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PDBsum entry 2ojw

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Ligase PDB id
2ojw
Jmol
Contents
Protein chains
360 a.a.
Ligands
PO4 ×5
ADP ×5
GOL ×6
Metals
_MN ×20
_CL ×5
Waters ×1390
HEADER    LIGASE                                  15-JAN-07   2OJW
TITLE     CRYSTAL STRUCTURE OF HUMAN GLUTAMINE SYNTHETASE IN COMPLEX WITH ADP
TITLE    2 AND PHOSPHATE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: GLUTAMINE SYNTHETASE;
COMPND   3 CHAIN: A, B, C, D, E;
COMPND   4 FRAGMENT: RESIDUES 4-364;
COMPND   5 SYNONYM: GLUTAMATE-AMMONIA LIGASE, GS;
COMPND   6 EC: 6.3.1.2;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: GLUL, GLNS;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PNIC-BSA4
KEYWDS    AMINO-ACID BIOSYNTHESIS, LIGASE, SYNTHETASE, STRUCTURAL GENOMICS,
KEYWDS   2 STRUCTURAL GENOMICS CONSORTIUM, SGC
EXPDTA    X-RAY DIFFRACTION
AUTHOR    T.KARLBERG,J.UPPENBERG,C.ARROWSMITH,H.BERGLUND,R.D.BUSAM,R.COLLINS,
AUTHOR   2 A.EDWARDS,S.FLODIN,A.FLORES,S.GRASLUND,B.M.HALLBERG,M.HAMMARSTROM,
AUTHOR   3 M.HOGBOM,I.JOHANSSON,T.KOTENYOVA,M.MOCHE,M.E.NILSSON,P.NORDLUND,
AUTHOR   4 T.NYMAN,D.OGG,C.PERSSON,J.SAGEMARK,P.STENMARK,M.SUNDSTROM,
AUTHOR   5 A.G.THORSELL,S.VAN DEN BERG,K.WALLDEN,J.WEIGELT,L.HOLMBERG-
AUTHOR   6 SCHIAVONE,STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT   5   13-JUL-11 2OJW    1       VERSN
REVDAT   4   24-FEB-09 2OJW    1       VERSN
REVDAT   3   18-DEC-07 2OJW    1       JRNL
REVDAT   2   27-NOV-07 2OJW    1       JRNL
REVDAT   1   13-MAR-07 2OJW    0
JRNL        AUTH   W.W.KRAJEWSKI,R.COLLINS,L.HOLMBERG-SCHIAVONE,T.A.JONES,
JRNL        AUTH 2 T.KARLBERG,S.L.MOWBRAY
JRNL        TITL   CRYSTAL STRUCTURES OF MAMMALIAN GLUTAMINE SYNTHETASES
JRNL        TITL 2 ILLUSTRATE SUBSTRATE-INDUCED CONFORMATIONAL CHANGES AND
JRNL        TITL 3 PROVIDE OPPORTUNITIES FOR DRUG AND HERBICIDE DESIGN.
JRNL        REF    J.MOL.BIOL.                   V. 375   217 2008
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   18005987
JRNL        DOI    10.1016/J.JMB.2007.10.029
REMARK   2
REMARK   2 RESOLUTION.    2.05 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.3.0021
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) : 2.05
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.25
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0
REMARK   3   NUMBER OF REFLECTIONS             : 121373
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) : 0.162
REMARK   3   R VALUE            (WORKING SET) : 0.159
REMARK   3   FREE R VALUE                     : 0.212
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 6388
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) : 2.05
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.10
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8909
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1980
REMARK   3   BIN FREE R VALUE SET COUNT          : 468
REMARK   3   BIN FREE R VALUE                    : 0.2890
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 14250
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 221
REMARK   3   SOLVENT ATOMS            : 1390
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) : 11.84
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.15000
REMARK   3    B22 (A**2) : 0.13000
REMARK   3    B33 (A**2) : 1.03000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 1.01000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.174
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.160
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.110
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.039
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953
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): 14840 ; 0.019 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A): 10359 ; 0.002 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 20083 ; 1.776 ; 1.958
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 24991 ; 1.094 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1796 ;12.756 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   729 ;36.810 ;23.388
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2414 ;14.792 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   122 ;17.345 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2023 ; 0.118 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 16607 ; 0.009 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  3167 ; 0.001 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2676 ; 0.203 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A): 10497 ; 0.204 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  6671 ; 0.176 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  7178 ; 0.084 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  1047 ; 0.187 ; 0.200
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):    24 ; 0.182 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):    77 ; 0.195 ; 0.200
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    14 ; 0.234 ; 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): 11515 ; 1.096 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  3658 ; 0.244 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 14361 ; 1.301 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  7035 ; 2.203 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  5719 ; 3.051 ; 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 : 1
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 1
REMARK   3     CHAIN NAMES                    : A B C D E
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 10
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     A     18       A     310      5
REMARK   3           2     B     18       B     310      5
REMARK   3           3     C     18       C     310      5
REMARK   3           4     D     18       D     310      5
REMARK   3           5     E     18       E     310      5
REMARK   3           6     A    317       A     365      5
REMARK   3           7     B    317       B     365      5
REMARK   3           8     C    317       C     365      5
REMARK   3           9     D    317       D     365      5
REMARK   3          10     E    317       E     364      5
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1940 ;  0.15 ;  0.50
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   1940 ;  0.13 ;  0.00
REMARK   3   MEDIUM POSITIONAL  1    C    (A):   1940 ;  0.13 ;  0.00
REMARK   3   MEDIUM POSITIONAL  1    D    (A):   1940 ;  0.14 ;  0.00
REMARK   3   MEDIUM POSITIONAL  1    E    (A):   1940 ;  0.15 ;  0.00
REMARK   3   LOOSE POSITIONAL   1    A    (A):   2571 ;  0.46 ;  5.00
REMARK   3   LOOSE POSITIONAL   1    B    (A):   2571 ;  0.45 ;  0.00
REMARK   3   LOOSE POSITIONAL   1    C    (A):   2571 ;  0.45 ;  0.00
REMARK   3   LOOSE POSITIONAL   1    D    (A):   2571 ;  0.44 ;  0.00
REMARK   3   LOOSE POSITIONAL   1    E    (A):   2571 ;  0.44 ;  0.00
REMARK   3   MEDIUM THERMAL     1    A (A**2):   1940 ;  0.87 ;  2.00
REMARK   3   MEDIUM THERMAL     1    B (A**2):   1940 ;  0.68 ;  0.00
REMARK   3   MEDIUM THERMAL     1    C (A**2):   1940 ;  0.61 ;  0.00
REMARK   3   MEDIUM THERMAL     1    D (A**2):   1940 ;  0.58 ;  0.00
REMARK   3   MEDIUM THERMAL     1    E (A**2):   1940 ;  0.79 ;  0.00
REMARK   3   LOOSE THERMAL      1    A (A**2):   2571 ;  0.89 ; 10.00
REMARK   3   LOOSE THERMAL      1    B (A**2):   2571 ;  0.78 ;  0.00
REMARK   3   LOOSE THERMAL      1    C (A**2):   2571 ;  0.82 ;  0.00
REMARK   3   LOOSE THERMAL      1    D (A**2):   2571 ;  0.78 ;  0.00
REMARK   3   LOOSE THERMAL      1    E (A**2):   2571 ;  0.83 ;  0.00
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 15
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    11        A   127
REMARK   3    ORIGIN FOR THE GROUP (A):  20.0970  17.9210 -36.1190
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0218 T22:   0.0321
REMARK   3      T33:  -0.0564 T12:   0.0028
REMARK   3      T13:   0.0129 T23:   0.0084
REMARK   3    L TENSOR
REMARK   3      L11:   0.3781 L22:   0.4079
REMARK   3      L33:   0.1311 L12:  -0.2948
REMARK   3      L13:  -0.1802 L23:   0.1315
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0136 S12:  -0.0020 S13:   0.0590
REMARK   3      S21:  -0.0562 S22:   0.0122 S23:  -0.0337
REMARK   3      S31:  -0.0269 S32:   0.0263 S33:   0.0015
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   128        A   177
REMARK   3    ORIGIN FOR THE GROUP (A):  19.2540  -3.8390 -26.5830
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0166 T22:   0.0396
REMARK   3      T33:  -0.0592 T12:   0.0043
REMARK   3      T13:  -0.0003 T23:  -0.0102
REMARK   3    L TENSOR
REMARK   3      L11:   0.0185 L22:   0.2633
REMARK   3      L33:   0.1844 L12:   0.0439
REMARK   3      L13:  -0.0569 L23:  -0.1731
REMARK   3    S TENSOR
REMARK   3      S11:   0.0243 S12:   0.0202 S13:  -0.0404
REMARK   3      S21:   0.0460 S22:  -0.0154 S23:   0.0091
REMARK   3      S31:   0.0276 S32:   0.0237 S33:  -0.0089
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   178        A   365
REMARK   3    ORIGIN FOR THE GROUP (A):  24.4500  -6.8830 -31.9490
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0249 T22:   0.0115
REMARK   3      T33:  -0.0566 T12:   0.0076
REMARK   3      T13:   0.0097 T23:  -0.0045
REMARK   3    L TENSOR
REMARK   3      L11:   0.2571 L22:   0.3035
REMARK   3      L33:   0.3167 L12:  -0.1111
REMARK   3      L13:  -0.1498 L23:   0.0639
REMARK   3    S TENSOR
REMARK   3      S11:   0.0091 S12:  -0.0030 S13:  -0.0199
REMARK   3      S21:  -0.0140 S22:  -0.0018 S23:  -0.0028
REMARK   3      S31:   0.0143 S32:  -0.0275 S33:  -0.0073
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    13        B   127
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.5190  43.3780 -28.6060
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0169 T22:  -0.0052
REMARK   3      T33:  -0.0272 T12:  -0.0082
REMARK   3      T13:  -0.0210 T23:   0.0402
REMARK   3    L TENSOR
REMARK   3      L11:   0.5337 L22:   0.2425
REMARK   3      L33:   0.1155 L12:   0.0154
REMARK   3      L13:  -0.1830 L23:   0.0912
REMARK   3    S TENSOR
REMARK   3      S11:   0.0127 S12:   0.0419 S13:   0.0658
REMARK   3      S21:  -0.0615 S22:  -0.0262 S23:   0.0090
REMARK   3      S31:  -0.0088 S32:  -0.0255 S33:   0.0135
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   128        B   177
REMARK   3    ORIGIN FOR THE GROUP (A):  16.8920  33.1850 -25.9550
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0250 T22:   0.0242
REMARK   3      T33:  -0.0311 T12:   0.0014
REMARK   3      T13:  -0.0012 T23:   0.0010
REMARK   3    L TENSOR
REMARK   3      L11:   0.2717 L22:   0.4343
REMARK   3      L33:   0.1710 L12:  -0.0925
REMARK   3      L13:   0.0680 L23:  -0.1235
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0394 S12:  -0.0051 S13:   0.0453
REMARK   3      S21:   0.0065 S22:   0.0442 S23:  -0.0310
REMARK   3      S31:   0.0064 S32:   0.0252 S33:  -0.0048
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   178        B   365
REMARK   3    ORIGIN FOR THE GROUP (A):  20.4790  38.3930 -30.9450
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0369 T22:   0.0169
REMARK   3      T33:  -0.0086 T12:  -0.0115
REMARK   3      T13:   0.0085 T23:  -0.0005
REMARK   3    L TENSOR
REMARK   3      L11:   0.3883 L22:   0.3221
REMARK   3      L33:   0.4896 L12:   0.0112
REMARK   3      L13:  -0.1807 L23:  -0.0560
REMARK   3    S TENSOR
REMARK   3      S11:   0.0064 S12:   0.0056 S13:   0.0791
REMARK   3      S21:  -0.0269 S22:   0.0459 S23:  -0.0535
REMARK   3      S31:   0.0161 S32:   0.0805 S33:  -0.0523
REMARK   3
REMARK   3   TLS GROUP : 7
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   C    10        C   127
REMARK   3    ORIGIN FOR THE GROUP (A): -34.7960  26.7420 -18.1960
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0450 T22:   0.0124
REMARK   3      T33:  -0.0093 T12:   0.0037
REMARK   3      T13:  -0.0360 T23:   0.0039
REMARK   3    L TENSOR
REMARK   3      L11:   0.1934 L22:   0.5267
REMARK   3      L33:   0.0710 L12:   0.0153
REMARK   3      L13:   0.0210 L23:  -0.1884
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0346 S12:   0.0240 S13:   0.0434
REMARK   3      S21:  -0.0211 S22:   0.0264 S23:   0.0493
REMARK   3      S31:   0.0193 S32:  -0.0299 S33:   0.0083
REMARK   3
REMARK   3   TLS GROUP : 8
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   C   128        C   177
REMARK   3    ORIGIN FOR THE GROUP (A): -17.1910  42.1910 -14.8590
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0408 T22:   0.0121
REMARK   3      T33:  -0.0159 T12:  -0.0008
REMARK   3      T13:  -0.0146 T23:  -0.0003
REMARK   3    L TENSOR
REMARK   3      L11:   0.6280 L22:   0.1937
REMARK   3      L33:   0.2841 L12:   0.0851
REMARK   3      L13:   0.3344 L23:   0.0947
REMARK   3    S TENSOR
REMARK   3      S11:   0.0017 S12:  -0.0959 S13:   0.0876
REMARK   3      S21:  -0.0225 S22:  -0.0124 S23:   0.0117
REMARK   3      S31:   0.0106 S32:  -0.0331 S33:   0.0107
REMARK   3
REMARK   3   TLS GROUP : 9
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   C   178        C   365
REMARK   3    ORIGIN FOR THE GROUP (A): -21.5050  48.4630 -17.2480
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0567 T22:  -0.0069
REMARK   3      T33:   0.0189 T12:   0.0103
REMARK   3      T13:  -0.0189 T23:   0.0043
REMARK   3    L TENSOR
REMARK   3      L11:   0.3925 L22:   0.3162
REMARK   3      L33:   0.2000 L12:  -0.0134
REMARK   3      L13:   0.1862 L23:   0.0024
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0313 S12:  -0.0285 S13:   0.0994
REMARK   3      S21:  -0.0373 S22:   0.0035 S23:   0.0475
REMARK   3      S31:   0.0084 S32:  -0.0028 S33:   0.0278
REMARK   3
REMARK   3   TLS GROUP : 10
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   D    11        D   127
REMARK   3    ORIGIN FOR THE GROUP (A): -29.3430  -8.9050 -20.3740
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0336 T22:   0.0194
REMARK   3      T33:  -0.0087 T12:  -0.0380
REMARK   3      T13:  -0.0079 T23:  -0.0312
REMARK   3    L TENSOR
REMARK   3      L11:   0.7508 L22:   0.3053
REMARK   3      L33:   0.0230 L12:  -0.1857
REMARK   3      L13:  -0.0946 L23:   0.0771
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0019 S12:   0.0547 S13:  -0.0986
REMARK   3      S21:  -0.0369 S22:  -0.0217 S23:   0.0688
REMARK   3      S31:   0.0197 S32:  -0.0121 S33:   0.0236
REMARK   3
REMARK   3   TLS GROUP : 11
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   D   128        D   177
REMARK   3    ORIGIN FOR THE GROUP (A): -36.0080  10.9340  -8.8470
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0271 T22:   0.0104
REMARK   3      T33:  -0.0176 T12:  -0.0189
REMARK   3      T13:  -0.0078 T23:  -0.0090
REMARK   3    L TENSOR
REMARK   3      L11:   0.4292 L22:   0.5658
REMARK   3      L33:   0.0609 L12:   0.1677
REMARK   3      L13:  -0.0045 L23:   0.1727
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0164 S12:   0.0060 S13:  -0.0202
REMARK   3      S21:   0.0396 S22:  -0.0194 S23:   0.0275
REMARK   3      S31:  -0.0133 S32:  -0.0069 S33:   0.0358
REMARK   3
REMARK   3   TLS GROUP : 12
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   D   178        D   365
REMARK   3    ORIGIN FOR THE GROUP (A): -43.7620   9.5070 -10.1480
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0538 T22:   0.0056
REMARK   3      T33:   0.0087 T12:  -0.0325
REMARK   3      T13:   0.0005 T23:  -0.0152
REMARK   3    L TENSOR
REMARK   3      L11:   0.4714 L22:   0.3507
REMARK   3      L33:   0.1699 L12:  -0.0955
REMARK   3      L13:   0.0407 L23:   0.2001
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0005 S12:   0.0250 S13:  -0.0389
REMARK   3      S21:   0.0250 S22:  -0.0508 S23:   0.0868
REMARK   3      S31:  -0.0039 S32:  -0.0021 S33:   0.0514
REMARK   3
REMARK   3   TLS GROUP : 13
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   E    15        E   127
REMARK   3    ORIGIN FOR THE GROUP (A):   4.6720 -14.5710 -31.8560
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0013 T22:   0.0189
REMARK   3      T33:  -0.0485 T12:   0.0039
REMARK   3      T13:   0.0046 T23:  -0.0404
REMARK   3    L TENSOR
REMARK   3      L11:   0.4080 L22:   0.4261
REMARK   3      L33:   0.1562 L12:   0.0491
REMARK   3      L13:  -0.1319 L23:   0.0603
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0124 S12:   0.1128 S13:  -0.0514
REMARK   3      S21:  -0.0137 S22:  -0.0233 S23:   0.0257
REMARK   3      S31:   0.0439 S32:   0.0324 S33:   0.0356
REMARK   3
REMARK   3   TLS GROUP : 14
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   E   128        E   177
REMARK   3    ORIGIN FOR THE GROUP (A): -13.4050 -17.6310 -16.3390
REMARK   3    T TENSOR
REMARK   3      T11:   0.0132 T22:   0.0129
REMARK   3      T33:  -0.0306 T12:  -0.0178
REMARK   3      T13:   0.0149 T23:  -0.0066
REMARK   3    L TENSOR
REMARK   3      L11:   0.5126 L22:   0.0362
REMARK   3      L33:   0.4101 L12:  -0.1326
REMARK   3      L13:  -0.2773 L23:   0.0498
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0443 S12:  -0.0258 S13:  -0.0555
REMARK   3      S21:   0.0303 S22:  -0.0122 S23:   0.0523
REMARK   3      S31:   0.0822 S32:  -0.0046 S33:   0.0566
REMARK   3
REMARK   3   TLS GROUP : 15
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   E   178        E   364
REMARK   3    ORIGIN FOR THE GROUP (A): -15.4560 -24.6800 -19.6390
REMARK   3    T TENSOR
REMARK   3      T11:   0.0011 T22:  -0.0047
REMARK   3      T33:   0.0083 T12:  -0.0180
REMARK   3      T13:   0.0185 T23:  -0.0343
REMARK   3    L TENSOR
REMARK   3      L11:   0.4787 L22:   0.3626
REMARK   3      L33:   0.3435 L12:   0.0835
REMARK   3      L13:  -0.0976 L23:   0.0768
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0465 S12:   0.0161 S13:  -0.1393
REMARK   3      S21:   0.0107 S22:   0.0093 S23:   0.0300
REMARK   3      S31:   0.0577 S32:  -0.0307 S33:   0.0372
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.40
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 2OJW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JAN-07.
REMARK 100 THE RCSB ID CODE IS RCSB041227.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 14-SEP-06
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 7.50
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : ID14-2
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.93300
REMARK 200  MONOCHROMATOR                  : DIAMOND (111), GE(220)
REMARK 200  OPTICS                         : FOCUSING: TOROIDAL MIRROR
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : XSCALE
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 125431
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.12050
REMARK 200  R SYM                      (I) : 0.14000
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.15
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.6
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80
REMARK 200  R MERGE FOR SHELL          (I) : 0.41600
REMARK 200  R SYM FOR SHELL            (I) : 0.48500
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2D3A
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 49.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% ISOPROPANOL, 200 MM NACL, 100 MM
REMARK 280  HEPES, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K,
REMARK 280  PH 7.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,Y,-Z
REMARK 290       3555   X+1/2,Y+1/2,Z
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        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       88.80000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       61.30000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       88.80000
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       61.30000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DECAMER GENERATED FROM THE
REMARK 300 PENTAMER IN THE ASYMMETRIC UNIT BY THE OPERATION: -X, Y, -Z
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: DECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DECAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 73600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 117210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -758.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E
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   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  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   -18
REMARK 465     HIS A   -17
REMARK 465     HIS A   -16
REMARK 465     HIS A   -15
REMARK 465     HIS A   -14
REMARK 465     HIS A   -13
REMARK 465     HIS A   -12
REMARK 465     SER A   -11
REMARK 465     SER A   -10
REMARK 465     GLY A    -9
REMARK 465     VAL A    -8
REMARK 465     ASP A    -7
REMARK 465     LEU A    -6
REMARK 465     GLY A    -5
REMARK 465     THR A    -4
REMARK 465     GLU A    -3
REMARK 465     ASN A    -2
REMARK 465     LEU A    -1
REMARK 465     THR A   142
REMARK 465     GLY A   302
REMARK 465     PHE A   303
REMARK 465     HIS A   304
REMARK 465     GLU A   305
REMARK 465     THR A   306
REMARK 465     MET B   -18
REMARK 465     HIS B   -17
REMARK 465     HIS B   -16
REMARK 465     HIS B   -15
REMARK 465     HIS B   -14
REMARK 465     HIS B   -13
REMARK 465     HIS B   -12
REMARK 465     SER B   -11
REMARK 465     SER B   -10
REMARK 465     GLY B    -9
REMARK 465     VAL B    -8
REMARK 465     ASP B    -7
REMARK 465     LEU B    -6
REMARK 465     GLY B    -5
REMARK 465     THR B    -4
REMARK 465     GLU B    -3
REMARK 465     ASN B    -2
REMARK 465     LEU B    -1
REMARK 465     THR B   142
REMARK 465     PHE B   303
REMARK 465     HIS B   304
REMARK 465     GLU B   305
REMARK 465     MET C   -18
REMARK 465     HIS C   -17
REMARK 465     HIS C   -16
REMARK 465     HIS C   -15
REMARK 465     HIS C   -14
REMARK 465     HIS C   -13
REMARK 465     HIS C   -12
REMARK 465     SER C   -11
REMARK 465     SER C   -10
REMARK 465     GLY C    -9
REMARK 465     VAL C    -8
REMARK 465     ASP C    -7
REMARK 465     LEU C    -6
REMARK 465     GLY C    -5
REMARK 465     THR C    -4
REMARK 465     GLU C    -3
REMARK 465     ASN C    -2
REMARK 465     PHE C   303
REMARK 465     HIS C   304
REMARK 465     GLU C   305
REMARK 465     MET D   -18
REMARK 465     HIS D   -17
REMARK 465     HIS D   -16
REMARK 465     HIS D   -15
REMARK 465     HIS D   -14
REMARK 465     HIS D   -13
REMARK 465     HIS D   -12
REMARK 465     SER D   -11
REMARK 465     SER D   -10
REMARK 465     GLY D    -9
REMARK 465     VAL D    -8
REMARK 465     ASP D    -7
REMARK 465     LEU D    -6
REMARK 465     GLY D    -5
REMARK 465     THR D    -4
REMARK 465     GLU D    -3
REMARK 465     ASN D    -2
REMARK 465     LEU D    -1
REMARK 465     GLY D   302
REMARK 465     PHE D   303
REMARK 465     HIS D   304
REMARK 465     GLU D   305
REMARK 465     MET E   -18
REMARK 465     HIS E   -17
REMARK 465     HIS E   -16
REMARK 465     HIS E   -15
REMARK 465     HIS E   -14
REMARK 465     HIS E   -13
REMARK 465     HIS E   -12
REMARK 465     SER E   -11
REMARK 465     SER E   -10
REMARK 465     GLY E    -9
REMARK 465     VAL E    -8
REMARK 465     ASP E    -7
REMARK 465     LEU E    -6
REMARK 465     GLY E    -5
REMARK 465     THR E    -4
REMARK 465     GLU E    -3
REMARK 465     ASN E    -2
REMARK 465     LEU E    -1
REMARK 465     TYR E     0
REMARK 465     PHE E     1
REMARK 465     GLN E     2
REMARK 465     SER E     3
REMARK 465     MET E     4
REMARK 465     THR E   301
REMARK 465     GLY E   302
REMARK 465     PHE E   303
REMARK 465     HIS E   304
REMARK 465     GLU E   305
REMARK 465     THR E   306
REMARK 465     GLY E   365
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 307    OG
REMARK 470     LEU C  -1    CG   CD1  CD2
REMARK 470     THR D 301    OG1  CG2
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   O    HOH A  1515     O    HOH A  1771              1.81
REMARK 500   O    HOH A  1561     O    HOH A  1791              1.97
REMARK 500   O    HOH A  1679     O    HOH A  1700              1.98
REMARK 500   OE1  GLU C   110     O    HOH C  1729              1.99
REMARK 500   O    GLY A    23     O    HOH A  1659              2.04
REMARK 500   OE2  GLU D    59     O    HOH D  1732              2.06
REMARK 500   O    HOH A  1671     O    HOH E  1752              2.08
REMARK 500   ND2  ASN E   126     O    HOH E  1660              2.10
REMARK 500   OD1  ASN B   126     O    HOH B  1771              2.10
REMARK 500   O    HOH E  1522     O    HOH E  1667              2.10
REMARK 500   OE1  GLN E   127     O    HOH E  1583              2.16
REMARK 500   N    THR B   306     O    HOH B  1717              2.16
REMARK 500   O    HOH A  1651     O    HOH A  1708              2.17
REMARK 500
REMARK 500 REMARK: NULL
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   ND2  ASN A   362     ND2  ASN A   362     2554     1.92
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 299   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES
REMARK 500    ARG A 299   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES
REMARK 500    ARG B 280   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES
REMARK 500    ARG B 299   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES
REMARK 500    ARG B 299   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES
REMARK 500    THR C 142   OG1 -  CB  -  CG2 ANGL. DEV. =  13.8 DEGREES
REMARK 500    ARG C 262   NE  -  CZ  -  NH1 ANGL. DEV. =   5.0 DEGREES
REMARK 500    ARG C 262   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.6 DEGREES
REMARK 500    ARG C 299   NE  -  CZ  -  NH1 ANGL. DEV. =   5.5 DEGREES
REMARK 500    ARG C 299   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.2 DEGREES
REMARK 500    ASP D 216   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES
REMARK 500    ARG D 299   NE  -  CZ  -  NH1 ANGL. DEV. =   5.4 DEGREES
REMARK 500    ARG D 299   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES
REMARK 500    ARG D 319   NE  -  CZ  -  NH1 ANGL. DEV. =   4.8 DEGREES
REMARK 500    ARG D 319   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 DEGREES
REMARK 500    MET E  77   CG  -  SD  -  CE  ANGL. DEV. =  10.5 DEGREES
REMARK 500    ARG E 299   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES
REMARK 500    ARG E 299   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES
REMARK 500    ARG E 327   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES
REMARK 500    ARG E 327   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    ASN A  74       65.44   -152.78
REMARK 500    LYS A  91      166.32     77.98
REMARK 500    ALA A 200       -4.65     88.47
REMARK 500    ASN B  74       68.97   -153.62
REMARK 500    LYS B  91      165.94     78.69
REMARK 500    ASP B  92      137.78    -38.27
REMARK 500    MET B 123       -9.99    -59.33
REMARK 500    ARG B 169      -50.44   -132.34
REMARK 500    LYS B 241       78.83   -150.02
REMARK 500    ASN B 246       51.08    -94.76
REMARK 500    ALA B 317       12.82     50.36
REMARK 500    LEU C  68       35.75     71.12
REMARK 500    ASN C  74       65.34   -152.95
REMARK 500    LYS C  91      162.45     74.07
REMARK 500    ARG C 169      -54.97   -121.31
REMARK 500    ALA C 200        0.39     81.40
REMARK 500    LYS C 241       74.01   -153.08
REMARK 500    ASN C 246       48.89    -84.89
REMARK 500    ASN D  74       66.74   -157.05
REMARK 500    LYS D  91      171.64     74.62
REMARK 500    ARG D 169      -56.46   -134.77
REMARK 500    ALA D 200        2.47     80.72
REMARK 500    LYS D 241       72.83   -150.57
REMARK 500    ASN D 246       48.94    -83.41
REMARK 500    ASN E  74       68.66   -152.74
REMARK 500    LYS E  91      160.00     71.58
REMARK 500    ARG E 169      -54.83   -131.25
REMARK 500    ALA E 200       -1.70     80.92
REMARK 500    LYS E 241       74.32   -154.04
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 ASP A   92     PRO A   93                   31.81
REMARK 500 GLY A  207     PRO A  208                  -35.83
REMARK 500 SER A  307     ASN A  308                  144.05
REMARK 500 ASP B  143     GLY B  144                 -131.03
REMARK 500 GLY B  207     PRO B  208                  -39.51
REMARK 500 LEU B  300     THR B  301                  139.17
REMARK 500 ASP C   92     PRO C   93                   36.29
REMARK 500 GLY C  207     PRO C  208                  -37.82
REMARK 500 ASP D   92     PRO D   93                   34.14
REMARK 500 GLY D  207     PRO D  208                  -37.02
REMARK 500 THR D  306     SER D  307                  148.58
REMARK 500 ASP E   92     PRO E   93                   33.13
REMARK 500 GLY E  207     PRO E  208                  -43.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        ANGLE
REMARK 500    ASP A  92         14.01
REMARK 500    GLY A 207        -13.75
REMARK 500    GLY B 207        -12.83
REMARK 500    ASP C  92         10.12
REMARK 500    GLY C 207        -13.83
REMARK 500    ASP D  92         11.31
REMARK 500    GLY D 207        -13.39
REMARK 500    GLY E 207        -12.85
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 358        22.9      L          L   OUTSIDE RANGE
REMARK 500    LEU C 218        24.8      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A1678        DISTANCE =  5.55 ANGSTROMS
REMARK 525    HOH B1668        DISTANCE =  5.33 ANGSTROMS
REMARK 525    HOH D1620        DISTANCE =  5.24 ANGSTROMS
REMARK 525    HOH D1670        DISTANCE =  6.04 ANGSTROMS
REMARK 525    HOH E1585        DISTANCE =  6.21 ANGSTROMS
REMARK 525    HOH E1653        DISTANCE =  5.75 ANGSTROMS
REMARK 525    HOH E1694        DISTANCE =  5.15 ANGSTROMS
REMARK 525    HOH E1697        DISTANCE =  6.33 ANGSTROMS
REMARK 525    HOH E1769        DISTANCE =  6.81 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                              MN A 402  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 134   OE1
REMARK 620 2 GLU A 338   OE2 142.7
REMARK 620 3 ADP A 501   O3B  94.0  95.3
REMARK 620 4 PO4 A 502   O1  102.8 112.7  92.9
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN A 403  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 134   OE1
REMARK 620 2 GLU A 203   OE2  90.9
REMARK 620 3 ADP A 501   O2A  86.1  88.8
REMARK 620 4 ADP A 501   O1B  97.2 169.0  84.5
REMARK 620 5 HOH A1635   O   178.7  88.3  94.8  83.7
REMARK 620 6 PO4 A 502   O2   84.5  98.8 168.1  89.4  94.6
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN A 401  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 136   OE2
REMARK 620 2 GLU A 196   OE1  86.3
REMARK 620 3 GLU A 203   OE1 105.8 100.0
REMARK 620 4 PO4 A 502   O4   98.5  81.8 155.8
REMARK 620 5 PO4 A 502   O2  155.0 105.8  93.8  62.8
REMARK 620 6 HOH A1686   O    82.2 168.3  84.9  98.2  84.3
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN A 404  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 196   OE1
REMARK 620 2 PO4 A 502   O4   82.5
REMARK 620 3 HOH A1730   O   169.8  87.4
REMARK 620 4 HOH A1729   O   106.6 164.6  83.5
REMARK 620 5 HOH A1731   O    92.0  83.9  88.2  83.4
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN B 402  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 134   OE1
REMARK 620 2 GLU B 134   OE2  57.0
REMARK 620 3 GLU B 338   OE2  94.5 150.5
REMARK 620 4 ADP B 501   O2B  87.1  92.5  93.5
REMARK 620 5 PO4 B 502   O2  156.1  99.3 109.4  91.4
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN B 403  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 134   OE2
REMARK 620 2 GLU B 203   OE2  84.3
REMARK 620 3 ADP B 501   O2A  83.6  93.0
REMARK 620 4 ADP B 501   O3B 103.7 169.7  81.6
REMARK 620 5 HOH B1616   O   168.7  84.9  93.9  86.7
REMARK 620 6 PO4 B 502   O3   91.7  97.5 168.0  88.8  92.9
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN B 401  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 136   OE2
REMARK 620 2 GLU B 196   OE1  86.0
REMARK 620 3 GLU B 203   OE1 110.2  94.7
REMARK 620 4 PO4 B 502   O3  156.6 106.6  88.8
REMARK 620 5 HOH B1747   O    83.3 169.0  86.2  84.4
REMARK 620 6 PO4 B 502   O4  100.7  87.8 149.1  61.1  97.0
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN C 403  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 134   OE1
REMARK 620 2 GLU C 203   OE1  97.3
REMARK 620 3 ADP C 501   O2A  79.8  95.2
REMARK 620 4 HOH C1604   O   171.3  83.1  91.5
REMARK 620 5 ADP C 501   O3B  91.5 169.2  80.2  87.3
REMARK 620 6 PO4 C 502   O1   86.5  97.1 162.7 102.1  89.6
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN C 402  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 134   OE1
REMARK 620 2 GLU C 338   OE2 139.1
REMARK 620 3 ADP C 501   O2B  87.6  97.6
REMARK 620 4 PO4 C 502   O3  104.6 114.3  99.9
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN C 401  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 136   OE2
REMARK 620 2 GLU C 196   OE1  81.3
REMARK 620 3 GLU C 203   OE2 108.7  95.7
REMARK 620 4 PO4 C 502   O1  151.5 111.3  95.7
REMARK 620 5 HOH C1745   O    81.8 163.0  91.1  83.4
REMARK 620 6 PO4 C 502   O4   98.4  79.4 151.4  61.1 101.6
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN C 404  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 196   OE1
REMARK 620 2 PO4 C 502   O4   81.6
REMARK 620 3 HOH B1741   O    97.1  95.2
REMARK 620 4 HOH C1718   O    90.2  86.0 172.8
REMARK 620 5 HOH C1719   O   173.8  97.0  89.0  83.7
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN D 402  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 134   OE1
REMARK 620 2 GLU D 338   OE2 144.2
REMARK 620 3 ADP D 501   O2B  91.6  93.8
REMARK 620 4 PO4 D 502   O3  102.7 110.7 101.8
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN D 403  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 134   OE1
REMARK 620 2 GLU D 203   OE1  91.9
REMARK 620 3 ADP D 501   O2A  79.3  94.1
REMARK 620 4 HOH D1615   O   173.8  85.1  95.5
REMARK 620 5 ADP D 501   O3B  99.0 166.9  80.8  83.4
REMARK 620 6 PO4 D 502   O1   89.5  98.6 163.3  96.3  88.9
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN D 401  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 136   OE2
REMARK 620 2 GLU D 196   OE2  89.2
REMARK 620 3 GLU D 203   OE2 107.5  94.1
REMARK 620 4 HOH D1741   O    83.7 172.7  86.5
REMARK 620 5 PO4 D 502   O1  156.1 104.4  91.2  82.8
REMARK 620 6 PO4 D 502   O4  102.8  83.6 149.6  99.6  60.5
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN E 402  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 134   OE1
REMARK 620 2 GLU E 338   OE1 143.7
REMARK 620 3 ADP E 501   O2B  90.2  96.1
REMARK 620 4 PO4 E 502   O3  100.4 115.2  91.2
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN E 403  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 134   OE1
REMARK 620 2 GLU E 203   OE2  91.7
REMARK 620 3 ADP E 501   O2A  84.9  94.2
REMARK 620 4 ADP E 501   O3B  98.7 167.3  79.6
REMARK 620 5 HOH E1609   O   174.7  85.3  90.9  83.8
REMARK 620 6 PO4 E 502   O1   86.5 100.8 162.9  87.2  98.4
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN E 401  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 136   OE2
REMARK 620 2 GLU E 196   OE1  82.7
REMARK 620 3 GLU E 203   OE1 113.9  92.2
REMARK 620 4 PO4 E 502   O1  153.6 109.0  89.8
REMARK 620 5 HOH E1666   O    81.5 163.9  91.4  86.7
REMARK 620 6 PO4 E 502   O4   95.8  86.2 149.8  62.6  98.4
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN B 404  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B1740   O
REMARK 620 2 PO4 B 502   O4   93.7
REMARK 620 3 HOH B1738   O    97.4  86.0
REMARK 620 4 HOH B1739   O    96.3 157.9  73.2
REMARK 620 5 HOH B1730   O   176.2  90.1  82.1  79.9
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN D 404  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PO4 D 502   O4
REMARK 620 2 HOH D1740   O    91.5
REMARK 620 3 HOH D1739   O    91.6 173.3
REMARK 620 4 HOH D1609   O    91.0  99.0  86.8
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN E 404  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PO4 E 502   O4
REMARK 620 2 HOH E1716   O    93.5
REMARK 620 3 HOH E1717   O    91.7 100.8
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 MN A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 E 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 1401
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 1402
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1403
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 1404
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1405
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP E 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1502
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 1503
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 1504
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 1505
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 1506
DBREF  2OJW A    5   365  UNP    P15104   GLNA_HUMAN       4    364
DBREF  2OJW B    5   365  UNP    P15104   GLNA_HUMAN       4    364
DBREF  2OJW C    5   365  UNP    P15104   GLNA_HUMAN       4    364
DBREF  2OJW D    5   365  UNP    P15104   GLNA_HUMAN       4    364
DBREF  2OJW E    5   365  UNP    P15104   GLNA_HUMAN       4    364
SEQADV 2OJW MET A  -18  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW HIS A  -17  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW HIS A  -16  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW HIS A  -15  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW HIS A  -14  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW HIS A  -13  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW HIS A  -12  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW SER A  -11  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW SER A  -10  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW GLY A   -9  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW VAL A   -8  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW ASP A   -7  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW LEU A   -6  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW GLY A   -5  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW THR A   -4  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW GLU A   -3  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW ASN A   -2  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW LEU A   -1  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW TYR A    0  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW PHE A    1  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW GLN A    2  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW SER A    3  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW MET A    4  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW MET B  -18  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW HIS B  -17  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW HIS B  -16  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW HIS B  -15  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW HIS B  -14  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW HIS B  -13  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW HIS B  -12  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW SER B  -11  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW SER B  -10  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW GLY B   -9  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW VAL B   -8  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW ASP B   -7  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW LEU B   -6  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW GLY B   -5  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW THR B   -4  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW GLU B   -3  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW ASN B   -2  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW LEU B   -1  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW TYR B    0  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW PHE B    1  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW GLN B    2  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW SER B    3  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW MET B    4  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW MET C  -18  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW HIS C  -17  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW HIS C  -16  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW HIS C  -15  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW HIS C  -14  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW HIS C  -13  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW HIS C  -12  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW SER C  -11  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW SER C  -10  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW GLY C   -9  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW VAL C   -8  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW ASP C   -7  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW LEU C   -6  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW GLY C   -5  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW THR C   -4  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW GLU C   -3  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW ASN C   -2  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW LEU C   -1  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW TYR C    0  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW PHE C    1  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW GLN C    2  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW SER C    3  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW MET C    4  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW MET D  -18  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW HIS D  -17  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW HIS D  -16  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW HIS D  -15  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW HIS D  -14  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW HIS D  -13  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW HIS D  -12  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW SER D  -11  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW SER D  -10  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW GLY D   -9  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW VAL D   -8  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW ASP D   -7  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW LEU D   -6  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW GLY D   -5  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW THR D   -4  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW GLU D   -3  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW ASN D   -2  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW LEU D   -1  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW TYR D    0  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW PHE D    1  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW GLN D    2  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW SER D    3  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW MET D    4  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW MET E  -18  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW HIS E  -17  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW HIS E  -16  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW HIS E  -15  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW HIS E  -14  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW HIS E  -13  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW HIS E  -12  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW SER E  -11  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW SER E  -10  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW GLY E   -9  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW VAL E   -8  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW ASP E   -7  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW LEU E   -6  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW GLY E   -5  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW THR E   -4  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW GLU E   -3  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW ASN E   -2  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW LEU E   -1  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW TYR E    0  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW PHE E    1  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW GLN E    2  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW SER E    3  UNP  P15104              EXPRESSION TAG
SEQADV 2OJW MET E    4  UNP  P15104              EXPRESSION TAG
SEQRES   1 A  384  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES   2 A  384  GLY THR GLU ASN LEU TYR PHE GLN SER MET ALA SER SER
SEQRES   3 A  384  HIS LEU ASN LYS GLY ILE LYS GLN VAL TYR MET SER LEU
SEQRES   4 A  384  PRO GLN GLY GLU LYS VAL GLN ALA MET TYR ILE TRP ILE
SEQRES   5 A  384  ASP GLY THR GLY GLU GLY LEU ARG CYS LYS THR ARG THR
SEQRES   6 A  384  LEU ASP SER GLU PRO LYS CYS VAL GLU GLU LEU PRO GLU
SEQRES   7 A  384  TRP ASN PHE ASP GLY SER SER THR LEU GLN SER GLU GLY
SEQRES   8 A  384  SER ASN SER ASP MET TYR LEU VAL PRO ALA ALA MET PHE
SEQRES   9 A  384  ARG ASP PRO PHE ARG LYS ASP PRO ASN LYS LEU VAL LEU
SEQRES  10 A  384  CYS GLU VAL PHE LYS TYR ASN ARG ARG PRO ALA GLU THR
SEQRES  11 A  384  ASN LEU ARG HIS THR CYS LYS ARG ILE MET ASP MET VAL
SEQRES  12 A  384  SER ASN GLN HIS PRO TRP PHE GLY MET GLU GLN GLU TYR
SEQRES  13 A  384  THR LEU MET GLY THR ASP GLY HIS PRO PHE GLY TRP PRO
SEQRES  14 A  384  SER ASN GLY PHE PRO GLY PRO GLN GLY PRO TYR TYR CYS
SEQRES  15 A  384  GLY VAL GLY ALA ASP ARG ALA TYR GLY ARG ASP ILE VAL
SEQRES  16 A  384  GLU ALA HIS TYR ARG ALA CYS LEU TYR ALA GLY VAL LYS
SEQRES  17 A  384  ILE ALA GLY THR ASN ALA GLU VAL MET PRO ALA GLN TRP
SEQRES  18 A  384  GLU PHE GLN ILE GLY PRO CYS GLU GLY ILE SER MET GLY
SEQRES  19 A  384  ASP HIS LEU TRP VAL ALA ARG PHE ILE LEU HIS ARG VAL
SEQRES  20 A  384  CYS GLU ASP PHE GLY VAL ILE ALA THR PHE ASP PRO LYS
SEQRES  21 A  384  PRO ILE PRO GLY ASN TRP ASN GLY ALA GLY CYS HIS THR
SEQRES  22 A  384  ASN PHE SER THR LYS ALA MET ARG GLU GLU ASN GLY LEU
SEQRES  23 A  384  LYS TYR ILE GLU GLU ALA ILE GLU LYS LEU SER LYS ARG
SEQRES  24 A  384  HIS GLN TYR HIS ILE ARG ALA TYR ASP PRO LYS GLY GLY
SEQRES  25 A  384  LEU ASP ASN ALA ARG ARG LEU THR GLY PHE HIS GLU THR
SEQRES  26 A  384  SER ASN ILE ASN ASP PHE SER ALA GLY VAL ALA ASN ARG
SEQRES  27 A  384  SER ALA SER ILE ARG ILE PRO ARG THR VAL GLY GLN GLU
SEQRES  28 A  384  LYS LYS GLY TYR PHE GLU ASP ARG ARG PRO SER ALA ASN
SEQRES  29 A  384  CYS ASP PRO PHE SER VAL THR GLU ALA LEU ILE ARG THR
SEQRES  30 A  384  CYS LEU LEU ASN GLU THR GLY
SEQRES   1 B  384  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES   2 B  384  GLY THR GLU ASN LEU TYR PHE GLN SER MET ALA SER SER
SEQRES   3 B  384  HIS LEU ASN LYS GLY ILE LYS GLN VAL TYR MET SER LEU
SEQRES   4 B  384  PRO GLN GLY GLU LYS VAL GLN ALA MET TYR ILE TRP ILE
SEQRES   5 B  384  ASP GLY THR GLY GLU GLY LEU ARG CYS LYS THR ARG THR
SEQRES   6 B  384  LEU ASP SER GLU PRO LYS CYS VAL GLU GLU LEU PRO GLU
SEQRES   7 B  384  TRP ASN PHE ASP GLY SER SER THR LEU GLN SER GLU GLY
SEQRES   8 B  384  SER ASN SER ASP MET TYR LEU VAL PRO ALA ALA MET PHE
SEQRES   9 B  384  ARG ASP PRO PHE ARG LYS ASP PRO ASN LYS LEU VAL LEU
SEQRES  10 B  384  CYS GLU VAL PHE LYS TYR ASN ARG ARG PRO ALA GLU THR
SEQRES  11 B  384  ASN LEU ARG HIS THR CYS LYS ARG ILE MET ASP MET VAL
SEQRES  12 B  384  SER ASN GLN HIS PRO TRP PHE GLY MET GLU GLN GLU TYR
SEQRES  13 B  384  THR LEU MET GLY THR ASP GLY HIS PRO PHE GLY TRP PRO
SEQRES  14 B  384  SER ASN GLY PHE PRO GLY PRO GLN GLY PRO TYR TYR CYS
SEQRES  15 B  384  GLY VAL GLY ALA ASP ARG ALA TYR GLY ARG ASP ILE VAL
SEQRES  16 B  384  GLU ALA HIS TYR ARG ALA CYS LEU TYR ALA GLY VAL LYS
SEQRES  17 B  384  ILE ALA GLY THR ASN ALA GLU VAL MET PRO ALA GLN TRP
SEQRES  18 B  384  GLU PHE GLN ILE GLY PRO CYS GLU GLY ILE SER MET GLY
SEQRES  19 B  384  ASP HIS LEU TRP VAL ALA ARG PHE ILE LEU HIS ARG VAL
SEQRES  20 B  384  CYS GLU ASP PHE GLY VAL ILE ALA THR PHE ASP PRO LYS
SEQRES  21 B  384  PRO ILE PRO GLY ASN TRP ASN GLY ALA GLY CYS HIS THR
SEQRES  22 B  384  ASN PHE SER THR LYS ALA MET ARG GLU GLU ASN GLY LEU
SEQRES  23 B  384  LYS TYR ILE GLU GLU ALA ILE GLU LYS LEU SER LYS ARG
SEQRES  24 B  384  HIS GLN TYR HIS ILE ARG ALA TYR ASP PRO LYS GLY GLY
SEQRES  25 B  384  LEU ASP ASN ALA ARG ARG LEU THR GLY PHE HIS GLU THR
SEQRES  26 B  384  SER ASN ILE ASN ASP PHE SER ALA GLY VAL ALA ASN ARG
SEQRES  27 B  384  SER ALA SER ILE ARG ILE PRO ARG THR VAL GLY GLN GLU
SEQRES  28 B  384  LYS LYS GLY TYR PHE GLU ASP ARG ARG PRO SER ALA ASN
SEQRES  29 B  384  CYS ASP PRO PHE SER VAL THR GLU ALA LEU ILE ARG THR
SEQRES  30 B  384  CYS LEU LEU ASN GLU THR GLY
SEQRES   1 C  384  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES   2 C  384  GLY THR GLU ASN LEU TYR PHE GLN SER MET ALA SER SER
SEQRES   3 C  384  HIS LEU ASN LYS GLY ILE LYS GLN VAL TYR MET SER LEU
SEQRES   4 C  384  PRO GLN GLY GLU LYS VAL GLN ALA MET TYR ILE TRP ILE
SEQRES   5 C  384  ASP GLY THR GLY GLU GLY LEU ARG CYS LYS THR ARG THR
SEQRES   6 C  384  LEU ASP SER GLU PRO LYS CYS VAL GLU GLU LEU PRO GLU
SEQRES   7 C  384  TRP ASN PHE ASP GLY SER SER THR LEU GLN SER GLU GLY
SEQRES   8 C  384  SER ASN SER ASP MET TYR LEU VAL PRO ALA ALA MET PHE
SEQRES   9 C  384  ARG ASP PRO PHE ARG LYS ASP PRO ASN LYS LEU VAL LEU
SEQRES  10 C  384  CYS GLU VAL PHE LYS TYR ASN ARG ARG PRO ALA GLU THR
SEQRES  11 C  384  ASN LEU ARG HIS THR CYS LYS ARG ILE MET ASP MET VAL
SEQRES  12 C  384  SER ASN GLN HIS PRO TRP PHE GLY MET GLU GLN GLU TYR
SEQRES  13 C  384  THR LEU MET GLY THR ASP GLY HIS PRO PHE GLY TRP PRO
SEQRES  14 C  384  SER ASN GLY PHE PRO GLY PRO GLN GLY PRO TYR TYR CYS
SEQRES  15 C  384  GLY VAL GLY ALA ASP ARG ALA TYR GLY ARG ASP ILE VAL
SEQRES  16 C  384  GLU ALA HIS TYR ARG ALA CYS LEU TYR ALA GLY VAL LYS
SEQRES  17 C  384  ILE ALA GLY THR ASN ALA GLU VAL MET PRO ALA GLN TRP
SEQRES  18 C  384  GLU PHE GLN ILE GLY PRO CYS GLU GLY ILE SER MET GLY
SEQRES  19 C  384  ASP HIS LEU TRP VAL ALA ARG PHE ILE LEU HIS ARG VAL
SEQRES  20 C  384  CYS GLU ASP PHE GLY VAL ILE ALA THR PHE ASP PRO LYS
SEQRES  21 C  384  PRO ILE PRO GLY ASN TRP ASN GLY ALA GLY CYS HIS THR
SEQRES  22 C  384  ASN PHE SER THR LYS ALA MET ARG GLU GLU ASN GLY LEU
SEQRES  23 C  384  LYS TYR ILE GLU GLU ALA ILE GLU LYS LEU SER LYS ARG
SEQRES  24 C  384  HIS GLN TYR HIS ILE ARG ALA TYR ASP PRO LYS GLY GLY
SEQRES  25 C  384  LEU ASP ASN ALA ARG ARG LEU THR GLY PHE HIS GLU THR
SEQRES  26 C  384  SER ASN ILE ASN ASP PHE SER ALA GLY VAL ALA ASN ARG
SEQRES  27 C  384  SER ALA SER ILE ARG ILE PRO ARG THR VAL GLY GLN GLU
SEQRES  28 C  384  LYS LYS GLY TYR PHE GLU ASP ARG ARG PRO SER ALA ASN
SEQRES  29 C  384  CYS ASP PRO PHE SER VAL THR GLU ALA LEU ILE ARG THR
SEQRES  30 C  384  CYS LEU LEU ASN GLU THR GLY
SEQRES   1 D  384  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES   2 D  384  GLY THR GLU ASN LEU TYR PHE GLN SER MET ALA SER SER
SEQRES   3 D  384  HIS LEU ASN LYS GLY ILE LYS GLN VAL TYR MET SER LEU
SEQRES   4 D  384  PRO GLN GLY GLU LYS VAL GLN ALA MET TYR ILE TRP ILE
SEQRES   5 D  384  ASP GLY THR GLY GLU GLY LEU ARG CYS LYS THR ARG THR
SEQRES   6 D  384  LEU ASP SER GLU PRO LYS CYS VAL GLU GLU LEU PRO GLU
SEQRES   7 D  384  TRP ASN PHE ASP GLY SER SER THR LEU GLN SER GLU GLY
SEQRES   8 D  384  SER ASN SER ASP MET TYR LEU VAL PRO ALA ALA MET PHE
SEQRES   9 D  384  ARG ASP PRO PHE ARG LYS ASP PRO ASN LYS LEU VAL LEU
SEQRES  10 D  384  CYS GLU VAL PHE LYS TYR ASN ARG ARG PRO ALA GLU THR
SEQRES  11 D  384  ASN LEU ARG HIS THR CYS LYS ARG ILE MET ASP MET VAL
SEQRES  12 D  384  SER ASN GLN HIS PRO TRP PHE GLY MET GLU GLN GLU TYR
SEQRES  13 D  384  THR LEU MET GLY THR ASP GLY HIS PRO PHE GLY TRP PRO
SEQRES  14 D  384  SER ASN GLY PHE PRO GLY PRO GLN GLY PRO TYR TYR CYS
SEQRES  15 D  384  GLY VAL GLY ALA ASP ARG ALA TYR GLY ARG ASP ILE VAL
SEQRES  16 D  384  GLU ALA HIS TYR ARG ALA CYS LEU TYR ALA GLY VAL LYS
SEQRES  17 D  384  ILE ALA GLY THR ASN ALA GLU VAL MET PRO ALA GLN TRP
SEQRES  18 D  384  GLU PHE GLN ILE GLY PRO CYS GLU GLY ILE SER MET GLY
SEQRES  19 D  384  ASP HIS LEU TRP VAL ALA ARG PHE ILE LEU HIS ARG VAL
SEQRES  20 D  384  CYS GLU ASP PHE GLY VAL ILE ALA THR PHE ASP PRO LYS
SEQRES  21 D  384  PRO ILE PRO GLY ASN TRP ASN GLY ALA GLY CYS HIS THR
SEQRES  22 D  384  ASN PHE SER THR LYS ALA MET ARG GLU GLU ASN GLY LEU
SEQRES  23 D  384  LYS TYR ILE GLU GLU ALA ILE GLU LYS LEU SER LYS ARG
SEQRES  24 D  384  HIS GLN TYR HIS ILE ARG ALA TYR ASP PRO LYS GLY GLY
SEQRES  25 D  384  LEU ASP ASN ALA ARG ARG LEU THR GLY PHE HIS GLU THR
SEQRES  26 D  384  SER ASN ILE ASN ASP PHE SER ALA GLY VAL ALA ASN ARG
SEQRES  27 D  384  SER ALA SER ILE ARG ILE PRO ARG THR VAL GLY GLN GLU
SEQRES  28 D  384  LYS LYS GLY TYR PHE GLU ASP ARG ARG PRO SER ALA ASN
SEQRES  29 D  384  CYS ASP PRO PHE SER VAL THR GLU ALA LEU ILE ARG THR
SEQRES  30 D  384  CYS LEU LEU ASN GLU THR GLY
SEQRES   1 E  384  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES   2 E  384  GLY THR GLU ASN LEU TYR PHE GLN SER MET ALA SER SER
SEQRES   3 E  384  HIS LEU ASN LYS GLY ILE LYS GLN VAL TYR MET SER LEU
SEQRES   4 E  384  PRO GLN GLY GLU LYS VAL GLN ALA MET TYR ILE TRP ILE
SEQRES   5 E  384  ASP GLY THR GLY GLU GLY LEU ARG CYS LYS THR ARG THR
SEQRES   6 E  384  LEU ASP SER GLU PRO LYS CYS VAL GLU GLU LEU PRO GLU
SEQRES   7 E  384  TRP ASN PHE ASP GLY SER SER THR LEU GLN SER GLU GLY
SEQRES   8 E  384  SER ASN SER ASP MET TYR LEU VAL PRO ALA ALA MET PHE
SEQRES   9 E  384  ARG ASP PRO PHE ARG LYS ASP PRO ASN LYS LEU VAL LEU
SEQRES  10 E  384  CYS GLU VAL PHE LYS TYR ASN ARG ARG PRO ALA GLU THR
SEQRES  11 E  384  ASN LEU ARG HIS THR CYS LYS ARG ILE MET ASP MET VAL
SEQRES  12 E  384  SER ASN GLN HIS PRO TRP PHE GLY MET GLU GLN GLU TYR
SEQRES  13 E  384  THR LEU MET GLY THR ASP GLY HIS PRO PHE GLY TRP PRO
SEQRES  14 E  384  SER ASN GLY PHE PRO GLY PRO GLN GLY PRO TYR TYR CYS
SEQRES  15 E  384  GLY VAL GLY ALA ASP ARG ALA TYR GLY ARG ASP ILE VAL
SEQRES  16 E  384  GLU ALA HIS TYR ARG ALA CYS LEU TYR ALA GLY VAL LYS
SEQRES  17 E  384  ILE ALA GLY THR ASN ALA GLU VAL MET PRO ALA GLN TRP
SEQRES  18 E  384  GLU PHE GLN ILE GLY PRO CYS GLU GLY ILE SER MET GLY
SEQRES  19 E  384  ASP HIS LEU TRP VAL ALA ARG PHE ILE LEU HIS ARG VAL
SEQRES  20 E  384  CYS GLU ASP PHE GLY VAL ILE ALA THR PHE ASP PRO LYS
SEQRES  21 E  384  PRO ILE PRO GLY ASN TRP ASN GLY ALA GLY CYS HIS THR
SEQRES  22 E  384  ASN PHE SER THR LYS ALA MET ARG GLU GLU ASN GLY LEU
SEQRES  23 E  384  LYS TYR ILE GLU GLU ALA ILE GLU LYS LEU SER LYS ARG
SEQRES  24 E  384  HIS GLN TYR HIS ILE ARG ALA TYR ASP PRO LYS GLY GLY
SEQRES  25 E  384  LEU ASP ASN ALA ARG ARG LEU THR GLY PHE HIS GLU THR
SEQRES  26 E  384  SER ASN ILE ASN ASP PHE SER ALA GLY VAL ALA ASN ARG
SEQRES  27 E  384  SER ALA SER ILE ARG ILE PRO ARG THR VAL GLY GLN GLU
SEQRES  28 E  384  LYS LYS GLY TYR PHE GLU ASP ARG ARG PRO SER ALA ASN
SEQRES  29 E  384  CYS ASP PRO PHE SER VAL THR GLU ALA LEU ILE ARG THR
SEQRES  30 E  384  CYS LEU LEU ASN GLU THR GLY
HET     MN  A 401       1
HET     MN  A 402       1
HET     MN  A 403       1
HET     MN  A 404       1
HET    PO4  A 502       5
HET     MN  B 401       1
HET     MN  B 402       1
HET     MN  B 403       1
HET     MN  B 404       1
HET    PO4  B 502       5
HET     MN  C 401       1
HET     MN  C 402       1
HET     MN  C 403       1
HET     MN  C 404       1
HET    PO4  C 502       5
HET     MN  D 401       1
HET     MN  D 402       1
HET     MN  D 403       1
HET     MN  D 404       1
HET    PO4  D 502       5
HET     MN  E 401       1
HET     MN  E 402       1
HET     MN  E 403       1
HET     MN  E 404       1
HET    PO4  E 502       5
HET     CL  B1401       1
HET     CL  C1402       1
HET     CL  A1403       1
HET     CL  D1404       1
HET     CL  A1405       1
HET    ADP  A 501      27
HET    ADP  B 501      27
HET    ADP  C 501      27
HET    ADP  D 501      27
HET    ADP  E 501      27
HET    GOL  A1501       6
HET    GOL  B1502       6
HET    GOL  C1503       6
HET    GOL  D1504       6
HET    GOL  E1505       6
HET    GOL  C1506       6
HETNAM      MN MANGANESE (II) ION
HETNAM     PO4 PHOSPHATE ION
HETNAM      CL CHLORIDE ION
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM     GOL GLYCEROL
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   6   MN    20(MN 2+)
FORMUL  10  PO4    5(O4 P 3-)
FORMUL  31   CL    5(CL 1-)
FORMUL  36  ADP    5(C10 H15 N5 O10 P2)
FORMUL  41  GOL    6(C3 H8 O3)
FORMUL  47  HOH   *1390(H2 O)
HELIX    1   1 MET A    4  LEU A    9  5                                   6
HELIX    2   2 ASN A   10  SER A   19  1                                  10
HELIX    3   3 CYS A   53  LEU A   57  5                                   5
HELIX    4   4 GLU A   71  ASN A   74  5                                   4
HELIX    5   5 LEU A  113  VAL A  124  1                                  12
HELIX    6   6 SER A  125  HIS A  128  5                                   4
HELIX    7   7 GLY A  172  GLY A  187  1                                  16
HELIX    8   8 ILE A  212  GLY A  233  1                                  22
HELIX    9   9 THR A  258  GLU A  263  1                                   6
HELIX   10  10 GLY A  266  LYS A  279  1                                  14
HELIX   11  11 ARG A  280  TYR A  288  1                                   9
HELIX   12  12 ASP A  295  ARG A  299  5                                   5
HELIX   13  13 PRO A  326  LYS A  333  1                                   8
HELIX   14  14 ASP A  347  LEU A  360  1                                  14
HELIX   15  15 MET B    4  LEU B    9  5                                   6
HELIX   16  16 ASN B   10  SER B   19  1                                  10
HELIX   17  17 CYS B   53  LEU B   57  5                                   5
HELIX   18  18 GLU B   71  ASN B   74  5                                   4
HELIX   19  19 LEU B  113  MET B  123  1                                  11
HELIX   20  20 VAL B  124  HIS B  128  5                                   5
HELIX   21  21 GLY B  172  GLY B  187  1                                  16
HELIX   22  22 ILE B  212  GLY B  233  1                                  22
HELIX   23  23 THR B  258  GLU B  263  1                                   6
HELIX   24  24 GLY B  266  LYS B  279  1                                  14
HELIX   25  25 ARG B  280  TYR B  288  1                                   9
HELIX   26  26 ASP B  295  ARG B  299  5                                   5
HELIX   27  27 PRO B  326  LYS B  333  1                                   8
HELIX   28  28 ASP B  347  LEU B  360  1                                  14
HELIX   29  29 ALA C    5  LEU C    9  5                                   5
HELIX   30  30 ASN C   10  SER C   19  1                                  10
HELIX   31  31 CYS C   53  LEU C   57  5                                   5
HELIX   32  32 GLU C   71  ASN C   74  5                                   4
HELIX   33  33 LEU C  113  VAL C  124  1                                  12
HELIX   34  34 SER C  125  HIS C  128  5                                   4
HELIX   35  35 GLY C  172  GLY C  187  1                                  16
HELIX   36  36 ILE C  212  GLY C  233  1                                  22
HELIX   37  37 THR C  258  GLU C  263  1                                   6
HELIX   38  38 GLY C  266  LYS C  279  1                                  14
HELIX   39  39 ARG C  280  TYR C  288  1                                   9
HELIX   40  40 GLY C  293  ARG C  298  1                                   6
HELIX   41  41 PRO C  326  LYS C  333  1                                   8
HELIX   42  42 ASP C  347  LEU C  360  1                                  14
HELIX   43  43 ALA D    5  LEU D    9  5                                   5
HELIX   44  44 ASN D   10  SER D   19  1                                  10
HELIX   45  45 CYS D   53  LEU D   57  5                                   5
HELIX   46  46 GLU D   71  ASN D   74  5                                   4
HELIX   47  47 LEU D  113  VAL D  124  1                                  12
HELIX   48  48 SER D  125  HIS D  128  5                                   4
HELIX   49  49 GLY D  172  GLY D  187  1                                  16
HELIX   50  50 ILE D  212  GLY D  233  1                                  22
HELIX   51  51 THR D  258  GLU D  263  1                                   6
HELIX   52  52 GLY D  266  LYS D  279  1                                  14
HELIX   53  53 ARG D  280  TYR D  288  1                                   9
HELIX   54  54 ASP D  295  ARG D  299  5                                   5
HELIX   55  55 PRO D  326  LYS D  333  1                                   8
HELIX   56  56 ASP D  347  LEU D  360  1                                  14
HELIX   57  57 ALA E    5  LEU E    9  5                                   5
HELIX   58  58 ASN E   10  SER E   19  1                                  10
HELIX   59  59 CYS E   53  LEU E   57  5                                   5
HELIX   60  60 GLU E   71  ASN E   74  5                                   4
HELIX   61  61 LEU E  113  MET E  123  1                                  11
HELIX   62  62 VAL E  124  HIS E  128  5                                   5
HELIX   63  63 GLY E  172  GLY E  187  1                                  16
HELIX   64  64 ILE E  212  GLY E  233  1                                  22
HELIX   65  65 THR E  258  GLU E  263  1                                   6
HELIX   66  66 GLY E  266  LYS E  279  1                                  14
HELIX   67  67 ARG E  280  TYR E  288  1                                   9
HELIX   68  68 ASP E  295  ARG E  299  5                                   5
HELIX   69  69 PRO E  326  LYS E  333  1                                   8
HELIX   70  70 ASP E  347  LEU E  360  1                                  14
SHEET    1   A 9 TRP A  60  ASP A  63  0
SHEET    2   A 9 ASP A  76  ARG A  86 -1  O  LEU A  79   N  TRP A  60
SHEET    3   A 9 LYS A  95  PHE A 102 -1  O  GLU A 100   N  VAL A  80
SHEET    4   A 9 VAL A  26  ILE A  33  1  N  ILE A  31   O  VAL A  97
SHEET    5   A 9 LEU A  40  LEU A  47 -1  O  LEU A  47   N  VAL A  26
SHEET    6   A 9 ILE B 190  ALA B 195 -1  O  ALA B 191   N  THR A  46
SHEET    7   A 9 GLN B 201  GLU B 210 -1  O  GLN B 205   N  ALA B 191
SHEET    8   A 9 TRP B 130  MET B 140 -1  N  PHE B 131   O  CYS B 209
SHEET    9   A 9 ILE B 235  THR B 237 -1  O  ILE B 235   N  MET B 140
SHEET    1   B12 TRP A  60  ASP A  63  0
SHEET    2   B12 ASP A  76  ARG A  86 -1  O  LEU A  79   N  TRP A  60
SHEET    3   B12 LYS A  95  PHE A 102 -1  O  GLU A 100   N  VAL A  80
SHEET    4   B12 VAL A  26  ILE A  33  1  N  ILE A  31   O  VAL A  97
SHEET    5   B12 LEU A  40  LEU A  47 -1  O  LEU A  47   N  VAL A  26
SHEET    6   B12 ILE B 190  ALA B 195 -1  O  ALA B 191   N  THR A  46
SHEET    7   B12 GLN B 201  GLU B 210 -1  O  GLN B 205   N  ALA B 191
SHEET    8   B12 TRP B 130  MET B 140 -1  N  PHE B 131   O  CYS B 209
SHEET    9   B12 CYS B 252  SER B 257 -1  O  ASN B 255   N  GLY B 132
SHEET   10   B12 PHE B 337  ASP B 339 -1  O  ASP B 339   N  THR B 254
SHEET   11   B12 ILE B 323  ILE B 325 -1  N  ARG B 324   O  GLU B 338
SHEET   12   B12 ALA B 314  VAL B 316  1  N  GLY B 315   O  ILE B 323
SHEET    1   C 6 ILE A 235  THR A 237  0
SHEET    2   C 6 TRP A 130  MET A 140 -1  N  MET A 140   O  ILE A 235
SHEET    3   C 6 CYS A 252  SER A 257 -1  O  ASN A 255   N  GLY A 132
SHEET    4   C 6 PHE A 337  ASP A 339 -1  O  ASP A 339   N  THR A 254
SHEET    5   C 6 ILE A 323  ILE A 325 -1  N  ARG A 324   O  GLU A 338
SHEET    6   C 6 ALA A 314  VAL A 316  1  N  GLY A 315   O  ILE A 323
SHEET    1   D 9 ILE A 235  THR A 237  0
SHEET    2   D 9 TRP A 130  MET A 140 -1  N  MET A 140   O  ILE A 235
SHEET    3   D 9 GLN A 201  GLU A 210 -1  O  CYS A 209   N  PHE A 131
SHEET    4   D 9 ILE A 190  ALA A 195 -1  N  ALA A 191   O  GLN A 205
SHEET    5   D 9 LEU E  40  LEU E  47 -1  O  THR E  44   N  THR A 193
SHEET    6   D 9 VAL E  26  ILE E  33 -1  N  VAL E  26   O  LEU E  47
SHEET    7   D 9 LYS E  95  PHE E 102  1  O  VAL E  97   N  MET E  29
SHEET    8   D 9 ASP E  76  ARG E  86 -1  N  ALA E  82   O  LEU E  98
SHEET    9   D 9 TRP E  60  ASP E  63 -1  N  TRP E  60   O  LEU E  79
SHEET    1   E 9 TRP B  60  ASP B  63  0
SHEET    2   E 9 ASP B  76  ARG B  86 -1  O  LEU B  79   N  TRP B  60
SHEET    3   E 9 LYS B  95  PHE B 102 -1  O  LEU B  98   N  ALA B  82
SHEET    4   E 9 VAL B  26  ILE B  33  1  N  MET B  29   O  LYS B  95
SHEET    5   E 9 LEU B  40  LEU B  47 -1  O  LEU B  47   N  VAL B  26
SHEET    6   E 9 ILE C 190  ALA C 195 -1  O  THR C 193   N  THR B  44
SHEET    7   E 9 GLN C 201  GLU C 210 -1  O  GLN C 205   N  GLY C 192
SHEET    8   E 9 TRP C 130  MET C 140 -1  N  PHE C 131   O  CYS C 209
SHEET    9   E 9 ILE C 235  THR C 237 -1  O  ILE C 235   N  MET C 140
SHEET    1   F12 TRP B  60  ASP B  63  0
SHEET    2   F12 ASP B  76  ARG B  86 -1  O  LEU B  79   N  TRP B  60
SHEET    3   F12 LYS B  95  PHE B 102 -1  O  LEU B  98   N  ALA B  82
SHEET    4   F12 VAL B  26  ILE B  33  1  N  MET B  29   O  LYS B  95
SHEET    5   F12 LEU B  40  LEU B  47 -1  O  LEU B  47   N  VAL B  26
SHEET    6   F12 ILE C 190  ALA C 195 -1  O  THR C 193   N  THR B  44
SHEET    7   F12 GLN C 201  GLU C 210 -1  O  GLN C 205   N  GLY C 192
SHEET    8   F12 TRP C 130  MET C 140 -1  N  PHE C 131   O  CYS C 209
SHEET    9   F12 CYS C 252  SER C 257 -1  O  ASN C 255   N  GLY C 132
SHEET   10   F12 PHE C 337  ASP C 339 -1  O  ASP C 339   N  THR C 254
SHEET   11   F12 ILE C 323  ILE C 325 -1  N  ARG C 324   O  GLU C 338
SHEET   12   F12 ALA C 314  VAL C 316  1  N  GLY C 315   O  ILE C 325
SHEET    1   G 9 TRP C  60  ASP C  63  0
SHEET    2   G 9 ASP C  76  ARG C  86 -1  O  LEU C  79   N  TRP C  60
SHEET    3   G 9 LYS C  95  PHE C 102 -1  O  LEU C  98   N  ALA C  82
SHEET    4   G 9 VAL C  26  ILE C  33  1  N  ILE C  31   O  VAL C  97
SHEET    5   G 9 LEU C  40  LEU C  47 -1  O  LEU C  47   N  VAL C  26
SHEET    6   G 9 ILE D 190  ALA D 195 -1  O  ALA D 191   N  THR C  46
SHEET    7   G 9 GLN D 201  GLU D 210 -1  O  GLN D 205   N  ALA D 191
SHEET    8   G 9 TRP D 130  MET D 140 -1  N  MET D 133   O  ILE D 206
SHEET    9   G 9 ILE D 235  THR D 237 -1  O  ILE D 235   N  MET D 140
SHEET    1   H12 TRP C  60  ASP C  63  0
SHEET    2   H12 ASP C  76  ARG C  86 -1  O  LEU C  79   N  TRP C  60
SHEET    3   H12 LYS C  95  PHE C 102 -1  O  LEU C  98   N  ALA C  82
SHEET    4   H12 VAL C  26  ILE C  33  1  N  ILE C  31   O  VAL C  97
SHEET    5   H12 LEU C  40  LEU C  47 -1  O  LEU C  47   N  VAL C  26
SHEET    6   H12 ILE D 190  ALA D 195 -1  O  ALA D 191   N  THR C  46
SHEET    7   H12 GLN D 201  GLU D 210 -1  O  GLN D 205   N  ALA D 191
SHEET    8   H12 TRP D 130  MET D 140 -1  N  MET D 133   O  ILE D 206
SHEET    9   H12 CYS D 252  SER D 257 -1  O  SER D 257   N  TRP D 130
SHEET   10   H12 PHE D 337  ASP D 339 -1  O  ASP D 339   N  THR D 254
SHEET   11   H12 ILE D 323  ILE D 325 -1  N  ARG D 324   O  GLU D 338
SHEET   12   H12 ALA D 314  VAL D 316  1  N  GLY D 315   O  ILE D 323
SHEET    1   I 9 TRP D  60  ASP D  63  0
SHEET    2   I 9 ASP D  76  ARG D  86 -1  O  LEU D  79   N  TRP D  60
SHEET    3   I 9 LYS D  95  PHE D 102 -1  O  LEU D  98   N  ALA D  83
SHEET    4   I 9 VAL D  26  ILE D  33  1  N  ILE D  31   O  VAL D  97
SHEET    5   I 9 LEU D  40  LEU D  47 -1  O  LEU D  47   N  VAL D  26
SHEET    6   I 9 ILE E 190  ALA E 195 -1  O  ALA E 191   N  THR D  46
SHEET    7   I 9 GLN E 201  GLU E 210 -1  O  GLN E 205   N  ALA E 191
SHEET    8   I 9 TRP E 130  MET E 140 -1  N  MET E 133   O  ILE E 206
SHEET    9   I 9 ILE E 235  THR E 237 -1  O  THR E 237   N  THR E 138
SHEET    1   J12 TRP D  60  ASP D  63  0
SHEET    2   J12 ASP D  76  ARG D  86 -1  O  LEU D  79   N  TRP D  60
SHEET    3   J12 LYS D  95  PHE D 102 -1  O  LEU D  98   N  ALA D  83
SHEET    4   J12 VAL D  26  ILE D  33  1  N  ILE D  31   O  VAL D  97
SHEET    5   J12 LEU D  40  LEU D  47 -1  O  LEU D  47   N  VAL D  26
SHEET    6   J12 ILE E 190  ALA E 195 -1  O  ALA E 191   N  THR D  46
SHEET    7   J12 GLN E 201  GLU E 210 -1  O  GLN E 205   N  ALA E 191
SHEET    8   J12 TRP E 130  MET E 140 -1  N  MET E 133   O  ILE E 206
SHEET    9   J12 CYS E 252  SER E 257 -1  O  ASN E 255   N  GLY E 132
SHEET   10   J12 PHE E 337  ASP E 339 -1  O  ASP E 339   N  THR E 254
SHEET   11   J12 ILE E 323  ILE E 325 -1  N  ARG E 324   O  GLU E 338
SHEET   12   J12 ALA E 314  VAL E 316  1  N  GLY E 315   O  ILE E 323
LINK         OE1 GLU A 134                MN    MN A 402     1555   1555  2.17
LINK         OE1 GLU A 134                MN    MN A 403     1555   1555  2.38
LINK         OE2 GLU A 136                MN    MN A 401     1555   1555  2.23
LINK         OE1 GLU A 196                MN    MN A 401     1555   1555  2.34
LINK         OE1 GLU A 196                MN    MN A 404     1555   1555  2.44
LINK         OE1 GLU A 203                MN    MN A 401     1555   1555  2.11
LINK         OE2 GLU A 203                MN    MN A 403     1555   1555  2.25
LINK         OE2 GLU A 338                MN    MN A 402     1555   1555  2.02
LINK         OE1 GLU B 134                MN    MN B 402     1555   1555  2.38
LINK         OE2 GLU B 134                MN    MN B 403     1555   1555  2.19
LINK         OE2 GLU B 134                MN    MN B 402     1555   1555  2.42
LINK         OE2 GLU B 136                MN    MN B 401     1555   1555  2.14
LINK         OE1 GLU B 196                MN    MN B 401     1555   1555  2.24
LINK         OE1 GLU B 203                MN    MN B 401     1555   1555  2.04
LINK         OE2 GLU B 203                MN    MN B 403     1555   1555  2.28
LINK         OE2 GLU B 338                MN    MN B 402     1555   1555  2.05
LINK         OE1 GLU C 134                MN    MN C 403     1555   1555  2.28
LINK         OE1 GLU C 134                MN    MN C 402     1555   1555  2.21
LINK         OE2 GLU C 136                MN    MN C 401     1555   1555  2.11
LINK         OE1 GLU C 196                MN    MN C 401     1555   1555  2.43
LINK         OE1 GLU C 196                MN    MN C 404     1555   1555  2.33
LINK         OE1 GLU C 203                MN    MN C 403     1555   1555  2.28
LINK         OE2 GLU C 203                MN    MN C 401     1555   1555  2.04
LINK         OE2 GLU C 338                MN    MN C 402     1555   1555  2.00
LINK         OE1 GLU D 134                MN    MN D 402     1555   1555  2.31
LINK         OE1 GLU D 134                MN    MN D 403     1555   1555  2.25
LINK         OE2 GLU D 136                MN    MN D 401     1555   1555  2.13
LINK         OE2 GLU D 196                MN    MN D 401     1555   1555  2.27
LINK         OE1 GLU D 203                MN    MN D 403     1555   1555  2.31
LINK         OE2 GLU D 203                MN    MN D 401     1555   1555  2.05
LINK         OE2 GLU D 338                MN    MN D 402     1555   1555  2.19
LINK         OE1 GLU E 134                MN    MN E 402     1555   1555  2.28
LINK         OE1 GLU E 134                MN    MN E 403     1555   1555  2.29
LINK         OE2 GLU E 136                MN    MN E 401     1555   1555  2.22
LINK         OE1 GLU E 196                MN    MN E 401     1555   1555  2.32
LINK         OE1 GLU E 203                MN    MN E 401     1555   1555  2.06
LINK         OE2 GLU E 203                MN    MN E 403     1555   1555  2.32
LINK         OE1 GLU E 338                MN    MN E 402     1555   1555  2.02
LINK        MN    MN A 401                 O4  PO4 A 502     1555   1555  2.37
LINK        MN    MN A 401                 O2  PO4 A 502     1555   1555  2.24
LINK        MN    MN A 401                 O   HOH A1686     1555   1555  2.34
LINK        MN    MN A 402                 O3B ADP A 501     1555   1555  2.12
LINK        MN    MN A 402                 O1  PO4 A 502     1555   1555  2.18
LINK        MN    MN A 403                 O2A ADP A 501     1555   1555  2.19
LINK        MN    MN A 403                 O1B ADP A 501     1555   1555  2.00
LINK        MN    MN A 403                 O   HOH A1635     1555   1555  2.29
LINK        MN    MN A 403                 O2  PO4 A 502     1555   1555  2.23
LINK        MN    MN A 404                 O4  PO4 A 502     1555   1555  2.24
LINK        MN    MN A 404                 O   HOH A1730     1555   1555  1.95
LINK        MN    MN A 404                 O   HOH A1729     1555   1555  2.15
LINK        MN    MN A 404                 O   HOH A1731     1555   1555  2.45
LINK        MN    MN B 401                 O3  PO4 B 502     1555   1555  2.36
LINK        MN    MN B 401                 O   HOH B1747     1555   1555  2.29
LINK        MN    MN B 401                 O4  PO4 B 502     1555   1555  2.44
LINK        MN    MN B 402                 O2B ADP B 501     1555   1555  2.26
LINK        MN    MN B 402                 O2  PO4 B 502     1555   1555  2.24
LINK        MN    MN B 403                 O2A ADP B 501     1555   1555  2.20
LINK        MN    MN B 403                 O3B ADP B 501     1555   1555  2.18
LINK        MN    MN B 403                 O   HOH B1616     1555   1555  2.14
LINK        MN    MN B 403                 O3  PO4 B 502     1555   1555  2.13
LINK        MN    MN B 404                 O   HOH B1740     1555   1555  2.31
LINK        MN    MN B 404                 O4  PO4 B 502     1555   1555  2.35
LINK        MN    MN B 404                 O   HOH B1738     1555   1555  2.31
LINK        MN    MN B 404                 O   HOH B1739     1555   1555  2.17
LINK        MN    MN B 404                 O   HOH B1730     1555   1555  2.20
LINK        MN    MN C 401                 O1  PO4 C 502     1555   1555  2.29
LINK        MN    MN C 401                 O   HOH C1745     1555   1555  2.37
LINK        MN    MN C 401                 O4  PO4 C 502     1555   1555  2.16
LINK        MN    MN C 402                 O2B ADP C 501     1555   1555  2.09
LINK        MN    MN C 402                 O3  PO4 C 502     1555   1555  2.27
LINK        MN    MN C 403                 O2A ADP C 501     1555   1555  2.10
LINK        MN    MN C 403                 O   HOH C1604     1555   1555  2.33
LINK        MN    MN C 403                 O3B ADP C 501     1555   1555  2.11
LINK        MN    MN C 403                 O1  PO4 C 502     1555   1555  2.13
LINK        MN    MN C 404                 O4  PO4 C 502     1555   1555  2.17
LINK        MN    MN C 404                 O   HOH B1741     1555   1555  2.30
LINK        MN    MN C 404                 O   HOH C1718     1555   1555  2.27
LINK        MN    MN C 404                 O   HOH C1719     1555   1555  2.22
LINK        MN    MN D 401                 O   HOH D1741     1555   1555  2.19
LINK        MN    MN D 401                 O1  PO4 D 502     1555   1555  2.37
LINK        MN    MN D 401                 O4  PO4 D 502     1555   1555  2.28
LINK        MN    MN D 402                 O2B ADP D 501     1555   1555  2.05
LINK        MN    MN D 402                 O3  PO4 D 502     1555   1555  2.16
LINK        MN    MN D 403                 O2A ADP D 501     1555   1555  2.06
LINK        MN    MN D 403                 O   HOH D1615     1555   1555  2.16
LINK        MN    MN D 403                 O3B ADP D 501     1555   1555  2.14
LINK        MN    MN D 403                 O1  PO4 D 502     1555   1555  2.16
LINK        MN    MN D 404                 O4  PO4 D 502     1555   1555  2.17
LINK        MN    MN D 404                 O   HOH D1740     1555   1555  2.08
LINK        MN    MN D 404                 O   HOH D1739     1555   1555  2.12
LINK        MN    MN D 404                 O   HOH D1609     1555   1555  2.34
LINK        MN    MN E 401                 O1  PO4 E 502     1555   1555  2.39
LINK        MN    MN E 401                 O   HOH E1666     1555   1555  2.39
LINK        MN    MN E 401                 O4  PO4 E 502     1555   1555  2.31
LINK        MN    MN E 402                 O2B ADP E 501     1555   1555  2.08
LINK        MN    MN E 402                 O3  PO4 E 502     1555   1555  2.20
LINK        MN    MN E 403                 O2A ADP E 501     1555   1555  2.04
LINK        MN    MN E 403                 O3B ADP E 501     1555   1555  2.33
LINK        MN    MN E 403                 O   HOH E1609     1555   1555  2.30
LINK        MN    MN E 403                 O1  PO4 E 502     1555   1555  2.04
LINK        MN    MN E 404                 O4  PO4 E 502     1555   1555  2.23
LINK        MN    MN E 404                 O   HOH E1716     1555   1555  2.12
LINK        MN    MN E 404                 O   HOH E1717     1555   1555  2.14
CISPEP   1 ASP B   92    PRO B   93          0        -3.72
SITE     1 AC1  6 GLU A 136  GLU A 196  GLU A 203   MN A 404
SITE     2 AC1  6 PO4 A 502  HOH A1686
SITE     1 AC2  6 GLU A 134  HIS A 253  GLU A 338  ARG A 340
SITE     2 AC2  6 ADP A 501  PO4 A 502
SITE     1 AC3  5 GLU A 134  GLU A 203  ADP A 501  PO4 A 502
SITE     2 AC3  5 HOH A1635
SITE     1 AC4  6 GLU A 196   MN A 401  PO4 A 502  HOH A1729
SITE     2 AC4  6 HOH A1730  HOH A1731
SITE     1 AC5 16 GLU A 134  GLU A 136  GLU A 196  GLU A 203
SITE     2 AC5 16 HIS A 253  ARG A 319  GLU A 338  ARG A 340
SITE     3 AC5 16  MN A 401   MN A 402   MN A 403   MN A 404
SITE     4 AC5 16 ADP A 501  HOH A1686  HOH A1730  HOH A1786
SITE     1 AC6  6 GLU B 136  GLU B 196  GLU B 203   MN B 404
SITE     2 AC6  6 PO4 B 502  HOH B1747
SITE     1 AC7  6 GLU B 134  HIS B 253  GLU B 338  ARG B 340
SITE     2 AC7  6 ADP B 501  PO4 B 502
SITE     1 AC8  5 GLU B 134  GLU B 203  ADP B 501  PO4 B 502
SITE     2 AC8  5 HOH B1616
SITE     1 AC9  7 GLU B 196   MN B 401  PO4 B 502  HOH B1730
SITE     2 AC9  7 HOH B1738  HOH B1739  HOH B1740
SITE     1 BC1 15 GLU B 134  GLU B 136  GLU B 196  GLU B 203
SITE     2 BC1 15 HIS B 253  ARG B 319  GLU B 338  ARG B 340
SITE     3 BC1 15  MN B 401   MN B 402   MN B 403   MN B 404
SITE     4 BC1 15 ADP B 501  HOH B1616  HOH B1740
SITE     1 BC2  6 GLU C 136  GLU C 196  GLU C 203   MN C 404
SITE     2 BC2  6 PO4 C 502  HOH C1745
SITE     1 BC3  6 GLU C 134  HIS C 253  GLU C 338  ARG C 340
SITE     2 BC3  6 ADP C 501  PO4 C 502
SITE     1 BC4  5 GLU C 134  GLU C 203  ADP C 501  PO4 C 502
SITE     2 BC4  5 HOH C1604
SITE     1 BC5  6 HOH B1741  GLU C 196   MN C 401  PO4 C 502
SITE     2 BC5  6 HOH C1718  HOH C1719
SITE     1 BC6 17 HOH B1741  GLU C 134  GLU C 136  GLU C 196
SITE     2 BC6 17 GLU C 203  HIS C 253  ARG C 319  GLU C 338
SITE     3 BC6 17 ARG C 340   MN C 401   MN C 402   MN C 403
SITE     4 BC6 17  MN C 404  ADP C 501  HOH C1707  HOH C1718
SITE     5 BC6 17 HOH C1745
SITE     1 BC7  6 GLU D 136  GLU D 196  GLU D 203   MN D 404
SITE     2 BC7  6 PO4 D 502  HOH D1741
SITE     1 BC8  6 GLU D 134  HIS D 253  GLU D 338  ARG D 340
SITE     2 BC8  6 ADP D 501  PO4 D 502
SITE     1 BC9  5 GLU D 134  GLU D 203  ADP D 501  PO4 D 502
SITE     2 BC9  5 HOH D1615
SITE     1 CC1  6 GLU D 196   MN D 401  PO4 D 502  HOH D1609
SITE     2 CC1  6 HOH D1739  HOH D1740
SITE     1 CC2 17 GLU D 134  GLU D 136  GLU D 196  GLU D 203
SITE     2 CC2 17 HIS D 253  ARG D 319  GLU D 338  ARG D 340
SITE     3 CC2 17  MN D 401   MN D 402   MN D 403   MN D 404
SITE     4 CC2 17 ADP D 501  HOH D1598  HOH D1739  HOH D1740
SITE     5 CC2 17 HOH D1741
SITE     1 CC3  6 GLU E 136  GLU E 196  GLU E 203   MN E 404
SITE     2 CC3  6 PO4 E 502  HOH E1666
SITE     1 CC4  6 GLU E 134  HIS E 253  GLU E 338  ARG E 340
SITE     2 CC4  6 ADP E 501  PO4 E 502
SITE     1 CC5  5 GLU E 134  GLU E 203  ADP E 501  PO4 E 502
SITE     2 CC5  5 HOH E1609
SITE     1 CC6  7 GLU E 136  GLU E 196   MN E 401  PO4 E 502
SITE     2 CC6  7 HOH E1611  HOH E1716  HOH E1717
SITE     1 CC7 15 GLU E 134  GLU E 136  GLU E 196  GLU E 203
SITE     2 CC7 15 HIS E 253  ARG E 319  GLU E 338  ARG E 340
SITE     3 CC7 15  MN E 401   MN E 402   MN E 403   MN E 404
SITE     4 CC7 15 ADP E 501  HOH E1699  HOH E1716
SITE     1 CC8  2 THR B  44  THR C 193
SITE     1 CC9  3 MET C  29  THR C  44  THR D 193
SITE     1 DC1  2 THR A 193  THR E  44
SITE     1 DC2  3 THR D  44  THR E 193  HOH E1531
SITE     1 DC3  2 THR A  44  THR B 193
SITE     1 DC4 23 TRP A 130  GLY A 132  GLU A 134  GLU A 203
SITE     2 DC4 23 GLN A 205  GLY A 207  PRO A 208  ASN A 255
SITE     3 DC4 23 SER A 257  ARG A 319  ARG A 324  TYR A 336
SITE     4 DC4 23 GLU A 338   MN A 402   MN A 403  PO4 A 502
SITE     5 DC4 23 HOH A1540  HOH A1587  HOH A1619  HOH A1620
SITE     6 DC4 23 HOH A1635  HOH A1664  HOH E1513
SITE     1 DC5 23 HOH A1575  TRP B 130  GLY B 132  GLU B 134
SITE     2 DC5 23 GLU B 203  GLN B 205  GLY B 207  PRO B 208
SITE     3 DC5 23 ASN B 255  SER B 257  ARG B 319  ARG B 324
SITE     4 DC5 23 TYR B 336  GLU B 338   MN B 402   MN B 403
SITE     5 DC5 23 PO4 B 502  HOH B1560  HOH B1570  HOH B1589
SITE     6 DC5 23 HOH B1616  HOH B1693  HOH B1753
SITE     1 DC6 23 TRP C 130  GLY C 132  GLU C 134  GLU C 203
SITE     2 DC6 23 GLN C 205  GLY C 207  PRO C 208  ASN C 255
SITE     3 DC6 23 SER C 257  ARG C 319  ARG C 324  TYR C 336
SITE     4 DC6 23 GLU C 338   MN C 402   MN C 403  PO4 C 502
SITE     5 DC6 23 HOH C1584  HOH C1600  HOH C1603  HOH C1604
SITE     6 DC6 23 HOH C1656  HOH C1674  HOH C1681
SITE     1 DC7 24 TRP D 130  GLY D 132  GLU D 134  GLU D 203
SITE     2 DC7 24 GLN D 205  GLY D 207  PRO D 208  ASN D 255
SITE     3 DC7 24 SER D 257  ARG D 319  ARG D 324  TYR D 336
SITE     4 DC7 24 GLU D 338   MN D 402   MN D 403  PO4 D 502
SITE     5 DC7 24 HOH D1585  HOH D1597  HOH D1615  HOH D1628
SITE     6 DC7 24 HOH D1631  HOH D1636  HOH D1716  HOH D1750
SITE     1 DC8 23 HOH D1617  TRP E 130  GLY E 132  GLU E 134
SITE     2 DC8 23 GLU E 203  GLN E 205  GLY E 207  PRO E 208
SITE     3 DC8 23 ASN E 255  SER E 257  ARG E 262  ARG E 319
SITE     4 DC8 23 ARG E 324  TYR E 336  GLU E 338   MN E 402
SITE     5 DC8 23  MN E 403  PO4 E 502  HOH E1540  HOH E1555
SITE     6 DC8 23 HOH E1609  HOH E1636  HOH E1644
SITE     1 DC9  6 LYS A  14  PRO A  88  PHE A  89  HOH A1543
SITE     2 DC9  6 HOH A1665  HOH A1694
SITE     1 EC1  8 TYR A  17  LYS B  14  PRO B  88  PHE B  89
SITE     2 EC1  8 HOH B1548  HOH B1674  HOH B1748  HOH B1756
SITE     1 EC2  5 LYS C  14  PRO C  88  PHE C  89  HOH C1557
SITE     2 EC2  5 HOH C1734
SITE     1 EC3  5 LYS D  14  PRO D  88  PHE D  89  HOH D1601
SITE     2 EC3  5 HOH D1752
SITE     1 EC4  7 VAL D  16  LYS E  14  PRO E  88  PHE E  89
SITE     2 EC4  7 HOH E1557  HOH E1594  HOH E1642
SITE     1 EC5  5 ALA C  82  SER C 213  ASP C 216  HIS C 217
SITE     2 EC5  5 HOH C1781
CRYST1  177.600  122.600  126.600  90.00 130.60  90.00 C 1 2 1      20
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      0.005631  0.000000  0.004826        0.00000
SCALE2      0.000000  0.008157  0.000000        0.00000
SCALE3      0.000000  0.000000  0.010403        0.00000
      
PROCHECK
Go to PROCHECK summary
 References