longtext: 7xmj-pdb

content
HEADER    STRUCTURAL PROTEIN                      26-APR-22   7XMJ
TITLE     CRYSTAL STRUCTURE OF CARBOHYDRATE ESTERASE FAMILY 7 ACETYL XYLAN
TITLE    2 ESTERASE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ACETYLXYLAN ESTERASE;
COMPND   3 CHAIN: A, B, C, D;
COMPND   4 EC: 3.1.1.-;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: LACTOCOCCUS LACTIS SUBSP. LACTIS (STRAIN
SOURCE   3 KF147);
SOURCE   4 ORGANISM_TAXID: 684738;
SOURCE   5 GENE: AXE, LLKF_1447;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS    CARBOHYDRATE ESTERASE, CARBOHYDRATE ESTERASE FAMILY 7, ACETYL XYLAN
KEYWDS   2 ESTERASE, STRUCTURAL PROTEIN
EXPDTA    X-RAY DIFFRACTION
AUTHOR    Z.Q.JIANG,J.W.MA
REVDAT   1   31-MAY-23 7XMJ    0
JRNL        AUTH   Z.Q.JIANG,J.W.MA
JRNL        TITL   CRYSTAL STRUCTURE OF CARBOHYDRATE ESTERASE FAMILY 7 ACETYL
JRNL        TITL 2 XYLAN ESTERASE
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    2.41 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX DEV_2474
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK   3
REMARK   3    REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.41
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.48
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.377
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8
REMARK   3   NUMBER OF REFLECTIONS             : 64477
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.250
REMARK   3   R VALUE            (WORKING SET) : 0.248
REMARK   3   FREE R VALUE                     : 0.280
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.971
REMARK   3   FREE R VALUE TEST SET COUNT      : 3205
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE
REMARK   3     1 35.4790 -  6.8399    0.99     2710   135  0.2268 0.2339
REMARK   3     2  6.8399 -  5.4353    1.00     2677   151  0.2372 0.2953
REMARK   3     3  5.4353 -  4.7501    1.00     2690   127  0.2297 0.2668
REMARK   3     4  4.7501 -  4.3166    1.00     2712   119  0.2273 0.2461
REMARK   3     5  4.3166 -  4.0077    1.00     2650   126  0.2226 0.2524
REMARK   3     6  4.0077 -  3.7717    1.00     2717   123  0.2285 0.2669
REMARK   3     7  3.7717 -  3.5830    1.00     2617   183  0.2411 0.2623
REMARK   3     8  3.5830 -  3.4271    1.00     2697   128  0.2446 0.2933
REMARK   3     9  3.4271 -  3.2953    1.00     2630   174  0.2561 0.2900
REMARK   3    10  3.2953 -  3.1817    1.00     2630   147  0.2582 0.2777
REMARK   3    11  3.1817 -  3.0822    1.00     2645   149  0.2682 0.2987
REMARK   3    12  3.0822 -  2.9942    1.00     2718   119  0.2833 0.3493
REMARK   3    13  2.9942 -  2.9154    1.00     2681   128  0.2850 0.3362
REMARK   3    14  2.9154 -  2.8443    1.00     2628   148  0.2709 0.3233
REMARK   3    15  2.8443 -  2.7797    1.00     2638   136  0.2832 0.2776
REMARK   3    16  2.7797 -  2.7205    1.00     2681   149  0.2867 0.3132
REMARK   3    17  2.7205 -  2.6661    1.00     2629   161  0.2884 0.3366
REMARK   3    18  2.6661 -  2.6158    1.00     2683   126  0.2918 0.3559
REMARK   3    19  2.6158 -  2.5691    1.00     2596   160  0.2880 0.3276
REMARK   3    20  2.5691 -  2.5256    1.00     2707   137  0.2853 0.3046
REMARK   3    21  2.5256 -  2.4849    1.00     2642   138  0.2893 0.2802
REMARK   3    22  2.4849 -  2.4466    1.00     2662   108  0.2897 0.3604
REMARK   3    23  2.4466 -  2.4107    0.99     2632   133  0.2997 0.3046
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.11
REMARK   3   SHRINKAGE RADIUS   : 0.90
REMARK   3   K_SOL              : NULL
REMARK   3   B_SOL              : NULL
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.346
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.949
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 48.84
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 56.58
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  TWINNING INFORMATION.
REMARK   3   FRACTION: NULL
REMARK   3   OPERATOR: NULL
REMARK   3
REMARK   3  DEVIATIONS FROM IDEAL VALUES.
REMARK   3                 RMSD          COUNT
REMARK   3   BOND      :  0.003          10018
REMARK   3   ANGLE     :  0.634          13600
REMARK   3   CHIRALITY :  0.045           1449
REMARK   3   PLANARITY :  0.004           1745
REMARK   3   DIHEDRAL  : 14.083           5856
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 1
REMARK   3   TLS GROUP : 1
REMARK   3    SELECTION: ALL
REMARK   3    ORIGIN FOR THE GROUP (A): -40.9049  14.3563  -0.4960
REMARK   3    T TENSOR
REMARK   3      T11:   0.4661 T22:   0.4299
REMARK   3      T33:   0.3662 T12:  -0.0171
REMARK   3      T13:  -0.1283 T23:   0.0542
REMARK   3    L TENSOR
REMARK   3      L11:   0.6515 L22:   0.2166
REMARK   3      L33:  -0.1199 L12:  -0.4121
REMARK   3      L13:  -0.0599 L23:   0.0289
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0425 S12:   0.0176 S13:   0.0101
REMARK   3      S21:  -0.0049 S22:   0.0043 S23:   0.0246
REMARK   3      S31:  -0.0520 S32:   0.0301 S33:   0.0321
REMARK   3
REMARK   3  NCS DETAILS
REMARK   3   NUMBER OF NCS GROUPS : 1
REMARK   3   NCS GROUP : 1
REMARK   3    NCS OPERATOR : 1
REMARK   3     REFERENCE SELECTION: (CHAIN 'A' AND (RESID 8:10 OR (RESID 11
REMARK   3                          AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK   3                          O OR NAME CB )) OR RESID 12:17 OR (RESID
REMARK   3                          18 AND (NAME N OR NAME CA OR NAME C OR
REMARK   3                          NAME O OR NAME CB )) OR RESID 19:21 OR
REMARK   3                          (RESID 22 AND (NAME N OR NAME CA OR NAME
REMARK   3                          C OR NAME O OR NAME CB )) OR RESID 23:25
REMARK   3                          OR (RESID 26 AND (NAME N OR NAME CA OR
REMARK   3                          NAME C OR NAME O OR NAME CB )) OR RESID
REMARK   3                          27:29 OR (RESID 30 AND (NAME N OR NAME CA
REMARK   3                          OR NAME C OR NAME O OR NAME CB OR NAME CG
REMARK   3                          OR NAME CD2)) OR RESID 31:34 OR (RESID 35
REMARK   3                          AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK   3                          O OR NAME CB )) OR RESID 36:43 OR (RESID
REMARK   3                          44:45 AND (NAME N OR NAME CA OR NAME C OR
REMARK   3                          NAME O )) OR RESID 46:47 OR (RESID 48 AND
REMARK   3                          (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK   3                          NAME CB )) OR RESID 49:73 OR (RESID 74
REMARK   3                          AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK   3                          CB )) OR (RESID 75 AND (NAME N OR NAME CA
REMARK   3                          OR NAME C OR NAME O OR NAME CB OR NAME CG
REMARK   3                          OR NAME CD2)) OR RESID 76:135 OR (RESID
REMARK   3                          136 AND (NAME N OR NAME CA OR NAME C OR
REMARK   3                          NAME O OR NAME CB OR NAME CG2)) OR RESID
REMARK   3                          137:143 OR (RESID 144 AND (NAME N OR NAME
REMARK   3                          CA OR NAME C OR NAME O OR NAME CB )) OR
REMARK   3                          RESID 145:171 OR (RESID 172 AND (NAME N
REMARK   3                          OR NAME CA OR NAME C OR NAME O OR NAME CB
REMARK   3                          OR NAME CG OR NAME ND2)) OR RESID 173:190
REMARK   3                          OR (RESID 191 AND (NAME N OR NAME CA OR
REMARK   3                          NAME C OR NAME O OR NAME CB )) OR RESID
REMARK   3                          192:193 OR (RESID 194 AND (NAME N OR NAME
REMARK   3                          CA OR NAME C OR NAME O OR NAME CB OR NAME
REMARK   3                          CG OR NAME CD2)) OR RESID 195:212 OR
REMARK   3                          (RESID 213 AND (NAME N OR NAME CA OR NAME
REMARK   3                          C OR NAME O OR NAME CB )) OR RESID 214:
REMARK   3                          257 OR (RESID 258:259 AND (NAME N OR NAME
REMARK   3                          CA OR NAME C OR NAME O OR NAME CB )) OR
REMARK   3                          RESID 260:308))
REMARK   3     SELECTION          : (CHAIN 'B' AND (RESID 8:10 OR (RESID 11
REMARK   3                          AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK   3                          O OR NAME CB )) OR RESID 12:17 OR (RESID
REMARK   3                          18 AND (NAME N OR NAME CA OR NAME C OR
REMARK   3                          NAME O OR NAME CB )) OR RESID 19:21 OR
REMARK   3                          (RESID 22 AND (NAME N OR NAME CA OR NAME
REMARK   3                          C OR NAME O OR NAME CB )) OR RESID 23:25
REMARK   3                          OR (RESID 26 AND (NAME N OR NAME CA OR
REMARK   3                          NAME C OR NAME O OR NAME CB )) OR RESID
REMARK   3                          27:29 OR (RESID 30 AND (NAME N OR NAME CA
REMARK   3                          OR NAME C OR NAME O OR NAME CB OR NAME CG
REMARK   3                          OR NAME CD2)) OR RESID 31:34 OR (RESID 35
REMARK   3                          AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK   3                          O OR NAME CB )) OR RESID 36 OR (RESID 37
REMARK   3                          AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK   3                          O OR NAME CB )) OR RESID 38:44 OR (RESID
REMARK   3                          45 AND (NAME N OR NAME CA OR NAME C OR
REMARK   3                          NAME O )) OR RESID 46:73 OR (RESID 74 AND
REMARK   3                          (NAME N OR NAME CA OR NAME C OR NAME CB ))
REMARK   3                          OR (RESID 75 AND (NAME N OR NAME CA OR
REMARK   3                          NAME C OR NAME O OR NAME CB OR NAME CG OR
REMARK   3                          NAME CD2)) OR RESID 76:77 OR (RESID 78
REMARK   3                          AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK   3                          O OR NAME CB )) OR RESID 79:135 OR (RESID
REMARK   3                          136 AND (NAME N OR NAME CA OR NAME C OR
REMARK   3                          NAME O OR NAME CB OR NAME CG2)) OR RESID
REMARK   3                          137:143 OR (RESID 144 AND (NAME N OR NAME
REMARK   3                          CA OR NAME C OR NAME O OR NAME CB )) OR
REMARK   3                          RESID 145:171 OR (RESID 172 AND (NAME N
REMARK   3                          OR NAME CA OR NAME C OR NAME O OR NAME CB
REMARK   3                          OR NAME CG OR NAME ND2)) OR RESID 173:190
REMARK   3                          OR (RESID 191 AND (NAME N OR NAME CA OR
REMARK   3                          NAME C OR NAME O OR NAME CB )) OR RESID
REMARK   3                          192:212 OR (RESID 213 AND (NAME N OR NAME
REMARK   3                          CA OR NAME C OR NAME O OR NAME CB )) OR
REMARK   3                          RESID 214:257 OR (RESID 258:259 AND (NAME
REMARK   3                          N OR NAME CA OR NAME C OR NAME O OR NAME
REMARK   3                          CB )) OR RESID 260:307 OR (RESID 308 AND
REMARK   3                          (NAME N OR NAME CA OR NAME C OR NAME CB
REMARK   3                          OR NAME CG OR NAME CD1 OR NAME CD2))))
REMARK   3     ATOM PAIRS NUMBER  : NULL
REMARK   3     RMSD               : NULL
REMARK   3    NCS OPERATOR : 2
REMARK   3     REFERENCE SELECTION: (CHAIN 'A' AND (RESID 8:10 OR (RESID 11
REMARK   3                          AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK   3                          O OR NAME CB )) OR RESID 12:17 OR (RESID
REMARK   3                          18 AND (NAME N OR NAME CA OR NAME C OR
REMARK   3                          NAME O OR NAME CB )) OR RESID 19:21 OR
REMARK   3                          (RESID 22 AND (NAME N OR NAME CA OR NAME
REMARK   3                          C OR NAME O OR NAME CB )) OR RESID 23:25
REMARK   3                          OR (RESID 26 AND (NAME N OR NAME CA OR
REMARK   3                          NAME C OR NAME O OR NAME CB )) OR RESID
REMARK   3                          27:29 OR (RESID 30 AND (NAME N OR NAME CA
REMARK   3                          OR NAME C OR NAME O OR NAME CB OR NAME CG
REMARK   3                          OR NAME CD2)) OR RESID 31:34 OR (RESID 35
REMARK   3                          AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK   3                          O OR NAME CB )) OR RESID 36:43 OR (RESID
REMARK   3                          44:45 AND (NAME N OR NAME CA OR NAME C OR
REMARK   3                          NAME O )) OR RESID 46:47 OR (RESID 48 AND
REMARK   3                          (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK   3                          NAME CB )) OR RESID 49:73 OR (RESID 74
REMARK   3                          AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK   3                          CB )) OR (RESID 75 AND (NAME N OR NAME CA
REMARK   3                          OR NAME C OR NAME O OR NAME CB OR NAME CG
REMARK   3                          OR NAME CD2)) OR RESID 76:135 OR (RESID
REMARK   3                          136 AND (NAME N OR NAME CA OR NAME C OR
REMARK   3                          NAME O OR NAME CB OR NAME CG2)) OR RESID
REMARK   3                          137:143 OR (RESID 144 AND (NAME N OR NAME
REMARK   3                          CA OR NAME C OR NAME O OR NAME CB )) OR
REMARK   3                          RESID 145:171 OR (RESID 172 AND (NAME N
REMARK   3                          OR NAME CA OR NAME C OR NAME O OR NAME CB
REMARK   3                          OR NAME CG OR NAME ND2)) OR RESID 173:190
REMARK   3                          OR (RESID 191 AND (NAME N OR NAME CA OR
REMARK   3                          NAME C OR NAME O OR NAME CB )) OR RESID
REMARK   3                          192:193 OR (RESID 194 AND (NAME N OR NAME
REMARK   3                          CA OR NAME C OR NAME O OR NAME CB OR NAME
REMARK   3                          CG OR NAME CD2)) OR RESID 195:212 OR
REMARK   3                          (RESID 213 AND (NAME N OR NAME CA OR NAME
REMARK   3                          C OR NAME O OR NAME CB )) OR RESID 214:
REMARK   3                          257 OR (RESID 258:259 AND (NAME N OR NAME
REMARK   3                          CA OR NAME C OR NAME O OR NAME CB )) OR
REMARK   3                          RESID 260:308))
REMARK   3     SELECTION          : (CHAIN 'C' AND (RESID 8:17 OR (RESID 18
REMARK   3                          AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK   3                          O OR NAME CB )) OR RESID 19:29 OR (RESID
REMARK   3                          30 AND (NAME N OR NAME CA OR NAME C OR
REMARK   3                          NAME O OR NAME CB OR NAME CG OR NAME CD2))
REMARK   3                          OR RESID 31:36 OR (RESID 37 AND (NAME N
REMARK   3                          OR NAME CA OR NAME C OR NAME O OR NAME CB
REMARK   3                          )) OR RESID 38:43 OR (RESID 44:45 AND
REMARK   3                          (NAME N OR NAME CA OR NAME C OR NAME O ))
REMARK   3                          OR RESID 46:73 OR (RESID 74 AND (NAME N
REMARK   3                          OR NAME CA OR NAME C OR NAME CB )) OR
REMARK   3                          (RESID 75 AND (NAME N OR NAME CA OR NAME
REMARK   3                          C OR NAME O OR NAME CB OR NAME CG OR NAME
REMARK   3                          CD2)) OR RESID 76:135 OR (RESID 136 AND
REMARK   3                          (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK   3                          NAME CB OR NAME CG2)) OR RESID 137:143 OR
REMARK   3                          (RESID 144 AND (NAME N OR NAME CA OR NAME
REMARK   3                          C OR NAME O OR NAME CB )) OR RESID 145:
REMARK   3                          171 OR (RESID 172 AND (NAME N OR NAME CA
REMARK   3                          OR NAME C OR NAME O OR NAME CB OR NAME CG
REMARK   3                          OR NAME ND2)) OR RESID 173:193 OR (RESID
REMARK   3                          194 AND (NAME N OR NAME CA OR NAME C OR
REMARK   3                          NAME O OR NAME CB OR NAME CG OR NAME CD2))
REMARK   3                          OR RESID 195:307 OR (RESID 308 AND (NAME
REMARK   3                          N OR NAME CA OR NAME C OR NAME CB OR NAME
REMARK   3                          CG OR NAME CD1 OR NAME CD2))))
REMARK   3     ATOM PAIRS NUMBER  : NULL
REMARK   3     RMSD               : NULL
REMARK   3    NCS OPERATOR : 3
REMARK   3     REFERENCE SELECTION: (CHAIN 'A' AND (RESID 8:10 OR (RESID 11
REMARK   3                          AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK   3                          O OR NAME CB )) OR RESID 12:17 OR (RESID
REMARK   3                          18 AND (NAME N OR NAME CA OR NAME C OR
REMARK   3                          NAME O OR NAME CB )) OR RESID 19:21 OR
REMARK   3                          (RESID 22 AND (NAME N OR NAME CA OR NAME
REMARK   3                          C OR NAME O OR NAME CB )) OR RESID 23:25
REMARK   3                          OR (RESID 26 AND (NAME N OR NAME CA OR
REMARK   3                          NAME C OR NAME O OR NAME CB )) OR RESID
REMARK   3                          27:29 OR (RESID 30 AND (NAME N OR NAME CA
REMARK   3                          OR NAME C OR NAME O OR NAME CB OR NAME CG
REMARK   3                          OR NAME CD2)) OR RESID 31:34 OR (RESID 35
REMARK   3                          AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK   3                          O OR NAME CB )) OR RESID 36:43 OR (RESID
REMARK   3                          44:45 AND (NAME N OR NAME CA OR NAME C OR
REMARK   3                          NAME O )) OR RESID 46:47 OR (RESID 48 AND
REMARK   3                          (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK   3                          NAME CB )) OR RESID 49:73 OR (RESID 74
REMARK   3                          AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK   3                          CB )) OR (RESID 75 AND (NAME N OR NAME CA
REMARK   3                          OR NAME C OR NAME O OR NAME CB OR NAME CG
REMARK   3                          OR NAME CD2)) OR RESID 76:135 OR (RESID
REMARK   3                          136 AND (NAME N OR NAME CA OR NAME C OR
REMARK   3                          NAME O OR NAME CB OR NAME CG2)) OR RESID
REMARK   3                          137:143 OR (RESID 144 AND (NAME N OR NAME
REMARK   3                          CA OR NAME C OR NAME O OR NAME CB )) OR
REMARK   3                          RESID 145:171 OR (RESID 172 AND (NAME N
REMARK   3                          OR NAME CA OR NAME C OR NAME O OR NAME CB
REMARK   3                          OR NAME CG OR NAME ND2)) OR RESID 173:190
REMARK   3                          OR (RESID 191 AND (NAME N OR NAME CA OR
REMARK   3                          NAME C OR NAME O OR NAME CB )) OR RESID
REMARK   3                          192:193 OR (RESID 194 AND (NAME N OR NAME
REMARK   3                          CA OR NAME C OR NAME O OR NAME CB OR NAME
REMARK   3                          CG OR NAME CD2)) OR RESID 195:212 OR
REMARK   3                          (RESID 213 AND (NAME N OR NAME CA OR NAME
REMARK   3                          C OR NAME O OR NAME CB )) OR RESID 214:
REMARK   3                          257 OR (RESID 258:259 AND (NAME N OR NAME
REMARK   3                          CA OR NAME C OR NAME O OR NAME CB )) OR
REMARK   3                          RESID 260:308))
REMARK   3     SELECTION          : (CHAIN 'D' AND (RESID 8:10 OR (RESID 11
REMARK   3                          AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK   3                          O OR NAME CB )) OR RESID 12:21 OR (RESID
REMARK   3                          22 AND (NAME N OR NAME CA OR NAME C OR
REMARK   3                          NAME O OR NAME CB )) OR RESID 23:36 OR
REMARK   3                          (RESID 37 AND (NAME N OR NAME CA OR NAME
REMARK   3                          C OR NAME O OR NAME CB )) OR RESID 38:43
REMARK   3                          OR (RESID 44:45 AND (NAME N OR NAME CA OR
REMARK   3                          NAME C OR NAME O )) OR RESID 46:47 OR
REMARK   3                          (RESID 48 AND (NAME N OR NAME CA OR NAME
REMARK   3                          C OR NAME O OR NAME CB )) OR RESID 49:73
REMARK   3                          OR (RESID 74 AND (NAME N OR NAME CA OR
REMARK   3                          NAME C OR NAME CB )) OR RESID 75 OR
REMARK   3                          (RESID 76 AND (NAME N OR NAME CA OR NAME
REMARK   3                          C OR NAME O OR NAME CB )) OR RESID 77:190
REMARK   3                          OR (RESID 191 AND (NAME N OR NAME CA OR
REMARK   3                          NAME C OR NAME O OR NAME CB )) OR RESID
REMARK   3                          192:193 OR (RESID 194 AND (NAME N OR NAME
REMARK   3                          CA OR NAME C OR NAME O OR NAME CB OR NAME
REMARK   3                          CG OR NAME CD2)) OR RESID 195:212 OR
REMARK   3                          (RESID 213 AND (NAME N OR NAME CA OR NAME
REMARK   3                          C OR NAME O OR NAME CB )) OR RESID 214:
REMARK   3                          257 OR (RESID 258:259 AND (NAME N OR NAME
REMARK   3                          CA OR NAME C OR NAME O OR NAME CB )) OR
REMARK   3                          RESID 260:307 OR (RESID 308 AND (NAME N
REMARK   3                          OR NAME CA OR NAME C OR NAME CB OR NAME
REMARK   3                          CG OR NAME CD1 OR NAME CD2))))
REMARK   3     ATOM PAIRS NUMBER  : NULL
REMARK   3     RMSD               : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 7XMJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-MAY-22.
REMARK 100 THE DEPOSITION ID IS D_1300029181.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 02-DEC-19
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SSRF
REMARK 200  BEAMLINE                       : BL18U1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9788
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : PIXEL
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 R CDTE 300K
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 64479
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.410
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.480
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0
REMARK 200  DATA REDUNDANCY                : 8.600
REMARK 200  R MERGE                    (I) : 0.10900
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 24.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 6.85
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 49.91
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.28700
REMARK 200  R SYM FOR SHELL            (I) : NULL
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: PHENIX
REMARK 200 STARTING MODEL: 3FCY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 58.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2M AMMONIUM SULFATE, 0.075M MES
REMARK 280  MONOHYDRATE PH 6.5, 7.5% (V/V) 1,4-DIOXANE, 25% (V/V) GLYCEROL,
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z
REMARK 290       3555   -X+Y,-X,Z
REMARK 290       4555   -X,-Y,Z+1/2
REMARK 290       5555   Y,-X+Y,Z+1/2
REMARK 290       6555   X-Y,X,Z+1/2
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 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       67.69450
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       67.69450
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       67.69450
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     MET A     1
REMARK 465     THR A     2
REMARK 465     LYS A     3
REMARK 465     ILE A     4
REMARK 465     ASN A     5
REMARK 465     ASN A     6
REMARK 465     ARG A   309
REMARK 465     GLU A   310
REMARK 465     ASN A   311
REMARK 465     GLN A   312
REMARK 465     MET B     1
REMARK 465     THR B     2
REMARK 465     LYS B     3
REMARK 465     ILE B     4
REMARK 465     ASN B   311
REMARK 465     GLN B   312
REMARK 465     MET C     1
REMARK 465     THR C     2
REMARK 465     LYS C     3
REMARK 465     ILE C     4
REMARK 465     ASN C   311
REMARK 465     GLN C   312
REMARK 465     MET D     1
REMARK 465     THR D     2
REMARK 465     LYS D     3
REMARK 465     ILE D     4
REMARK 465     ASN D     5
REMARK 465     ASN D     6
REMARK 465     TRP D     7
REMARK 465     GLN D   312
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     GLU A  37    CG   CD   OE1  OE2
REMARK 470     LEU A  45    CB   CG   CD1  CD2
REMARK 470     LYS A  76    CG   CD   CE   NZ
REMARK 470     LYS A  78    CG   CD   CE   NZ
REMARK 470     LEU A 308    O
REMARK 470     ASN B   6    CG   OD1  ND2
REMARK 470     ASN B  44    CB   CG   OD1  ND2
REMARK 470     LEU B  45    CG   CD1  CD2
REMARK 470     LYS B  48    CG   CD   CE   NZ
REMARK 470     ASN B  74    O
REMARK 470     LYS B  76    CG   CD   CE   NZ
REMARK 470     LEU B 194    CD1
REMARK 470     ASN C   5    CG   OD1  ND2
REMARK 470     GLN C  11    CG   CD   OE1  NE2
REMARK 470     LYS C  22    CG   CD   CE   NZ
REMARK 470     GLU C  26    CG   CD   OE1  OE2
REMARK 470     GLN C  35    CG   CD   OE1  NE2
REMARK 470     LYS C  48    CG   CD   CE   NZ
REMARK 470     LYS C  76    CG   CD   CE   NZ
REMARK 470     LYS C  78    CG   CD   CE   NZ
REMARK 470     LEU C 191    CG   CD1  CD2
REMARK 470     GLU C 213    CG   CD   OE1  OE2
REMARK 470     LYS C 258    CG   CD   CE   NZ
REMARK 470     GLU D  18    CG   CD   OE1  OE2
REMARK 470     GLU D  26    CG   CD   OE1  OE2
REMARK 470     LEU D  30    CD1
REMARK 470     GLN D  35    CG   CD   OE1  NE2
REMARK 470     ASN D  74    CG   OD1  ND2
REMARK 470     LEU D  75    CD1
REMARK 470     LYS D  78    CG   CD   CE   NZ
REMARK 470     VAL D 136    CG1
REMARK 470     GLU D 144    CG   CD   OE1  OE2
REMARK 470     ASN D 172    OD1
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   OH   TYR A    88     OE1  GLU A   223              2.18
REMARK 500   OH   TYR B    88     OE2  GLU B   223              2.18
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    LEU A  75        2.86   -154.82
REMARK 500    HIS A  89      -19.38     77.52
REMARK 500    SER A 179     -110.27     59.58
REMARK 500    TYR A 202       71.97     19.91
REMARK 500    ASP A 232       66.10   -156.23
REMARK 500    LYS A 303      -35.22     70.71
REMARK 500    ASN B   6       26.26    -76.24
REMARK 500    ASN B  44       42.56    -78.70
REMARK 500    ASN B  74      -91.12    -70.16
REMARK 500    LEU B  75      -10.95    104.68
REMARK 500    HIS B  89      -19.07     78.08
REMARK 500    GLN B 116     -130.73   -110.86
REMARK 500    SER B 179     -109.90     58.58
REMARK 500    TYR B 202       71.03     19.74
REMARK 500    ASP B 232       65.41   -157.43
REMARK 500    LYS B 303      -34.67     68.01
REMARK 500    LEU C  15       70.93   -119.83
REMARK 500    HIS C  89      -19.53     76.88
REMARK 500    ASP C  91     -169.06   -125.45
REMARK 500    GLN C 116     -133.03   -111.19
REMARK 500    SER C 179     -110.65     59.16
REMARK 500    TYR C 202       71.92     20.59
REMARK 500    ASP C 232       63.56   -157.57
REMARK 500    LYS C 303      -35.00     68.62
REMARK 500    LEU D  15       67.18     70.32
REMARK 500    ASN D  44       47.03    -81.35
REMARK 500    HIS D  89      -20.82     77.28
REMARK 500    GLN D 116     -138.08   -111.17
REMARK 500    SER D 179     -110.01     58.81
REMARK 500    TYR D 202       70.99     21.10
REMARK 500    ASP D 232       64.29   -156.99
REMARK 500    LYS D 303      -34.95     69.05
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 A 585        DISTANCE =  5.85 ANGSTROMS
REMARK 525    HOH A 586        DISTANCE =  5.87 ANGSTROMS
REMARK 525    HOH A 587        DISTANCE =  6.23 ANGSTROMS
REMARK 525    HOH A 588        DISTANCE =  6.54 ANGSTROMS
REMARK 525    HOH A 589        DISTANCE =  7.31 ANGSTROMS
REMARK 525    HOH A 590        DISTANCE =  7.34 ANGSTROMS
REMARK 525    HOH C 572        DISTANCE =  8.42 ANGSTROMS
DBREF  7XMJ A    1   312  UNP    A9QSE8   A9QSE8_LACLK     1    312
DBREF  7XMJ B    1   312  UNP    A9QSE8   A9QSE8_LACLK     1    312
DBREF  7XMJ C    1   312  UNP    A9QSE8   A9QSE8_LACLK     1    312
DBREF  7XMJ D    1   312  UNP    A9QSE8   A9QSE8_LACLK     1    312
SEQRES   1 A  312  MET THR LYS ILE ASN ASN TRP GLN ASP TYR GLN GLY SER
SEQRES   2 A  312  SER LEU LYS PRO GLU ASP PHE ASP LYS PHE TRP ASP GLU
SEQRES   3 A  312  LYS ILE ASN LEU VAL SER ASN HIS GLN PHE GLU PHE GLU
SEQRES   4 A  312  LEU ILE GLU LYS ASN LEU SER SER LYS VAL VAL ASN PHE
SEQRES   5 A  312  TYR HIS LEU TRP PHE THR ALA ILE ASP GLY ALA LYS ILE
SEQRES   6 A  312  HIS ALA GLN LEU ILE VAL PRO LYS ASN LEU LYS GLU LYS
SEQRES   7 A  312  TYR PRO ALA ILE LEU GLN PHE HIS GLY TYR HIS CYS ASP
SEQRES   8 A  312  SER GLY ASP TRP VAL ASP LYS ILE GLY ILE VAL ALA GLU
SEQRES   9 A  312  GLY ASN VAL VAL LEU ALA LEU ASP CYS ARG GLY GLN GLY
SEQRES  10 A  312  GLY LEU SER GLN ASP ASN ILE GLN THR MET GLY MET THR
SEQRES  11 A  312  MET LYS GLY LEU ILE VAL ARG GLY ILE ASP GLU GLY TYR
SEQRES  12 A  312  GLU ASN LEU TYR TYR VAL ARG GLN PHE MET ASP LEU ILE
SEQRES  13 A  312  THR ALA THR LYS ILE LEU SER GLU PHE ASP PHE VAL ASP
SEQRES  14 A  312  GLU THR ASN ILE SER ALA GLN GLY ALA SER GLN GLY GLY
SEQRES  15 A  312  ALA LEU ALA VAL ALA CYS ALA ALA LEU SER PRO LEU ILE
SEQRES  16 A  312  LYS LYS VAL THR ALA THR TYR PRO PHE LEU SER ASP TYR
SEQRES  17 A  312  ARG LYS ALA TYR GLU LEU GLY ALA GLU GLU SER ALA PHE
SEQRES  18 A  312  GLU GLU LEU PRO TYR TRP PHE GLN PHE LYS ASP PRO LEU
SEQRES  19 A  312  HIS LEU ARG GLU ASP TRP PHE PHE ASN GLN LEU GLU TYR
SEQRES  20 A  312  ILE ASP ILE GLN ASN LEU ALA PRO ARG ILE LYS ALA GLU
SEQRES  21 A  312  VAL ILE TRP ILE LEU GLY GLY LYS ASP THR VAL VAL PRO
SEQRES  22 A  312  PRO ILE THR GLN MET ALA ALA TYR ASN LYS ILE GLN SER
SEQRES  23 A  312  LYS LYS SER LEU TYR VAL LEU PRO GLU TYR GLY HIS GLU
SEQRES  24 A  312  TYR LEU PRO LYS ILE SER ASP TRP LEU ARG GLU ASN GLN
SEQRES   1 B  312  MET THR LYS ILE ASN ASN TRP GLN ASP TYR GLN GLY SER
SEQRES   2 B  312  SER LEU LYS PRO GLU ASP PHE ASP LYS PHE TRP ASP GLU
SEQRES   3 B  312  LYS ILE ASN LEU VAL SER ASN HIS GLN PHE GLU PHE GLU
SEQRES   4 B  312  LEU ILE GLU LYS ASN LEU SER SER LYS VAL VAL ASN PHE
SEQRES   5 B  312  TYR HIS LEU TRP PHE THR ALA ILE ASP GLY ALA LYS ILE
SEQRES   6 B  312  HIS ALA GLN LEU ILE VAL PRO LYS ASN LEU LYS GLU LYS
SEQRES   7 B  312  TYR PRO ALA ILE LEU GLN PHE HIS GLY TYR HIS CYS ASP
SEQRES   8 B  312  SER GLY ASP TRP VAL ASP LYS ILE GLY ILE VAL ALA GLU
SEQRES   9 B  312  GLY ASN VAL VAL LEU ALA LEU ASP CYS ARG GLY GLN GLY
SEQRES  10 B  312  GLY LEU SER GLN ASP ASN ILE GLN THR MET GLY MET THR
SEQRES  11 B  312  MET LYS GLY LEU ILE VAL ARG GLY ILE ASP GLU GLY TYR
SEQRES  12 B  312  GLU ASN LEU TYR TYR VAL ARG GLN PHE MET ASP LEU ILE
SEQRES  13 B  312  THR ALA THR LYS ILE LEU SER GLU PHE ASP PHE VAL ASP
SEQRES  14 B  312  GLU THR ASN ILE SER ALA GLN GLY ALA SER GLN GLY GLY
SEQRES  15 B  312  ALA LEU ALA VAL ALA CYS ALA ALA LEU SER PRO LEU ILE
SEQRES  16 B  312  LYS LYS VAL THR ALA THR TYR PRO PHE LEU SER ASP TYR
SEQRES  17 B  312  ARG LYS ALA TYR GLU LEU GLY ALA GLU GLU SER ALA PHE
SEQRES  18 B  312  GLU GLU LEU PRO TYR TRP PHE GLN PHE LYS ASP PRO LEU
SEQRES  19 B  312  HIS LEU ARG GLU ASP TRP PHE PHE ASN GLN LEU GLU TYR
SEQRES  20 B  312  ILE ASP ILE GLN ASN LEU ALA PRO ARG ILE LYS ALA GLU
SEQRES  21 B  312  VAL ILE TRP ILE LEU GLY GLY LYS ASP THR VAL VAL PRO
SEQRES  22 B  312  PRO ILE THR GLN MET ALA ALA TYR ASN LYS ILE GLN SER
SEQRES  23 B  312  LYS LYS SER LEU TYR VAL LEU PRO GLU TYR GLY HIS GLU
SEQRES  24 B  312  TYR LEU PRO LYS ILE SER ASP TRP LEU ARG GLU ASN GLN
SEQRES   1 C  312  MET THR LYS ILE ASN ASN TRP GLN ASP TYR GLN GLY SER
SEQRES   2 C  312  SER LEU LYS PRO GLU ASP PHE ASP LYS PHE TRP ASP GLU
SEQRES   3 C  312  LYS ILE ASN LEU VAL SER ASN HIS GLN PHE GLU PHE GLU
SEQRES   4 C  312  LEU ILE GLU LYS ASN LEU SER SER LYS VAL VAL ASN PHE
SEQRES   5 C  312  TYR HIS LEU TRP PHE THR ALA ILE ASP GLY ALA LYS ILE
SEQRES   6 C  312  HIS ALA GLN LEU ILE VAL PRO LYS ASN LEU LYS GLU LYS
SEQRES   7 C  312  TYR PRO ALA ILE LEU GLN PHE HIS GLY TYR HIS CYS ASP
SEQRES   8 C  312  SER GLY ASP TRP VAL ASP LYS ILE GLY ILE VAL ALA GLU
SEQRES   9 C  312  GLY ASN VAL VAL LEU ALA LEU ASP CYS ARG GLY GLN GLY
SEQRES  10 C  312  GLY LEU SER GLN ASP ASN ILE GLN THR MET GLY MET THR
SEQRES  11 C  312  MET LYS GLY LEU ILE VAL ARG GLY ILE ASP GLU GLY TYR
SEQRES  12 C  312  GLU ASN LEU TYR TYR VAL ARG GLN PHE MET ASP LEU ILE
SEQRES  13 C  312  THR ALA THR LYS ILE LEU SER GLU PHE ASP PHE VAL ASP
SEQRES  14 C  312  GLU THR ASN ILE SER ALA GLN GLY ALA SER GLN GLY GLY
SEQRES  15 C  312  ALA LEU ALA VAL ALA CYS ALA ALA LEU SER PRO LEU ILE
SEQRES  16 C  312  LYS LYS VAL THR ALA THR TYR PRO PHE LEU SER ASP TYR
SEQRES  17 C  312  ARG LYS ALA TYR GLU LEU GLY ALA GLU GLU SER ALA PHE
SEQRES  18 C  312  GLU GLU LEU PRO TYR TRP PHE GLN PHE LYS ASP PRO LEU
SEQRES  19 C  312  HIS LEU ARG GLU ASP TRP PHE PHE ASN GLN LEU GLU TYR
SEQRES  20 C  312  ILE ASP ILE GLN ASN LEU ALA PRO ARG ILE LYS ALA GLU
SEQRES  21 C  312  VAL ILE TRP ILE LEU GLY GLY LYS ASP THR VAL VAL PRO
SEQRES  22 C  312  PRO ILE THR GLN MET ALA ALA TYR ASN LYS ILE GLN SER
SEQRES  23 C  312  LYS LYS SER LEU TYR VAL LEU PRO GLU TYR GLY HIS GLU
SEQRES  24 C  312  TYR LEU PRO LYS ILE SER ASP TRP LEU ARG GLU ASN GLN
SEQRES   1 D  312  MET THR LYS ILE ASN ASN TRP GLN ASP TYR GLN GLY SER
SEQRES   2 D  312  SER LEU LYS PRO GLU ASP PHE ASP LYS PHE TRP ASP GLU
SEQRES   3 D  312  LYS ILE ASN LEU VAL SER ASN HIS GLN PHE GLU PHE GLU
SEQRES   4 D  312  LEU ILE GLU LYS ASN LEU SER SER LYS VAL VAL ASN PHE
SEQRES   5 D  312  TYR HIS LEU TRP PHE THR ALA ILE ASP GLY ALA LYS ILE
SEQRES   6 D  312  HIS ALA GLN LEU ILE VAL PRO LYS ASN LEU LYS GLU LYS
SEQRES   7 D  312  TYR PRO ALA ILE LEU GLN PHE HIS GLY TYR HIS CYS ASP
SEQRES   8 D  312  SER GLY ASP TRP VAL ASP LYS ILE GLY ILE VAL ALA GLU
SEQRES   9 D  312  GLY ASN VAL VAL LEU ALA LEU ASP CYS ARG GLY GLN GLY
SEQRES  10 D  312  GLY LEU SER GLN ASP ASN ILE GLN THR MET GLY MET THR
SEQRES  11 D  312  MET LYS GLY LEU ILE VAL ARG GLY ILE ASP GLU GLY TYR
SEQRES  12 D  312  GLU ASN LEU TYR TYR VAL ARG GLN PHE MET ASP LEU ILE
SEQRES  13 D  312  THR ALA THR LYS ILE LEU SER GLU PHE ASP PHE VAL ASP
SEQRES  14 D  312  GLU THR ASN ILE SER ALA GLN GLY ALA SER GLN GLY GLY
SEQRES  15 D  312  ALA LEU ALA VAL ALA CYS ALA ALA LEU SER PRO LEU ILE
SEQRES  16 D  312  LYS LYS VAL THR ALA THR TYR PRO PHE LEU SER ASP TYR
SEQRES  17 D  312  ARG LYS ALA TYR GLU LEU GLY ALA GLU GLU SER ALA PHE
SEQRES  18 D  312  GLU GLU LEU PRO TYR TRP PHE GLN PHE LYS ASP PRO LEU
SEQRES  19 D  312  HIS LEU ARG GLU ASP TRP PHE PHE ASN GLN LEU GLU TYR
SEQRES  20 D  312  ILE ASP ILE GLN ASN LEU ALA PRO ARG ILE LYS ALA GLU
SEQRES  21 D  312  VAL ILE TRP ILE LEU GLY GLY LYS ASP THR VAL VAL PRO
SEQRES  22 D  312  PRO ILE THR GLN MET ALA ALA TYR ASN LYS ILE GLN SER
SEQRES  23 D  312  LYS LYS SER LEU TYR VAL LEU PRO GLU TYR GLY HIS GLU
SEQRES  24 D  312  TYR LEU PRO LYS ILE SER ASP TRP LEU ARG GLU ASN GLN
HET     CA  A 401       1
HET     CA  C 401       1
HET     CA  D 401       1
HETNAM      CA CALCIUM ION
FORMUL   5   CA    3(CA 2+)
FORMUL   8  HOH   *302(H2 O)
HELIX    1 AA1 ASP A   19  ASN A   33  1                                  15
HELIX    2 AA2 ASP A   94  ASP A   97  5                                   4
HELIX    3 AA3 LYS A   98  GLU A  104  1                                   7
HELIX    4 AA4 GLY A  138  ASN A  145  5                                   8
HELIX    5 AA5 LEU A  146  GLU A  164  1                                  19
HELIX    6 AA6 SER A  179  SER A  192  1                                  14
HELIX    7 AA7 ASP A  207  LEU A  214  1                                   8
HELIX    8 AA8 GLU A  222  ASP A  232  1                                  11
HELIX    9 AA9 ARG A  237  GLU A  246  1                                  10
HELIX   10 AB1 ASP A  249  ALA A  254  1                                   6
HELIX   11 AB2 PRO A  255  ILE A  257  5                                   3
HELIX   12 AB3 PRO A  273  ASN A  282  1                                  10
HELIX   13 AB4 LYS A  303  LEU A  308  1                                   6
HELIX   14 AB5 ASP B   19  ASN B   33  1                                  15
HELIX   15 AB6 ASP B   94  ASP B   97  5                                   4
HELIX   16 AB7 LYS B   98  GLU B  104  1                                   7
HELIX   17 AB8 GLY B  138  ASN B  145  5                                   8
HELIX   18 AB9 LEU B  146  GLU B  164  1                                  19
HELIX   19 AC1 SER B  179  SER B  192  1                                  14
HELIX   20 AC2 ASP B  207  LEU B  214  1                                   8
HELIX   21 AC3 GLU B  222  ASP B  232  1                                  11
HELIX   22 AC4 ARG B  237  GLU B  246  1                                  10
HELIX   23 AC5 ASP B  249  ALA B  254  1                                   6
HELIX   24 AC6 PRO B  255  ILE B  257  5                                   3
HELIX   25 AC7 PRO B  273  ASN B  282  1                                  10
HELIX   26 AC8 LYS B  303  GLU B  310  1                                   8
HELIX   27 AC9 ASN C    6  TYR C   10  1                                   5
HELIX   28 AD1 ASP C   19  ASN C   33  1                                  15
HELIX   29 AD2 ASP C   94  ASP C   97  5                                   4
HELIX   30 AD3 LYS C   98  GLU C  104  1                                   7
HELIX   31 AD4 GLY C  138  ASN C  145  5                                   8
HELIX   32 AD5 LEU C  146  GLU C  164  1                                  19
HELIX   33 AD6 SER C  179  SER C  192  1                                  14
HELIX   34 AD7 ASP C  207  LEU C  214  1                                   8
HELIX   35 AD8 GLU C  222  ASP C  232  1                                  11
HELIX   36 AD9 ARG C  237  GLU C  246  1                                  10
HELIX   37 AE1 ASP C  249  ALA C  254  1                                   6
HELIX   38 AE2 PRO C  255  ILE C  257  5                                   3
HELIX   39 AE3 PRO C  273  ASN C  282  1                                  10
HELIX   40 AE4 LYS C  303  GLU C  310  1                                   8
HELIX   41 AE5 ASP D   19  ASN D   33  1                                  15
HELIX   42 AE6 ASP D   94  ASP D   97  5                                   4
HELIX   43 AE7 LYS D   98  GLU D  104  1                                   7
HELIX   44 AE8 GLY D  138  ASN D  145  5                                   8
HELIX   45 AE9 LEU D  146  GLU D  164  1                                  19
HELIX   46 AF1 SER D  179  SER D  192  1                                  14
HELIX   47 AF2 ASP D  207  LEU D  214  1                                   8
HELIX   48 AF3 GLU D  222  ASP D  232  1                                  11
HELIX   49 AF4 ARG D  237  GLU D  246  1                                  10
HELIX   50 AF5 ASP D  249  ALA D  254  1                                   6
HELIX   51 AF6 PRO D  255  ILE D  257  5                                   3
HELIX   52 AF7 PRO D  273  ASN D  282  1                                  10
HELIX   53 AF8 LYS D  303  LEU D  308  1                                   6
SHEET    1 AA1 9 PHE A  38  GLU A  42  0
SHEET    2 AA1 9 VAL A  50  THR A  58 -1  O  HIS A  54   N  ILE A  41
SHEET    3 AA1 9 LYS A  64  PRO A  72 -1  O  ILE A  65   N  PHE A  57
SHEET    4 AA1 9 VAL A 107  LEU A 111 -1  O  ALA A 110   N  GLN A  68
SHEET    5 AA1 9 TYR A  79  PHE A  85  1  N  ILE A  82   O  VAL A 107
SHEET    6 AA1 9 VAL A 168  ALA A 178  1  O  ASP A 169   N  TYR A  79
SHEET    7 AA1 9 LYS A 197  THR A 201  1  O  THR A 201   N  GLY A 177
SHEET    8 AA1 9 GLU A 260  GLY A 266  1  O  ILE A 262   N  VAL A 198
SHEET    9 AA1 9 LYS A 288  LEU A 293  1  O  TYR A 291   N  TRP A 263
SHEET    1 AA2 9 PHE B  38  GLU B  42  0
SHEET    2 AA2 9 VAL B  50  THR B  58 -1  O  HIS B  54   N  ILE B  41
SHEET    3 AA2 9 LYS B  64  PRO B  72 -1  O  VAL B  71   N  ASN B  51
SHEET    4 AA2 9 VAL B 107  LEU B 111 -1  O  ALA B 110   N  GLN B  68
SHEET    5 AA2 9 TYR B  79  PHE B  85  1  N  ILE B  82   O  VAL B 107
SHEET    6 AA2 9 VAL B 168  ALA B 178  1  O  ASP B 169   N  TYR B  79
SHEET    7 AA2 9 LYS B 197  THR B 201  1  O  LYS B 197   N  ALA B 175
SHEET    8 AA2 9 GLU B 260  GLY B 266  1  O  ILE B 262   N  VAL B 198
SHEET    9 AA2 9 LYS B 288  LEU B 293  1  O  TYR B 291   N  TRP B 263
SHEET    1 AA3 9 PHE C  38  GLU C  42  0
SHEET    2 AA3 9 VAL C  50  THR C  58 -1  O  HIS C  54   N  ILE C  41
SHEET    3 AA3 9 LYS C  64  PRO C  72 -1  O  ILE C  65   N  PHE C  57
SHEET    4 AA3 9 VAL C 107  LEU C 111 -1  O  ALA C 110   N  GLN C  68
SHEET    5 AA3 9 TYR C  79  PHE C  85  1  N  ILE C  82   O  VAL C 107
SHEET    6 AA3 9 VAL C 168  ALA C 178  1  O  ASP C 169   N  TYR C  79
SHEET    7 AA3 9 LYS C 197  THR C 201  1  O  THR C 199   N  ALA C 175
SHEET    8 AA3 9 GLU C 260  GLY C 266  1  O  ILE C 264   N  ALA C 200
SHEET    9 AA3 9 LYS C 288  LEU C 293  1  O  TYR C 291   N  TRP C 263
SHEET    1 AA4 9 PHE D  38  LYS D  43  0
SHEET    2 AA4 9 VAL D  50  THR D  58 -1  O  HIS D  54   N  ILE D  41
SHEET    3 AA4 9 LYS D  64  PRO D  72 -1  O  VAL D  71   N  ASN D  51
SHEET    4 AA4 9 VAL D 107  LEU D 111 -1  O  ALA D 110   N  GLN D  68
SHEET    5 AA4 9 TYR D  79  PHE D  85  1  N  ILE D  82   O  VAL D 107
SHEET    6 AA4 9 VAL D 168  ALA D 178  1  O  ASP D 169   N  TYR D  79
SHEET    7 AA4 9 LYS D 197  THR D 201  1  O  THR D 199   N  ALA D 175
SHEET    8 AA4 9 GLU D 260  GLY D 266  1  O  ILE D 262   N  VAL D 198
SHEET    9 AA4 9 LYS D 288  LEU D 293  1  O  TYR D 291   N  TRP D 263
CISPEP   1 TYR B  296    GLY B  297          0         6.39
CRYST1  147.714  147.714  135.389  90.00  90.00 120.00 P 63         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      0.006770  0.003909  0.000000        0.00000
SCALE2      0.000000  0.007817  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007386        0.00000
TER    2428      LEU A 308
TER    4889      GLU B 310
TER    7328      GLU C 310
TER    9760      ASN D 311
MASTER      625    0    3   53   36    0    0    610061    4    0   96
END