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PDBsum entry 1qh4

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Top Page protein ligands metals Protein-protein interface(s) links
Transferase PDB id
1qh4
Jmol
Contents
Protein chains
380 a.a. *
Ligands
ACT ×6
Metals
_CA
Waters ×1467
* Residue conservation analysis
HEADER    TRANSFERASE                             11-MAY-99   1QH4
TITLE     CRYSTAL STRUCTURE OF CHICKEN BRAIN-TYPE CREATINE KINASE AT
TITLE    2 1.41 ANGSTROM RESOLUTION
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CREATINE KINASE;
COMPND   3 CHAIN: A, B, C, D;
COMPND   4 FRAGMENT: B CHAIN;
COMPND   5 SYNONYM: BB-CK, BRAIN-TYPE CREATINE KINASE;
COMPND   6 EC: 2.7.3.2;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE   3 ORGANISM_COMMON: CHICKEN;
SOURCE   4 ORGANISM_TAXID: 9031;
SOURCE   5 ORGAN: BRAIN;
SOURCE   6 CELLULAR_LOCATION: CYTOPLASM;
SOURCE   7 GENE: EMBL-NR. X03509;
SOURCE   8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE  10 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE  11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  12 EXPRESSION_SYSTEM_VECTOR: PET-3B;
SOURCE  13 EXPRESSION_SYSTEM_PLASMID: PRF23
KEYWDS    BRAIN-TYPE CREATINE KINASE, CANCER, CELLULAR ENERGY
KEYWDS   2 METABOLISM, GUANIDINO KINASE, NEURODEGENERATIVE DISORDERS,
KEYWDS   3 TRANSFERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    M.EDER,U.SCHLATTNER,A.BECKER,T.WALLIMANN,W.KABSCH,K.FRITZ-
AUTHOR   2 WOLF
REVDAT   2   24-FEB-09 1QH4    1       VERSN
REVDAT   1   19-NOV-99 1QH4    0
JRNL        AUTH   M.EDER,U.SCHLATTNER,A.BECKER,T.WALLIMANN,W.KABSCH,
JRNL        AUTH 2 K.FRITZ-WOLF
JRNL        TITL   CRYSTAL STRUCTURE OF BRAIN-TYPE CREATINE KINASE AT
JRNL        TITL 2 1.41 A RESOLUTION.
JRNL        REF    PROTEIN SCI.                  V.   8  2258 1999
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   10595529
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   G.ZHOU,T.SOMASUNDARAM,E.BLANC,G.PARTHASARATHY,
REMARK   1  AUTH 2 W.R.ELLINGTON,M.S.CHAPMAN
REMARK   1  TITL   TRANSITION STATE STRUCTURE OF ARGININE KINASE:
REMARK   1  TITL 2 IMPLICATIONS FOR CATALYSIS OF BIMOLECULAR REACTIONS
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  95  8449 1998
REMARK   1  REFN                   ISSN 0027-8424
REMARK   1  DOI    10.1073/PNAS.95.15.8449
REMARK   1 REFERENCE 2
REMARK   1  AUTH   K.FRITZ-WOLF,T.SCHNYDER,T.WALLIMANN,W.KABSCH
REMARK   1  TITL   STRUCTURE OF MITOCHONDRIAL CREATINE KINASE.
REMARK   1  REF    NATURE                        V. 381   341 1996
REMARK   1  REFN                   ISSN 0028-0836
REMARK   1  DOI    10.1038/381341A0
REMARK   2
REMARK   2 RESOLUTION.    1.41 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : SHELXL-97
REMARK   3   AUTHORS     : G.M.SHELDRICK
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.41
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1
REMARK   3   CROSS-VALIDATION METHOD           : FREE R
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.137
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.134
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.188
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.300
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 14886
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 282461
REMARK   3
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : NULL
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : NULL
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : NULL
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : NULL
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS      : 12067
REMARK   3   NUCLEIC ACID ATOMS : 0
REMARK   3   HETEROGEN ATOMS    : 25
REMARK   3   SOLVENT ATOMS      : 1467
REMARK   3
REMARK   3  MODEL REFINEMENT.
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 13358.00
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 11644.00
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 15
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 12204
REMARK   3   NUMBER OF RESTRAINTS                     : 14868
REMARK   3
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK   3   BOND LENGTHS                         (A) : 0.010
REMARK   3   ANGLE DISTANCES                      (A) : 0.029
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.022
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.059
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.067
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.014
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.004
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.055
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.079
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED: MOEWS & KRETSINGER, J.MOL.BIOL.91(1973)201-2
REMARK   3
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER
REMARK   3   SPECIAL CASE: NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: X-PLOR AND CNS WERE USED FOR INITIAL
REMARK   3  REFINEMENT. ANISOTROPIC REFINEMENT IN SHELX REDUCED FREE R (NO
REMARK   3  CUTOFF) BY 2.6% DISORDERED RESIDUES 321 - 330 (CHAIN A-D) WERE
REMARK   3  MODELED
REMARK   4
REMARK   4 1QH4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAY-99.
REMARK 100 THE RCSB ID CODE IS RCSB001035.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 22-JUL-98
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG
REMARK 200  BEAMLINE                       : BW7B
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.84
REMARK 200  MONOCHROMATOR                  : GE SINGLE CRYSTAL
REMARK 200  OPTICS                         : BENT CRYSTAL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS V. 99
REMARK 200  DATA SCALING SOFTWARE          : XDS V. 99
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 301191
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.410
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1
REMARK 200  DATA REDUNDANCY                : 4.000
REMARK 200  R MERGE                    (I) : 0.04200
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 17.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.41
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.50
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.1
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50
REMARK 200  R MERGE FOR SHELL          (I) : 0.21500
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 5.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE, CNS, SHELXL-97
REMARK 200 STARTING MODEL: 1CRK, MITOCHONDRIAL CREATINE KINASE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 48.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES, 0.4M CA(OAC)2, 15% PE 2MM
REMARK 280  DTT, PH 6.5, 8 MG/ML PROTEIN
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       87.99500
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 59730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       38.70641
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000       87.99500
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       94.90317
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  43   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES
REMARK 500    TYR A  82   CB  -  CG  -  CD1 ANGL. DEV. =  -3.6 DEGREES
REMARK 500    ARG A 130   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES
REMARK 500    ARG A 151   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES
REMARK 500    PHE A 192   O   -  C   -  N   ANGL. DEV. = -11.0 DEGREES
REMARK 500    ARG A 209   NE  -  CZ  -  NH1 ANGL. DEV. =   5.1 DEGREES
REMARK 500    ARG A 209   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES
REMARK 500    MET A 240   CA  -  CB  -  CG  ANGL. DEV. =  13.0 DEGREES
REMARK 500    ARG A 252   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.3 DEGREES
REMARK 500    ARG A 292   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES
REMARK 500    ARG A 316   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES
REMARK 500    GLY A 331   C   -  N   -  CA  ANGL. DEV. =  17.7 DEGREES
REMARK 500    ARG B  43   NE  -  CZ  -  NH1 ANGL. DEV. =   4.9 DEGREES
REMARK 500    ARG B  43   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.6 DEGREES
REMARK 500    GLN B  46   CA  -  CB  -  CG  ANGL. DEV. =  14.4 DEGREES
REMARK 500    ARG B  96   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES
REMARK 500    GLU B 105   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.7 DEGREES
REMARK 500    ARG B 130   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES
REMARK 500    ARG B 132   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.6 DEGREES
REMARK 500    ARG B 151   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES
REMARK 500    LYS B 156   CD  -  CE  -  NZ  ANGL. DEV. =  14.7 DEGREES
REMARK 500    ARG B 209   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES
REMARK 500    ARG B 236   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 DEGREES
REMARK 500    ARG B 252   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES
REMARK 500    ARG B 292   NE  -  CZ  -  NH1 ANGL. DEV. =   5.1 DEGREES
REMARK 500    ARG B 292   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES
REMARK 500    ARG C  43   CD  -  NE  -  CZ  ANGL. DEV. =  14.0 DEGREES
REMARK 500    ARG C  43   NE  -  CZ  -  NH1 ANGL. DEV. =   5.3 DEGREES
REMARK 500    ARG C  45   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.4 DEGREES
REMARK 500    GLN C  46   CA  -  CB  -  CG  ANGL. DEV. =  16.5 DEGREES
REMARK 500    ARG C 130   CD  -  NE  -  CZ  ANGL. DEV. =  41.2 DEGREES
REMARK 500    ARG C 130   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES
REMARK 500    ARG C 132   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES
REMARK 500    ARG C 132   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.7 DEGREES
REMARK 500    ARG C 138   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES
REMARK 500    ARG C 148   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES
REMARK 500    ARG C 151   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES
REMARK 500    ARG C 209   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES
REMARK 500    ARG C 236   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES
REMARK 500    ARG C 236   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.8 DEGREES
REMARK 500    PHE C 264   CB  -  CG  -  CD1 ANGL. DEV. =   4.5 DEGREES
REMARK 500    PHE C 271   CB  -  CG  -  CD1 ANGL. DEV. =   4.6 DEGREES
REMARK 500    ARG C 292   NE  -  CZ  -  NH1 ANGL. DEV. =   5.8 DEGREES
REMARK 500    THR C 322   C   -  N   -  CA  ANGL. DEV. =  18.7 DEGREES
REMARK 500    ARG C 341   NE  -  CZ  -  NH2 ANGL. DEV. =   4.1 DEGREES
REMARK 500    ASP C 375   CB  -  CG  -  OD1 ANGL. DEV. =  -6.2 DEGREES
REMARK 500    PHE D   3   CB  -  CG  -  CD1 ANGL. DEV. =   5.3 DEGREES
REMARK 500    ARG D  43   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES
REMARK 500    ARG D  96   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.9 DEGREES
REMARK 500    ARG D 130   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS      60 ANGLE DEVIATIONS.
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    PHE A  68      -82.48    -91.53
REMARK 500    GLU A 231     -110.09    -87.88
REMARK 500    VAL A 325     -178.17    -69.12
REMARK 500    ASP A 326       95.44    -69.55
REMARK 500    THR A 327      -36.14    163.48
REMARK 500    ALA A 329     -155.63     47.81
REMARK 500    ARG A 341      -41.78   -134.48
REMARK 500    PHE B   3     -155.04     55.97
REMARK 500    ILE B  69       97.13   -160.92
REMARK 500    ASP B 122      109.48    -48.88
REMARK 500    GLU B 231     -111.13    -87.10
REMARK 500    VAL B 325      169.96     49.47
REMARK 500    THR B 327      -67.30   -170.21
REMARK 500    ALA B 328      151.10    179.63
REMARK 500    ALA B 329      143.64    -35.93
REMARK 500    ARG B 341      -40.73   -134.30
REMARK 500    PHE C   3     -150.19     55.58
REMARK 500    PHE C  68       -6.87   -154.23
REMARK 500    ASP C 120       56.40   -149.11
REMARK 500    GLU C 231     -111.31    -91.26
REMARK 500    THR C 322      -21.56    117.65
REMARK 500    ASP C 326      -16.59     87.15
REMARK 500    ARG C 341      -36.98   -131.54
REMARK 500    ASN D   5       64.56   -101.02
REMARK 500    ASP D 122      108.35    -48.64
REMARK 500    ASN D 230       34.84     70.26
REMARK 500    GLU D 231     -110.30    -89.38
REMARK 500    VAL D 325      -84.33   -131.17
REMARK 500    THR D 327      -30.02     54.48
REMARK 500    ALA D 328      171.23    -49.41
REMARK 500    ARG D 341      -41.97   -130.20
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 B1564        DISTANCE =  6.03 ANGSTROMS
REMARK 525    HOH B1616        DISTANCE =  5.67 ANGSTROMS
REMARK 525    HOH A1671        DISTANCE =  5.25 ANGSTROMS
REMARK 525    HOH C1702        DISTANCE =  6.84 ANGSTROMS
REMARK 525    HOH C1732        DISTANCE =  6.81 ANGSTROMS
REMARK 525    HOH A1735        DISTANCE =  8.81 ANGSTROMS
REMARK 525    HOH C1772        DISTANCE =  8.51 ANGSTROMS
REMARK 525    HOH C1780        DISTANCE =  7.15 ANGSTROMS
REMARK 525    HOH B1781        DISTANCE =  6.63 ANGSTROMS
REMARK 525    HOH C1811        DISTANCE =  7.68 ANGSTROMS
REMARK 525    HOH A1829        DISTANCE =  6.70 ANGSTROMS
REMARK 525    HOH B1877        DISTANCE =  9.03 ANGSTROMS
REMARK 525    HOH B1883        DISTANCE =  5.08 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 D 382  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D  44   OD1
REMARK 620 2 ASP D  44   OD2  53.2
REMARK 620 3 LYS D  41   O    70.6 117.8
REMARK 620 N                    1     2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 382
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 1501
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 1502
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 1503
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 1504
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 1505
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT D 1506
DBREF  1QH4 A    2   381  UNP    P05122   KCRB_CHICK       2    381
DBREF  1QH4 B    2   381  UNP    P05122   KCRB_CHICK       2    381
DBREF  1QH4 C    2   381  UNP    P05122   KCRB_CHICK       2    381
DBREF  1QH4 D    2   381  UNP    P05122   KCRB_CHICK       2    381
SEQRES   1 A  380  PRO PHE SER ASN SER HIS ASN LEU LEU LYS MET LYS TYR
SEQRES   2 A  380  SER VAL ASP ASP GLU TYR PRO ASP LEU SER VAL HIS ASN
SEQRES   3 A  380  ASN HIS MET ALA LYS VAL LEU THR LEU ASP LEU TYR LYS
SEQRES   4 A  380  LYS LEU ARG ASP ARG GLN THR SER SER GLY PHE THR LEU
SEQRES   5 A  380  ASP ASP VAL ILE GLN THR GLY VAL ASP ASN PRO GLY HIS
SEQRES   6 A  380  PRO PHE ILE MET THR VAL GLY CYS VAL ALA GLY ASP GLU
SEQRES   7 A  380  GLU SER TYR GLU VAL PHE LYS GLU LEU PHE ASP PRO VAL
SEQRES   8 A  380  ILE GLU ASP ARG HIS GLY GLY TYR LYS PRO THR ASP GLU
SEQRES   9 A  380  HIS LYS THR ASP LEU ASN ALA ASP ASN LEU GLN GLY GLY
SEQRES  10 A  380  ASP ASP LEU ASP PRO ASN TYR VAL LEU SER SER ARG VAL
SEQRES  11 A  380  ARG THR GLY ARG SER ILE ARG GLY PHE CYS LEU PRO PRO
SEQRES  12 A  380  HIS CYS SER ARG GLY GLU ARG ARG ALA ILE GLU LYS LEU
SEQRES  13 A  380  SER VAL GLU ALA LEU GLY SER LEU GLY GLY ASP LEU LYS
SEQRES  14 A  380  GLY LYS TYR TYR ALA LEU ARG ASN MET THR ASP ALA GLU
SEQRES  15 A  380  GLN GLN GLN LEU ILE ASP ASP HIS PHE LEU PHE ASP LYS
SEQRES  16 A  380  PRO VAL SER PRO LEU LEU LEU ALA SER GLY MET ALA ARG
SEQRES  17 A  380  ASP TRP PRO ASP ALA ARG GLY ILE TRP HIS ASN ASP ASN
SEQRES  18 A  380  LYS THR PHE LEU VAL TRP ILE ASN GLU GLU ASP HIS LEU
SEQRES  19 A  380  ARG VAL ILE SER MET GLN LYS GLY GLY ASN MET LYS GLU
SEQRES  20 A  380  VAL PHE THR ARG PHE CYS THR GLY LEU THR GLN ILE GLU
SEQRES  21 A  380  THR LEU PHE LYS SER LYS ASN TYR GLU PHE MET TRP ASN
SEQRES  22 A  380  PRO HIS LEU GLY TYR ILE LEU THR CYS PRO SER ASN LEU
SEQRES  23 A  380  GLY THR GLY LEU ARG ALA GLY VAL HIS ILE LYS LEU PRO
SEQRES  24 A  380  ASN LEU GLY LYS HIS GLU LYS PHE GLY GLU VAL LEU LYS
SEQRES  25 A  380  ARG LEU ARG LEU GLN LYS ARG GLY THR GLY GLY VAL ASP
SEQRES  26 A  380  THR ALA ALA VAL GLY GLY VAL PHE ASP VAL SER ASN ALA
SEQRES  27 A  380  ASP ARG LEU GLY PHE SER GLU VAL GLU LEU VAL GLN MET
SEQRES  28 A  380  VAL VAL ASP GLY VAL LYS LEU LEU ILE GLU MET GLU LYS
SEQRES  29 A  380  ARG LEU GLU LYS GLY GLN SER ILE ASP ASP LEU MET PRO
SEQRES  30 A  380  ALA GLN LYS
SEQRES   1 B  380  PRO PHE SER ASN SER HIS ASN LEU LEU LYS MET LYS TYR
SEQRES   2 B  380  SER VAL ASP ASP GLU TYR PRO ASP LEU SER VAL HIS ASN
SEQRES   3 B  380  ASN HIS MET ALA LYS VAL LEU THR LEU ASP LEU TYR LYS
SEQRES   4 B  380  LYS LEU ARG ASP ARG GLN THR SER SER GLY PHE THR LEU
SEQRES   5 B  380  ASP ASP VAL ILE GLN THR GLY VAL ASP ASN PRO GLY HIS
SEQRES   6 B  380  PRO PHE ILE MET THR VAL GLY CYS VAL ALA GLY ASP GLU
SEQRES   7 B  380  GLU SER TYR GLU VAL PHE LYS GLU LEU PHE ASP PRO VAL
SEQRES   8 B  380  ILE GLU ASP ARG HIS GLY GLY TYR LYS PRO THR ASP GLU
SEQRES   9 B  380  HIS LYS THR ASP LEU ASN ALA ASP ASN LEU GLN GLY GLY
SEQRES  10 B  380  ASP ASP LEU ASP PRO ASN TYR VAL LEU SER SER ARG VAL
SEQRES  11 B  380  ARG THR GLY ARG SER ILE ARG GLY PHE CYS LEU PRO PRO
SEQRES  12 B  380  HIS CYS SER ARG GLY GLU ARG ARG ALA ILE GLU LYS LEU
SEQRES  13 B  380  SER VAL GLU ALA LEU GLY SER LEU GLY GLY ASP LEU LYS
SEQRES  14 B  380  GLY LYS TYR TYR ALA LEU ARG ASN MET THR ASP ALA GLU
SEQRES  15 B  380  GLN GLN GLN LEU ILE ASP ASP HIS PHE LEU PHE ASP LYS
SEQRES  16 B  380  PRO VAL SER PRO LEU LEU LEU ALA SER GLY MET ALA ARG
SEQRES  17 B  380  ASP TRP PRO ASP ALA ARG GLY ILE TRP HIS ASN ASP ASN
SEQRES  18 B  380  LYS THR PHE LEU VAL TRP ILE ASN GLU GLU ASP HIS LEU
SEQRES  19 B  380  ARG VAL ILE SER MET GLN LYS GLY GLY ASN MET LYS GLU
SEQRES  20 B  380  VAL PHE THR ARG PHE CYS THR GLY LEU THR GLN ILE GLU
SEQRES  21 B  380  THR LEU PHE LYS SER LYS ASN TYR GLU PHE MET TRP ASN
SEQRES  22 B  380  PRO HIS LEU GLY TYR ILE LEU THR CYS PRO SER ASN LEU
SEQRES  23 B  380  GLY THR GLY LEU ARG ALA GLY VAL HIS ILE LYS LEU PRO
SEQRES  24 B  380  ASN LEU GLY LYS HIS GLU LYS PHE GLY GLU VAL LEU LYS
SEQRES  25 B  380  ARG LEU ARG LEU GLN LYS ARG GLY THR GLY GLY VAL ASP
SEQRES  26 B  380  THR ALA ALA VAL GLY GLY VAL PHE ASP VAL SER ASN ALA
SEQRES  27 B  380  ASP ARG LEU GLY PHE SER GLU VAL GLU LEU VAL GLN MET
SEQRES  28 B  380  VAL VAL ASP GLY VAL LYS LEU LEU ILE GLU MET GLU LYS
SEQRES  29 B  380  ARG LEU GLU LYS GLY GLN SER ILE ASP ASP LEU MET PRO
SEQRES  30 B  380  ALA GLN LYS
SEQRES   1 C  380  PRO PHE SER ASN SER HIS ASN LEU LEU LYS MET LYS TYR
SEQRES   2 C  380  SER VAL ASP ASP GLU TYR PRO ASP LEU SER VAL HIS ASN
SEQRES   3 C  380  ASN HIS MET ALA LYS VAL LEU THR LEU ASP LEU TYR LYS
SEQRES   4 C  380  LYS LEU ARG ASP ARG GLN THR SER SER GLY PHE THR LEU
SEQRES   5 C  380  ASP ASP VAL ILE GLN THR GLY VAL ASP ASN PRO GLY HIS
SEQRES   6 C  380  PRO PHE ILE MET THR VAL GLY CYS VAL ALA GLY ASP GLU
SEQRES   7 C  380  GLU SER TYR GLU VAL PHE LYS GLU LEU PHE ASP PRO VAL
SEQRES   8 C  380  ILE GLU ASP ARG HIS GLY GLY TYR LYS PRO THR ASP GLU
SEQRES   9 C  380  HIS LYS THR ASP LEU ASN ALA ASP ASN LEU GLN GLY GLY
SEQRES  10 C  380  ASP ASP LEU ASP PRO ASN TYR VAL LEU SER SER ARG VAL
SEQRES  11 C  380  ARG THR GLY ARG SER ILE ARG GLY PHE CYS LEU PRO PRO
SEQRES  12 C  380  HIS CYS SER ARG GLY GLU ARG ARG ALA ILE GLU LYS LEU
SEQRES  13 C  380  SER VAL GLU ALA LEU GLY SER LEU GLY GLY ASP LEU LYS
SEQRES  14 C  380  GLY LYS TYR TYR ALA LEU ARG ASN MET THR ASP ALA GLU
SEQRES  15 C  380  GLN GLN GLN LEU ILE ASP ASP HIS PHE LEU PHE ASP LYS
SEQRES  16 C  380  PRO VAL SER PRO LEU LEU LEU ALA SER GLY MET ALA ARG
SEQRES  17 C  380  ASP TRP PRO ASP ALA ARG GLY ILE TRP HIS ASN ASP ASN
SEQRES  18 C  380  LYS THR PHE LEU VAL TRP ILE ASN GLU GLU ASP HIS LEU
SEQRES  19 C  380  ARG VAL ILE SER MET GLN LYS GLY GLY ASN MET LYS GLU
SEQRES  20 C  380  VAL PHE THR ARG PHE CYS THR GLY LEU THR GLN ILE GLU
SEQRES  21 C  380  THR LEU PHE LYS SER LYS ASN TYR GLU PHE MET TRP ASN
SEQRES  22 C  380  PRO HIS LEU GLY TYR ILE LEU THR CYS PRO SER ASN LEU
SEQRES  23 C  380  GLY THR GLY LEU ARG ALA GLY VAL HIS ILE LYS LEU PRO
SEQRES  24 C  380  ASN LEU GLY LYS HIS GLU LYS PHE GLY GLU VAL LEU LYS
SEQRES  25 C  380  ARG LEU ARG LEU GLN LYS ARG GLY THR GLY GLY VAL ASP
SEQRES  26 C  380  THR ALA ALA VAL GLY GLY VAL PHE ASP VAL SER ASN ALA
SEQRES  27 C  380  ASP ARG LEU GLY PHE SER GLU VAL GLU LEU VAL GLN MET
SEQRES  28 C  380  VAL VAL ASP GLY VAL LYS LEU LEU ILE GLU MET GLU LYS
SEQRES  29 C  380  ARG LEU GLU LYS GLY GLN SER ILE ASP ASP LEU MET PRO
SEQRES  30 C  380  ALA GLN LYS
SEQRES   1 D  380  PRO PHE SER ASN SER HIS ASN LEU LEU LYS MET LYS TYR
SEQRES   2 D  380  SER VAL ASP ASP GLU TYR PRO ASP LEU SER VAL HIS ASN
SEQRES   3 D  380  ASN HIS MET ALA LYS VAL LEU THR LEU ASP LEU TYR LYS
SEQRES   4 D  380  LYS LEU ARG ASP ARG GLN THR SER SER GLY PHE THR LEU
SEQRES   5 D  380  ASP ASP VAL ILE GLN THR GLY VAL ASP ASN PRO GLY HIS
SEQRES   6 D  380  PRO PHE ILE MET THR VAL GLY CYS VAL ALA GLY ASP GLU
SEQRES   7 D  380  GLU SER TYR GLU VAL PHE LYS GLU LEU PHE ASP PRO VAL
SEQRES   8 D  380  ILE GLU ASP ARG HIS GLY GLY TYR LYS PRO THR ASP GLU
SEQRES   9 D  380  HIS LYS THR ASP LEU ASN ALA ASP ASN LEU GLN GLY GLY
SEQRES  10 D  380  ASP ASP LEU ASP PRO ASN TYR VAL LEU SER SER ARG VAL
SEQRES  11 D  380  ARG THR GLY ARG SER ILE ARG GLY PHE CYS LEU PRO PRO
SEQRES  12 D  380  HIS CYS SER ARG GLY GLU ARG ARG ALA ILE GLU LYS LEU
SEQRES  13 D  380  SER VAL GLU ALA LEU GLY SER LEU GLY GLY ASP LEU LYS
SEQRES  14 D  380  GLY LYS TYR TYR ALA LEU ARG ASN MET THR ASP ALA GLU
SEQRES  15 D  380  GLN GLN GLN LEU ILE ASP ASP HIS PHE LEU PHE ASP LYS
SEQRES  16 D  380  PRO VAL SER PRO LEU LEU LEU ALA SER GLY MET ALA ARG
SEQRES  17 D  380  ASP TRP PRO ASP ALA ARG GLY ILE TRP HIS ASN ASP ASN
SEQRES  18 D  380  LYS THR PHE LEU VAL TRP ILE ASN GLU GLU ASP HIS LEU
SEQRES  19 D  380  ARG VAL ILE SER MET GLN LYS GLY GLY ASN MET LYS GLU
SEQRES  20 D  380  VAL PHE THR ARG PHE CYS THR GLY LEU THR GLN ILE GLU
SEQRES  21 D  380  THR LEU PHE LYS SER LYS ASN TYR GLU PHE MET TRP ASN
SEQRES  22 D  380  PRO HIS LEU GLY TYR ILE LEU THR CYS PRO SER ASN LEU
SEQRES  23 D  380  GLY THR GLY LEU ARG ALA GLY VAL HIS ILE LYS LEU PRO
SEQRES  24 D  380  ASN LEU GLY LYS HIS GLU LYS PHE GLY GLU VAL LEU LYS
SEQRES  25 D  380  ARG LEU ARG LEU GLN LYS ARG GLY THR GLY GLY VAL ASP
SEQRES  26 D  380  THR ALA ALA VAL GLY GLY VAL PHE ASP VAL SER ASN ALA
SEQRES  27 D  380  ASP ARG LEU GLY PHE SER GLU VAL GLU LEU VAL GLN MET
SEQRES  28 D  380  VAL VAL ASP GLY VAL LYS LEU LEU ILE GLU MET GLU LYS
SEQRES  29 D  380  ARG LEU GLU LYS GLY GLN SER ILE ASP ASP LEU MET PRO
SEQRES  30 D  380  ALA GLN LYS
HET     CA  D 382       1
HET    ACT  B1501       4
HET    ACT  A1502       4
HET    ACT  B1503       4
HET    ACT  C1504       4
HET    ACT  C1505       4
HET    ACT  D1506       4
HETNAM      CA CALCIUM ION
HETNAM     ACT ACETATE ION
FORMUL   5   CA    CA 2+
FORMUL   6  ACT    6(C2 H3 O2 1-)
FORMUL  12  HOH   *1467(H2 O)
HELIX    1   1 SER A    6  LYS A   13  1                                   8
HELIX    2   2 VAL A   16  GLU A   19  1                                   4
HELIX    3   3 HIS A   29  VAL A   33  1                                   5
HELIX    4   4 LEU A   36  LEU A   42  1                                   7
HELIX    5   5 LEU A   53  ASP A   62  1                                  10
HELIX    6   6 GLU A   79  VAL A   84  5                                   6
HELIX    7   7 LYS A   86  ARG A   96  1                                  11
HELIX    8   8 ALA A  112  ASN A  114  5                                   3
HELIX    9   9 ARG A  148  SER A  164  1                                  17
HELIX   10  10 GLY A  167  LEU A  169  5                                   3
HELIX   11  11 LEU A  176  ASN A  178  5                                   3
HELIX   12  12 ASP A  181  ASP A  189  1                                   9
HELIX   13  13 PRO A  200  SER A  205  1                                   6
HELIX   14  14 MET A  246  LYS A  267  1                                  22
HELIX   15  15 PRO A  284  ASN A  286  5                                   3
HELIX   16  16 PRO A  300  LYS A  304  1                                   5
HELIX   17  17 PHE A  308  LEU A  315  1                                   8
HELIX   18  18 GLU A  346  LYS A  369  1                                  24
HELIX   19  19 ASP A  374  LEU A  376  5                                   3
HELIX   20  20 PHE B    3  HIS B    7  5                                   5
HELIX   21  21 LEU B    9  LYS B   13  5                                   5
HELIX   22  22 VAL B   16  GLU B   19  1                                   4
HELIX   23  23 HIS B   29  VAL B   33  1                                   5
HELIX   24  24 LEU B   36  LEU B   42  1                                   7
HELIX   25  25 LEU B   53  ASP B   62  1                                  10
HELIX   26  26 GLU B   79  VAL B   84  5                                   6
HELIX   27  27 LYS B   86  ARG B   96  1                                  11
HELIX   28  28 ALA B  112  ASN B  114  5                                   3
HELIX   29  29 ARG B  148  SER B  164  1                                  17
HELIX   30  30 GLY B  167  LEU B  169  5                                   3
HELIX   31  31 ASP B  181  ASP B  190  1                                  10
HELIX   32  32 PRO B  200  SER B  205  1                                   6
HELIX   33  33 MET B  246  LYS B  267  1                                  22
HELIX   34  34 PRO B  284  ASN B  286  5                                   3
HELIX   35  35 PRO B  300  LYS B  304  1                                   5
HELIX   36  36 PHE B  308  LEU B  315  1                                   8
HELIX   37  37 GLU B  346  LYS B  369  1                                  24
HELIX   38  38 ASP B  374  LEU B  376  5                                   3
HELIX   39  39 PHE C    3  HIS C    7  5                                   5
HELIX   40  40 LEU C    9  LYS C   13  5                                   5
HELIX   41  41 VAL C   16  GLU C   19  1                                   4
HELIX   42  42 HIS C   29  VAL C   33  1                                   5
HELIX   43  43 LEU C   36  LEU C   42  1                                   7
HELIX   44  44 LEU C   53  ASP C   62  1                                  10
HELIX   45  45 GLU C   79  VAL C   84  5                                   6
HELIX   46  46 LYS C   86  ARG C   96  1                                  11
HELIX   47  47 ALA C  112  ASN C  114  5                                   3
HELIX   48  48 ARG C  148  SER C  164  1                                  17
HELIX   49  49 GLY C  167  LEU C  169  5                                   3
HELIX   50  50 ASP C  181  ASP C  189  1                                   9
HELIX   51  51 PRO C  200  SER C  205  1                                   6
HELIX   52  52 MET C  246  LYS C  267  1                                  22
HELIX   53  53 PRO C  284  ASN C  286  5                                   3
HELIX   54  54 PRO C  300  LYS C  304  1                                   5
HELIX   55  55 PHE C  308  LEU C  315  1                                   8
HELIX   56  56 VAL C  325  THR C  327  5                                   3
HELIX   57  57 GLU C  346  LYS C  369  1                                  24
HELIX   58  58 ASP C  374  LEU C  376  5                                   3
HELIX   59  59 SER D    6  LYS D   13  1                                   8
HELIX   60  60 VAL D   16  GLU D   19  1                                   4
HELIX   61  61 HIS D   29  VAL D   33  1                                   5
HELIX   62  62 LEU D   36  LEU D   42  1                                   7
HELIX   63  63 LEU D   53  ASP D   62  1                                  10
HELIX   64  64 GLU D   79  VAL D   84  5                                   6
HELIX   65  65 LYS D   86  ARG D   96  1                                  11
HELIX   66  66 ALA D  112  ASN D  114  5                                   3
HELIX   67  67 ARG D  148  GLY D  163  1                                  16
HELIX   68  68 GLY D  167  LEU D  169  5                                   3
HELIX   69  69 ASP D  181  ASP D  189  1                                   9
HELIX   70  70 PRO D  200  SER D  205  1                                   6
HELIX   71  71 MET D  246  LYS D  267  1                                  22
HELIX   72  72 PRO D  284  ASN D  286  5                                   3
HELIX   73  73 PRO D  300  LYS D  304  1                                   5
HELIX   74  74 PHE D  308  ARG D  314  1                                   7
HELIX   75  75 GLU D  346  LYS D  369  1                                  24
HELIX   76  76 ASP D  374  LEU D  376  5                                   3
SHEET    1   A 8 GLY A 171  ALA A 175  0
SHEET    2   A 8 GLY A 216  ASN A 220 -1  N  HIS A 219   O  LYS A 172
SHEET    3   A 8 PHE A 225  ILE A 229 -1  N  ILE A 229   O  GLY A 216
SHEET    4   A 8 LEU A 235  LYS A 242 -1  N  ILE A 238   O  LEU A 226
SHEET    5   A 8 VAL A 126  ARG A 135 -1  N  ARG A 135   O  LEU A 235
SHEET    6   A 8 ARG A 292  LYS A 298 -1  N  HIS A 296   O  LEU A 127
SHEET    7   A 8 VAL A 333  ASN A 338 -1  N  VAL A 336   O  VAL A 295
SHEET    8   A 8 LEU A 317  ARG A 320 -1  N  ARG A 320   O  ASP A 335
SHEET    1   B 8 GLY B 171  ALA B 175  0
SHEET    2   B 8 GLY B 216  ASN B 220 -1  N  HIS B 219   O  LYS B 172
SHEET    3   B 8 PHE B 225  ILE B 229 -1  N  ILE B 229   O  GLY B 216
SHEET    4   B 8 LEU B 235  LYS B 242 -1  N  ILE B 238   O  LEU B 226
SHEET    5   B 8 VAL B 126  ARG B 135 -1  N  ARG B 135   O  LEU B 235
SHEET    6   B 8 ARG B 292  LYS B 298 -1  N  HIS B 296   O  LEU B 127
SHEET    7   B 8 VAL B 333  ASN B 338 -1  N  VAL B 336   O  VAL B 295
SHEET    8   B 8 LEU B 317  GLY B 321 -1  N  ARG B 320   O  ASP B 335
SHEET    1   C 8 GLY C 171  ALA C 175  0
SHEET    2   C 8 GLY C 216  ASN C 220 -1  N  HIS C 219   O  LYS C 172
SHEET    3   C 8 PHE C 225  ILE C 229 -1  N  ILE C 229   O  GLY C 216
SHEET    4   C 8 LEU C 235  LYS C 242 -1  N  ILE C 238   O  LEU C 226
SHEET    5   C 8 VAL C 126  ARG C 135 -1  N  ARG C 135   O  LEU C 235
SHEET    6   C 8 ARG C 292  LYS C 298 -1  N  HIS C 296   O  LEU C 127
SHEET    7   C 8 VAL C 333  ASN C 338 -1  N  VAL C 336   O  VAL C 295
SHEET    8   C 8 LEU C 317  GLY C 321 -1  N  ARG C 320   O  ASP C 335
SHEET    1   D 8 GLY D 171  ALA D 175  0
SHEET    2   D 8 GLY D 216  ASN D 220 -1  N  HIS D 219   O  LYS D 172
SHEET    3   D 8 PHE D 225  ILE D 229 -1  N  ILE D 229   O  GLY D 216
SHEET    4   D 8 LEU D 235  LYS D 242 -1  N  ILE D 238   O  LEU D 226
SHEET    5   D 8 VAL D 126  ARG D 135 -1  N  ARG D 135   O  LEU D 235
SHEET    6   D 8 ARG D 292  LYS D 298 -1  N  HIS D 296   O  LEU D 127
SHEET    7   D 8 VAL D 333  ASN D 338 -1  N  VAL D 336   O  VAL D 295
SHEET    8   D 8 LEU D 317  LYS D 319 -1  N  GLN D 318   O  SER D 337
LINK        CA    CA D 382                 OD1 ASP D  44     1555   1555  2.46
LINK        CA    CA D 382                 OD2 ASP D  44     1555   1555  2.44
LINK        CA    CA D 382                 O   LYS D  41     1555   1555  2.64
CISPEP   1 TRP A  211    PRO A  212          0         4.72
CISPEP   2 TRP B  211    PRO B  212          0         3.05
CISPEP   3 TRP C  211    PRO C  212          0         1.27
CISPEP   4 TRP D  211    PRO D  212          0         1.00
SITE     1 AC1  2 LYS D  41  ASP D  44
SITE     1 AC2  4 SER B  15  VAL B  16  ARG B  43  HOH B1850
SITE     1 AC3  6 THR A  71  VAL A  72  LEU A 201  HOH A1662
SITE     2 AC3  6 HOH A1692  HOH A1834
SITE     1 AC4  6 THR B  71  VAL B  72  LEU B 201  HOH B1574
SITE     2 AC4  6 HOH B1706  HOH B1833
SITE     1 AC5  6 THR C  71  VAL C  72  LEU C 201  HOH C1638
SITE     2 AC5  6 HOH C1728  HOH C1788
SITE     1 AC6  5 ASN C 222  THR C 224  GLN C 241  LYS C 242
SITE     2 AC6  5 HOH C1653
SITE     1 AC7  6 THR D  71  VAL D  72  LEU D 201  HOH D1552
SITE     2 AC7  6 HOH D1604  HOH D1616
CRYST1   48.430  175.990   95.400  90.00  95.85  90.00 P 1 21 1      8
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      0.020648  0.000000  0.002115        0.00000
SCALE2      0.000000  0.005682  0.000000        0.00000
SCALE3      0.000000  0.000000  0.010537        0.00000
      
PROCHECK
Go to PROCHECK summary
 References