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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 |