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PDBsum entry 2yjk

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Metal-binding protein PDB id
2yjk
Jmol
Contents
Protein chains
149 a.a.
(+ 2 more) 157 a.a.
Ligands
OFE ×11
Metals
_FE ×6
Waters ×705
HEADER    METAL-BINDING PROTEIN                   19-MAY-11   2YJK
TITLE     STRUCTURE OF DPS FROM MICROBACTERIUM ARBORESCENS IN THE
TITLE    2 HIGH IRON FORM
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: AFP;
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;
COMPND   4 SYNONYM: DPS
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: MICROBACTERIUM ARBORESCENS;
SOURCE   3 ORGANISM_TAXID: 33883
KEYWDS    METAL-BINDING PROTEIN, IRON UPTAKE, FERRITIN FOLD
EXPDTA    X-RAY DIFFRACTION
AUTHOR    K.ZETH,R.BUECHELER,W.BOLAND
REVDAT   2   12-OCT-11 2YJK    1       JRNL   REMARK VERSN
REVDAT   1   01-JUN-11 2YJK    0
JRNL        AUTH   J.PESEK,R.BUECHELER,R.ALBRECHT,W.BOLAND,K.ZETH
JRNL        TITL   STRUCTURE AND MECHANISM OF IRON TRANSLOCATION BY A
JRNL        TITL 2 DPS PROTEIN FROM MICROBACTERIUM ARBORESCENS.
JRNL        REF    J.BIOL.CHEM.                  V. 286 34872 2011
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   21768097
JRNL        DOI    10.1074/JBC.M111.246108
REMARK   2
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0109
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.98
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.00
REMARK   3   NUMBER OF REFLECTIONS             : 129604
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) : 0.17227
REMARK   3   R VALUE            (WORKING SET) : 0.16992
REMARK   3   FREE R VALUE                     : 0.21650
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0
REMARK   3   FREE R VALUE TEST SET COUNT      : 6821
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) : 1.998
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.050
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 9110
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK   3   BIN R VALUE           (WORKING SET) : 0.276
REMARK   3   BIN FREE R VALUE SET COUNT          : 479
REMARK   3   BIN FREE R VALUE                    : 0.309
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 13759
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 705
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.239
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.95
REMARK   3    B22 (A**2) : 0.89
REMARK   3    B33 (A**2) : -0.11
REMARK   3    B12 (A**2) : 0.00
REMARK   3    B13 (A**2) : -0.80
REMARK   3    B23 (A**2) : 0.00
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.155
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.147
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.108
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.706
REMARK   3
REMARK   3  CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.962
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.935
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 13994 ; 0.025 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 19111 ; 1.821 ; 1.936
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1821 ; 6.557 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   628 ;41.545 ;25.605
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2228 ;16.151 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    60 ;11.309 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2308 ; 0.138 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 10548 ; 0.009 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  9080 ; 1.168 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 14533 ; 2.159 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4914 ; 3.721 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4571 ; 6.166 ; 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 F G H I J K L
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     A     10       A     160      4
REMARK   3           1     B     10       B     160      4
REMARK   3           1     C     10       C     160      4
REMARK   3           1     D     10       D     160      4
REMARK   3           1     E     10       E     160      4
REMARK   3           1     F     10       F     160      4
REMARK   3           1     G     10       G     160      4
REMARK   3           1     H     10       H     160      4
REMARK   3           1     I     10       I     160      4
REMARK   3           1     J     10       J     160      4
REMARK   3           1     K     10       K     160      4
REMARK   3           1     L     10       L     160      4
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1100 ;  0.36 ;  0.50
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   1100 ;  0.22 ;  0.50
REMARK   3   MEDIUM POSITIONAL  1    C    (A):   1100 ;  0.23 ;  0.50
REMARK   3   MEDIUM POSITIONAL  1    D    (A):   1100 ;  0.19 ;  0.50
REMARK   3   MEDIUM POSITIONAL  1    E    (A):   1100 ;  0.33 ;  0.50
REMARK   3   MEDIUM POSITIONAL  1    F    (A):   1100 ;  0.36 ;  0.50
REMARK   3   MEDIUM POSITIONAL  1    G    (A):   1100 ;  0.30 ;  0.50
REMARK   3   MEDIUM POSITIONAL  1    H    (A):   1100 ;  0.24 ;  0.50
REMARK   3   MEDIUM POSITIONAL  1    I    (A):   1100 ;  0.18 ;  0.50
REMARK   3   MEDIUM POSITIONAL  1    J    (A):   1100 ;  0.27 ;  0.50
REMARK   3   MEDIUM POSITIONAL  1    K    (A):   1100 ;  0.29 ;  0.50
REMARK   3   MEDIUM POSITIONAL  1    L    (A):   1100 ;  0.27 ;  0.50
REMARK   3   MEDIUM THERMAL     1    A (A**2):   1100 ;  1.26 ;  2.00
REMARK   3   MEDIUM THERMAL     1    B (A**2):   1100 ;  1.23 ;  2.00
REMARK   3   MEDIUM THERMAL     1    C (A**2):   1100 ;  1.35 ;  2.00
REMARK   3   MEDIUM THERMAL     1    D (A**2):   1100 ;  1.29 ;  2.00
REMARK   3   MEDIUM THERMAL     1    E (A**2):   1100 ;  1.23 ;  2.00
REMARK   3   MEDIUM THERMAL     1    F (A**2):   1100 ;  1.67 ;  2.00
REMARK   3   MEDIUM THERMAL     1    G (A**2):   1100 ;  1.56 ;  2.00
REMARK   3   MEDIUM THERMAL     1    H (A**2):   1100 ;  1.68 ;  2.00
REMARK   3   MEDIUM THERMAL     1    I (A**2):   1100 ;  1.32 ;  2.00
REMARK   3   MEDIUM THERMAL     1    J (A**2):   1100 ;  1.36 ;  2.00
REMARK   3   MEDIUM THERMAL     1    K (A**2):   1100 ;  1.17 ;  2.00
REMARK   3   MEDIUM THERMAL     1    L (A**2):   1100 ;  1.19 ;  2.00
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 12
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    10        A   158
REMARK   3    ORIGIN FOR THE GROUP (A):  10.3580   3.7507   2.9134
REMARK   3    T TENSOR
REMARK   3      T11:   0.0964 T22:   0.1439
REMARK   3      T33:   0.0262 T12:   0.0092
REMARK   3      T13:  -0.0201 T23:   0.0257
REMARK   3    L TENSOR
REMARK   3      L11:   1.0688 L22:   1.2374
REMARK   3      L33:   0.4726 L12:   0.1263
REMARK   3      L13:  -0.2205 L23:   0.1650
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0216 S12:   0.1919 S13:   0.0512
REMARK   3      S21:  -0.0321 S22:  -0.0298 S23:  -0.0287
REMARK   3      S31:  -0.0972 S32:  -0.0166 S33:   0.0514
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 :   B     7        B   158
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.3684  -1.8379  15.0941
REMARK   3    T TENSOR
REMARK   3      T11:   0.0320 T22:   0.1106
REMARK   3      T33:   0.0430 T12:   0.0164
REMARK   3      T13:  -0.0044 T23:  -0.0266
REMARK   3    L TENSOR
REMARK   3      L11:   0.7098 L22:   1.4764
REMARK   3      L33:   0.7284 L12:   0.0284
REMARK   3      L13:  -0.0526 L23:  -0.1184
REMARK   3    S TENSOR
REMARK   3      S11:   0.0036 S12:   0.1000 S13:   0.0196
REMARK   3      S21:  -0.0153 S22:  -0.0194 S23:   0.0872
REMARK   3      S31:  -0.0620 S32:  -0.0979 S33:   0.0158
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 :   C     2        C   158
REMARK   3    ORIGIN FOR THE GROUP (A):  17.2327  28.6702  21.5173
REMARK   3    T TENSOR
REMARK   3      T11:   0.2059 T22:   0.0410
REMARK   3      T33:   0.1393 T12:   0.0097
REMARK   3      T13:  -0.0564 T23:   0.0600
REMARK   3    L TENSOR
REMARK   3      L11:   1.3063 L22:   0.5342
REMARK   3      L33:   1.1055 L12:   0.0241
REMARK   3      L13:   0.3021 L23:   0.0703
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0793 S12:   0.1365 S13:   0.1828
REMARK   3      S21:  -0.0476 S22:  -0.0265 S23:  -0.0385
REMARK   3      S31:  -0.1443 S32:   0.0522 S33:   0.1058
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 :   D     7        D   158
REMARK   3    ORIGIN FOR THE GROUP (A):   5.0697 -27.8019  26.2796
REMARK   3    T TENSOR
REMARK   3      T11:   0.0683 T22:   0.0347
REMARK   3      T33:   0.1243 T12:  -0.0132
REMARK   3      T13:  -0.0014 T23:  -0.0377
REMARK   3    L TENSOR
REMARK   3      L11:   1.1654 L22:   0.4016
REMARK   3      L33:   1.2178 L12:  -0.1886
REMARK   3      L13:   0.2261 L23:   0.0143
REMARK   3    S TENSOR
REMARK   3      S11:   0.0417 S12:   0.0290 S13:  -0.1544
REMARK   3      S21:   0.0216 S22:  -0.0312 S23:   0.0622
REMARK   3      S31:   0.0391 S32:  -0.1055 S33:  -0.0105
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 :   E     7        E   158
REMARK   3    ORIGIN FOR THE GROUP (A):  39.6256   8.5351  14.1301
REMARK   3    T TENSOR
REMARK   3      T11:   0.0813 T22:   0.1512
REMARK   3      T33:   0.0713 T12:  -0.0248
REMARK   3      T13:   0.0218 T23:   0.0633
REMARK   3    L TENSOR
REMARK   3      L11:   0.9102 L22:   1.1620
REMARK   3      L33:   0.7771 L12:  -0.1711
REMARK   3      L13:   0.4998 L23:  -0.1261
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0276 S12:   0.2589 S13:   0.1138
REMARK   3      S21:  -0.1136 S22:  -0.0202 S23:   0.0312
REMARK   3      S31:  -0.0864 S32:   0.0668 S33:   0.0478
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 :   F     7        F   158
REMARK   3    ORIGIN FOR THE GROUP (A):  41.7097 -13.1876  20.7625
REMARK   3    T TENSOR
REMARK   3      T11:   0.0320 T22:   0.0910
REMARK   3      T33:   0.0709 T12:   0.0093
REMARK   3      T13:   0.0440 T23:  -0.0035
REMARK   3    L TENSOR
REMARK   3      L11:   1.1184 L22:   1.0107
REMARK   3      L33:   1.2012 L12:   0.0731
REMARK   3      L13:   0.4864 L23:  -0.1449
REMARK   3    S TENSOR
REMARK   3      S11:   0.0100 S12:   0.0874 S13:  -0.0566
REMARK   3      S21:  -0.0392 S22:  -0.0061 S23:  -0.0106
REMARK   3      S31:  -0.0021 S32:   0.0635 S33:  -0.0039
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 :   G     6        G   158
REMARK   3    ORIGIN FOR THE GROUP (A):  23.8831   3.4395  62.7274
REMARK   3    T TENSOR
REMARK   3      T11:   0.0706 T22:   0.0629
REMARK   3      T33:   0.0186 T12:  -0.0043
REMARK   3      T13:  -0.0078 T23:  -0.0211
REMARK   3    L TENSOR
REMARK   3      L11:   0.8989 L22:   1.2479
REMARK   3      L33:   0.6666 L12:  -0.1303
REMARK   3      L13:  -0.0223 L23:   0.2343
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0212 S12:  -0.1294 S13:   0.0490
REMARK   3      S21:  -0.0044 S22:  -0.0544 S23:   0.0622
REMARK   3      S31:  -0.0646 S32:  -0.0543 S33:   0.0756
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 :   H     7        H   158
REMARK   3    ORIGIN FOR THE GROUP (A):  40.9379  -6.0671  51.0622
REMARK   3    T TENSOR
REMARK   3      T11:   0.0169 T22:   0.0329
REMARK   3      T33:   0.0222 T12:  -0.0009
REMARK   3      T13:  -0.0089 T23:   0.0202
REMARK   3    L TENSOR
REMARK   3      L11:   1.0104 L22:   1.3737
REMARK   3      L33:   1.0117 L12:  -0.2505
REMARK   3      L13:  -0.0373 L23:   0.3967
REMARK   3    S TENSOR
REMARK   3      S11:   0.0101 S12:  -0.0520 S13:  -0.0550
REMARK   3      S21:   0.0163 S22:  -0.0137 S23:  -0.0282
REMARK   3      S31:   0.0359 S32:   0.0638 S33:   0.0036
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 :   I    11        I   158
REMARK   3    ORIGIN FOR THE GROUP (A):  22.4593  28.3857  43.7271
REMARK   3    T TENSOR
REMARK   3      T11:   0.1798 T22:   0.0066
REMARK   3      T33:   0.1353 T12:   0.0170
REMARK   3      T13:  -0.0483 T23:  -0.0197
REMARK   3    L TENSOR
REMARK   3      L11:   1.2070 L22:   0.3978
REMARK   3      L33:   1.3410 L12:   0.0076
REMARK   3      L13:   0.1135 L23:  -0.1582
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0761 S12:  -0.0323 S13:   0.2087
REMARK   3      S21:   0.0098 S22:  -0.0321 S23:   0.0341
REMARK   3      S31:  -0.1786 S32:  -0.0445 S33:   0.1082
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 :   J    11        J   158
REMARK   3    ORIGIN FOR THE GROUP (A):  22.7924 -29.3318  40.5757
REMARK   3    T TENSOR
REMARK   3      T11:   0.0835 T22:   0.0038
REMARK   3      T33:   0.1276 T12:  -0.0034
REMARK   3      T13:  -0.0059 T23:   0.0088
REMARK   3    L TENSOR
REMARK   3      L11:   1.4410 L22:   0.2694
REMARK   3      L33:   1.0896 L12:   0.0745
REMARK   3      L13:   0.2087 L23:   0.0227
REMARK   3    S TENSOR
REMARK   3      S11:   0.0308 S12:   0.0458 S13:  -0.1514
REMARK   3      S21:   0.0240 S22:  -0.0122 S23:  -0.0241
REMARK   3      S31:   0.0868 S32:   0.0056 S33:  -0.0186
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 :   K     7        K   158
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.2276  12.7411  51.8780
REMARK   3    T TENSOR
REMARK   3      T11:   0.0841 T22:   0.1223
REMARK   3      T33:   0.1057 T12:   0.0520
REMARK   3      T13:   0.0258 T23:  -0.0738
REMARK   3    L TENSOR
REMARK   3      L11:   1.1590 L22:   1.2060
REMARK   3      L33:   1.0342 L12:   0.2536
REMARK   3      L13:   0.6768 L23:   0.0788
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0670 S12:  -0.1941 S13:   0.1001
REMARK   3      S21:   0.0715 S22:   0.0046 S23:  -0.0206
REMARK   3      S31:  -0.1121 S32:  -0.1473 S33:   0.0624
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 :   L     7        L   158
REMARK   3    ORIGIN FOR THE GROUP (A): -10.3140  -8.3160  45.3297
REMARK   3    T TENSOR
REMARK   3      T11:   0.0304 T22:   0.1320
REMARK   3      T33:   0.0721 T12:  -0.0073
REMARK   3      T13:   0.0418 T23:  -0.0184
REMARK   3    L TENSOR
REMARK   3      L11:   0.7990 L22:   0.7574
REMARK   3      L33:   1.2367 L12:   0.0616
REMARK   3      L13:   0.6741 L23:   0.1764
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0020 S12:  -0.0368 S13:  -0.0175
REMARK   3      S21:   0.0586 S22:  -0.0076 S23:  -0.0008
REMARK   3      S31:  -0.0093 S32:  -0.1286 S33:   0.0096
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
REMARK   3   RIDING POSITIONS.
REMARK   4
REMARK   4 2YJK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-MAY-11.
REMARK 100 THE PDBE ID CODE IS EBI-48353.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SLS
REMARK 200  BEAMLINE                       : X06DA
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD (MX-225)
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : XDS
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 129605
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.00
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.00
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.5
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0
REMARK 200  DATA REDUNDANCY                : 2.05
REMARK 200  R MERGE                    (I) : 0.10
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 7.30
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.05
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.8
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.0
REMARK 200  R MERGE FOR SHELL          (I) : 0.88
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 1.50
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 1O9R
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS  (%): 51.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG 8000, 2% ISO-PROPANOL, 0.1
REMARK 280  M NA-ACETATE, PH 7.5.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       46.02500
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DODECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 42800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 55180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -346.9 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350                    AND CHAINS: K, L
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     MET A    -2
REMARK 465     THR A    -1
REMARK 465     ASP A     0
REMARK 465     THR A     1
REMARK 465     ASN A     2
REMARK 465     ILE A     3
REMARK 465     THR A     4
REMARK 465     THR A     5
REMARK 465     PRO A     6
REMARK 465     ALA A     7
REMARK 465     LEU A     8
REMARK 465     THR A     9
REMARK 465     MET B    -2
REMARK 465     THR B    -1
REMARK 465     ASP B     0
REMARK 465     THR B     1
REMARK 465     ASN B     2
REMARK 465     ILE B     3
REMARK 465     THR B     4
REMARK 465     THR B     5
REMARK 465     PRO B     6
REMARK 465     MET C    -2
REMARK 465     THR C    -1
REMARK 465     ASP C     0
REMARK 465     THR C     1
REMARK 465     MET D    -2
REMARK 465     THR D    -1
REMARK 465     ASP D     0
REMARK 465     THR D     1
REMARK 465     ASN D     2
REMARK 465     ILE D     3
REMARK 465     THR D     4
REMARK 465     THR D     5
REMARK 465     PRO D     6
REMARK 465     MET E    -2
REMARK 465     THR E    -1
REMARK 465     ASP E     0
REMARK 465     THR E     1
REMARK 465     ASN E     2
REMARK 465     ILE E     3
REMARK 465     THR E     4
REMARK 465     THR E     5
REMARK 465     PRO E     6
REMARK 465     MET F    -2
REMARK 465     THR F    -1
REMARK 465     ASP F     0
REMARK 465     THR F     1
REMARK 465     ASN F     2
REMARK 465     ILE F     3
REMARK 465     THR F     4
REMARK 465     THR F     5
REMARK 465     PRO F     6
REMARK 465     MET G    -2
REMARK 465     THR G    -1
REMARK 465     ASP G     0
REMARK 465     THR G     1
REMARK 465     ASN G     2
REMARK 465     ILE G     3
REMARK 465     THR G     4
REMARK 465     THR G     5
REMARK 465     MET H    -2
REMARK 465     THR H    -1
REMARK 465     ASP H     0
REMARK 465     THR H     1
REMARK 465     ASN H     2
REMARK 465     ILE H     3
REMARK 465     THR H     4
REMARK 465     THR H     5
REMARK 465     PRO H     6
REMARK 465     MET I    -2
REMARK 465     THR I    -1
REMARK 465     ASP I     0
REMARK 465     THR I     1
REMARK 465     ASN I     2
REMARK 465     ILE I     3
REMARK 465     THR I     4
REMARK 465     THR I     5
REMARK 465     PRO I     6
REMARK 465     ALA I     7
REMARK 465     LEU I     8
REMARK 465     THR I     9
REMARK 465     ALA I    10
REMARK 465     MET J    -2
REMARK 465     THR J    -1
REMARK 465     ASP J     0
REMARK 465     THR J     1
REMARK 465     ASN J     2
REMARK 465     ILE J     3
REMARK 465     THR J     4
REMARK 465     THR J     5
REMARK 465     PRO J     6
REMARK 465     ALA J     7
REMARK 465     LEU J     8
REMARK 465     THR J     9
REMARK 465     ALA J    10
REMARK 465     MET K    -2
REMARK 465     THR K    -1
REMARK 465     ASP K     0
REMARK 465     THR K     1
REMARK 465     ASN K     2
REMARK 465     ILE K     3
REMARK 465     THR K     4
REMARK 465     THR K     5
REMARK 465     PRO K     6
REMARK 465     MET L    -2
REMARK 465     THR L    -1
REMARK 465     ASP L     0
REMARK 465     THR L     1
REMARK 465     ASN L     2
REMARK 465     ILE L     3
REMARK 465     THR L     4
REMARK 465     THR L     5
REMARK 465     PRO L     6
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     ASN C   2    CG   OD1  ND2
REMARK 470     ILE C   3    CG1  CG2  CD1
REMARK 470     THR C   4    OG1  CG2
REMARK 470     THR C   5    OG1  CG2
REMARK 470     PRO C   6    CG   CD
REMARK 470     THR D   9    OG1  CG2
REMARK 470     THR E   9    OG1  CG2
REMARK 470     THR F   9    OG1  CG2
REMARK 470     PRO G   6    CG   CD
REMARK 470     THR H   9    OG1  CG2
REMARK 470     THR K   9    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   NE2  GLN A    20     O    HOH A  2002              1.76
REMARK 500   CB   ASP B    64     O    HOH B  2018              2.01
REMARK 500   OG   SER B    82     O    HOH B  2023              2.11
REMARK 500   CB   ASP F    67     O    HOH E  2013              2.08
REMARK 500   CE   LYS J    90     O    HOH J  2033              2.19
REMARK 500   O    GLU J   158     O    HOH G  2022              2.18
REMARK 500   O    ASP K    11     O    HOH K  2001              1.95
REMARK 500   OD1  ASN L    47     O    HOH L  2012              1.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500    ASP A 112   CB    ASP A 112   CG      0.130
REMARK 500    ASP B 112   CB    ASP B 112   CG      0.155
REMARK 500    ASP C 112   CB    ASP C 112   CG      0.134
REMARK 500    ASP D 112   CB    ASP D 112   CG      0.153
REMARK 500    GLU E  89   CG    GLU E  89   CD      0.110
REMARK 500    ASP E 112   CB    ASP E 112   CG      0.145
REMARK 500    ASP F 112   CB    ASP F 112   CG      0.158
REMARK 500    ASP G 112   CB    ASP G 112   CG      0.145
REMARK 500    ASP H 112   CB    ASP H 112   CG      0.190
REMARK 500    ASP I 112   CB    ASP I 112   CG      0.163
REMARK 500    ASP J  67   CB    ASP J  67   CG     -0.143
REMARK 500    ASP J 112   CB    ASP J 112   CG      0.163
REMARK 500    GLU K 140   CG    GLU K 140   CD      0.101
REMARK 500    ASP L 112   CB    ASP L 112   CG      0.135
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    ASP A  11   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES
REMARK 500    ASP A 112   CB  -  CG  -  OD1 ANGL. DEV. =   6.6 DEGREES
REMARK 500    ASP B 112   CB  -  CG  -  OD1 ANGL. DEV. =   7.1 DEGREES
REMARK 500    PRO C   6   N   -  CA  -  CB  ANGL. DEV. =   7.9 DEGREES
REMARK 500    ASP C  67   CB  -  CG  -  OD1 ANGL. DEV. =  -9.1 DEGREES
REMARK 500    ARG C  72   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES
REMARK 500    ARG D  44   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES
REMARK 500    ASP F 112   CB  -  CG  -  OD1 ANGL. DEV. =   6.2 DEGREES
REMARK 500    ASP G 112   CB  -  CG  -  OD1 ANGL. DEV. =   6.8 DEGREES
REMARK 500    ARG H  44   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.3 DEGREES
REMARK 500    ASP H 112   CB  -  CG  -  OD1 ANGL. DEV. =   7.1 DEGREES
REMARK 500    ASP I  67   CB  -  CG  -  OD2 ANGL. DEV. =  -7.9 DEGREES
REMARK 500    ASP J  67   CB  -  CG  -  OD1 ANGL. DEV. =  -7.0 DEGREES
REMARK 500    ASP L 112   CB  -  CG  -  OD1 ANGL. DEV. =   8.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    ASP A 131       99.11   -161.22
REMARK 500    LEU B   8      -80.26   -144.14
REMARK 500    THR B   9     -150.17   -145.98
REMARK 500    ALA B  10      -81.63    -51.01
REMARK 500    THR C   5      124.24     83.26
REMARK 500    PRO C   6     -153.93   -108.18
REMARK 500    ALA C   7      -91.22     92.00
REMARK 500    LEU D   8     -142.88     80.14
REMARK 500    ALA D  10     -140.64    -73.98
REMARK 500    ASP D 131       98.17   -161.93
REMARK 500    THR E   9      131.38    177.55
REMARK 500    ALA E  10     -155.77     79.10
REMARK 500    ASP E 131       95.81   -160.75
REMARK 500    LEU F   8     -166.00     70.37
REMARK 500    ALA F  10     -140.17   -134.17
REMARK 500    LEU G   8      -58.35     96.94
REMARK 500    VAL G 130      -50.39   -120.55
REMARK 500    LEU H   8       -6.19   -161.53
REMARK 500    THR H   9      -89.97    -89.14
REMARK 500    ALA H  10       46.49   -168.11
REMARK 500    ASP H  11       95.70    -11.83
REMARK 500    VAL I 130      -51.06   -125.29
REMARK 500    LEU K   8     -177.25     65.25
REMARK 500    ALA K  10       80.43    -60.44
REMARK 500    ASP K  11      114.84    -17.66
REMARK 500    VAL K 130      -60.02   -124.64
REMARK 500    THR L   9     -112.75   -161.22
REMARK 500    ALA L  10      160.05     56.02
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 ALA B  157     GLU B  158                  148.29
REMARK 500 ALA C  157     GLU C  158                  148.45
REMARK 500 ALA D   10     ASP D   11                 -145.31
REMARK 500 ALA F   10     ASP F   11                 -141.56
REMARK 500 ALA G  157     GLU G  158                  146.31
REMARK 500 ALA H  157     GLU H  158                  142.58
REMARK 500 ALA J  157     GLU J  158                  129.80
REMARK 500 ALA L  157     GLU L  158                  141.13
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    ILE H  49        24.7      L          L   OUTSIDE RANGE
REMARK 500    GLU J 158        20.4      L          L   OUTSIDE RANGE
REMARK 500    LEU K   8        24.9      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
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                             OFE A1159  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B  40   NE2
REMARK 620 2 ASP A  67   OD1 101.2
REMARK 620 3 ASP A  67   OD2 153.1  53.1
REMARK 620 4 GLU A  71   OE2  93.9  98.9  97.7
REMARK 620 5 HOH A2027   O   105.9 151.1 100.9  69.7
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             OFE B1159  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  40   NE2
REMARK 620 2 ASP B  67   OD1 100.3
REMARK 620 3 GLU B  71   OE2  92.3 100.4
REMARK 620 4 ASP B  67   OD2 154.5  54.4  95.4
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             OFE C1159  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C  67   OD2
REMARK 620 2 GLU C  71   OE2  96.3
REMARK 620 3 HIS I  40   NE2  96.8  86.3
REMARK 620 4 HOH C2024   O   163.9  77.7  97.7
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             OFE D1159  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D  67   OD2
REMARK 620 2 ASP D  67   OD1  53.9
REMARK 620 3 GLU D  71   OE2  95.5  96.0
REMARK 620 4 HIS J  40   NE2 161.2 108.0  91.4
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             OFE E1159  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH E2029   O
REMARK 620 2 ASP E  67   OD1 159.7
REMARK 620 3 GLU E  71   OE2  74.1  95.0
REMARK 620 4 HIS F  40   NE2  94.5 103.2  93.3
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             OFE F1159  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH E2012   O
REMARK 620 2 ASP F  67   OD1  85.5
REMARK 620 3 ASP F  67   OD2  85.5  54.4
REMARK 620 4 GLU F  71   OE2 171.4  96.2  88.7
REMARK 620 5 HIS E  40   NE2  88.7 100.9 154.9  99.3
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             OFE G1159  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH G2040   O
REMARK 620 2 ASP G  67   OD1 155.1
REMARK 620 3 ASP G  67   OD2 104.5  54.0
REMARK 620 4 GLU G  71   OE2  71.3  95.7  93.5
REMARK 620 5 HIS H  40   NE2 101.8  98.6 152.6  87.6
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             OFE H1159  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C  40   NE2
REMARK 620 2 HOH C2011   O    91.5
REMARK 620 3 GLU I  71   OE2  91.1  81.8
REMARK 620 4 ASP I  67   OD1 107.9 160.4  94.8
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             OFE J1159  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D  40   NE2
REMARK 620 2 GLU J  71   OE2  93.5
REMARK 620 3 ASP J  67   OD2 113.5  91.5
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             OFE K1159  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP K  67   OD1
REMARK 620 2 HIS L  40   NE2 104.8
REMARK 620 3 ASP K  67   OD2  53.7 158.3
REMARK 620 4 GLU K  71   OE2  95.2  92.4  88.0
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             OFE L1159  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP L  67   OD1
REMARK 620 2 ASP L  67   OD2  49.9
REMARK 620 3 GLU L  71   OE2 100.4  87.7
REMARK 620 4 HIS K  40   NE2 101.4 150.7  93.2
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              FE B1160  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B2047   O
REMARK 620 2 HOH L2050   O    82.8
REMARK 620 3 HOH D2055   O    89.8  87.9
REMARK 620 4 HOH D2059   O   102.4 174.8  91.6
REMARK 620 5 HOH B2051   O    85.5  95.5 173.8  85.5
REMARK 620 6 HOH L2053   O   167.3  89.3  99.8  85.7  85.4
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              FE D1160  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH G2080   O
REMARK 620 2 HOH G2081   O    96.3
REMARK 620 3 HOH I2036   O   113.0  74.9
REMARK 620 4 HOH I2037   O   170.0  78.1  73.8
REMARK 620 5 HOH K2046   O   106.0 156.0  88.1  81.0
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              FE L1160  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B2045   O
REMARK 620 2 HOH B2046   O    83.4
REMARK 620 3 HOH D2054   O    97.2  91.8
REMARK 620 4 HOH L2048   O    89.9  87.0 172.6
REMARK 620 5 HOH L2049   O    90.2 172.1  93.6  88.4
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              FE J1160  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH F2050   O
REMARK 620 2 HOH F2051   O    96.6
REMARK 620 3 HOH H2060   O   172.8  87.9
REMARK 620 4 HOH H2061   O    96.4  94.0  88.9
REMARK 620 5 HOH J2050   O    87.0  94.2  87.0 170.7
REMARK 620 6 HOH J2051   O    86.2 168.0  88.2  97.2  74.3
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              FE I1159  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH G2029   O
REMARK 620 2 HIS G  40   NE2 103.3
REMARK 620 3 GLU H  71   OE2  83.9  97.0
REMARK 620 4 ASP H  67   OD1 156.2 100.5  95.3
REMARK 620 5 ASP H  67   OD2  99.6 157.0  88.1  56.6
REMARK 620 N                    1     2     3     4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OFE A1159
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OFE B1159
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  FE B1160
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OFE C1159
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OFE D1159
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  FE D1160
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OFE E1159
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OFE F1159
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OFE G1159
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OFE H1159
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  FE I1159
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OFE J1159
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OFE K1159
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OFE L1159
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  FE L1160
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  FE J1160
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2YJJ   RELATED DB: PDB
REMARK 900  STRUCTURE OF DPS FROM MICROBACTERIUM ARBORESCENS IN THE
REMARK 900   LOW IRON FORM
DBREF  2YJK A   -2   158  UNP    Q1X6M4   Q1X6M4_9MICO     1    161
DBREF  2YJK B   -2   158  UNP    Q1X6M4   Q1X6M4_9MICO     1    161
DBREF  2YJK C   -2   158  UNP    Q1X6M4   Q1X6M4_9MICO     1    161
DBREF  2YJK D   -2   158  UNP    Q1X6M4   Q1X6M4_9MICO     1    161
DBREF  2YJK E   -2   158  UNP    Q1X6M4   Q1X6M4_9MICO     1    161
DBREF  2YJK F   -2   158  UNP    Q1X6M4   Q1X6M4_9MICO     1    161
DBREF  2YJK G   -2   158  UNP    Q1X6M4   Q1X6M4_9MICO     1    161
DBREF  2YJK H   -2   158  UNP    Q1X6M4   Q1X6M4_9MICO     1    161
DBREF  2YJK I   -2   158  UNP    Q1X6M4   Q1X6M4_9MICO     1    161
DBREF  2YJK J   -2   158  UNP    Q1X6M4   Q1X6M4_9MICO     1    161
DBREF  2YJK K   -2   158  UNP    Q1X6M4   Q1X6M4_9MICO     1    161
DBREF  2YJK L   -2   158  UNP    Q1X6M4   Q1X6M4_9MICO     1    161
SEQRES   1 A  161  MET THR ASP THR ASN ILE THR THR PRO ALA LEU THR ALA
SEQRES   2 A  161  ASP PRO GLU VAL ALA ALA ALA ALA ALA GLN PHE LEU THR
SEQRES   3 A  161  PRO VAL VAL HIS LYS MET GLN ALA LEU VAL VAL ASN GLY
SEQRES   4 A  161  LYS GLN ALA HIS TRP ASN VAL ARG GLY SER ASN PHE ILE
SEQRES   5 A  161  ALA ILE HIS GLU LEU LEU ASP SER VAL VAL ALA HIS ALA
SEQRES   6 A  161  GLN ASP TYR ALA ASP THR ALA ALA GLU ARG ILE VAL ALA
SEQRES   7 A  161  LEU GLY LEU PRO ILE ASP SER ARG VAL SER THR MET ALA
SEQRES   8 A  161  GLU LYS THR SER THR ALA VAL PRO ALA GLY PHE ALA GLN
SEQRES   9 A  161  TRP GLN ASP GLU ILE LYS ALA ILE VAL SER ASP ILE ASP
SEQRES  10 A  161  ALA ALA LEU VAL ASP LEU GLN ALA ALA ILE ASP GLY LEU
SEQRES  11 A  161  ASP GLU VAL ASP LEU THR SER GLN ASP VAL ALA ILE GLU
SEQRES  12 A  161  ILE LYS ARG GLY VAL ASP LYS ASP ARG TRP PHE LEU LEU
SEQRES  13 A  161  ALA HIS LEU ALA GLU
SEQRES   1 B  161  MET THR ASP THR ASN ILE THR THR PRO ALA LEU THR ALA
SEQRES   2 B  161  ASP PRO GLU VAL ALA ALA ALA ALA ALA GLN PHE LEU THR
SEQRES   3 B  161  PRO VAL VAL HIS LYS MET GLN ALA LEU VAL VAL ASN GLY
SEQRES   4 B  161  LYS GLN ALA HIS TRP ASN VAL ARG GLY SER ASN PHE ILE
SEQRES   5 B  161  ALA ILE HIS GLU LEU LEU ASP SER VAL VAL ALA HIS ALA
SEQRES   6 B  161  GLN ASP TYR ALA ASP THR ALA ALA GLU ARG ILE VAL ALA
SEQRES   7 B  161  LEU GLY LEU PRO ILE ASP SER ARG VAL SER THR MET ALA
SEQRES   8 B  161  GLU LYS THR SER THR ALA VAL PRO ALA GLY PHE ALA GLN
SEQRES   9 B  161  TRP GLN ASP GLU ILE LYS ALA ILE VAL SER ASP ILE ASP
SEQRES  10 B  161  ALA ALA LEU VAL ASP LEU GLN ALA ALA ILE ASP GLY LEU
SEQRES  11 B  161  ASP GLU VAL ASP LEU THR SER GLN ASP VAL ALA ILE GLU
SEQRES  12 B  161  ILE LYS ARG GLY VAL ASP LYS ASP ARG TRP PHE LEU LEU
SEQRES  13 B  161  ALA HIS LEU ALA GLU
SEQRES   1 C  161  MET THR ASP THR ASN ILE THR THR PRO ALA LEU THR ALA
SEQRES   2 C  161  ASP PRO GLU VAL ALA ALA ALA ALA ALA GLN PHE LEU THR
SEQRES   3 C  161  PRO VAL VAL HIS LYS MET GLN ALA LEU VAL VAL ASN GLY
SEQRES   4 C  161  LYS GLN ALA HIS TRP ASN VAL ARG GLY SER ASN PHE ILE
SEQRES   5 C  161  ALA ILE HIS GLU LEU LEU ASP SER VAL VAL ALA HIS ALA
SEQRES   6 C  161  GLN ASP TYR ALA ASP THR ALA ALA GLU ARG ILE VAL ALA
SEQRES   7 C  161  LEU GLY LEU PRO ILE ASP SER ARG VAL SER THR MET ALA
SEQRES   8 C  161  GLU LYS THR SER THR ALA VAL PRO ALA GLY PHE ALA GLN
SEQRES   9 C  161  TRP GLN ASP GLU ILE LYS ALA ILE VAL SER ASP ILE ASP
SEQRES  10 C  161  ALA ALA LEU VAL ASP LEU GLN ALA ALA ILE ASP GLY LEU
SEQRES  11 C  161  ASP GLU VAL ASP LEU THR SER GLN ASP VAL ALA ILE GLU
SEQRES  12 C  161  ILE LYS ARG GLY VAL ASP LYS ASP ARG TRP PHE LEU LEU
SEQRES  13 C  161  ALA HIS LEU ALA GLU
SEQRES   1 D  161  MET THR ASP THR ASN ILE THR THR PRO ALA LEU THR ALA
SEQRES   2 D  161  ASP PRO GLU VAL ALA ALA ALA ALA ALA GLN PHE LEU THR
SEQRES   3 D  161  PRO VAL VAL HIS LYS MET GLN ALA LEU VAL VAL ASN GLY
SEQRES   4 D  161  LYS GLN ALA HIS TRP ASN VAL ARG GLY SER ASN PHE ILE
SEQRES   5 D  161  ALA ILE HIS GLU LEU LEU ASP SER VAL VAL ALA HIS ALA
SEQRES   6 D  161  GLN ASP TYR ALA ASP THR ALA ALA GLU ARG ILE VAL ALA
SEQRES   7 D  161  LEU GLY LEU PRO ILE ASP SER ARG VAL SER THR MET ALA
SEQRES   8 D  161  GLU LYS THR SER THR ALA VAL PRO ALA GLY PHE ALA GLN
SEQRES   9 D  161  TRP GLN ASP GLU ILE LYS ALA ILE VAL SER ASP ILE ASP
SEQRES  10 D  161  ALA ALA LEU VAL ASP LEU GLN ALA ALA ILE ASP GLY LEU
SEQRES  11 D  161  ASP GLU VAL ASP LEU THR SER GLN ASP VAL ALA ILE GLU
SEQRES  12 D  161  ILE LYS ARG GLY VAL ASP LYS ASP ARG TRP PHE LEU LEU
SEQRES  13 D  161  ALA HIS LEU ALA GLU
SEQRES   1 E  161  MET THR ASP THR ASN ILE THR THR PRO ALA LEU THR ALA
SEQRES   2 E  161  ASP PRO GLU VAL ALA ALA ALA ALA ALA GLN PHE LEU THR
SEQRES   3 E  161  PRO VAL VAL HIS LYS MET GLN ALA LEU VAL VAL ASN GLY
SEQRES   4 E  161  LYS GLN ALA HIS TRP ASN VAL ARG GLY SER ASN PHE ILE
SEQRES   5 E  161  ALA ILE HIS GLU LEU LEU ASP SER VAL VAL ALA HIS ALA
SEQRES   6 E  161  GLN ASP TYR ALA ASP THR ALA ALA GLU ARG ILE VAL ALA
SEQRES   7 E  161  LEU GLY LEU PRO ILE ASP SER ARG VAL SER THR MET ALA
SEQRES   8 E  161  GLU LYS THR SER THR ALA VAL PRO ALA GLY PHE ALA GLN
SEQRES   9 E  161  TRP GLN ASP GLU ILE LYS ALA ILE VAL SER ASP ILE ASP
SEQRES  10 E  161  ALA ALA LEU VAL ASP LEU GLN ALA ALA ILE ASP GLY LEU
SEQRES  11 E  161  ASP GLU VAL ASP LEU THR SER GLN ASP VAL ALA ILE GLU
SEQRES  12 E  161  ILE LYS ARG GLY VAL ASP LYS ASP ARG TRP PHE LEU LEU
SEQRES  13 E  161  ALA HIS LEU ALA GLU
SEQRES   1 F  161  MET THR ASP THR ASN ILE THR THR PRO ALA LEU THR ALA
SEQRES   2 F  161  ASP PRO GLU VAL ALA ALA ALA ALA ALA GLN PHE LEU THR
SEQRES   3 F  161  PRO VAL VAL HIS LYS MET GLN ALA LEU VAL VAL ASN GLY
SEQRES   4 F  161  LYS GLN ALA HIS TRP ASN VAL ARG GLY SER ASN PHE ILE
SEQRES   5 F  161  ALA ILE HIS GLU LEU LEU ASP SER VAL VAL ALA HIS ALA
SEQRES   6 F  161  GLN ASP TYR ALA ASP THR ALA ALA GLU ARG ILE VAL ALA
SEQRES   7 F  161  LEU GLY LEU PRO ILE ASP SER ARG VAL SER THR MET ALA
SEQRES   8 F  161  GLU LYS THR SER THR ALA VAL PRO ALA GLY PHE ALA GLN
SEQRES   9 F  161  TRP GLN ASP GLU ILE LYS ALA ILE VAL SER ASP ILE ASP
SEQRES  10 F  161  ALA ALA LEU VAL ASP LEU GLN ALA ALA ILE ASP GLY LEU
SEQRES  11 F  161  ASP GLU VAL ASP LEU THR SER GLN ASP VAL ALA ILE GLU
SEQRES  12 F  161  ILE LYS ARG GLY VAL ASP LYS ASP ARG TRP PHE LEU LEU
SEQRES  13 F  161  ALA HIS LEU ALA GLU
SEQRES   1 G  161  MET THR ASP THR ASN ILE THR THR PRO ALA LEU THR ALA
SEQRES   2 G  161  ASP PRO GLU VAL ALA ALA ALA ALA ALA GLN PHE LEU THR
SEQRES   3 G  161  PRO VAL VAL HIS LYS MET GLN ALA LEU VAL VAL ASN GLY
SEQRES   4 G  161  LYS GLN ALA HIS TRP ASN VAL ARG GLY SER ASN PHE ILE
SEQRES   5 G  161  ALA ILE HIS GLU LEU LEU ASP SER VAL VAL ALA HIS ALA
SEQRES   6 G  161  GLN ASP TYR ALA ASP THR ALA ALA GLU ARG ILE VAL ALA
SEQRES   7 G  161  LEU GLY LEU PRO ILE ASP SER ARG VAL SER THR MET ALA
SEQRES   8 G  161  GLU LYS THR SER THR ALA VAL PRO ALA GLY PHE ALA GLN
SEQRES   9 G  161  TRP GLN ASP GLU ILE LYS ALA ILE VAL SER ASP ILE ASP
SEQRES  10 G  161  ALA ALA LEU VAL ASP LEU GLN ALA ALA ILE ASP GLY LEU
SEQRES  11 G  161  ASP GLU VAL ASP LEU THR SER GLN ASP VAL ALA ILE GLU
SEQRES  12 G  161  ILE LYS ARG GLY VAL ASP LYS ASP ARG TRP PHE LEU LEU
SEQRES  13 G  161  ALA HIS LEU ALA GLU
SEQRES   1 H  161  MET THR ASP THR ASN ILE THR THR PRO ALA LEU THR ALA
SEQRES   2 H  161  ASP PRO GLU VAL ALA ALA ALA ALA ALA GLN PHE LEU THR
SEQRES   3 H  161  PRO VAL VAL HIS LYS MET GLN ALA LEU VAL VAL ASN GLY
SEQRES   4 H  161  LYS GLN ALA HIS TRP ASN VAL ARG GLY SER ASN PHE ILE
SEQRES   5 H  161  ALA ILE HIS GLU LEU LEU ASP SER VAL VAL ALA HIS ALA
SEQRES   6 H  161  GLN ASP TYR ALA ASP THR ALA ALA GLU ARG ILE VAL ALA
SEQRES   7 H  161  LEU GLY LEU PRO ILE ASP SER ARG VAL SER THR MET ALA
SEQRES   8 H  161  GLU LYS THR SER THR ALA VAL PRO ALA GLY PHE ALA GLN
SEQRES   9 H  161  TRP GLN ASP GLU ILE LYS ALA ILE VAL SER ASP ILE ASP
SEQRES  10 H  161  ALA ALA LEU VAL ASP LEU GLN ALA ALA ILE ASP GLY LEU
SEQRES  11 H  161  ASP GLU VAL ASP LEU THR SER GLN ASP VAL ALA ILE GLU
SEQRES  12 H  161  ILE LYS ARG GLY VAL ASP LYS ASP ARG TRP PHE LEU LEU
SEQRES  13 H  161  ALA HIS LEU ALA GLU
SEQRES   1 I  161  MET THR ASP THR ASN ILE THR THR PRO ALA LEU THR ALA
SEQRES   2 I  161  ASP PRO GLU VAL ALA ALA ALA ALA ALA GLN PHE LEU THR
SEQRES   3 I  161  PRO VAL VAL HIS LYS MET GLN ALA LEU VAL VAL ASN GLY
SEQRES   4 I  161  LYS GLN ALA HIS TRP ASN VAL ARG GLY SER ASN PHE ILE
SEQRES   5 I  161  ALA ILE HIS GLU LEU LEU ASP SER VAL VAL ALA HIS ALA
SEQRES   6 I  161  GLN ASP TYR ALA ASP THR ALA ALA GLU ARG ILE VAL ALA
SEQRES   7 I  161  LEU GLY LEU PRO ILE ASP SER ARG VAL SER THR MET ALA
SEQRES   8 I  161  GLU LYS THR SER THR ALA VAL PRO ALA GLY PHE ALA GLN
SEQRES   9 I  161  TRP GLN ASP GLU ILE LYS ALA ILE VAL SER ASP ILE ASP
SEQRES  10 I  161  ALA ALA LEU VAL ASP LEU GLN ALA ALA ILE ASP GLY LEU
SEQRES  11 I  161  ASP GLU VAL ASP LEU THR SER GLN ASP VAL ALA ILE GLU
SEQRES  12 I  161  ILE LYS ARG GLY VAL ASP LYS ASP ARG TRP PHE LEU LEU
SEQRES  13 I  161  ALA HIS LEU ALA GLU
SEQRES   1 J  161  MET THR ASP THR ASN ILE THR THR PRO ALA LEU THR ALA
SEQRES   2 J  161  ASP PRO GLU VAL ALA ALA ALA ALA ALA GLN PHE LEU THR
SEQRES   3 J  161  PRO VAL VAL HIS LYS MET GLN ALA LEU VAL VAL ASN GLY
SEQRES   4 J  161  LYS GLN ALA HIS TRP ASN VAL ARG GLY SER ASN PHE ILE
SEQRES   5 J  161  ALA ILE HIS GLU LEU LEU ASP SER VAL VAL ALA HIS ALA
SEQRES   6 J  161  GLN ASP TYR ALA ASP THR ALA ALA GLU ARG ILE VAL ALA
SEQRES   7 J  161  LEU GLY LEU PRO ILE ASP SER ARG VAL SER THR MET ALA
SEQRES   8 J  161  GLU LYS THR SER THR ALA VAL PRO ALA GLY PHE ALA GLN
SEQRES   9 J  161  TRP GLN ASP GLU ILE LYS ALA ILE VAL SER ASP ILE ASP
SEQRES  10 J  161  ALA ALA LEU VAL ASP LEU GLN ALA ALA ILE ASP GLY LEU
SEQRES  11 J  161  ASP GLU VAL ASP LEU THR SER GLN ASP VAL ALA ILE GLU
SEQRES  12 J  161  ILE LYS ARG GLY VAL ASP LYS ASP ARG TRP PHE LEU LEU
SEQRES  13 J  161  ALA HIS LEU ALA GLU
SEQRES   1 K  161  MET THR ASP THR ASN ILE THR THR PRO ALA LEU THR ALA
SEQRES   2 K  161  ASP PRO GLU VAL ALA ALA ALA ALA ALA GLN PHE LEU THR
SEQRES   3 K  161  PRO VAL VAL HIS LYS MET GLN ALA LEU VAL VAL ASN GLY
SEQRES   4 K  161  LYS GLN ALA HIS TRP ASN VAL ARG GLY SER ASN PHE ILE
SEQRES   5 K  161  ALA ILE HIS GLU LEU LEU ASP SER VAL VAL ALA HIS ALA
SEQRES   6 K  161  GLN ASP TYR ALA ASP THR ALA ALA GLU ARG ILE VAL ALA
SEQRES   7 K  161  LEU GLY LEU PRO ILE ASP SER ARG VAL SER THR MET ALA
SEQRES   8 K  161  GLU LYS THR SER THR ALA VAL PRO ALA GLY PHE ALA GLN
SEQRES   9 K  161  TRP GLN ASP GLU ILE LYS ALA ILE VAL SER ASP ILE ASP
SEQRES  10 K  161  ALA ALA LEU VAL ASP LEU GLN ALA ALA ILE ASP GLY LEU
SEQRES  11 K  161  ASP GLU VAL ASP LEU THR SER GLN ASP VAL ALA ILE GLU
SEQRES  12 K  161  ILE LYS ARG GLY VAL ASP LYS ASP ARG TRP PHE LEU LEU
SEQRES  13 K  161  ALA HIS LEU ALA GLU
SEQRES   1 L  161  MET THR ASP THR ASN ILE THR THR PRO ALA LEU THR ALA
SEQRES   2 L  161  ASP PRO GLU VAL ALA ALA ALA ALA ALA GLN PHE LEU THR
SEQRES   3 L  161  PRO VAL VAL HIS LYS MET GLN ALA LEU VAL VAL ASN GLY
SEQRES   4 L  161  LYS GLN ALA HIS TRP ASN VAL ARG GLY SER ASN PHE ILE
SEQRES   5 L  161  ALA ILE HIS GLU LEU LEU ASP SER VAL VAL ALA HIS ALA
SEQRES   6 L  161  GLN ASP TYR ALA ASP THR ALA ALA GLU ARG ILE VAL ALA
SEQRES   7 L  161  LEU GLY LEU PRO ILE ASP SER ARG VAL SER THR MET ALA
SEQRES   8 L  161  GLU LYS THR SER THR ALA VAL PRO ALA GLY PHE ALA GLN
SEQRES   9 L  161  TRP GLN ASP GLU ILE LYS ALA ILE VAL SER ASP ILE ASP
SEQRES  10 L  161  ALA ALA LEU VAL ASP LEU GLN ALA ALA ILE ASP GLY LEU
SEQRES  11 L  161  ASP GLU VAL ASP LEU THR SER GLN ASP VAL ALA ILE GLU
SEQRES  12 L  161  ILE LYS ARG GLY VAL ASP LYS ASP ARG TRP PHE LEU LEU
SEQRES  13 L  161  ALA HIS LEU ALA GLU
HET    OFE  A1159       2
HET    OFE  B1159       2
HET     FE  B1160       1
HET    OFE  C1159       2
HET     FE  C1160       1
HET    OFE  D1159       2
HET     FE  D1160       1
HET    OFE  E1159       2
HET    OFE  F1159       2
HET    OFE  G1159       2
HET    OFE  H1159       2
HET     FE  I1159       1
HET    OFE  J1159       2
HET    OFE  K1159       2
HET    OFE  L1159       2
HET     FE  L1160       1
HET     FE  J1160       1
HETNAM     OFE IRON(II) OXIDE
HETNAM      FE FE (III) ION
HETSYN     OFE FERROUS OXIDE
FORMUL  13  OFE    11(FE O)
FORMUL  14   FE    6(FE 3+)
FORMUL  15  HOH   *705(H2 O)
HELIX    1   1 ASP A   11  ASN A   42  1                                  32
HELIX    2   2 ASN A   47  LEU A   76  1                                  30
HELIX    3   3 ARG A   83  LYS A   90  1                                   8
HELIX    4   4 TRP A  102  ASP A  128  1                                  27
HELIX    5   5 ASP A  131  ALA A  154  1                                  24
HELIX    6   6 HIS A  155  ALA A  157  5                                   3
HELIX    7   7 ASP B   11  ASN B   42  1                                  32
HELIX    8   8 ASN B   47  LEU B   76  1                                  30
HELIX    9   9 ARG B   83  THR B   91  1                                   9
HELIX   10  10 TRP B  102  ASP B  128  1                                  27
HELIX   11  11 ASP B  131  ALA B  154  1                                  24
HELIX   12  12 ASP C   11  ASN C   42  1                                  32
HELIX   13  13 ASN C   47  LEU C   76  1                                  30
HELIX   14  14 ARG C   83  LYS C   90  1                                   8
HELIX   15  15 TRP C  102  ASP C  128  1                                  27
HELIX   16  16 ASP C  131  ALA C  154  1                                  24
HELIX   17  17 HIS C  155  ALA C  157  5                                   3
HELIX   18  18 ASP D   11  ASN D   42  1                                  32
HELIX   19  19 ASN D   47  LEU D   76  1                                  30
HELIX   20  20 ARG D   83  THR D   91  1                                   9
HELIX   21  21 TRP D  102  ASP D  128  1                                  27
HELIX   22  22 ASP D  131  ALA D  154  1                                  24
HELIX   23  23 HIS D  155  ALA D  157  5                                   3
HELIX   24  24 ASP E   11  ASN E   42  1                                  32
HELIX   25  25 ASN E   47  LEU E   76  1                                  30
HELIX   26  26 ARG E   83  THR E   91  1                                   9
HELIX   27  27 TRP E  102  ASP E  128  1                                  27
HELIX   28  28 ASP E  131  ALA E  154  1                                  24
HELIX   29  29 HIS E  155  ALA E  157  5                                   3
HELIX   30  30 ASP F   11  ASN F   42  1                                  32
HELIX   31  31 ASN F   47  LEU F   76  1                                  30
HELIX   32  32 ARG F   83  LYS F   90  1                                   8
HELIX   33  33 TRP F  102  ASP F  128  1                                  27
HELIX   34  34 ASP F  131  ALA F  154  1                                  24
HELIX   35  35 HIS F  155  GLU F  158  5                                   4
HELIX   36  36 ASP G   11  ASN G   42  1                                  32
HELIX   37  37 ASN G   47  LEU G   76  1                                  30
HELIX   38  38 ARG G   83  THR G   91  1                                   9
HELIX   39  39 TRP G  102  ASP G  128  1                                  27
HELIX   40  40 ASP G  131  ALA G  154  1                                  24
HELIX   41  41 HIS G  155  ALA G  157  5                                   3
HELIX   42  42 ASP H   11  ASN H   42  1                                  32
HELIX   43  43 ASN H   47  LEU H   76  1                                  30
HELIX   44  44 ARG H   83  LYS H   90  1                                   8
HELIX   45  45 TRP H  102  ASP H  128  1                                  27
HELIX   46  46 ASP H  131  HIS H  155  1                                  25
HELIX   47  47 ASP I   11  ASN I   42  1                                  32
HELIX   48  48 ASN I   47  LEU I   76  1                                  30
HELIX   49  49 ARG I   83  LYS I   90  1                                   8
HELIX   50  50 TRP I  102  ASP I  128  1                                  27
HELIX   51  51 ASP I  131  ALA I  154  1                                  24
HELIX   52  52 HIS I  155  ALA I  157  5                                   3
HELIX   53  53 ASP J   11  ASN J   42  1                                  32
HELIX   54  54 ASN J   47  LEU J   76  1                                  30
HELIX   55  55 ARG J   83  LYS J   90  1                                   8
HELIX   56  56 TRP J  102  ASP J  128  1                                  27
HELIX   57  57 ASP J  131  ALA J  154  1                                  24
HELIX   58  58 HIS J  155  ALA J  157  5                                   3
HELIX   59  59 ASP K   11  ASN K   42  1                                  32
HELIX   60  60 ASN K   47  LEU K   76  1                                  30
HELIX   61  61 ARG K   83  THR K   91  1                                   9
HELIX   62  62 TRP K  102  ASP K  128  1                                  27
HELIX   63  63 ASP K  131  ALA K  154  1                                  24
HELIX   64  64 HIS K  155  ALA K  157  5                                   3
HELIX   65  65 ASP L   11  ASN L   42  1                                  32
HELIX   66  66 ASN L   47  LEU L   76  1                                  30
HELIX   67  67 ARG L   83  THR L   91  1                                   9
HELIX   68  68 TRP L  102  ASP L  128  1                                  27
HELIX   69  69 ASP L  131  ALA L  154  1                                  24
HELIX   70  70 HIS L  155  ALA L  157  5                                   3
SHEET    1  AA 2 VAL A  43  ARG A  44  0
SHEET    2  AA 2 ALA A 100  GLN A 101  1  O  ALA A 100   N  ARG A  44
SHEET    1  BA 2 VAL B  43  ARG B  44  0
SHEET    2  BA 2 ALA B 100  GLN B 101  1  O  ALA B 100   N  ARG B  44
SHEET    1  CA 2 VAL C  43  ARG C  44  0
SHEET    2  CA 2 ALA C 100  GLN C 101  1  O  ALA C 100   N  ARG C  44
SHEET    1  DA 2 VAL D  43  ARG D  44  0
SHEET    2  DA 2 ALA D 100  GLN D 101  1  O  ALA D 100   N  ARG D  44
SHEET    1  EA 2 VAL E  43  ARG E  44  0
SHEET    2  EA 2 ALA E 100  GLN E 101  1  O  ALA E 100   N  ARG E  44
SHEET    1  FA 2 VAL F  43  ARG F  44  0
SHEET    2  FA 2 ALA F 100  GLN F 101  1  O  ALA F 100   N  ARG F  44
SHEET    1  GA 2 VAL G  43  ARG G  44  0
SHEET    2  GA 2 ALA G 100  GLN G 101  1  O  ALA G 100   N  ARG G  44
SHEET    1  HA 2 VAL H  43  ARG H  44  0
SHEET    2  HA 2 ALA H 100  GLN H 101  1  O  ALA H 100   N  ARG H  44
SHEET    1  IA 2 VAL I  43  ARG I  44  0
SHEET    2  IA 2 ALA I 100  GLN I 101  1  O  ALA I 100   N  ARG I  44
SHEET    1  JA 2 VAL J  43  ARG J  44  0
SHEET    2  JA 2 ALA J 100  GLN J 101  1  O  ALA J 100   N  ARG J  44
SHEET    1  KA 2 VAL K  43  ARG K  44  0
SHEET    2  KA 2 ALA K 100  GLN K 101  1  O  ALA K 100   N  ARG K  44
SHEET    1  LA 2 VAL L  43  ARG L  44  0
SHEET    2  LA 2 ALA L 100  GLN L 101  1  O  ALA L 100   N  ARG L  44
LINK        FE   OFE A1159                 NE2 HIS B  40     1555   1555  2.40
LINK        FE   OFE A1159                 OD1 ASP A  67     1555   1555  2.46
LINK        FE   OFE A1159                 OD2 ASP A  67     1555   1555  2.49
LINK        FE   OFE A1159                 OE2 GLU A  71     1555   1555  2.43
LINK        FE   OFE A1159                 O   HOH A2027     1555   1555  2.62
LINK        FE   OFE B1159                 NE2 HIS A  40     1555   1555  2.30
LINK        FE   OFE B1159                 OD1 ASP B  67     1555   1555  2.42
LINK        FE   OFE B1159                 OE2 GLU B  71     1555   1555  2.21
LINK        FE   OFE B1159                 OD2 ASP B  67     1555   1555  2.57
LINK        FE    FE B1160                 O   HOH B2047     1555   1555  1.91
LINK        FE    FE B1160                 O   HOH L2050     1555   1555  2.11
LINK        FE    FE B1160                 O   HOH D2055     1555   1555  1.88
LINK        FE    FE B1160                 O   HOH D2059     1555   1555  1.89
LINK        FE    FE B1160                 O   HOH B2051     1555   1555  1.86
LINK        FE    FE B1160                 O   HOH L2053     1555   1555  2.09
LINK        FE   OFE C1159                 OD2 ASP C  67     1555   1555  2.57
LINK        FE   OFE C1159                 OE2 GLU C  71     1555   1555  2.17
LINK        FE   OFE C1159                 NE2 HIS I  40     1555   1555  2.45
LINK        FE   OFE C1159                 O   HOH C2024     1555   1555  2.61
LINK        FE   OFE D1159                 OE2 GLU D  71     1555   1555  2.26
LINK        FE   OFE D1159                 NE2 HIS J  40     1555   1555  2.33
LINK        FE   OFE D1159                 OD2AASP D  67     1555   1555  2.52
LINK        FE   OFE D1159                 OD1AASP D  67     1555   1555  2.34
LINK        FE    FE D1160                 O   HOH G2081     1555   1555  1.91
LINK        FE    FE D1160                 O   HOH G2080     1555   1555  2.03
LINK        FE    FE D1160                 O   HOH K2046     1555   1555  1.85
LINK        FE    FE D1160                 O   HOH I2037     1555   1555  2.09
LINK        FE    FE D1160                 O   HOH I2036     1555   1555  1.73
LINK        FE   OFE E1159                 OD1 ASP E  67     1555   1555  2.36
LINK        FE   OFE E1159                 O   HOH E2029     1555   1555  2.64
LINK        FE   OFE E1159                 NE2 HIS F  40     1555   1555  2.40
LINK        FE   OFE E1159                 OE2 GLU E  71     1555   1555  2.17
LINK        FE   OFE F1159                 NE2 HIS E  40     1555   1555  2.35
LINK        FE   OFE F1159                 OD2 ASP F  67     1555   1555  2.46
LINK        FE   OFE F1159                 OE2 GLU F  71     1555   1555  2.06
LINK        FE   OFE F1159                 O   HOH E2012     1555   1555  2.38
LINK        FE   OFE F1159                 OD1 ASP F  67     1555   1555  2.47
LINK        FE   OFE G1159                 OD2 ASP G  67     1555   1555  2.43
LINK        FE   OFE G1159                 NE2 HIS H  40     1555   1555  2.23
LINK        FE   OFE G1159                 OE2 GLU G  71     1555   1555  2.28
LINK        FE   OFE G1159                 O   HOH G2040     1555   1555  2.49
LINK        FE   OFE G1159                 OD1 ASP G  67     1555   1555  2.49
LINK        FE   OFE H1159                 OD1 ASP I  67     1555   1555  2.40
LINK        FE   OFE H1159                 OE2 GLU I  71     1555   1555  2.22
LINK        FE   OFE H1159                 O   HOH C2011     1555   1555  2.36
LINK        FE   OFE H1159                 NE2 HIS C  40     1555   1555  2.51
LINK        FE    FE I1159                 OD2 ASP H  67     1555   1555  2.46
LINK        FE    FE I1159                 NE2 HIS G  40     1555   1555  2.33
LINK        FE    FE I1159                 O   HOH G2029     1555   1555  2.38
LINK        FE    FE I1159                 OD1 ASP H  67     1555   1555  2.34
LINK        FE    FE I1159                 OE2 GLU H  71     1555   1555  2.13
LINK        FE   OFE J1159                 OD2 ASP J  67     1555   1555  2.34
LINK        FE   OFE J1159                 OE2 GLU J  71     1555   1555  2.16
LINK        FE   OFE J1159                 NE2 HIS D  40     1555   1555  2.35
LINK        FE    FE J1160                 O   HOH H2060     1555   1555  1.72
LINK        FE    FE J1160                 O   HOH H2061     1555   1555  2.20
LINK        FE    FE J1160                 O   HOH J2050     1555   1555  2.04
LINK        FE    FE J1160                 O   HOH J2051     1555   1555  1.84
LINK        FE    FE J1160                 O   HOH F2050     1555   1555  1.88
LINK        FE    FE J1160                 O   HOH F2051     1555   1555  1.83
LINK        FE   OFE K1159                 OE2 GLU K  71     1555   1555  2.24
LINK        FE   OFE K1159                 OD2AASP K  67     1555   1555  2.50
LINK        FE   OFE K1159                 NE2 HIS L  40     1555   1555  2.29
LINK        FE   OFE K1159                 OD1AASP K  67     1555   1555  2.50
LINK        FE   OFE L1159                 NE2 HIS K  40     1555   1555  2.33
LINK        FE   OFE L1159                 OE2 GLU L  71     1555   1555  2.19
LINK        FE   OFE L1159                 OD2AASP L  67     1555   1555  2.63
LINK        FE   OFE L1159                 OD1AASP L  67     1555   1555  2.53
LINK        FE    FE L1160                 O   HOH L2049     1555   1555  1.97
LINK        FE    FE L1160                 O   HOH L2048     1555   1555  2.02
LINK        FE    FE L1160                 O   HOH D2054     1555   1555  2.07
LINK        FE    FE L1160                 O   HOH B2046     1555   1555  1.63
LINK        FE    FE L1160                 O   HOH B2045     1555   1555  2.08
CISPEP   1 ALA B    7    LEU B    8          0         0.84
CISPEP   2 LEU B    8    THR B    9          0         8.83
CISPEP   3 THR C    9    ALA C   10          0         0.52
CISPEP   4 ALA C   10    ASP C   11          0       -14.91
CISPEP   5 ALA E    7    LEU E    8          0         0.46
CISPEP   6 THR E    9    ALA E   10          0        25.01
CISPEP   7 ALA H    7    LEU H    8          0       -14.35
CISPEP   8 THR H    9    ALA H   10          0         5.20
CISPEP   9 ALA L    7    LEU L    8          0        -5.32
SITE     1 AC1  6 ASP A  67  GLU A  71  HOH A2027  LYS B  37
SITE     2 AC1  6 HIS B  40  ASP B  56
SITE     1 AC2  5 LYS A  37  HIS A  40  ASP A  56  ASP B  67
SITE     2 AC2  5 GLU B  71
SITE     1 AC3  6 HOH B2047  HOH B2051  HOH D2055  HOH D2059
SITE     2 AC3  6 HOH L2050  HOH L2053
SITE     1 AC4  6 ASP C  67  GLU C  71  HOH C2024  LYS I  37
SITE     2 AC4  6 HIS I  40  ASP I  56
SITE     1 AC5  6 ASP D  67  GLU D  71  HOH D2026  LYS J  37
SITE     2 AC5  6 HIS J  40  ASP J  56
SITE     1 AC6  6 HOH G2080  HOH G2081  HOH I2036  HOH I2037
SITE     2 AC6  6 HOH K2046  HOH K2047
SITE     1 AC7  6 ASP E  67  GLU E  71  HOH E2029  LYS F  37
SITE     2 AC7  6 HIS F  40  ASP F  56
SITE     1 AC8  5 HIS E  40  HIS E  52  HOH E2012  ASP F  67
SITE     2 AC8  5 GLU F  71
SITE     1 AC9  6 ASP G  67  GLU G  71  HOH G2040  LYS H  37
SITE     2 AC9  6 HIS H  40  ASP H  56
SITE     1 BC1  6 LYS C  37  HIS C  40  ASP C  56  HOH C2011
SITE     2 BC1  6 ASP I  67  GLU I  71
SITE     1 BC2  4 HIS G  40  HOH G2029  ASP H  67  GLU H  71
SITE     1 BC3  6 LYS D  37  HIS D  40  ASP D  56  HOH D2018
SITE     2 BC3  6 ASP J  67  GLU J  71
SITE     1 BC4  6 ASP K  67  GLU K  71  HOH K2022  LYS L  37
SITE     2 BC4  6 HIS L  40  ASP L  56
SITE     1 BC5  6 LYS K  37  HIS K  40  ASP K  56  HOH K2014
SITE     2 BC5  6 ASP L  67  GLU L  71
SITE     1 BC6  6 HOH B2045  HOH B2046  HOH D2053  HOH D2054
SITE     2 BC6  6 HOH L2048  HOH L2049
SITE     1 BC7  6 HOH F2050  HOH F2051  HOH H2060  HOH H2061
SITE     2 BC7  6 HOH J2050  HOH J2051
CRYST1   87.580   92.050  128.580  90.00  96.04  90.00 P 1 21 1     24
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      0.011418  0.000000  0.001208        0.00000
SCALE2      0.000000  0.010864  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007821        0.00000
      
PROCHECK
Go to PROCHECK summary
 References