spacer
spacer

PDBsum entry 1jfh

Go to PDB code: 
Top Page protein ligands metals links
Hydrolase PDB id
1jfh
Jmol
Contents
Protein chain
496 a.a.
Ligands
MA2-MA3
GLC-MA1 ×2
Metals
_CA
_CL
_HG
Waters ×383
HEADER    HYDROLASE                               19-SEP-97   1JFH
TITLE     STRUCTURE OF A PANCREATIC ALPHA-AMYLASE BOUND TO A
TITLE    2 SUBSTRATE ANALOGUE AT 2.03 ANGSTROM RESOLUTION
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ALPHA-AMYLASE;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: PPA;
COMPND   5 EC: 3.2.1.1;
COMPND   6 OTHER_DETAILS: COMPLEXED WITH METHYL 4,4'-DITHIO-ALPHA-
COMPND   7 MALTOTRIOSIDE
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE   3 ORGANISM_COMMON: PIG;
SOURCE   4 ORGANISM_TAXID: 9823;
SOURCE   5 ORGAN: PANCREAS
KEYWDS    HYDROLASE, O-GLYCOSYL, ALPHA-AMYLASE, METHYL 4,4'-DITHIO-
KEYWDS   2 ALPHA-MALTOTRIOSIDE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    M.QIAN,F.PAYAN
REVDAT   3   24-FEB-09 1JFH    1       VERSN
REVDAT   2   13-JAN-99 1JFH    1       COMPND REMARK TITLE  SEQADV
REVDAT   2 2                   1       HEADER MODRES SOURCE KEYWDS
REVDAT   1   02-DEC-98 1JFH    0
JRNL        AUTH   M.QIAN,S.SPINELLI,H.DRIGUEZ,F.PAYAN
JRNL        TITL   STRUCTURE OF A PANCREATIC ALPHA-AMYLASE BOUND TO A
JRNL        TITL 2 SUBSTRATE ANALOGUE AT 2.03 A RESOLUTION.
JRNL        REF    PROTEIN SCI.                  V.   6  2285 1997
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   9385631
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   C.GILLES,J.P.ASTIER,G.MARCHIS-MOUREN,C.CAMBILLAU,
REMARK   1  AUTH 2 F.PAYAN
REMARK   1  TITL   CRYSTAL STRUCTURE OF PIG PANCREATIC ALPHA-AMYLASE
REMARK   1  TITL 2 ISOENZYME II, IN COMPLEX WITH THE CARBOHYDRATE
REMARK   1  TITL 3 INHIBITOR ACARBOSE
REMARK   1  REF    EUR.J.BIOCHEM.                V. 238   561 1996
REMARK   1  REFN                   ISSN 0014-2956
REMARK   1 REFERENCE 2
REMARK   1  AUTH   M.QIAN,R.HASER,F.PAYAN
REMARK   1  TITL   CARBOHYDRATE BINDING SITES IN A PANCREATIC
REMARK   1  TITL 2 ALPHA-AMYLASE-SUBSTRATE COMPLEX, DERIVED FROM
REMARK   1  TITL 3 X-RAY STRUCTURE ANALYSIS AT 2.1 A RESOLUTION
REMARK   1  REF    PROTEIN SCI.                  V.   4   747 1995
REMARK   1  REFN                   ISSN 0961-8368
REMARK   1 REFERENCE 3
REMARK   1  AUTH   M.QIAN,R.HASER,G.BUISSON,E.DUEE,F.PAYAN
REMARK   1  TITL   THE ACTIVE CENTER OF A MAMMALIAN ALPHA-AMYLASE.
REMARK   1  TITL 2 STRUCTURE OF THE COMPLEX OF A PANCREATIC
REMARK   1  TITL 3 ALPHA-AMYLASE WITH A CARBOHYDRATE INHIBITOR
REMARK   1  TITL 4 REFINED TO 2.2-A RESOLUTION
REMARK   1  REF    BIOCHEMISTRY                  V.  33  6284 1994
REMARK   1  REFN                   ISSN 0006-2960
REMARK   1 REFERENCE 4
REMARK   1  AUTH   M.QIAN,R.HASER,F.PAYAN
REMARK   1  TITL   STRUCTURE AND MOLECULAR MODEL REFINEMENT OF PIG
REMARK   1  TITL 2 PANCREATIC ALPHA-AMYLASE AT 2.1 A RESOLUTION
REMARK   1  REF    J.MOL.BIOL.                   V. 231   785 1993
REMARK   1  REFN                   ISSN 0022-2836
REMARK   2
REMARK   2 RESOLUTION.    2.03 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.843
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.03
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.00
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)   (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 33421
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) : 0.160
REMARK   3   FREE R VALUE                     : 0.185
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            : 3908
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 71
REMARK   3   SOLVENT ATOMS            : 384
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) : 0.20
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) : 0.010
REMARK   3   BOND ANGLES            (DEGREES) : 1.40
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 1JFH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
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                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 180 MM PLATE
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33718
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4
REMARK 200  DATA REDUNDANCY                : 9.500
REMARK 200  R MERGE                    (I) : 0.05700
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR 3.843
REMARK 200 STARTING MODEL: NULL
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): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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       28.15000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       51.70000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.90000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       51.70000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.15000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       43.90000
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      -61.53   -140.97
REMARK 500    MET A 102     -140.66   -113.27
REMARK 500    ASP A 317       58.35   -115.32
REMARK 500    SER A 414     -103.40   -133.61
REMARK 500    PRO A 486       40.74    -75.96
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 853        DISTANCE =  5.16 ANGSTROMS
REMARK 525    HOH A 888        DISTANCE =  6.61 ANGSTROMS
REMARK 525    HOH A 894        DISTANCE =  8.18 ANGSTROMS
REMARK 525    HOH A 897        DISTANCE =  7.25 ANGSTROMS
REMARK 525    HOH A 905        DISTANCE =  6.43 ANGSTROMS
REMARK 525    HOH A 920        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 931        DISTANCE =  5.22 ANGSTROMS
REMARK 525    HOH A 937        DISTANCE =  5.58 ANGSTROMS
REMARK 525    HOH A 947        DISTANCE =  5.47 ANGSTROMS
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 500  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 201   O
REMARK 620 2 HOH A 520   O   123.0
REMARK 620 3 ASN A 100   OD1  72.8  69.9
REMARK 620 4 HOH A 539   O    83.8  63.2 100.7
REMARK 620 5 ASP A 167   OD1 138.7  78.2  85.1 135.4
REMARK 620 6 HOH A 527   O    81.4 146.0 100.0 149.6  68.4
REMARK 620 7 ARG A 158   O    82.6 123.3 155.0  72.2 117.1  79.6
REMARK 620 8 ASP A 167   OD2 159.6  73.4 127.2  95.0  50.8  89.9  77.7
REMARK 620 N                    1     2     3     4     5     6     7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              HG A 499  HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 103   SG
REMARK 620 2 CYS A 119   SG  168.2
REMARK 620 N                    1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MA2 A 991
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MA3 A 992
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 993
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MA1 A 994
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 995
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MA1 A 996
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 498
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 499
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 500
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PPI   RELATED DB: PDB
REMARK 900 STRUCTURE OBTAINED AT ROOM TEMPERATURE WITH DIFFERENT
REMARK 900 LIGANDS
DBREF  1JFH A    2   496  UNP    P00690   AMYP_PIG         2    496
SEQADV 1JFH VAL A   49  UNP  P00690    ILE    49 CONFLICT
SEQADV 1JFH LYS A  243  UNP  P00690    GLN   243 CONFLICT
SEQADV 1JFH SER A  310  UNP  P00690    ALA   310 CONFLICT
SEQADV 1JFH ILE A  323  UNP  P00690    VAL   323 CONFLICT
SEQRES   1 A  496  PCA TYR ALA PRO GLN THR GLN SER 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 GLY PRO LYS GLY PHE GLY GLY
SEQRES   4 A  496  VAL GLN VAL SER PRO PRO ASN GLU ASN VAL VAL VAL THR
SEQRES   5 A  496  ASN PRO SER 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 ASN GLU
SEQRES   7 A  496  PHE ARG ASP 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  SER GLY ALA ALA ALA GLY THR GLY THR THR CYS GLY SER
SEQRES  10 A  496  TYR CYS ASN PRO GLY SER ARG GLU PHE PRO ALA VAL PRO
SEQRES  11 A  496  TYR SER ALA TRP ASP PHE ASN ASP GLY LYS CYS LYS THR
SEQRES  12 A  496  ALA SER GLY GLY ILE GLU SER TYR ASN ASP PRO TYR GLN
SEQRES  13 A  496  VAL ARG ASP CYS GLN LEU VAL GLY LEU LEU ASP LEU ALA
SEQRES  14 A  496  LEU GLU LYS ASP TYR VAL ARG SER MET ILE ALA ASP TYR
SEQRES  15 A  496  LEU ASN LYS LEU ILE ASP ILE GLY VAL ALA GLY PHE ARG
SEQRES  16 A  496  ILE ASP ALA SER LYS HIS MET TRP PRO GLY ASP ILE LYS
SEQRES  17 A  496  ALA VAL LEU ASP LYS LEU HIS ASN LEU ASN THR ASN TRP
SEQRES  18 A  496  PHE PRO ALA GLY SER ARG PRO PHE ILE PHE GLN GLU VAL
SEQRES  19 A  496  ILE ASP LEU GLY GLY GLU ALA ILE LYS SER SER GLU 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 VAL ARG LYS TRP SER GLY GLU LYS
SEQRES  22 A  496  MET SER TYR LEU LYS ASN TRP GLY GLU GLY TRP GLY PHE
SEQRES  23 A  496  MET 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 SER SER ILE
SEQRES  25 A  496  LEU THR PHE TRP ASP ALA ARG LEU TYR LYS ILE 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 ALA ARG ASN PHE VAL ASN GLY
SEQRES  28 A  496  GLU ASP VAL ASN ASP TRP ILE GLY PRO PRO ASN ASN ASN
SEQRES  29 A  496  GLY VAL ILE LYS GLU VAL THR ILE ASN ALA ASP THR THR
SEQRES  30 A  496  CYS GLY ASN ASP TRP VAL CYS GLU HIS ARG TRP ARG GLU
SEQRES  31 A  496  ILE ARG ASN MET VAL TRP PHE ARG ASN VAL VAL ASP GLY
SEQRES  32 A  496  GLU PRO PHE ALA ASN TRP TRP 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 GLN LEU SER SER THR LEU GLN THR
SEQRES  35 A  496  GLY LEU PRO GLY GLY THR TYR CYS ASP VAL ILE SER GLY
SEQRES  36 A  496  ASP LYS VAL GLY ASN SER CYS THR GLY ILE LYS VAL TYR
SEQRES  37 A  496  VAL SER SER ASP GLY THR ALA GLN 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 1JFH PCA A    1  GLU  PYROGLUTAMIC ACID
HET    PCA  A   1       8
HET    MA2  A 991      12
HET    MA3  A 992      13
HET    GLC  A 993      11
HET    MA1  A 994      12
HET    GLC  A 995      11
HET    MA1  A 996      12
HET     CL  A 498       1
HET     HG  A 499       1
HET     CA  A 500       1
HETNAM     PCA PYROGLUTAMIC ACID
HETNAM     MA2 4-S-METHYL-4-THIO-ALPHA-D-GLUCOPYRANOSE
HETNAM     MA3 O1-METHYL-4-DEOXY-4-THIO-ALPHA-D-GLUCOSE
HETNAM     GLC ALPHA-D-GLUCOSE
HETNAM     MA1 1,4-DITHIO-ALPHA-D-GLUCOPYRANOSE
HETNAM      CL CHLORIDE ION
HETNAM      HG MERCURY (II) ION
HETNAM      CA CALCIUM ION
FORMUL   1  PCA    C5 H7 N O3
FORMUL   2  MA2    C7 H14 O5 S
FORMUL   3  MA3    C7 H14 O5 S
FORMUL   4  GLC    2(C6 H12 O6)
FORMUL   5  MA1    2(C6 H12 O4 S2)
FORMUL   8   CL    CL 1-
FORMUL   9   HG    HG 2+
FORMUL  10   CA    CA 2+
FORMUL  11  HOH   *383(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 PRO A  121  SER A  123  5                                   3
HELIX    5   5 ALA A  133  ASP A  135  5                                   3
HELIX    6   6 PRO A  154  ASP A  159  1                                   6
HELIX    7   7 LEU A  162  GLY A  164  5                                   3
HELIX    8   8 ASP A  173  ILE A  189  1                                  17
HELIX    9   9 SER A  199  HIS A  201  5                                   3
HELIX   10  10 PRO A  204  LYS A  213  1                                  10
HELIX   11  11 SER A  244  TYR A  247  5                                   4
HELIX   12  12 PHE A  256  VAL A  266  1                                  11
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 PHE A  315  ALA A  330  5                                  16
HELIX   18  18 GLU A  385  ARG A  387  5                                   3
HELIX   19  19 ARG A  389  VAL A  400  1                                  12
HELIX   20  20 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  ILE 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 LEU A 436  GLN A 441  0
SHEET    2   C 2 THR A 474  ILE A 479 -1  N  ILE A 479   O  LEU 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         C   PCA A   1                 N   TYR A   2     1555   1555  1.33
LINK        CA    CA A 500                 O   HIS A 201     1555   1555  2.39
LINK         C1  MA2 A 991                 S4  MA3 A 992     1555   1555  1.82
LINK        HG    HG A 499                 SG  CYS A 103     1555   1555  2.31
LINK        HG    HG A 499                 SG  CYS A 119     1555   1555  2.40
LINK        CA    CA A 500                 O   HOH A 520     1555   1555  2.64
LINK        CA    CA A 500                 OD1 ASN A 100     1555   1555  2.40
LINK        CA    CA A 500                 O   HOH A 539     1555   1555  2.54
LINK        CA    CA A 500                 OD1 ASP A 167     1555   1555  2.57
LINK        CA    CA A 500                 O   HOH A 527     1555   1555  2.61
LINK        CA    CA A 500                 O   ARG A 158     1555   1555  2.41
LINK        CA    CA A 500                 OD2 ASP A 167     1555   1555  2.54
LINK         C1  GLC A 993                 S4  MA1 A 994     1555   1555  1.82
LINK         C1  GLC A 995                 S4  MA1 A 996     1555   1555  1.84
CISPEP   1 ASN A   53    PRO A   54          0        -0.05
CISPEP   2 VAL A  129    PRO A  130          0        -0.29
SITE     1 AC1  5 TRP A  59  GLN A  63  VAL A 163  HOH A 666
SITE     2 AC1  5 MA3 A 992
SITE     1 AC2  7 TRP A  59  GLN A  63  HIS A 305  HOH A 566
SITE     2 AC2  7 HOH A 970  MA2 A 991  GLC A 993
SITE     1 AC3 11 TYR A 151  LEU A 162  HIS A 201  GLU A 233
SITE     2 AC3 11 HOH A 748  HOH A 764  HOH A 950  HOH A 970
SITE     3 AC3 11 HOH A 986  MA3 A 992  MA1 A 994
SITE     1 AC4  5 LYS A 200  GLU A 240  GLY A 306  HOH A 964
SITE     2 AC4  5 GLC A 993
SITE     1 AC5  9 ASP A 375  THR A 376  ARG A 387  TRP A 388
SITE     2 AC5  9 ARG A 389  GLU A 390  HOH A 906  HOH A 925
SITE     3 AC5  9 MA1 A 996
SITE     1 AC6 10 TRP A 134  ALA A 318  LYS A 322  TRP A 388
SITE     2 AC6 10 GLU A 390  HOH A 661  HOH A 875  HOH A 885
SITE     3 AC6 10 HOH A 931  GLC A 995
SITE     1 AC7  3 ARG A 195  ASN A 298  ARG A 337
SITE     1 AC8  4 CYS A 103  CYS A 119  PRO A 121  PHE A 126
SITE     1 AC9  7 ASN A 100  ARG A 158  ASP A 167  HIS A 201
SITE     2 AC9  7 HOH A 520  HOH A 527  HOH A 539
CRYST1   56.300   87.800  103.400  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      0.017762  0.000000  0.000000        0.00000
SCALE2      0.000000  0.011390  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009671        0.00000
      
PROCHECK
Go to PROCHECK summary
 References