELATED DB: PDB
REMARK 900 THREE DIMENSIONAL STRUCTURE ANALYSIS OF THE R337Q VARIANT
REMARK 900 OF HUMAN PANCREATIC ALPHA-AMYLASE
DBREF  1KGX A    1   496  UNP    P04746   AMYP_HUMAN      16    511
SEQADV 1KGX PCA A    1  UNP  P04746    GLN    16 MODIFIED RESIDUE
SEQADV 1KGX GLN A  195  UNP  P04746    ARG   210 ENGINEERED
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 GLN
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 1KGX ASN A  461  ASN  GLYCOSYLATION SITE
MODRES 1KGX PCA A    1  GLU  PYROGLUTAMIC ACID
HET    PCA  A   1       8
HET    NAG  A 497      14
HET     CA  A 498       1
HETNAM     PCA PYROGLUTAMIC ACID
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM      CA CALCIUM ION
FORMUL   1  PCA    C5 H7 N O3
FORMUL   2  NAG    C8 H15 N O6
FORMUL   3   CA    CA 2+
FORMUL   4  HOH   *261(H2 O)
HELIX    1   1 ARG A   20  TYR A   31  1                                  12
HELIX    2   2 PRO A   57  GLN A   63  5                                   7
HELIX    3   3 ASN A   75  ASN A   88  1                                  14
HELIX    4   4 ASN A  120  ARG A  124  5                                   5
HELIX    5   5 SER A  132  PHE A  136  5                                   5
HELIX    6   6 ASP A  153  CYS A  160  1                                   8
HELIX    7   7 LYS A  172  GLY A  190  1                                  19
HELIX    8   8 ALA A  198  MET A  202  5                                   5
HELIX    9   9 TRP A  203  ASP A  212  1                                  10
HELIX   10  10 LYS A  243  PHE A  248  5                                   6
HELIX   11  11 GLU A  255  ARG A  267  1                                  13
HELIX   12  12 LYS A  268  GLU A  272  5                                   5
HELIX   13  13 LYS A  273  TRP A  280  5                                   8
HELIX   14  14 GLY A  281  GLY A  285  5                                   5
HELIX   15  15 PRO A  288  ASP A  290  5                                   3
HELIX   16  16 ASP A  300  GLY A  304  5                                   5
HELIX   17  17 THR A  314  TRP A  316  5                                   3
HELIX   18  18 ASP A  317  HIS A  331  1                                  15
HELIX   19  19 CYS A  384  ARG A  387  5                                   4
HELIX   20  20 TRP A  388  VAL A  401  1                                  14
HELIX   21  21 GLU A  493  LYS A  495  5                                   3
SHEET    1   A 9 SER A  12  LEU A  16  0
SHEET    2   A 9 GLY A  39  VAL A  42  1  O  GLY A  39   N  VAL A  14
SHEET    3   A 9 ARG A  92  ALA A  97  1  O  ARG A  92   N  VAL A  40
SHEET    4   A 9 GLY A 193  LEU A 196  1  O  GLY A 193   N  VAL A  95
SHEET    5   A 9 PHE A 229  GLN A 232  1  O  PHE A 229   N  PHE A 194
SHEET    6   A 9 ARG A 252  THR A 254  1  O  ARG A 252   N  GLN A 232
SHEET    7   A 9 ALA A 292  VAL A 294  1  N  LEU A 293   O  VAL A 253
SHEET    8   A 9 PHE A 335  SER A 340  1  O  PHE A 335   N  VAL A 294
SHEET    9   A 9 SER A  12  LEU A  16  1  O  ILE A  13   N  VAL A 338
SHEET    1   B 2 HIS A 101  GLY A 104  0
SHEET    2   B 2 LEU A 165  ASP A 167 -1  N  LEU A 166   O  CYS A 103
SHEET    1   C 2 ASN A 362  ASN A 363  0
SHEET    2   C 2 VAL A 366  ILE A 367 -1  O  VAL A 366   N  ASN A 363
SHEET    1   D 4 PHE A 406  ASP A 411  0
SHEET    2   D 4 GLN A 416  ARG A 421 -1  O  ALA A 418   N  TYR A 410
SHEET    3   D 4 GLY A 425  ASN A 430 -1  O  GLY A 425   N  ARG A 421
SHEET    4   D 4 PHE A 487  HIS A 491 -1  O  ILE A 488   N  VAL A 428
SHEET    1   E 2 PHE A 436  GLN A 441  0
SHEET    2   E 2 LYS A 474  ILE A 479 -1  O  ALA A 475   N  LEU A 440
SHEET    1   F 2 GLY A 447  CYS A 450  0
SHEET    2   F 2 LYS A 466  VAL A 469 -1  O  ILE A 467   N  TYR A 449
SSBOND   1 CYS A   28    CYS A   86                          1555   1555  2.03
SSBOND   2 CYS A   70    CYS A  115                          1555   1555  2.05
SSBOND   3 CYS A  141    CYS A  160                          1555   1555  2.03
SSBOND   4 CYS A  378    CYS A  384                          1555   1555  2.02
SSBOND   5 CYS A  450    CYS A  462                          1555   1555  2.02
LINK         ND2 ASN A 461                 C1  NAG A 497     1555   1555  1.46
LINK         C   PCA A   1                 N   TYR A   2     1555   1555  1.33
LINK        CA    CA A 498                 O   HOH A 502     1555   1555  2.58
LINK        CA    CA A 498                 OD2 ASP A 167     1555   1555  2.55
LINK        CA    CA A 498                 O   HOH A 510     1555   1555  2.74
LINK        CA    CA A 498                 OD1 ASN A 100     1555   1555  2.59
LINK        CA    CA A 498                 O   HIS A 201     1555   1555  2.53
LINK        CA    CA A 498                 OD1 ASP A 167     1555   1555  2.61
LINK        CA    CA A 498                 O   ARG A 158     1555   1555  2.45
CISPEP   1 ASN A   53    PRO A   54          0         0.08
CISPEP   2 VAL A  129    PRO A  130          0        -0.20
SITE     1 AC1  9 LYS A 140  GLU A 171  ASP A 206  ASN A 459
SITE     2 AC1  9 GLY A 460  ASN A 461  HOH A 560  HOH A 595
SITE     3 AC1  9 HOH A 721
SITE     1 AC2  6 ASN A 100  ARG A 158  ASP A 167  HIS A 201
SITE     2 AC2  6 HOH A 502  HOH A 510
CRYST1   53.081   69.027  131.827  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      0.018839  0.000000  0.000000        0.00000
SCALE2      0.000000  0.014487  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007586        0.00000
      
PROCHECK
Go to PROCHECK summary
 References