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PDBsum entry 1hdi

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Phosphotransferase PDB id
1hdi
Jmol
Contents
Protein chain
413 a.a. *
Ligands
AMP
3PG
Metals
_MG
Waters ×208
* Residue conservation analysis
HEADER    PHOSPHOTRANSFERASE                      16-NOV-00   1HDI
TITLE     PIG MUSCLE 3-PHOSPHOGLYCERATE KINASE COMPLEXED WITH 3-PG
TITLE    2 AND MGADP.
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PHOSPHOGLYCERATE KINASE;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: PGK;
COMPND   5 EC: 2.7.2.3
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE   3 ORGANISM_COMMON: PIG;
SOURCE   4 ORGANISM_TAXID: 9823;
SOURCE   5 TISSUE: MUSCLE
KEYWDS    PHOSPHOTRANSFERASE, KINASE, PHOSPHOGLYCERATE, TERNARY
KEYWDS   2 COMPLEX, GLYCOLYSIS
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.N.SZILAGYI,M.GHOSH,E.GARMAN,M.VAS
REVDAT   2   24-FEB-09 1HDI    1       VERSN
REVDAT   1   26-FEB-01 1HDI    0
JRNL        AUTH   A.N.SZILAGYI,M.GHOSH,E.GARMAN,M.VAS
JRNL        TITL   A 1.8 A RESOLUTION STRUCTURE OF PIG MUSCLE
JRNL        TITL 2 3-PHOSPHOGLYCERATE KINASE WITH BOUND MGADP AND
JRNL        TITL 3 3-PHOSPHOGLYCERATE IN OPEN CONFORMATION: NEW
JRNL        TITL 4 INSIGHT INTO THE ROLE OF THE NUCLEOTIDE IN DOMAIN
JRNL        TITL 5 CLOSURE
JRNL        REF    J.MOL.BIOL.                   V. 306   499 2001
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   11178909
JRNL        DOI    10.1006/JMBI.2000.4294
REMARK   2
REMARK   2 RESOLUTION.    1.8  ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.8
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.8
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.0
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.5
REMARK   3   NUMBER OF REFLECTIONS             : 32755
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) : 0.207
REMARK   3   FREE R VALUE                     : 0.262
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0
REMARK   3   FREE R VALUE TEST SET COUNT      : 1662
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           : 10
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.8
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.86
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3086
REMARK   3   BIN R VALUE           (WORKING SET) : 0.237
REMARK   3   BIN FREE R VALUE                    : 0.299
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            : 3037
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 35
REMARK   3   SOLVENT ATOMS            : 208
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 21.8
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.5
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) : 0.011
REMARK   3   BOND ANGLES            (DEGREES) : 1.62
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.7
REMARK   3   IMPROPER ANGLES        (DEGREES) : 2.4
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED
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  PARAMETER FILE  2  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1HDI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-NOV-00.
REMARK 100 THE PDBE ID CODE IS EBI-5532.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 15-JUN-97
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 7.70
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SRS
REMARK 200  BEAMLINE                       : PX7.2
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.488
REMARK 200  MONOCHROMATOR                  : GE111 BENT AASYMMETRIC
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   : 34292
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800
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     (%) : 95.6
REMARK 200  DATA REDUNDANCY                : 2.400
REMARK 200  R MERGE                    (I) : 0.08100
REMARK 200  R SYM                      (I) : 0.08100
REMARK 200   FOR THE DATA SET  : 17.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.88
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.1
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30
REMARK 200  R MERGE FOR SHELL          (I) : 0.24400
REMARK 200  R SYM FOR SHELL            (I) : 0.24400
REMARK 200   FOR SHELL         : 3.000
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: THE STARTING MODEL WAS CHOSEN AS THE STRUCTURE
REMARK 200  OF THE MNADP BINARY COMPLEX OF PIG MUSCLE PGK CRYSTALLISED IN
REMARK 200  THE PRESENCE OF AMMONIUM SULPHATE (MAY ET AL., PERSONAL COMM.).
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS  (%): 41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.1
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS:  THE ENZYME WAS DIALYSED IN
REMARK 280  30 MM NAK-PHOSPHATE BUFFER, PH=8.0.  SINGLE CRYSTALS WERE
REMARK 280  GROWN AT 15C WITHIN A FEW WEEKS IN HANGING DROPS
REMARK 280  (10-15 ML EACH) INITIALLY CONTAINING 1.25 M NAK-PHOSPHATE
REMARK 280  (PH=8.0), 100 MM 3-PG, 25 MM MGCL2, 20 MM ADP, 10 MM
REMARK 280  DITHIOTHREITOL, 0.02% NAN3 AND 15 MG/ML PGK.
REMARK 280  RESERVOIR SOLUTIONS CONTAINED 2.4-2.75 M NAK-PHOSPHATE(PH=8.0).
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,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        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       52.60000
REMARK 290   SMTRY3   2  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 GENERATING THE BIOMOLECULE
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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: 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    ARG A  38   NE  -  CZ  -  NH2 ANGL. DEV. =   3.4 DEGREES
REMARK 500    MET A  71   CG  -  SD  -  CE  ANGL. DEV. =   9.7 DEGREES
REMARK 500    HIS A 169   CB  -  CG  -  ND1 ANGL. DEV. =   9.5 DEGREES
REMARK 500    VAL A 416   N   -  CA  -  C   ANGL. DEV. =  17.5 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 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    ASN A  25       71.06    -66.89
REMARK 500    ALA A  29      123.27   -170.96
REMARK 500    ALA A  30       72.50     33.09
REMARK 500    ASN A  35      119.28   -169.66
REMARK 500    ALA A  37      -61.15    -11.40
REMARK 500    PRO A  70      107.36    -55.74
REMARK 500    MET A  71       63.07   -115.45
REMARK 500    ASN A 120      118.13    -36.46
REMARK 500    ALA A 171       57.26    -90.90
REMARK 500    GLU A 201      -68.36   -129.14
REMARK 500    ALA A 214      -65.00    -97.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    VAL A 416        19.2      L          L   OUTSIDE RANGE
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 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                              MG A 418  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 AMP A 417   O1P
REMARK 620 2 ASP A 374   OD1 101.3
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  MG A 418
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP A 417
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3PG A 419
DBREF  1HDI A    4   416  PDB    1HDI     1HDI             4    416
SEQRES   1 A  413  ASN LYS LEU THR LEU ASP LYS LEU ASN VAL LYS GLY LYS
SEQRES   2 A  413  ARG VAL VAL MET ARG VAL ASP PHE ASN VAL PRO MET ALA
SEQRES   3 A  413  ALA ALA GLN ILE THR ASN ASN ALA ARG ILE LYS ALA ALA
SEQRES   4 A  413  VAL PRO SER ILE LYS PHE CYS LEU ASP ASP GLY ALA LYS
SEQRES   5 A  413  SER VAL VAL LEU MET SER HIS LEU GLY ARG PRO ASP GLY
SEQRES   6 A  413  SER PRO MET PRO ASP LYS TYR SER LEU GLN PRO VAL ALA
SEQRES   7 A  413  ALA GLU LEU LYS SER ALA LEU GLY LYS ALA VAL LEU PHE
SEQRES   8 A  413  LEU LYS ASP CYS VAL GLY PRO ALA VAL GLU LYS ALA CYS
SEQRES   9 A  413  ALA ASP PRO ALA ALA GLY SER VAL ILE LEU LEU GLU ASN
SEQRES  10 A  413  LEU ARG PHE HIS VAL GLU GLU GLU GLY LYS GLY LYS ASP
SEQRES  11 A  413  ALA SER GLY ASN LYS ALA ALA GLY GLU PRO ALA LYS ILE
SEQRES  12 A  413  LYS ALA PHE ARG ALA SER LEU SER ALA LEU GLY ASP VAL
SEQRES  13 A  413  TYR VAL ASN ASP ALA PHE GLY THR ALA HIS ARG ALA HIS
SEQRES  14 A  413  SER SER MET VAL GLY VAL ASN LEU PRO LYS LYS ALA GLY
SEQRES  15 A  413  ALA PHE LEU MET LYS LYS GLU LEU ASN TYR PHE ALA ALA
SEQRES  16 A  413  ALA ALA GLU SER PRO GLU ARG PRO PHE LEU ALA ILE LEU
SEQRES  17 A  413  GLY GLY ALA LYS VAL ALA ASP LYS ILE GLN LEU ILE ASN
SEQRES  18 A  413  ASN MET LEU ASP LYS VAL ASN GLU MET ILE ILE GLY GLY
SEQRES  19 A  413  GLY MET ALA PHE THR PHE LEU LYS VAL LEU ASN ASN MET
SEQRES  20 A  413  GLU ILE GLY THR SER LEU PHE ASP GLU ALA GLY LYS LYS
SEQRES  21 A  413  ILE VAL LYS ASN LEU MET SER LYS ALA ALA ALA ASN GLY
SEQRES  22 A  413  VAL LYS ILE THR LEU PRO VAL ASP PHE VAL THR ALA ASP
SEQRES  23 A  413  LYS PHE ASP GLU GLN ALA LYS ILE GLY GLN ALA THR VAL
SEQRES  24 A  413  ALA SER GLY ILE PRO ALA GLY TRP MET GLY LEU ASP CYS
SEQRES  25 A  413  GLY PRO LYS SER SER ALA LYS TYR SER GLU ALA VAL ALA
SEQRES  26 A  413  ARG ALA LYS GLN ILE VAL TRP ASN GLY PRO VAL GLY VAL
SEQRES  27 A  413  PHE GLU TRP GLU ALA PHE ALA GLN GLY THR LYS ALA LEU
SEQRES  28 A  413  MET ASP GLU VAL VAL LYS ALA THR SER ARG GLY CYS ILE
SEQRES  29 A  413  THR ILE ILE GLY GLY GLY ASP THR ALA THR CYS CYS ALA
SEQRES  30 A  413  LYS TRP ASN THR GLU ASP ASN VAL SER HIS VAL SER THR
SEQRES  31 A  413  GLY GLY GLY ALA SER LEU GLU LEU LEU GLU GLY LYS VAL
SEQRES  32 A  413  LEU PRO GLY VAL ASP ALA LEU SER ASN VAL
HET     MG  A 418       1
HET    AMP  A 417      23
HET    3PG  A 419      11
HETNAM      MG MAGNESIUM ION
HETNAM     AMP ADENOSINE MONOPHOSPHATE
HETNAM     3PG 3-PHOSPHOGLYCERIC ACID
FORMUL   2   MG    MG 2+
FORMUL   3  AMP    C10 H14 N5 O7 P
FORMUL   4  3PG    C3 H7 O7 P1
FORMUL   5  HOH   *208(H2 O1)
HELIX    1   1 LEU A    8  LEU A   11  5                                   4
HELIX    2   2 ASN A   36  ASP A   52  1                                  17
HELIX    3   3 LEU A   77  GLY A   89  1                                  13
HELIX    4   4 GLY A  100  ASP A  109  1                                  10
HELIX    5   5 ASN A  120  HIS A  124  5                                   5
HELIX    6   6 GLU A  142  LEU A  156  1                                  15
HELIX    7   7 ALA A  164  ALA A  168  5                                   5
HELIX    8   8 HIS A  172  GLY A  177  1                                   6
HELIX    9   9 ALA A  186  GLU A  201  1                                  16
HELIX   10  10 VAL A  216  ASP A  218  5                                   3
HELIX   11  11 LYS A  219  ASP A  228  1                                  10
HELIX   12  12 MET A  239  ASN A  249  1                                  11
HELIX   13  13 ALA A  260  LYS A  263  5                                   4
HELIX   14  14 ILE A  264  GLY A  276  1                                  13
HELIX   15  15 GLY A  316  ALA A  330  1                                  15
HELIX   16  16 TRP A  344  PHE A  347  5                                   4
HELIX   17  17 ALA A  348  ARG A  364  1                                  17
HELIX   18  18 GLY A  373  TRP A  382  1                                  10
HELIX   19  19 GLY A  394  GLU A  403  1                                  10
HELIX   20  20 LEU A  407  ALA A  412  1                                   6
SHEET    1  AA 6 LEU A  93  PHE A  94  0
SHEET    2  AA 6 SER A 114  LEU A 117  1  O  VAL A 115   N  LEU A  93
SHEET    3  AA 6 SER A  56  MET A  60  1  O  VAL A  57   N  ILE A 116
SHEET    4  AA 6 ARG A  17  ARG A  21  1  O  VAL A  18   N  VAL A  58
SHEET    5  AA 6 VAL A 159  ASN A 162  1  O  VAL A 159   N  VAL A  19
SHEET    6  AA 6 LYS A 183  GLY A 185  1  O  ALA A 184   N  ASN A 162
SHEET    1  AB 2 LYS A 130  LYS A 132  0
SHEET    2  AB 2 LYS A 138  ALA A 140 -1  O  ALA A 139   N  GLY A 131
SHEET    1  AC 6 LYS A 278  THR A 280  0
SHEET    2  AC 6 GLU A 232  ILE A 235  1  O  MET A 233   N  THR A 280
SHEET    3  AC 6 PHE A 207  LEU A 211  1  O  ALA A 209   N  ILE A 234
SHEET    4  AC 6 GLN A 332  ASN A 336  1  O  GLN A 332   N  LEU A 208
SHEET    5  AC 6 ILE A 367  ILE A 370  1  O  ILE A 367   N  ILE A 333
SHEET    6  AC 6 HIS A 390  VAL A 391  1  O  HIS A 390   N  ILE A 370
SHEET    1  AD 3 ILE A 297  THR A 301  0
SHEET    2  AD 3 ASP A 284  ALA A 288 -1  O  PHE A 285   N  ALA A 300
SHEET    3  AD 3 MET A 311  CYS A 315 -1  O  MET A 311   N  ALA A 288
LINK        MG    MG A 418                 O1P AMP A 417     1555   1555  2.99
LINK        MG    MG A 418                 OD1 ASP A 374     1555   1555  2.73
CISPEP   1 ARG A  205    PRO A  206          0        -0.13
SITE     1 AC1  2 ASP A 374  AMP A 417
SITE     1 AC2 21 ALA A 214  LYS A 215  LYS A 219  GLY A 237
SITE     2 AC2 21 GLY A 238  LEU A 256  GLY A 312  LEU A 313
SITE     3 AC2 21 GLY A 340  VAL A 341  GLU A 343  ASP A 374
SITE     4 AC2 21  MG A 418  HOH A2111  HOH A2182  HOH A2201
SITE     5 AC2 21 HOH A2202  HOH A2203  HOH A2204  HOH A2205
SITE     6 AC2 21 HOH A2206
SITE     1 AC3 11 ASP A  23  ASN A  25  ARG A  38  HIS A  62
SITE     2 AC3 11 ARG A  65  ARG A 122  GLY A 166  ARG A 170
SITE     3 AC3 11 HOH A2009  HOH A2207  HOH A2208
CRYST1   50.500  105.200   35.900  90.00  98.40  90.00 P 1 21 1      2
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      0.019802  0.000000  0.002924        0.00000
SCALE2      0.000000  0.009506  0.000000        0.00000
SCALE3      0.000000  0.000000  0.028157        0.00000
      
PROCHECK
Go to PROCHECK summary
 References