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PDBsum entry 2i87

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Ligase PDB id
2i87
Jmol
Contents
Protein chains
345 a.a.
Ligands
SO4 ×2
Waters ×91
HEADER    LIGASE                                  01-SEP-06   2I87
TITLE     ALLOSTERIC INHIBITION OF STAPHYLOCOCCUS AUREUS D-ALANINE:D-ALANINE
TITLE    2 LIGASE REVEALED BY CRYSTALLOGRAPHIC STUDIES
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: D-ALANINE-D-ALANINE LIGASE;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: D-ALANYLALANINE SYNTHETASE, D-ALA-D-ALA LIGASE;
COMPND   5 EC: 6.3.2.4;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS;
SOURCE   3 ORGANISM_TAXID: 93062;
SOURCE   4 STRAIN: COL;
SOURCE   5 GENE: DDL;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: M15[PREP4];
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PQE-60
KEYWDS    D-ALANINE:D-ALANINE LIGASE, APO, LIGASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.LIU,J.S.CHANG,J.T.HERBERG,M.HORNG,P.K.TOMICH,A.H.LIN,K.R.MAROTTI
REVDAT   4   13-JUL-11 2I87    1       VERSN
REVDAT   3   24-FEB-09 2I87    1       VERSN
REVDAT   2   24-OCT-06 2I87    1       JRNL
REVDAT   1   03-OCT-06 2I87    0
JRNL        AUTH   S.LIU,J.S.CHANG,J.T.HERBERG,M.M.HORNG,P.K.TOMICH,A.H.LIN,
JRNL        AUTH 2 K.R.MAROTTI
JRNL        TITL   ALLOSTERIC INHIBITION OF STAPHYLOCOCCUS AUREUS
JRNL        TITL 2 D-ALANINE:D-ALANINE LIGASE REVEALED BY CRYSTALLOGRAPHIC
JRNL        TITL 3 STUDIES.
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 103 15178 2006
JRNL        REFN                   ISSN 0027-8424
JRNL        PMID   17015835
JRNL        DOI    10.1073/PNAS.0604905103
REMARK   2
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.3.0008
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 79.06
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6
REMARK   3   NUMBER OF REFLECTIONS             : 44470
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) : 0.202
REMARK   3   R VALUE            (WORKING SET) : 0.200
REMARK   3   FREE R VALUE                     : 0.241
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 2336
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) : 2.00
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3276
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.63
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1880
REMARK   3   BIN FREE R VALUE SET COUNT          : 181
REMARK   3   BIN FREE R VALUE                    : 0.2560
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 5479
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 10
REMARK   3   SOLVENT ATOMS            : 91
REMARK   3
REMARK   3  B VALUES.
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL
REMARK   3   FROM WILSON PLOT           (A**2) : 37.80
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.84
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.07000
REMARK   3    B22 (A**2) : 0.27000
REMARK   3    B33 (A**2) : -0.20000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.01000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.204
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.174
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.121
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.699
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.944
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.920
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5593 ; 0.024 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  3746 ; 0.001 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7567 ; 1.991 ; 1.967
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9214 ; 1.034 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   683 ; 7.330 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   277 ;39.448 ;25.957
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1001 ;16.746 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;17.457 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   839 ; 0.128 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6195 ; 0.008 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  1033 ; 0.001 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1276 ; 0.230 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  4000 ; 0.206 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2750 ; 0.194 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  3100 ; 0.097 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   195 ; 0.170 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):     2 ; 0.013 ; 0.200
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):    37 ; 0.248 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):    58 ; 0.221 ; 0.200
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    10 ; 0.278 ; 0.200
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):  4305 ; 1.567 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1388 ; 0.357 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5534 ; 1.933 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2471 ; 3.074 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2033 ; 4.256 ; 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  : 6
REMARK   3
REMARK   3   TLS GROUP : 1
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A     3        A   125
REMARK   3    ORIGIN FOR THE GROUP (A):  26.1095   0.0007  -5.1906
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0912 T22:  -0.0183
REMARK   3      T33:  -0.0665 T12:   0.0001
REMARK   3      T13:   0.0216 T23:   0.0125
REMARK   3    L TENSOR
REMARK   3      L11:   2.8176 L22:   1.0428
REMARK   3      L33:   3.8172 L12:   0.0960
REMARK   3      L13:  -1.1314 L23:  -0.5410
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0808 S12:   0.2836 S13:  -0.1780
REMARK   3      S21:  -0.1294 S22:  -0.0572 S23:  -0.1273
REMARK   3      S31:   0.3010 S32:   0.1069 S33:   0.1380
REMARK   3
REMARK   3   TLS GROUP : 2
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   126        A   219
REMARK   3    ORIGIN FOR THE GROUP (A):  10.0311 -16.9728  20.9210
REMARK   3    T TENSOR
REMARK   3      T11:   0.0290 T22:  -0.0949
REMARK   3      T33:  -0.0577 T12:  -0.1019
REMARK   3      T13:  -0.0025 T23:  -0.0197
REMARK   3    L TENSOR
REMARK   3      L11:   2.7842 L22:   1.9108
REMARK   3      L33:   2.3811 L12:  -0.7507
REMARK   3      L13:   1.0821 L23:  -0.8895
REMARK   3    S TENSOR
REMARK   3      S11:   0.1414 S12:  -0.0567 S13:  -0.2658
REMARK   3      S21:  -0.0581 S22:   0.0818 S23:   0.1248
REMARK   3      S31:   0.5534 S32:  -0.3375 S33:  -0.2232
REMARK   3
REMARK   3   TLS GROUP : 3
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   220        A   220
REMARK   3    ORIGIN FOR THE GROUP (A):   5.9584   1.6338   3.1506
REMARK   3    T TENSOR
REMARK   3      T11:  -0.1432 T22:  -0.0335
REMARK   3      T33:  -0.0202 T12:   0.0095
REMARK   3      T13:  -0.0153 T23:   0.0143
REMARK   3    L TENSOR
REMARK   3      L11:   2.3343 L22:   1.9984
REMARK   3      L33:   1.6377 L12:   1.2442
REMARK   3      L13:  -0.3259 L23:  -0.0209
REMARK   3    S TENSOR
REMARK   3      S11:   0.0238 S12:   0.1753 S13:   0.1533
REMARK   3      S21:  -0.0569 S22:   0.0100 S23:   0.2097
REMARK   3      S31:  -0.0641 S32:  -0.2265 S33:  -0.0338
REMARK   3
REMARK   3   TLS GROUP : 4
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B     3        B   125
REMARK   3    ORIGIN FOR THE GROUP (A):  42.5284   2.4622  17.2792
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0702 T22:   0.0822
REMARK   3      T33:  -0.0433 T12:  -0.0660
REMARK   3      T13:  -0.0338 T23:   0.0996
REMARK   3    L TENSOR
REMARK   3      L11:   3.4722 L22:   0.8558
REMARK   3      L33:   3.1648 L12:   0.0115
REMARK   3      L13:   0.4896 L23:   0.9196
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0618 S12:   0.4833 S13:   0.2837
REMARK   3      S21:   0.0097 S22:   0.0337 S23:  -0.1253
REMARK   3      S31:  -0.3656 S32:   0.6357 S33:   0.0281
REMARK   3
REMARK   3   TLS GROUP : 5
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   126        B   219
REMARK   3    ORIGIN FOR THE GROUP (A):  10.9505  14.9154  26.2898
REMARK   3    T TENSOR
REMARK   3      T11:   0.0616 T22:  -0.0774
REMARK   3      T33:  -0.0117 T12:   0.0646
REMARK   3      T13:   0.0546 T23:  -0.0368
REMARK   3    L TENSOR
REMARK   3      L11:   0.7547 L22:   2.1390
REMARK   3      L33:   4.3812 L12:  -1.0082
REMARK   3      L13:   0.5391 L23:  -1.2032
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1099 S12:  -0.1268 S13:   0.0779
REMARK   3      S21:   0.3554 S22:   0.1852 S23:   0.0990
REMARK   3      S31:  -0.7323 S32:  -0.3419 S33:  -0.0753
REMARK   3
REMARK   3   TLS GROUP : 6
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   220        B   360
REMARK   3    ORIGIN FOR THE GROUP (A):  28.6661  -2.6782  32.9995
REMARK   3    T TENSOR
REMARK   3      T11:   0.0196 T22:  -0.1035
REMARK   3      T33:  -0.1024 T12:   0.0054
REMARK   3      T13:  -0.0153 T23:   0.0104
REMARK   3    L TENSOR
REMARK   3      L11:   1.8050 L22:   1.4840
REMARK   3      L33:   1.8605 L12:  -0.3121
REMARK   3      L13:  -0.0870 L23:   0.6152
REMARK   3    S TENSOR
REMARK   3      S11:   0.0029 S12:  -0.0648 S13:  -0.0218
REMARK   3      S21:   0.2393 S22:  -0.0528 S23:  -0.0226
REMARK   3      S31:   0.0319 S32:   0.1055 S33:   0.0499
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH 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 2I87 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-SEP-06.
REMARK 100 THE RCSB ID CODE IS RCSB039259.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 10-OCT-01
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 17-ID
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0
REMARK 200  MONOCHROMATOR                  : MIRROR
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46823
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 79.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7
REMARK 200  DATA REDUNDANCY                : 3.700
REMARK 200  R MERGE                    (I) : 0.00000
REMARK 200  R SYM                      (I) : 0.03800
REMARK 200   FOR THE DATA SET  : 26.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.05
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80
REMARK 200  R MERGE FOR SHELL          (I) : 0.16200
REMARK 200  R SYM FOR SHELL            (I) : 0.16200
REMARK 200   FOR SHELL         : 4.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB CODE 1EHI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 42.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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       33.20400
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 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: 4800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 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 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     THR A     2
REMARK 465     TYR A   246
REMARK 465     ASP A   247
REMARK 465     TYR A   248
REMARK 465     LYS A   249
REMARK 465     SER A   250
REMARK 465     LYS A   251
REMARK 465     TYR A   252
REMARK 465     LYS A   253
REMARK 465     ASP A   254
REMARK 465     GLY A   255
REMARK 465     LYS A   256
REMARK 465     HIS A   359
REMARK 465     HIS A   360
REMARK 465     HIS A   361
REMARK 465     HIS A   362
REMARK 465     HIS A   363
REMARK 465     HIS A   364
REMARK 465     MET B     1
REMARK 465     THR B     2
REMARK 465     ALA B    72
REMARK 465     ASN B    99
REMARK 465     GLY B   100
REMARK 465     TYR B   246
REMARK 465     ASP B   247
REMARK 465     TYR B   248
REMARK 465     LYS B   249
REMARK 465     SER B   250
REMARK 465     LYS B   251
REMARK 465     TYR B   252
REMARK 465     LYS B   253
REMARK 465     ASP B   254
REMARK 465     GLY B   255
REMARK 465     LYS B   256
REMARK 465     HIS B   361
REMARK 465     HIS B   362
REMARK 465     HIS B   363
REMARK 465     HIS B   364
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   NZ   LYS B   189     O    GLY B   327     2656     2.08
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    GLU A  18   CB    GLU A  18   CG      0.120
REMARK 500    GLU A 101   CB    GLU A 101   CG      0.134
REMARK 500    GLU A 101   CD    GLU A 101   OE1     0.078
REMARK 500    GLU A 222   CG    GLU A 222   CD     -0.183
REMARK 500    ASN B 192   CG    ASN B 192   ND2     0.169
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    ARG A 152   NE  -  CZ  -  NH1 ANGL. DEV. =   4.8 DEGREES
REMARK 500    ARG A 152   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES
REMARK 500    ARG A 219   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES
REMARK 500    GLU A 222   OE1 -  CD  -  OE2 ANGL. DEV. =   7.4 DEGREES
REMARK 500    ASP A 293   CB  -  CG  -  OD2 ANGL. DEV. =  -5.4 DEGREES
REMARK 500    LEU B 131   CB  -  CG  -  CD2 ANGL. DEV. = -10.4 DEGREES
REMARK 500    ARG B 219   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 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    LYS A  13       34.72    -69.89
REMARK 500    LEU A  67     -116.94     55.71
REMARK 500    LEU A  94       51.18   -111.64
REMARK 500    HIS A  96     -159.28    -97.81
REMARK 500    SER A 184       -0.80     57.46
REMARK 500    ASN A 228      -83.13   -116.43
REMARK 500    ASP A 356      -34.82    -38.73
REMARK 500    ALA B  15       35.39    -79.92
REMARK 500    ASN B  54       75.45     50.88
REMARK 500    ASN B 228      -86.37   -124.78
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 ALA B   15     GLU B   16                  143.83
REMARK 500 GLY B   97     PRO B   98                  149.18
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 SO4 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2I80   RELATED DB: PDB
REMARK 900 ALLOSTERIC INHIBITION OF STAPHYLOCOCCUS AUREUS D-ALANINE:D-
REMARK 900 ALANINE LIGASE REVEALED BY CRYSTALLOGRAPHIC STUDIES
REMARK 900 RELATED ID: 2I8C   RELATED DB: PDB
REMARK 900 ALLOSTERIC INHIBITION OF STAPHYLOCOCCUS AUREUS D-ALANINE:D-
REMARK 900 ALANINE LIGASE REVEALED BY CRYSTALLOGRAPHIC STUDIES
DBREF  2I87 A    1   356  UNP    Q5HEB7   DDL_STAAC        1    356
DBREF  2I87 B    1   356  UNP    Q5HEB7   DDL_STAAC        1    356
SEQADV 2I87 ARG A  357  UNP  Q5HEB7              CLONING ARTIFACT
SEQADV 2I87 SER A  358  UNP  Q5HEB7              CLONING ARTIFACT
SEQADV 2I87 HIS A  359  UNP  Q5HEB7              EXPRESSION TAG
SEQADV 2I87 HIS A  360  UNP  Q5HEB7              EXPRESSION TAG
SEQADV 2I87 HIS A  361  UNP  Q5HEB7              EXPRESSION TAG
SEQADV 2I87 HIS A  362  UNP  Q5HEB7              EXPRESSION TAG
SEQADV 2I87 HIS A  363  UNP  Q5HEB7              EXPRESSION TAG
SEQADV 2I87 HIS A  364  UNP  Q5HEB7              EXPRESSION TAG
SEQADV 2I87 ARG B  357  UNP  Q5HEB7              CLONING ARTIFACT
SEQADV 2I87 SER B  358  UNP  Q5HEB7              CLONING ARTIFACT
SEQADV 2I87 HIS B  359  UNP  Q5HEB7              EXPRESSION TAG
SEQADV 2I87 HIS B  360  UNP  Q5HEB7              EXPRESSION TAG
SEQADV 2I87 HIS B  361  UNP  Q5HEB7              EXPRESSION TAG
SEQADV 2I87 HIS B  362  UNP  Q5HEB7              EXPRESSION TAG
SEQADV 2I87 HIS B  363  UNP  Q5HEB7              EXPRESSION TAG
SEQADV 2I87 HIS B  364  UNP  Q5HEB7              EXPRESSION TAG
SEQRES   1 A  364  MET THR LYS GLU ASN ILE CYS ILE VAL PHE GLY GLY LYS
SEQRES   2 A  364  SER ALA GLU HIS GLU VAL SER ILE LEU THR ALA GLN ASN
SEQRES   3 A  364  VAL LEU ASN ALA ILE ASP LYS ASP LYS TYR HIS VAL ASP
SEQRES   4 A  364  ILE ILE TYR ILE THR ASN ASP GLY ASP TRP ARG LYS GLN
SEQRES   5 A  364  ASN ASN ILE THR ALA GLU ILE LYS SER THR ASP GLU LEU
SEQRES   6 A  364  HIS LEU GLU ASN GLY GLU ALA LEU GLU ILE SER GLN LEU
SEQRES   7 A  364  LEU LYS GLU SER SER SER GLY GLN PRO TYR ASP ALA VAL
SEQRES   8 A  364  PHE PRO LEU LEU HIS GLY PRO ASN GLY GLU ASP GLY THR
SEQRES   9 A  364  ILE GLN GLY LEU PHE GLU VAL LEU ASP VAL PRO TYR VAL
SEQRES  10 A  364  GLY ASN GLY VAL LEU SER ALA ALA SER SER MET ASP LYS
SEQRES  11 A  364  LEU VAL MET LYS GLN LEU PHE GLU HIS ARG GLY LEU PRO
SEQRES  12 A  364  GLN LEU PRO TYR ILE SER PHE LEU ARG SER GLU TYR GLU
SEQRES  13 A  364  LYS TYR GLU HIS ASN ILE LEU LYS LEU VAL ASN ASP LYS
SEQRES  14 A  364  LEU ASN TYR PRO VAL PHE VAL LYS PRO ALA ASN LEU GLY
SEQRES  15 A  364  SER SER VAL GLY ILE SER LYS CYS ASN ASN GLU ALA GLU
SEQRES  16 A  364  LEU LYS GLU GLY ILE LYS GLU ALA PHE GLN PHE ASP ARG
SEQRES  17 A  364  LYS LEU VAL ILE GLU GLN GLY VAL ASN ALA ARG GLU ILE
SEQRES  18 A  364  GLU VAL ALA VAL LEU GLY ASN ASP TYR PRO GLU ALA THR
SEQRES  19 A  364  TRP PRO GLY GLU VAL VAL LYS ASP VAL ALA PHE TYR ASP
SEQRES  20 A  364  TYR LYS SER LYS TYR LYS ASP GLY LYS VAL GLN LEU GLN
SEQRES  21 A  364  ILE PRO ALA ASP LEU ASP GLU ASP VAL GLN LEU THR LEU
SEQRES  22 A  364  ARG ASN MET ALA LEU GLU ALA PHE LYS ALA THR ASP CYS
SEQRES  23 A  364  SER GLY LEU VAL ARG ALA ASP PHE PHE VAL THR GLU ASP
SEQRES  24 A  364  ASN GLN ILE TYR ILE ASN GLU THR ASN ALA MET PRO GLY
SEQRES  25 A  364  PHE THR ALA PHE SER MET TYR PRO LYS LEU TRP GLU ASN
SEQRES  26 A  364  MET GLY LEU SER TYR PRO GLU LEU ILE THR LYS LEU ILE
SEQRES  27 A  364  GLU LEU ALA LYS GLU ARG HIS GLN ASP LYS GLN LYS ASN
SEQRES  28 A  364  LYS TYR LYS ILE ASP ARG SER HIS HIS HIS HIS HIS HIS
SEQRES   1 B  364  MET THR LYS GLU ASN ILE CYS ILE VAL PHE GLY GLY LYS
SEQRES   2 B  364  SER ALA GLU HIS GLU VAL SER ILE LEU THR ALA GLN ASN
SEQRES   3 B  364  VAL LEU ASN ALA ILE ASP LYS ASP LYS TYR HIS VAL ASP
SEQRES   4 B  364  ILE ILE TYR ILE THR ASN ASP GLY ASP TRP ARG LYS GLN
SEQRES   5 B  364  ASN ASN ILE THR ALA GLU ILE LYS SER THR ASP GLU LEU
SEQRES   6 B  364  HIS LEU GLU ASN GLY GLU ALA LEU GLU ILE SER GLN LEU
SEQRES   7 B  364  LEU LYS GLU SER SER SER GLY GLN PRO TYR ASP ALA VAL
SEQRES   8 B  364  PHE PRO LEU LEU HIS GLY PRO ASN GLY GLU ASP GLY THR
SEQRES   9 B  364  ILE GLN GLY LEU PHE GLU VAL LEU ASP VAL PRO TYR VAL
SEQRES  10 B  364  GLY ASN GLY VAL LEU SER ALA ALA SER SER MET ASP LYS
SEQRES  11 B  364  LEU VAL MET LYS GLN LEU PHE GLU HIS ARG GLY LEU PRO
SEQRES  12 B  364  GLN LEU PRO TYR ILE SER PHE LEU ARG SER GLU TYR GLU
SEQRES  13 B  364  LYS TYR GLU HIS ASN ILE LEU LYS LEU VAL ASN ASP LYS
SEQRES  14 B  364  LEU ASN TYR PRO VAL PHE VAL LYS PRO ALA ASN LEU GLY
SEQRES  15 B  364  SER SER VAL GLY ILE SER LYS CYS ASN ASN GLU ALA GLU
SEQRES  16 B  364  LEU LYS GLU GLY ILE LYS GLU ALA PHE GLN PHE ASP ARG
SEQRES  17 B  364  LYS LEU VAL ILE GLU GLN GLY VAL ASN ALA ARG GLU ILE
SEQRES  18 B  364  GLU VAL ALA VAL LEU GLY ASN ASP TYR PRO GLU ALA THR
SEQRES  19 B  364  TRP PRO GLY GLU VAL VAL LYS ASP VAL ALA PHE TYR ASP
SEQRES  20 B  364  TYR LYS SER LYS TYR LYS ASP GLY LYS VAL GLN LEU GLN
SEQRES  21 B  364  ILE PRO ALA ASP LEU ASP GLU ASP VAL GLN LEU THR LEU
SEQRES  22 B  364  ARG ASN MET ALA LEU GLU ALA PHE LYS ALA THR ASP CYS
SEQRES  23 B  364  SER GLY LEU VAL ARG ALA ASP PHE PHE VAL THR GLU ASP
SEQRES  24 B  364  ASN GLN ILE TYR ILE ASN GLU THR ASN ALA MET PRO GLY
SEQRES  25 B  364  PHE THR ALA PHE SER MET TYR PRO LYS LEU TRP GLU ASN
SEQRES  26 B  364  MET GLY LEU SER TYR PRO GLU LEU ILE THR LYS LEU ILE
SEQRES  27 B  364  GLU LEU ALA LYS GLU ARG HIS GLN ASP LYS GLN LYS ASN
SEQRES  28 B  364  LYS TYR LYS ILE ASP ARG SER HIS HIS HIS HIS HIS HIS
HET    SO4  A 401       5
HET    SO4  B 402       5
HETNAM     SO4 SULFATE ION
FORMUL   3  SO4    2(O4 S 2-)
FORMUL   5  HOH   *91(H2 O)
HELIX    1   1 GLU A   16  ALA A   30  1                                  15
HELIX    2   2 SER A   61  LEU A   65  5                                   5
HELIX    3   3 HIS A   66  GLY A   70  5                                   5
HELIX    4   4 SER A   76  GLU A   81  5                                   6
HELIX    5   5 GLY A  103  ASP A  113  1                                  11
HELIX    6   6 GLY A  120  ASP A  129  1                                  10
HELIX    7   7 ASP A  129  GLY A  141  1                                  13
HELIX    8   8 ARG A  152  LEU A  170  1                                  19
HELIX    9   9 ASN A  192  GLN A  205  1                                  14
HELIX   10  10 ASP A  266  THR A  284  1                                  19
HELIX   11  11 SER A  317  MET A  326  1                                  10
HELIX   12  12 SER A  329  SER A  358  1                                  30
HELIX   13  13 GLU B   16  ILE B   31  1                                  16
HELIX   14  14 SER B   61  HIS B   66  5                                   6
HELIX   15  15 GLU B   74  GLU B   81  1                                   8
HELIX   16  16 GLY B  103  ASP B  113  1                                  11
HELIX   17  17 GLY B  120  ASP B  129  1                                  10
HELIX   18  18 ASP B  129  GLY B  141  1                                  13
HELIX   19  19 ARG B  152  LEU B  170  1                                  19
HELIX   20  20 ASN B  192  PHE B  204  1                                  13
HELIX   21  21 ASP B  266  THR B  284  1                                  19
HELIX   22  22 SER B  317  MET B  326  1                                  10
HELIX   23  23 SER B  329  HIS B  360  1                                  32
SHEET    1   A 5 GLU A  71  LEU A  73  0
SHEET    2   A 5 TRP A  49  GLN A  52 -1  N  LYS A  51   O  GLU A  71
SHEET    3   A 5 TYR A  36  ILE A  43 -1  N  TYR A  42   O  ARG A  50
SHEET    4   A 5 GLU A   4  GLY A  11  1  N  GLU A   4   O  HIS A  37
SHEET    5   A 5 ALA A  90  LEU A  94  1  O  LEU A  94   N  VAL A   9
SHEET    1   B 4 TYR A 147  LEU A 151  0
SHEET    2   B 4 LYS A 209  GLN A 214 -1  O  ILE A 212   N  ILE A 148
SHEET    3   B 4 VAL A 174  PRO A 178 -1  N  LYS A 177   O  VAL A 211
SHEET    4   B 4 SER A 188  CYS A 190 -1  O  CYS A 190   N  VAL A 174
SHEET    1   C 4 GLU A 232  ALA A 233  0
SHEET    2   C 4 ARG A 219  GLY A 227 -1  N  LEU A 226   O  GLU A 232
SHEET    3   C 4 GLY A 237  VAL A 239 -1  O  GLY A 237   N  GLU A 222
SHEET    4   C 4 LEU A 259  GLN A 260 -1  O  GLN A 260   N  GLU A 238
SHEET    1   D 4 GLU A 232  ALA A 233  0
SHEET    2   D 4 ARG A 219  GLY A 227 -1  N  LEU A 226   O  GLU A 232
SHEET    3   D 4 GLY A 288  VAL A 296 -1  O  PHE A 294   N  ILE A 221
SHEET    4   D 4 ILE A 302  ASN A 308 -1  O  TYR A 303   N  PHE A 295
SHEET    1   E 4 TRP B  49  GLN B  52  0
SHEET    2   E 4 TYR B  36  ILE B  43 -1  N  ILE B  40   O  GLN B  52
SHEET    3   E 4 GLU B   4  GLY B  11  1  N  ILE B   6   O  HIS B  37
SHEET    4   E 4 ALA B  90  PRO B  93  1  O  PHE B  92   N  CYS B   7
SHEET    1   F 4 TYR B 147  LEU B 151  0
SHEET    2   F 4 LYS B 209  GLN B 214 -1  O  ILE B 212   N  ILE B 148
SHEET    3   F 4 VAL B 174  PRO B 178 -1  N  PHE B 175   O  GLU B 213
SHEET    4   F 4 SER B 188  CYS B 190 -1  O  CYS B 190   N  VAL B 174
SHEET    1   G 4 GLU B 232  ALA B 233  0
SHEET    2   G 4 ARG B 219  GLY B 227 -1  N  LEU B 226   O  GLU B 232
SHEET    3   G 4 GLY B 237  VAL B 239 -1  O  GLY B 237   N  GLU B 222
SHEET    4   G 4 LEU B 259  GLN B 260 -1  O  GLN B 260   N  GLU B 238
SHEET    1   H 4 GLU B 232  ALA B 233  0
SHEET    2   H 4 ARG B 219  GLY B 227 -1  N  LEU B 226   O  GLU B 232
SHEET    3   H 4 GLY B 288  VAL B 296 -1  O  PHE B 294   N  ILE B 221
SHEET    4   H 4 ILE B 302  ASN B 308 -1  O  TYR B 303   N  PHE B 295
CISPEP   1 TYR A  172    PRO A  173          0         3.42
CISPEP   2 ILE A  261    PRO A  262          0        -0.12
CISPEP   3 TYR B  172    PRO B  173          0        -7.51
CISPEP   4 ILE B  261    PRO B  262          0        -1.87
SITE     1 AC1  4 ARG A 291  ASN A 308  PRO A 311  GLY A 312
SITE     1 AC2  4 ARG B 291  ASN B 308  PRO B 311  GLY B 312
CRYST1   67.661   66.408   78.590  90.00  96.24  90.00 P 1 21 1      4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.014780  0.000000  0.001616        0.00000
SCALE2      0.000000  0.015058  0.000000        0.00000
SCALE3      0.000000  0.000000  0.012800        0.00000
      
PROCHECK
Go to PROCHECK summary
 References