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PDBsum entry 3i12

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Ligase PDB id
3i12
Jmol
Contents
Protein chains
360 a.a.
Ligands
ADP ×4
Waters ×315
HEADER    LIGASE                                  25-JUN-09   3I12
TITLE     THE CRYSTAL STRUCTURE OF THE D-ALANYL-ALANINE SYNTHETASE A FROM
TITLE    2 SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR TYPHIMURIUM STR. LT2
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: D-ALANINE-D-ALANINE LIGASE A;
COMPND   3 CHAIN: A, B, C, D;
COMPND   4 SYNONYM: D-ALANYLALANINE SYNTHETASE A, D-ALA-D-ALA LIGASE A;
COMPND   5 EC: 6.3.2.4;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM;
SOURCE   3 ORGANISM_TAXID: 90371;
SOURCE   4 STRAIN: LT2';
SOURCE   5 GENE: DDLA, STM0380;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PMCSG19C
KEYWDS    D-ALANYL-ALANINE SYNTHETASE A, ADP BINDING PROTEIN, CSGID, ATP-
KEYWDS   2 BINDING, CELL SHAPE, CELL WALL BIOGENESIS/DEGRADATION, LIGASE,
KEYWDS   3 MAGNESIUM, MANGANESE, METAL-BINDING, NUCLEOTIDE-BINDING,
KEYWDS   4 PEPTIDOGLYCAN SYNTHESIS, STRUCTURAL GENOMICS, NIAID STRUCTURAL
KEYWDS   5 GENOMICS, CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES
EXPDTA    X-RAY DIFFRACTION
AUTHOR    R.ZHANG,N.MALTSEVA,L.PAPAZISI,W.ANDERSON,A.JOACHIMIAK
REVDAT   2   13-JUL-11 3I12    1       VERSN
REVDAT   1   18-AUG-09 3I12    0
JRNL        AUTH   R.ZHANG,N.MALTSEVA,L.PAPAZISI,W.ANDERSON,A.JOACHIMIAK
JRNL        TITL   THE CRYSTAL STRUCTURE OF THE D-ALANYL-ALANINE SYNTHETASE A
JRNL        TITL 2 FROM SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR TYPHIMURIUM
JRNL        TITL 3 STR. LT2
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0054
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.54
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9
REMARK   3   NUMBER OF REFLECTIONS             : 82073
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 + TEST SET) : 0.200
REMARK   3   R VALUE            (WORKING SET) : 0.197
REMARK   3   FREE R VALUE                     : 0.249
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 4332
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5909
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.76
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2200
REMARK   3   BIN FREE R VALUE SET COUNT          : 323
REMARK   3   BIN FREE R VALUE                    : 0.2890
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 10681
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 108
REMARK   3   SOLVENT ATOMS            : 315
REMARK   3
REMARK   3  B VALUES.
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.03
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.82000
REMARK   3    B22 (A**2) : -0.16000
REMARK   3    B33 (A**2) : 0.98000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.241
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.206
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.138
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.774
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.952
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.926
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 11020 ; 0.022 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  7161 ; 0.001 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 15000 ; 1.976 ; 1.967
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 17605 ; 1.097 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1407 ; 7.250 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   491 ;39.509 ;25.316
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1806 ;18.166 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    56 ;23.242 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1755 ; 0.128 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 12347 ; 0.008 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  2053 ; 0.001 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  7020 ; 1.052 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2867 ; 0.247 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11295 ; 1.927 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4000 ; 3.101 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3705 ; 4.911 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 4
REMARK   3
REMARK   3   TLS GROUP : 1
REMARK   3    NUMBER OF COMPONENTS GROUP : 4
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A     2        A   100
REMARK   3    RESIDUE RANGE :   A   101        A   200
REMARK   3    RESIDUE RANGE :   A   201        A   300
REMARK   3    RESIDUE RANGE :   A   301        A   363
REMARK   3    ORIGIN FOR THE GROUP (A):  44.0560  26.3660  49.0370
REMARK   3    T TENSOR
REMARK   3      T11:   0.1059 T22:   0.0156
REMARK   3      T33:   0.0535 T12:  -0.0064
REMARK   3      T13:   0.0527 T23:  -0.0004
REMARK   3    L TENSOR
REMARK   3      L11:   0.4112 L22:   0.7188
REMARK   3      L33:   0.8869 L12:   0.1618
REMARK   3      L13:  -0.1329 L23:  -0.6823
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0270 S12:   0.0204 S13:  -0.0227
REMARK   3      S21:  -0.0349 S22:   0.0664 S23:   0.0523
REMARK   3      S31:   0.1236 S32:  -0.0519 S33:  -0.0394
REMARK   3
REMARK   3   TLS GROUP : 2
REMARK   3    NUMBER OF COMPONENTS GROUP : 4
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B     2        B   100
REMARK   3    RESIDUE RANGE :   B   101        B   200
REMARK   3    RESIDUE RANGE :   B   201        B   300
REMARK   3    RESIDUE RANGE :   B   301        B   363
REMARK   3    ORIGIN FOR THE GROUP (A):  62.9590  43.5170  36.6810
REMARK   3    T TENSOR
REMARK   3      T11:   0.0653 T22:   0.0749
REMARK   3      T33:   0.0644 T12:  -0.0139
REMARK   3      T13:   0.0422 T23:   0.0004
REMARK   3    L TENSOR
REMARK   3      L11:   1.2044 L22:   0.2018
REMARK   3      L33:   0.4110 L12:   0.0241
REMARK   3      L13:   0.1340 L23:  -0.2137
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0563 S12:   0.1117 S13:   0.1559
REMARK   3      S21:   0.0059 S22:   0.0455 S23:   0.0156
REMARK   3      S31:   0.0087 S32:   0.0557 S33:   0.0109
REMARK   3
REMARK   3   TLS GROUP : 3
REMARK   3    NUMBER OF COMPONENTS GROUP : 4
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   C     2        C   100
REMARK   3    RESIDUE RANGE :   C   101        C   200
REMARK   3    RESIDUE RANGE :   C   201        C   300
REMARK   3    RESIDUE RANGE :   C   301        C   364
REMARK   3    ORIGIN FOR THE GROUP (A):  92.2480  34.4490   2.5640
REMARK   3    T TENSOR
REMARK   3      T11:   0.0378 T22:   0.0469
REMARK   3      T33:   0.0787 T12:   0.0107
REMARK   3      T13:   0.0267 T23:  -0.0239
REMARK   3    L TENSOR
REMARK   3      L11:   0.5407 L22:   0.3529
REMARK   3      L33:   0.8511 L12:   0.1603
REMARK   3      L13:  -0.2339 L23:  -0.0748
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0392 S12:   0.0313 S13:  -0.0761
REMARK   3      S21:  -0.0399 S22:  -0.0764 S23:   0.0717
REMARK   3      S31:   0.1385 S32:  -0.0386 S33:   0.1155
REMARK   3
REMARK   3   TLS GROUP : 4
REMARK   3    NUMBER OF COMPONENTS GROUP : 4
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   D     3        D   100
REMARK   3    RESIDUE RANGE :   D   101        D   200
REMARK   3    RESIDUE RANGE :   D   201        D   300
REMARK   3    RESIDUE RANGE :   D   301        D   363
REMARK   3    ORIGIN FOR THE GROUP (A): 108.5330  57.3570   5.6250
REMARK   3    T TENSOR
REMARK   3      T11:   0.0066 T22:   0.0845
REMARK   3      T33:   0.1119 T12:   0.0138
REMARK   3      T13:   0.0135 T23:   0.0523
REMARK   3    L TENSOR
REMARK   3      L11:   0.8494 L22:   0.5663
REMARK   3      L33:   0.4012 L12:   0.4847
REMARK   3      L13:  -0.2587 L23:  -0.1912
REMARK   3    S TENSOR
REMARK   3      S11:   0.0276 S12:   0.0161 S13:   0.1346
REMARK   3      S21:   0.0266 S22:  -0.0726 S23:   0.0344
REMARK   3      S31:   0.0186 S32:   0.0579 S33:   0.0450
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 3I12 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUN-09.
REMARK 100 THE RCSB ID CODE IS RCSB053830.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 02-DEC-08
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 19-ID
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9794, 0.9796
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL3000
REMARK 200  DATA SCALING SOFTWARE          : HKL3000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 82073
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200
REMARK 200  RESOLUTION RANGE LOW       (A) : 115.470
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9
REMARK 200  DATA REDUNDANCY                : 9.800
REMARK 200  R MERGE                    (I) : 0.08800
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 29.5600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.26
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.8
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.00
REMARK 200  R MERGE FOR SHELL          (I) : 0.79900
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.340
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: HKL3000_SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 54.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, 25% PEG3350, PH 7.5, VAPOR
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 289K
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       42.57650
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      115.44650
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.90650
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      115.44650
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       42.57650
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.90650
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 5960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 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: 5790 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27660 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     MET A     1
REMARK 465     TYR A   254
REMARK 465     ALA A   255
REMARK 465     MET A   364
REMARK 465     ASN B   250
REMARK 465     SER B   251
REMARK 465     GLU B   252
REMARK 465     PHE B   253
REMARK 465     TYR B   254
REMARK 465     ALA B   255
REMARK 465     TYR B   256
REMARK 465     ASP B   257
REMARK 465     THR B   258
REMARK 465     LYS B   259
REMARK 465     TYR B   260
REMARK 465     ILE B   261
REMARK 465     ASP B   262
REMARK 465     ASP B   263
REMARK 465     ASN B   264
REMARK 465     GLY B   265
REMARK 465     ALA B   266
REMARK 465     MET B   364
REMARK 465     MET C     1
REMARK 465     ASN C   250
REMARK 465     SER C   251
REMARK 465     GLU C   252
REMARK 465     PHE C   253
REMARK 465     TYR C   254
REMARK 465     ALA C   255
REMARK 465     TYR C   256
REMARK 465     ASP C   257
REMARK 465     THR C   258
REMARK 465     LYS C   259
REMARK 465     TYR C   260
REMARK 465     ILE C   261
REMARK 465     ASP C   262
REMARK 465     ASP C   263
REMARK 465     ASN C   264
REMARK 465     MET D     1
REMARK 465     ALA D     2
REMARK 465     TYR D   254
REMARK 465     ALA D   255
REMARK 465     TYR D   256
REMARK 465     ASP D   257
REMARK 465     THR D   258
REMARK 465     LYS D   259
REMARK 465     MET D   364
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     SER A  72    OG
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   OE1  GLU D   315     O1A  ADP D   365              2.02
REMARK 500   NE2  GLN C   273     O    HOH C   381              2.09
REMARK 500   OG1  THR D   306     OD1  ASP D   308              2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500    ASP A  44   CB    ASP A  44   CG     -0.151
REMARK 500    GLU B 221   CB    GLU B 221   CG     -0.130
REMARK 500    GLU B 348   CB    GLU B 348   CG     -0.145
REMARK 500    ASP C  44   CB    ASP C  44   CG     -0.194
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    LEU A  41   CB  -  CG  -  CD1 ANGL. DEV. =  12.1 DEGREES
REMARK 500    ASP A  44   CB  -  CA  -  C   ANGL. DEV. = -17.0 DEGREES
REMARK 500    ASP A  44   CB  -  CG  -  OD1 ANGL. DEV. =  -6.6 DEGREES
REMARK 500    ARG A 353   CG  -  CD  -  NE  ANGL. DEV. = -16.8 DEGREES
REMARK 500    ARG A 353   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES
REMARK 500    ARG A 353   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.5 DEGREES
REMARK 500    VAL B 101   CB  -  CA  -  C   ANGL. DEV. = -12.8 DEGREES
REMARK 500    MET B 139   CG  -  SD  -  CE  ANGL. DEV. = -15.8 DEGREES
REMARK 500    ARG B 163   NE  -  CZ  -  NH1 ANGL. DEV. =   5.8 DEGREES
REMARK 500    ARG B 163   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.6 DEGREES
REMARK 500    ARG B 283   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES
REMARK 500    LEU B 293   CA  -  CB  -  CG  ANGL. DEV. = -14.5 DEGREES
REMARK 500    ASP C  44   CB  -  CG  -  OD1 ANGL. DEV. = -16.2 DEGREES
REMARK 500    ASP C  44   CB  -  CG  -  OD2 ANGL. DEV. =   8.1 DEGREES
REMARK 500    ALA C  54   N   -  CA  -  C   ANGL. DEV. =  21.4 DEGREES
REMARK 500    GLU C  55   N   -  CA  -  CB  ANGL. DEV. = -25.8 DEGREES
REMARK 500    VAL C 101   CB  -  CA  -  C   ANGL. DEV. = -12.0 DEGREES
REMARK 500    ARG C 146   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES
REMARK 500    ARG C 163   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.2 DEGREES
REMARK 500    ARG C 353   NE  -  CZ  -  NH1 ANGL. DEV. =   5.4 DEGREES
REMARK 500    ARG C 353   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.8 DEGREES
REMARK 500    VAL D 101   CB  -  CA  -  C   ANGL. DEV. = -12.7 DEGREES
REMARK 500    ARG D 146   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES
REMARK 500    MET D 298   CG  -  SD  -  CE  ANGL. DEV. = -15.2 DEGREES
REMARK 500    LEU D 319   CB  -  CG  -  CD1 ANGL. DEV. =  10.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    ASP A  32       91.81    -58.02
REMARK 500    ASP A  44      161.42    -46.98
REMARK 500    ILE A 105       32.87   -140.60
REMARK 500    GLN A 189     -128.37   -120.89
REMARK 500    SER A 192       -7.97     56.23
REMARK 500    ASN A 236      -82.50   -115.04
REMARK 500    THR A 258       43.57   -146.87
REMARK 500    ALA B   2      135.75    178.65
REMARK 500    ASP B  32       98.04    -66.30
REMARK 500    ASN B  56       67.58   -162.09
REMARK 500    HIS B  66      -15.82     83.84
REMARK 500    GLN B 189      154.96    176.27
REMARK 500    SER B 191       80.57    -11.26
REMARK 500    ASN B 236     -101.21   -110.23
REMARK 500    ASN B 238       76.20   -117.48
REMARK 500    ASP C  32       97.92    -64.96
REMARK 500    ASP C  44      157.66    -45.77
REMARK 500    ALA C  54      -35.78    -38.80
REMARK 500    ASN C  56       76.97   -159.49
REMARK 500    ASP C  63       95.97    -60.48
REMARK 500    HIS C  66       -7.11     99.64
REMARK 500    ASN C  92       -1.04   -142.99
REMARK 500    GLN C 189     -113.04   -136.41
REMARK 500    SER C 192       -7.45     43.72
REMARK 500    ASN C 236     -102.80   -110.54
REMARK 500    ASN C 238       70.28   -113.01
REMARK 500    SER D  14      146.94    -35.88
REMARK 500    LEU D  41       76.97   -109.24
REMARK 500    ASN D  56       78.65   -159.57
REMARK 500    ILE D 105       32.94   -141.01
REMARK 500    GLN D 189      -81.89   -142.55
REMARK 500    SER D 192       10.08     41.63
REMARK 500    ASN D 236      -81.99   -115.24
REMARK 500    ASN D 264       16.30     86.59
REMARK 500    ALA D 266      166.22    -48.29
REMARK 500    THR D 362      -61.20   -130.51
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 ASN C  188     GLN C  189                   64.25
REMARK 500 SER D  191     SER D  192                 -145.68
REMARK 500 VAL D  193     GLY D  194                  -64.25
REMARK 500 ASN D  264     GLY D  265                  -43.46
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 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
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    THR A 109        22.6      L          L   OUTSIDE RANGE
REMARK 500    THR B 109        23.9      L          L   OUTSIDE RANGE
REMARK 500    VAL B 128        22.8      L          L   OUTSIDE RANGE
REMARK 500    VAL B 143        20.7      L          L   OUTSIDE RANGE
REMARK 500    THR B 160        24.4      L          L   OUTSIDE RANGE
REMARK 500    SER B 191        24.3      L          L   OUTSIDE RANGE
REMARK 500    ALA C  54        14.9      L          L   OUTSIDE RANGE
REMARK 500    GLU C  55        54.3      L          L   OUTSIDE RANGE
REMARK 500    THR D 109        25.0      L          L   OUTSIDE RANGE
REMARK 500    VAL D 128        23.6      L          L   OUTSIDE RANGE
REMARK 500    VAL D 143        22.8      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 365
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 365
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 365
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP D 365
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: IDP00919   RELATED DB: TARGETDB
DBREF  3I12 A    1   364  UNP    P0A1F0   DDLA_SALTY       1    364
DBREF  3I12 B    1   364  UNP    P0A1F0   DDLA_SALTY       1    364
DBREF  3I12 C    1   364  UNP    P0A1F0   DDLA_SALTY       1    364
DBREF  3I12 D    1   364  UNP    P0A1F0   DDLA_SALTY       1    364
SEQRES   1 A  364  MET ALA LYS LEU ARG VAL GLY ILE VAL PHE GLY GLY LYS
SEQRES   2 A  364  SER ALA GLU HIS GLU VAL SER LEU GLN SER ALA LYS ASN
SEQRES   3 A  364  ILE VAL ASP ALA ILE ASP LYS THR ARG PHE ASP VAL VAL
SEQRES   4 A  364  LEU LEU GLY ILE ASP LYS ALA GLY GLN TRP HIS VAL ASN
SEQRES   5 A  364  ASP ALA GLU ASN TYR LEU GLN ASN ALA ASP ASP PRO ALA
SEQRES   6 A  364  HIS ILE ALA LEU ARG PRO SER ALA ILE SER LEU ALA GLN
SEQRES   7 A  364  VAL PRO GLY LYS HIS GLN HIS GLN LEU ILE ASN ALA GLN
SEQRES   8 A  364  ASN GLY GLN PRO LEU PRO THR VAL ASP VAL ILE PHE PRO
SEQRES   9 A  364  ILE VAL HIS GLY THR LEU GLY GLU ASP GLY SER LEU GLN
SEQRES  10 A  364  GLY MET LEU ARG VAL ALA ASN LEU PRO PHE VAL GLY SER
SEQRES  11 A  364  ASP VAL LEU SER SER ALA ALA CYS MET ASP LYS ASP VAL
SEQRES  12 A  364  ALA LYS ARG LEU LEU ARG ASP ALA GLY LEU ASN ILE ALA
SEQRES  13 A  364  PRO PHE ILE THR LEU THR ARG THR ASN ARG HIS ALA PHE
SEQRES  14 A  364  SER PHE ALA GLU VAL GLU SER ARG LEU GLY LEU PRO LEU
SEQRES  15 A  364  PHE VAL LYS PRO ALA ASN GLN GLY SER SER VAL GLY VAL
SEQRES  16 A  364  SER LYS VAL ALA ASN GLU ALA GLN TYR GLN GLN ALA VAL
SEQRES  17 A  364  ALA LEU ALA PHE GLU PHE ASP HIS LYS VAL VAL VAL GLU
SEQRES  18 A  364  GLN GLY ILE LYS GLY ARG GLU ILE GLU CYS ALA VAL LEU
SEQRES  19 A  364  GLY ASN ASP ASN PRO GLN ALA SER THR CYS GLY GLU ILE
SEQRES  20 A  364  VAL LEU ASN SER GLU PHE TYR ALA TYR ASP THR LYS TYR
SEQRES  21 A  364  ILE ASP ASP ASN GLY ALA GLN VAL VAL VAL PRO ALA GLN
SEQRES  22 A  364  ILE PRO SER GLU VAL ASN ASP LYS ILE ARG ALA ILE ALA
SEQRES  23 A  364  ILE GLN ALA TYR GLN THR LEU GLY CYS ALA GLY MET ALA
SEQRES  24 A  364  ARG VAL ASP VAL PHE LEU THR ALA ASP ASN GLU VAL VAL
SEQRES  25 A  364  ILE ASN GLU ILE ASN THR LEU PRO GLY PHE THR ASN ILE
SEQRES  26 A  364  SER MET TYR PRO LYS LEU TRP GLN ALA SER GLY LEU GLY
SEQRES  27 A  364  TYR THR ASP LEU ILE SER ARG LEU ILE GLU LEU ALA LEU
SEQRES  28 A  364  GLU ARG HIS THR ALA ASN ASN ALA LEU LYS THR THR MET
SEQRES   1 B  364  MET ALA LYS LEU ARG VAL GLY ILE VAL PHE GLY GLY LYS
SEQRES   2 B  364  SER ALA GLU HIS GLU VAL SER LEU GLN SER ALA LYS ASN
SEQRES   3 B  364  ILE VAL ASP ALA ILE ASP LYS THR ARG PHE ASP VAL VAL
SEQRES   4 B  364  LEU LEU GLY ILE ASP LYS ALA GLY GLN TRP HIS VAL ASN
SEQRES   5 B  364  ASP ALA GLU ASN TYR LEU GLN ASN ALA ASP ASP PRO ALA
SEQRES   6 B  364  HIS ILE ALA LEU ARG PRO SER ALA ILE SER LEU ALA GLN
SEQRES   7 B  364  VAL PRO GLY LYS HIS GLN HIS GLN LEU ILE ASN ALA GLN
SEQRES   8 B  364  ASN GLY GLN PRO LEU PRO THR VAL ASP VAL ILE PHE PRO
SEQRES   9 B  364  ILE VAL HIS GLY THR LEU GLY GLU ASP GLY SER LEU GLN
SEQRES  10 B  364  GLY MET LEU ARG VAL ALA ASN LEU PRO PHE VAL GLY SER
SEQRES  11 B  364  ASP VAL LEU SER SER ALA ALA CYS MET ASP LYS ASP VAL
SEQRES  12 B  364  ALA LYS ARG LEU LEU ARG ASP ALA GLY LEU ASN ILE ALA
SEQRES  13 B  364  PRO PHE ILE THR LEU THR ARG THR ASN ARG HIS ALA PHE
SEQRES  14 B  364  SER PHE ALA GLU VAL GLU SER ARG LEU GLY LEU PRO LEU
SEQRES  15 B  364  PHE VAL LYS PRO ALA ASN GLN GLY SER SER VAL GLY VAL
SEQRES  16 B  364  SER LYS VAL ALA ASN GLU ALA GLN TYR GLN GLN ALA VAL
SEQRES  17 B  364  ALA LEU ALA PHE GLU PHE ASP HIS LYS VAL VAL VAL GLU
SEQRES  18 B  364  GLN GLY ILE LYS GLY ARG GLU ILE GLU CYS ALA VAL LEU
SEQRES  19 B  364  GLY ASN ASP ASN PRO GLN ALA SER THR CYS GLY GLU ILE
SEQRES  20 B  364  VAL LEU ASN SER GLU PHE TYR ALA TYR ASP THR LYS TYR
SEQRES  21 B  364  ILE ASP ASP ASN GLY ALA GLN VAL VAL VAL PRO ALA GLN
SEQRES  22 B  364  ILE PRO SER GLU VAL ASN ASP LYS ILE ARG ALA ILE ALA
SEQRES  23 B  364  ILE GLN ALA TYR GLN THR LEU GLY CYS ALA GLY MET ALA
SEQRES  24 B  364  ARG VAL ASP VAL PHE LEU THR ALA ASP ASN GLU VAL VAL
SEQRES  25 B  364  ILE ASN GLU ILE ASN THR LEU PRO GLY PHE THR ASN ILE
SEQRES  26 B  364  SER MET TYR PRO LYS LEU TRP GLN ALA SER GLY LEU GLY
SEQRES  27 B  364  TYR THR ASP LEU ILE SER ARG LEU ILE GLU LEU ALA LEU
SEQRES  28 B  364  GLU ARG HIS THR ALA ASN ASN ALA LEU LYS THR THR MET
SEQRES   1 C  364  MET ALA LYS LEU ARG VAL GLY ILE VAL PHE GLY GLY LYS
SEQRES   2 C  364  SER ALA GLU HIS GLU VAL SER LEU GLN SER ALA LYS ASN
SEQRES   3 C  364  ILE VAL ASP ALA ILE ASP LYS THR ARG PHE ASP VAL VAL
SEQRES   4 C  364  LEU LEU GLY ILE ASP LYS ALA GLY GLN TRP HIS VAL ASN
SEQRES   5 C  364  ASP ALA GLU ASN TYR LEU GLN ASN ALA ASP ASP PRO ALA
SEQRES   6 C  364  HIS ILE ALA LEU ARG PRO SER ALA ILE SER LEU ALA GLN
SEQRES   7 C  364  VAL PRO GLY LYS HIS GLN HIS GLN LEU ILE ASN ALA GLN
SEQRES   8 C  364  ASN GLY GLN PRO LEU PRO THR VAL ASP VAL ILE PHE PRO
SEQRES   9 C  364  ILE VAL HIS GLY THR LEU GLY GLU ASP GLY SER LEU GLN
SEQRES  10 C  364  GLY MET LEU ARG VAL ALA ASN LEU PRO PHE VAL GLY SER
SEQRES  11 C  364  ASP VAL LEU SER SER ALA ALA CYS MET ASP LYS ASP VAL
SEQRES  12 C  364  ALA LYS ARG LEU LEU ARG ASP ALA GLY LEU ASN ILE ALA
SEQRES  13 C  364  PRO PHE ILE THR LEU THR ARG THR ASN ARG HIS ALA PHE
SEQRES  14 C  364  SER PHE ALA GLU VAL GLU SER ARG LEU GLY LEU PRO LEU
SEQRES  15 C  364  PHE VAL LYS PRO ALA ASN GLN GLY SER SER VAL GLY VAL
SEQRES  16 C  364  SER LYS VAL ALA ASN GLU ALA GLN TYR GLN GLN ALA VAL
SEQRES  17 C  364  ALA LEU ALA PHE GLU PHE ASP HIS LYS VAL VAL VAL GLU
SEQRES  18 C  364  GLN GLY ILE LYS GLY ARG GLU ILE GLU CYS ALA VAL LEU
SEQRES  19 C  364  GLY ASN ASP ASN PRO GLN ALA SER THR CYS GLY GLU ILE
SEQRES  20 C  364  VAL LEU ASN SER GLU PHE TYR ALA TYR ASP THR LYS TYR
SEQRES  21 C  364  ILE ASP ASP ASN GLY ALA GLN VAL VAL VAL PRO ALA GLN
SEQRES  22 C  364  ILE PRO SER GLU VAL ASN ASP LYS ILE ARG ALA ILE ALA
SEQRES  23 C  364  ILE GLN ALA TYR GLN THR LEU GLY CYS ALA GLY MET ALA
SEQRES  24 C  364  ARG VAL ASP VAL PHE LEU THR ALA ASP ASN GLU VAL VAL
SEQRES  25 C  364  ILE ASN GLU ILE ASN THR LEU PRO GLY PHE THR ASN ILE
SEQRES  26 C  364  SER MET TYR PRO LYS LEU TRP GLN ALA SER GLY LEU GLY
SEQRES  27 C  364  TYR THR ASP LEU ILE SER ARG LEU ILE GLU LEU ALA LEU
SEQRES  28 C  364  GLU ARG HIS THR ALA ASN ASN ALA LEU LYS THR THR MET
SEQRES   1 D  364  MET ALA LYS LEU ARG VAL GLY ILE VAL PHE GLY GLY LYS
SEQRES   2 D  364  SER ALA GLU HIS GLU VAL SER LEU GLN SER ALA LYS ASN
SEQRES   3 D  364  ILE VAL ASP ALA ILE ASP LYS THR ARG PHE ASP VAL VAL
SEQRES   4 D  364  LEU LEU GLY ILE ASP LYS ALA GLY GLN TRP HIS VAL ASN
SEQRES   5 D  364  ASP ALA GLU ASN TYR LEU GLN ASN ALA ASP ASP PRO ALA
SEQRES   6 D  364  HIS ILE ALA LEU ARG PRO SER ALA ILE SER LEU ALA GLN
SEQRES   7 D  364  VAL PRO GLY LYS HIS GLN HIS GLN LEU ILE ASN ALA GLN
SEQRES   8 D  364  ASN GLY GLN PRO LEU PRO THR VAL ASP VAL ILE PHE PRO
SEQRES   9 D  364  ILE VAL HIS GLY THR LEU GLY GLU ASP GLY SER LEU GLN
SEQRES  10 D  364  GLY MET LEU ARG VAL ALA ASN LEU PRO PHE VAL GLY SER
SEQRES  11 D  364  ASP VAL LEU SER SER ALA ALA CYS MET ASP LYS ASP VAL
SEQRES  12 D  364  ALA LYS ARG LEU LEU ARG ASP ALA GLY LEU ASN ILE ALA
SEQRES  13 D  364  PRO PHE ILE THR LEU THR ARG THR ASN ARG HIS ALA PHE
SEQRES  14 D  364  SER PHE ALA GLU VAL GLU SER ARG LEU GLY LEU PRO LEU
SEQRES  15 D  364  PHE VAL LYS PRO ALA ASN GLN GLY SER SER VAL GLY VAL
SEQRES  16 D  364  SER LYS VAL ALA ASN GLU ALA GLN TYR GLN GLN ALA VAL
SEQRES  17 D  364  ALA LEU ALA PHE GLU PHE ASP HIS LYS VAL VAL VAL GLU
SEQRES  18 D  364  GLN GLY ILE LYS GLY ARG GLU ILE GLU CYS ALA VAL LEU
SEQRES  19 D  364  GLY ASN ASP ASN PRO GLN ALA SER THR CYS GLY GLU ILE
SEQRES  20 D  364  VAL LEU ASN SER GLU PHE TYR ALA TYR ASP THR LYS TYR
SEQRES  21 D  364  ILE ASP ASP ASN GLY ALA GLN VAL VAL VAL PRO ALA GLN
SEQRES  22 D  364  ILE PRO SER GLU VAL ASN ASP LYS ILE ARG ALA ILE ALA
SEQRES  23 D  364  ILE GLN ALA TYR GLN THR LEU GLY CYS ALA GLY MET ALA
SEQRES  24 D  364  ARG VAL ASP VAL PHE LEU THR ALA ASP ASN GLU VAL VAL
SEQRES  25 D  364  ILE ASN GLU ILE ASN THR LEU PRO GLY PHE THR ASN ILE
SEQRES  26 D  364  SER MET TYR PRO LYS LEU TRP GLN ALA SER GLY LEU GLY
SEQRES  27 D  364  TYR THR ASP LEU ILE SER ARG LEU ILE GLU LEU ALA LEU
SEQRES  28 D  364  GLU ARG HIS THR ALA ASN ASN ALA LEU LYS THR THR MET
HET    ADP  A 365      27
HET    ADP  B 365      27
HET    ADP  C 365      27
HET    ADP  D 365      27
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE
FORMUL   5  ADP    4(C10 H15 N5 O10 P2)
FORMUL   9  HOH   *315(H2 O)
HELIX    1   1 GLU A   16  ILE A   31  1                                  16
HELIX    2   2 GLY A  114  ALA A  123  1                                  10
HELIX    3   3 ASP A  131  ASP A  140  1                                  10
HELIX    4   4 ASP A  140  ALA A  151  1                                  12
HELIX    5   5 ASN A  165  PHE A  169  5                                   5
HELIX    6   6 SER A  170  GLY A  179  1                                  10
HELIX    7   7 ASN A  200  ASP A  215  1                                  16
HELIX    8   8 ILE A  261  ALA A  266  5                                   6
HELIX    9   9 PRO A  275  LEU A  293  1                                  19
HELIX   10  10 SER A  326  ALA A  334  1                                   9
HELIX   11  11 GLY A  338  LEU A  360  1                                  23
HELIX   12  12 GLU B   16  ILE B   31  1                                  16
HELIX   13  13 GLY B  114  ALA B  123  1                                  10
HELIX   14  14 ASP B  131  ASP B  140  1                                  10
HELIX   15  15 ASP B  140  ALA B  151  1                                  12
HELIX   16  16 SER B  170  GLY B  179  1                                  10
HELIX   17  17 ASN B  200  PHE B  212  1                                  13
HELIX   18  18 PRO B  275  LEU B  293  1                                  19
HELIX   19  19 SER B  326  ALA B  334  1                                   9
HELIX   20  20 GLY B  338  ALA B  359  1                                  22
HELIX   21  21 GLU C   16  ILE C   31  1                                  16
HELIX   22  22 GLY C  108  ASP C  113  1                                   6
HELIX   23  23 GLY C  114  ALA C  123  1                                  10
HELIX   24  24 ASP C  131  ASP C  140  1                                  10
HELIX   25  25 ASP C  140  ALA C  151  1                                  12
HELIX   26  26 SER C  170  GLY C  179  1                                  10
HELIX   27  27 ASN C  200  PHE C  212  1                                  13
HELIX   28  28 PRO C  275  LEU C  293  1                                  19
HELIX   29  29 SER C  326  ALA C  334  1                                   9
HELIX   30  30 GLY C  338  LEU C  360  1                                  23
HELIX   31  31 GLU D   16  ILE D   31  1                                  16
HELIX   32  32 GLY D  114  ALA D  123  1                                  10
HELIX   33  33 ASP D  131  ASP D  140  1                                  10
HELIX   34  34 ASP D  140  ALA D  151  1                                  12
HELIX   35  35 ASN D  165  PHE D  169  5                                   5
HELIX   36  36 SER D  170  GLY D  179  1                                  10
HELIX   37  37 ASN D  200  ASP D  215  1                                  16
HELIX   38  38 ILE D  261  ALA D  266  5                                   6
HELIX   39  39 PRO D  275  LEU D  293  1                                  19
HELIX   40  40 SER D  326  ALA D  334  1                                   9
HELIX   41  41 GLY D  338  LEU D  360  1                                  23
SHEET    1   A 4 TRP A  49  ASN A  52  0
SHEET    2   A 4 PHE A  36  ILE A  43 -1  N  LEU A  40   O  ASN A  52
SHEET    3   A 4 LEU A   4  GLY A  11  1  N  VAL A   6   O  ASP A  37
SHEET    4   A 4 VAL A 101  PRO A 104  1  O  PHE A 103   N  GLY A   7
SHEET    1   B 2 LEU A  76  GLN A  78  0
SHEET    2   B 2 LEU A  87  ASN A  89 -1  O  ILE A  88   N  ALA A  77
SHEET    1   C 4 PHE A 158  THR A 162  0
SHEET    2   C 4 LYS A 217  GLN A 222 -1  O  VAL A 218   N  LEU A 161
SHEET    3   C 4 LEU A 182  PRO A 186 -1  N  LYS A 185   O  VAL A 219
SHEET    4   C 4 SER A 196  VAL A 198 -1  O  VAL A 198   N  LEU A 182
SHEET    1   D 5 GLN A 267  VAL A 269  0
SHEET    2   D 5 GLN A 240  VAL A 248 -1  N  GLU A 246   O  VAL A 269
SHEET    3   D 5 ARG A 227  GLY A 235 -1  N  LEU A 234   O  GLN A 240
SHEET    4   D 5 GLY A 297  LEU A 305 -1  O  VAL A 303   N  ILE A 229
SHEET    5   D 5 VAL A 311  ASN A 317 -1  O  VAL A 312   N  PHE A 304
SHEET    1   E 4 TRP B  49  ASN B  52  0
SHEET    2   E 4 PHE B  36  ILE B  43 -1  N  LEU B  40   O  ASN B  52
SHEET    3   E 4 LEU B   4  GLY B  11  1  N  PHE B  10   O  ILE B  43
SHEET    4   E 4 VAL B 101  PRO B 104  1  O  PHE B 103   N  GLY B   7
SHEET    1   F 2 LEU B  58  GLN B  59  0
SHEET    2   F 2 ALA B  68  LEU B  69 -1  O  ALA B  68   N  GLN B  59
SHEET    1   G 2 LEU B  76  GLN B  78  0
SHEET    2   G 2 LEU B  87  ASN B  89 -1  O  ILE B  88   N  ALA B  77
SHEET    1   H 4 PHE B 158  THR B 162  0
SHEET    2   H 4 LYS B 217  GLN B 222 -1  O  VAL B 218   N  LEU B 161
SHEET    3   H 4 LEU B 182  PRO B 186 -1  N  LYS B 185   O  VAL B 219
SHEET    4   H 4 SER B 196  VAL B 198 -1  O  VAL B 198   N  LEU B 182
SHEET    1   I 5 VAL B 268  VAL B 269  0
SHEET    2   I 5 GLN B 240  ILE B 247 -1  N  GLU B 246   O  VAL B 269
SHEET    3   I 5 ARG B 227  GLY B 235 -1  N  ALA B 232   O  SER B 242
SHEET    4   I 5 GLY B 297  LEU B 305 -1  O  ALA B 299   N  VAL B 233
SHEET    5   I 5 VAL B 311  ASN B 317 -1  O  VAL B 312   N  PHE B 304
SHEET    1   J 4 TRP C  49  ASN C  52  0
SHEET    2   J 4 PHE C  36  ILE C  43 -1  N  LEU C  40   O  ASN C  52
SHEET    3   J 4 LEU C   4  GLY C  11  1  N  PHE C  10   O  ILE C  43
SHEET    4   J 4 VAL C 101  PRO C 104  1  O  VAL C 101   N  GLY C   7
SHEET    1   K 2 LEU C  58  GLN C  59  0
SHEET    2   K 2 ALA C  68  LEU C  69 -1  O  ALA C  68   N  GLN C  59
SHEET    1   L 2 LEU C  76  GLN C  78  0
SHEET    2   L 2 LEU C  87  ASN C  89 -1  O  ILE C  88   N  ALA C  77
SHEET    1   M 4 PHE C 158  THR C 162  0
SHEET    2   M 4 LYS C 217  GLN C 222 -1  O  VAL C 218   N  LEU C 161
SHEET    3   M 4 LEU C 182  PRO C 186 -1  N  LYS C 185   O  VAL C 219
SHEET    4   M 4 SER C 196  VAL C 198 -1  O  VAL C 198   N  LEU C 182
SHEET    1   N 4 GLN C 240  ALA C 241  0
SHEET    2   N 4 ARG C 227  GLY C 235 -1  N  LEU C 234   O  GLN C 240
SHEET    3   N 4 GLY C 245  VAL C 248 -1  O  GLY C 245   N  GLU C 230
SHEET    4   N 4 GLN C 267  VAL C 269 -1  O  VAL C 269   N  GLU C 246
SHEET    1   O 4 GLN C 240  ALA C 241  0
SHEET    2   O 4 ARG C 227  GLY C 235 -1  N  LEU C 234   O  GLN C 240
SHEET    3   O 4 GLY C 297  LEU C 305 -1  O  VAL C 301   N  CYS C 231
SHEET    4   O 4 VAL C 311  ASN C 317 -1  O  VAL C 312   N  PHE C 304
SHEET    1   P 4 TRP D  49  ASN D  52  0
SHEET    2   P 4 PHE D  36  ILE D  43 -1  N  LEU D  40   O  ASN D  52
SHEET    3   P 4 LEU D   4  GLY D  11  1  N  ILE D   8   O  LEU D  41
SHEET    4   P 4 VAL D 101  PRO D 104  1  O  VAL D 101   N  GLY D   7
SHEET    1   Q 2 LEU D  58  GLN D  59  0
SHEET    2   Q 2 ALA D  68  LEU D  69 -1  O  ALA D  68   N  GLN D  59
SHEET    1   R 2 LEU D  76  GLN D  78  0
SHEET    2   R 2 LEU D  87  ASN D  89 -1  O  ILE D  88   N  ALA D  77
SHEET    1   S 4 PHE D 158  THR D 162  0
SHEET    2   S 4 LYS D 217  GLN D 222 -1  O  VAL D 218   N  LEU D 161
SHEET    3   S 4 LEU D 182  PRO D 186 -1  N  LYS D 185   O  VAL D 219
SHEET    4   S 4 SER D 196  VAL D 198 -1  O  VAL D 198   N  LEU D 182
SHEET    1   T 5 GLN D 267  VAL D 269  0
SHEET    2   T 5 GLN D 240  VAL D 248 -1  N  GLU D 246   O  VAL D 269
SHEET    3   T 5 ARG D 227  GLY D 235 -1  N  ALA D 232   O  SER D 242
SHEET    4   T 5 GLY D 297  LEU D 305 -1  O  ALA D 299   N  VAL D 233
SHEET    5   T 5 VAL D 311  ASN D 317 -1  O  VAL D 312   N  PHE D 304
CISPEP   1 LEU A  180    PRO A  181          0         3.06
CISPEP   2 VAL A  270    PRO A  271          0         1.74
CISPEP   3 LEU B  180    PRO B  181          0        -6.03
CISPEP   4 VAL B  270    PRO B  271          0        -0.19
CISPEP   5 LEU C  180    PRO C  181          0       -11.97
CISPEP   6 VAL C  270    PRO C  271          0       -10.32
CISPEP   7 LEU D  180    PRO D  181          0        -7.94
CISPEP   8 GLY D  190    SER D  191          0        19.41
CISPEP   9 VAL D  270    PRO D  271          0        -1.83
SITE     1 AC1 17 LYS A 141  PHE A 183  LYS A 185  GLY A 190
SITE     2 AC1 17 SER A 191  SER A 192  GLU A 221  GLN A 222
SITE     3 AC1 17 GLY A 223  ILE A 224  GLU A 228  LEU A 249
SITE     4 AC1 17 PHE A 304  ASN A 314  GLU A 315  HOH A 371
SITE     5 AC1 17 HOH A 374
SITE     1 AC2 14 LYS B 141  PHE B 183  LYS B 185  GLY B 190
SITE     2 AC2 14 SER B 191  SER B 192  GLU B 221  GLN B 222
SITE     3 AC2 14 GLY B 223  ILE B 224  GLU B 228  PHE B 304
SITE     4 AC2 14 ASN B 314  GLU B 315
SITE     1 AC3 13 PHE C 183  LYS C 185  GLY C 190  SER C 191
SITE     2 AC3 13 SER C 192  GLU C 221  GLN C 222  GLY C 223
SITE     3 AC3 13 ILE C 224  GLU C 228  PHE C 304  ASN C 314
SITE     4 AC3 13 GLU C 315
SITE     1 AC4 16 LYS D 141  PHE D 183  LYS D 185  SER D 191
SITE     2 AC4 16 SER D 192  GLU D 221  GLN D 222  GLY D 223
SITE     3 AC4 16 ILE D 224  GLU D 228  LEU D 249  PHE D 304
SITE     4 AC4 16 ASN D 314  GLU D 315  HOH D 415  HOH D 443
CRYST1   85.153   85.813  230.893  90.00  90.00  90.00 P 21 21 21   16
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      0.011744  0.000000  0.000000        0.00000
SCALE2      0.000000  0.011653  0.000000        0.00000
SCALE3      0.000000  0.000000  0.004331        0.00000
      
PROCHECK
Go to PROCHECK summary
 References