HEADER IMMUNE SYSTEM 28-NOV-16 5U1R
TITLE STRUCTURE OF HUMAN MR1-DICLOFENAC IN COMPLEX WITH HUMAN MAIT A-F7 TCR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MAJOR HISTOCOMPATIBILITY COMPLEX CLASS I-RELATED GENE
COMPND 3 PROTEIN;
COMPND 4 CHAIN: C, A;
COMPND 5 FRAGMENT: UNP RESIDUES 23-292;
COMPND 6 SYNONYM: MHC CLASS I-RELATED GENE PROTEIN,CLASS I HISTOCOMPATIBILITY
COMPND 7 ANTIGEN-LIKE PROTEIN;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: MAIT T-CELL RECEPTOR ALPHA CHAIN;
COMPND 11 CHAIN: D, B;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: MAIT T-CELL RECEPTOR BETA CHAIN;
COMPND 15 CHAIN: E, G;
COMPND 16 ENGINEERED: YES;
COMPND 17 MOL_ID: 4;
COMPND 18 MOLECULE: BETA-2-MICROGLOBULIN;
COMPND 19 CHAIN: F, H;
COMPND 20 FRAGMENT: UNP RESIDUES 21-119;
COMPND 21 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: MR1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET30;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 GENE: B2M;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 17 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 19 EXPRESSION_SYSTEM_PLASMID: PET30;
SOURCE 20 MOL_ID: 3;
SOURCE 21 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 22 ORGANISM_TAXID: 9606;
SOURCE 23 GENE: TRAV/TRAC;
SOURCE 24 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 25 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 26 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 27 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 28 EXPRESSION_SYSTEM_PLASMID: PET30;
SOURCE 29 MOL_ID: 4;
SOURCE 30 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 31 ORGANISM_COMMON: HUMAN;
SOURCE 32 ORGANISM_TAXID: 9606;
SOURCE 33 GENE: B2M, CDABP0092, HDCMA22P;
SOURCE 34 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 35 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 36 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 37 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 38 EXPRESSION_SYSTEM_PLASMID: PET30
KEYWDS T-CELL RECEPTOR, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR A.N.KELLER,J.ROSSJOHN
REVDAT 4 04-OCT-23 5U1R 1 REMARK
REVDAT 3 01-JAN-20 5U1R 1 REMARK
REVDAT 2 05-APR-17 5U1R 1 JRNL REMARK
REVDAT 1 15-MAR-17 5U1R 0
JRNL AUTH A.N.KELLER,S.B.ECKLE,W.XU,L.LIU,V.A.HUGHES,J.Y.MAK,
JRNL AUTH 2 B.S.MEEHAN,T.PEDIONGCO,R.W.BIRKINSHAW,Z.CHEN,H.WANG,
JRNL AUTH 3 C.D'SOUZA,L.KJER-NIELSEN,N.A.GHERARDIN,D.I.GODFREY,
JRNL AUTH 4 L.KOSTENKO,A.J.CORBETT,A.W.PURCELL,D.P.FAIRLIE,J.MCCLUSKEY,
JRNL AUTH 5 J.ROSSJOHN
JRNL TITL DRUGS AND DRUG-LIKE MOLECULES CAN MODULATE THE FUNCTION OF
JRNL TITL 2 MUCOSAL-ASSOCIATED INVARIANT T CELLS.
JRNL REF NAT. IMMUNOL. V. 18 402 2017
JRNL REFN ESSN 1529-2916
JRNL PMID 28166217
JRNL DOI 10.1038/NI.3679
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.11.1_2575
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 55436
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 2779
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 49.0028 - 7.3213 0.99 2775 137 0.1861 0.2263
REMARK 3 2 7.3213 - 5.8142 0.99 2695 146 0.1947 0.2308
REMARK 3 3 5.8142 - 5.0801 0.96 2583 126 0.1577 0.1947
REMARK 3 4 5.0801 - 4.6160 0.96 2580 140 0.1295 0.1627
REMARK 3 5 4.6160 - 4.2853 0.98 2618 139 0.1312 0.1705
REMARK 3 6 4.2853 - 4.0328 0.99 2627 153 0.1486 0.2048
REMARK 3 7 4.0328 - 3.8309 0.99 2624 149 0.1604 0.2088
REMARK 3 8 3.8309 - 3.6642 0.99 2627 142 0.1678 0.2172
REMARK 3 9 3.6642 - 3.5232 0.99 2661 142 0.1742 0.2276
REMARK 3 10 3.5232 - 3.4017 0.99 2610 137 0.1857 0.2450
REMARK 3 11 3.4017 - 3.2953 0.99 2633 132 0.2034 0.2907
REMARK 3 12 3.2953 - 3.2011 0.99 2663 128 0.2215 0.2564
REMARK 3 13 3.2011 - 3.1169 0.99 2621 127 0.2261 0.3150
REMARK 3 14 3.1169 - 3.0408 0.98 2575 149 0.2338 0.2982
REMARK 3 15 3.0408 - 2.9717 0.99 2662 142 0.2389 0.2691
REMARK 3 16 2.9717 - 2.9085 0.99 2600 128 0.2450 0.3399
REMARK 3 17 2.9085 - 2.8503 0.99 2641 137 0.2594 0.3281
REMARK 3 18 2.8503 - 2.7965 0.99 2618 123 0.2856 0.3393
REMARK 3 19 2.7965 - 2.7466 0.99 2625 158 0.3068 0.3735
REMARK 3 20 2.7466 - 2.7000 0.99 2619 144 0.3176 0.3712
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) : 0.370
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.830
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 43.34
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 54.42
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 : 0.005 13249
REMARK 3 ANGLE : 1.369 18025
REMARK 3 CHIRALITY : 0.042 1900
REMARK 3 PLANARITY : 0.004 2372
REMARK 3 DIHEDRAL : 17.169 4786
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 39
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 0 THROUGH 133 )
REMARK 3 ORIGIN FOR THE GROUP (A): -42.7021 44.7907 188.5231
REMARK 3 T TENSOR
REMARK 3 T11: 0.3343 T22: 0.5242
REMARK 3 T33: 0.4932 T12: 0.1134
REMARK 3 T13: -0.1369 T23: 0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 2.7574 L22: 2.9464
REMARK 3 L33: 1.5509 L12: -0.1092
REMARK 3 L13: -0.6345 L23: -0.2344
REMARK 3 S TENSOR
REMARK 3 S11: -0.1067 S12: -0.2799 S13: 0.6121
REMARK 3 S21: 0.1333 S22: 0.0568 S23: -0.0436
REMARK 3 S31: -0.2605 S32: -0.1016 S33: 0.0705
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 134 THROUGH 182 )
REMARK 3 ORIGIN FOR THE GROUP (A): -38.6965 36.7911 182.2790
REMARK 3 T TENSOR
REMARK 3 T11: 0.2463 T22: 0.2422
REMARK 3 T33: 0.4270 T12: 0.0369
REMARK 3 T13: -0.0380 T23: 0.1372
REMARK 3 L TENSOR
REMARK 3 L11: 1.3917 L22: 2.6771
REMARK 3 L33: 2.6024 L12: -1.8316
REMARK 3 L13: 0.2836 L23: -0.8774
REMARK 3 S TENSOR
REMARK 3 S11: 0.1327 S12: 0.2664 S13: -0.1879
REMARK 3 S21: -0.1384 S22: -0.0678 S23: -0.7945
REMARK 3 S31: 0.1030 S32: 0.2954 S33: -0.0437
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 183 THROUGH 269 )
REMARK 3 ORIGIN FOR THE GROUP (A): -63.4482 46.0772 160.2495
REMARK 3 T TENSOR
REMARK 3 T11: 0.4130 T22: 0.7435
REMARK 3 T33: 0.5987 T12: -0.1663
REMARK 3 T13: -0.2118 T23: 0.2490
REMARK 3 L TENSOR
REMARK 3 L11: 1.6385 L22: 4.2013
REMARK 3 L33: 6.4081 L12: -0.9428
REMARK 3 L13: 0.1088 L23: -0.2052
REMARK 3 S TENSOR
REMARK 3 S11: -0.2314 S12: 0.6419 S13: 0.7951
REMARK 3 S21: -0.4409 S22: -0.1580 S23: -0.2597
REMARK 3 S31: -0.8446 S32: 0.2403 S33: 0.3515
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 103 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.8105 23.9215 193.8607
REMARK 3 T TENSOR
REMARK 3 T11: 0.3019 T22: 0.1971
REMARK 3 T33: 0.1954 T12: 0.0125
REMARK 3 T13: -0.0536 T23: 0.0156
REMARK 3 L TENSOR
REMARK 3 L11: 7.8902 L22: 3.4586
REMARK 3 L33: 2.9218 L12: -3.5262
REMARK 3 L13: 1.9776 L23: -0.2886
REMARK 3 S TENSOR
REMARK 3 S11: -0.0429 S12: -0.1863 S13: 0.2741
REMARK 3 S21: -0.1316 S22: 0.1228 S23: -0.1103
REMARK 3 S31: 0.0280 S32: -0.1923 S33: -0.0600
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 104 THROUGH 116 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.1036 14.3149 202.1913
REMARK 3 T TENSOR
REMARK 3 T11: 0.3887 T22: 0.4784
REMARK 3 T33: 0.2022 T12: 0.1029
REMARK 3 T13: -0.1008 T23: -0.1351
REMARK 3 L TENSOR
REMARK 3 L11: 9.4780 L22: 4.2501
REMARK 3 L33: 2.5540 L12: -6.2315
REMARK 3 L13: 4.9063 L23: -3.2597
REMARK 3 S TENSOR
REMARK 3 S11: 0.6797 S12: 1.1627 S13: -0.0538
REMARK 3 S21: -0.6618 S22: -0.4491 S23: 0.0259
REMARK 3 S31: 0.5663 S32: 0.5886 S33: -0.1359
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 117 THROUGH 199 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.0098 8.5158 216.9089
REMARK 3 T TENSOR
REMARK 3 T11: 0.3871 T22: 0.1854
REMARK 3 T33: 0.3206 T12: 0.0315
REMARK 3 T13: -0.0355 T23: -0.0662
REMARK 3 L TENSOR
REMARK 3 L11: 4.9368 L22: 4.9406
REMARK 3 L33: 7.1667 L12: 0.1529
REMARK 3 L13: -0.7704 L23: 0.5954
REMARK 3 S TENSOR
REMARK 3 S11: 0.0514 S12: -0.0788 S13: -0.4719
REMARK 3 S21: 0.5062 S22: -0.0680 S23: -0.1136
REMARK 3 S31: 0.7597 S32: -0.0447 S33: 0.0776
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 2 THROUGH 94 )
REMARK 3 ORIGIN FOR THE GROUP (A): -29.8753 32.2490 213.7458
REMARK 3 T TENSOR
REMARK 3 T11: 0.3902 T22: 0.7017
REMARK 3 T33: 0.3800 T12: 0.1490
REMARK 3 T13: -0.1105 T23: -0.2027
REMARK 3 L TENSOR
REMARK 3 L11: 3.3014 L22: 2.8402
REMARK 3 L33: 2.8325 L12: -0.1600
REMARK 3 L13: 0.2017 L23: -1.4816
REMARK 3 S TENSOR
REMARK 3 S11: -0.0308 S12: -0.7637 S13: 0.5748
REMARK 3 S21: 0.3237 S22: -0.1498 S23: 0.1148
REMARK 3 S31: -0.5623 S32: -0.7186 S33: 0.1444
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 95 THROUGH 124 )
REMARK 3 ORIGIN FOR THE GROUP (A): -23.8165 27.5638 215.2527
REMARK 3 T TENSOR
REMARK 3 T11: 0.4787 T22: 0.5357
REMARK 3 T33: 0.3493 T12: 0.0057
REMARK 3 T13: -0.1215 T23: -0.1712
REMARK 3 L TENSOR
REMARK 3 L11: 3.0721 L22: 3.0514
REMARK 3 L33: 7.2725 L12: -1.7428
REMARK 3 L13: 3.2133 L23: -3.6839
REMARK 3 S TENSOR
REMARK 3 S11: -0.0227 S12: -0.5559 S13: 0.1197
REMARK 3 S21: -0.6182 S22: 0.1828 S23: 0.3080
REMARK 3 S31: 0.6292 S32: -1.3846 S33: -0.1252
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 125 THROUGH 244 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.1898 21.2692 224.9291
REMARK 3 T TENSOR
REMARK 3 T11: 0.2917 T22: 0.1933
REMARK 3 T33: 0.1738 T12: 0.0221
REMARK 3 T13: -0.0771 T23: -0.0544
REMARK 3 L TENSOR
REMARK 3 L11: 6.7290 L22: 1.1328
REMARK 3 L33: 4.2611 L12: 0.1634
REMARK 3 L13: -2.1227 L23: 0.4045
REMARK 3 S TENSOR
REMARK 3 S11: 0.0389 S12: 0.2311 S13: -0.0622
REMARK 3 S21: 0.1134 S22: -0.1475 S23: 0.0521
REMARK 3 S31: -0.0013 S32: -0.3768 S33: 0.0830
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 1 THROUGH 11 )
REMARK 3 ORIGIN FOR THE GROUP (A): -58.2888 57.6125 178.0679
REMARK 3 T TENSOR
REMARK 3 T11: 0.5753 T22: 0.5903
REMARK 3 T33: 1.0630 T12: 0.1067
REMARK 3 T13: -0.3517 T23: 0.0742
REMARK 3 L TENSOR
REMARK 3 L11: 1.9941 L22: 2.7295
REMARK 3 L33: 1.8986 L12: -0.4379
REMARK 3 L13: -0.5070 L23: -0.4848
REMARK 3 S TENSOR
REMARK 3 S11: -0.4739 S12: -0.7154 S13: 1.4131
REMARK 3 S21: -0.3956 S22: -0.0386 S23: -0.0463
REMARK 3 S31: -0.5269 S32: -0.3501 S33: 0.5093
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 12 THROUGH 19 )
REMARK 3 ORIGIN FOR THE GROUP (A): -78.1147 45.7610 174.5226
REMARK 3 T TENSOR
REMARK 3 T11: 0.3150 T22: 0.9904
REMARK 3 T33: 0.8585 T12: 0.1637
REMARK 3 T13: -0.2909 T23: -0.1380
REMARK 3 L TENSOR
REMARK 3 L11: 5.6872 L22: 6.0737
REMARK 3 L33: 3.0647 L12: -3.7858
REMARK 3 L13: -1.7341 L23: 0.8298
REMARK 3 S TENSOR
REMARK 3 S11: -0.7094 S12: -0.4744 S13: -0.9217
REMARK 3 S21: -0.3063 S22: 0.8049 S23: 1.9215
REMARK 3 S31: -0.2374 S32: -1.2958 S33: -0.3701
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 20 THROUGH 35 )
REMARK 3 ORIGIN FOR THE GROUP (A): -61.5581 53.2395 182.6094
REMARK 3 T TENSOR
REMARK 3 T11: 0.5682 T22: 0.5988
REMARK 3 T33: 0.8628 T12: 0.2160
REMARK 3 T13: -0.3579 T23: -0.1095
REMARK 3 L TENSOR
REMARK 3 L11: 2.6760 L22: 6.3926
REMARK 3 L33: 3.5021 L12: 3.4407
REMARK 3 L13: -2.5048 L23: -2.0702
REMARK 3 S TENSOR
REMARK 3 S11: -0.5030 S12: 0.0798 S13: 1.8772
REMARK 3 S21: 0.4921 S22: 0.2732 S23: 0.4687
REMARK 3 S31: -0.4836 S32: -0.4007 S33: 0.1258
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 36 THROUGH 46 )
REMARK 3 ORIGIN FOR THE GROUP (A): -71.7186 59.1063 187.0523
REMARK 3 T TENSOR
REMARK 3 T11: 0.7312 T22: 1.1845
REMARK 3 T33: 1.3208 T12: 0.5652
REMARK 3 T13: -0.2078 T23: -0.3135
REMARK 3 L TENSOR
REMARK 3 L11: 6.5033 L22: 4.8471
REMARK 3 L33: 3.8115 L12: -3.4467
REMARK 3 L13: -3.9803 L23: 0.0708
REMARK 3 S TENSOR
REMARK 3 S11: -0.5690 S12: -0.9978 S13: 1.1410
REMARK 3 S21: 1.1559 S22: 0.9609 S23: 0.7867
REMARK 3 S31: -0.7461 S32: -0.6382 S33: -0.4999
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 47 THROUGH 61 )
REMARK 3 ORIGIN FOR THE GROUP (A): -56.8476 49.6314 185.6300
REMARK 3 T TENSOR
REMARK 3 T11: 0.5121 T22: 0.7390
REMARK 3 T33: 0.4420 T12: 0.0469
REMARK 3 T13: -0.2809 T23: 0.0095
REMARK 3 L TENSOR
REMARK 3 L11: 4.6657 L22: 7.0652
REMARK 3 L33: 5.3583 L12: 1.1085
REMARK 3 L13: -4.0794 L23: -3.2372
REMARK 3 S TENSOR
REMARK 3 S11: -0.2293 S12: -1.0040 S13: -0.7374
REMARK 3 S21: 0.5301 S22: -0.1501 S23: -0.2776
REMARK 3 S31: -0.9040 S32: -0.5765 S33: 0.2607
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 62 THROUGH 71 )
REMARK 3 ORIGIN FOR THE GROUP (A): -66.5692 49.4658 183.9369
REMARK 3 T TENSOR
REMARK 3 T11: 0.5382 T22: 0.4858
REMARK 3 T33: 0.7665 T12: 0.2100
REMARK 3 T13: -0.0807 T23: -0.0284
REMARK 3 L TENSOR
REMARK 3 L11: 1.9148 L22: 3.4258
REMARK 3 L33: 6.1379 L12: 0.4052
REMARK 3 L13: 1.7868 L23: 0.1119
REMARK 3 S TENSOR
REMARK 3 S11: -0.7900 S12: -0.7113 S13: 1.4939
REMARK 3 S21: 1.1276 S22: 0.5024 S23: 0.4369
REMARK 3 S31: -0.4773 S32: -0.4599 S33: 0.2874
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 72 THROUGH 77 )
REMARK 3 ORIGIN FOR THE GROUP (A): -82.6398 55.9371 177.9022
REMARK 3 T TENSOR
REMARK 3 T11: 0.2910 T22: 1.2506
REMARK 3 T33: 1.1062 T12: 0.2457
REMARK 3 T13: -0.3033 T23: -0.0477
REMARK 3 L TENSOR
REMARK 3 L11: 1.8537 L22: 0.4653
REMARK 3 L33: 1.1002 L12: -0.6390
REMARK 3 L13: -0.6338 L23: -0.2468
REMARK 3 S TENSOR
REMARK 3 S11: 0.0232 S12: -0.5004 S13: 0.0012
REMARK 3 S21: 0.1419 S22: 0.1862 S23: 0.1393
REMARK 3 S31: -0.0441 S32: -0.0639 S33: -0.0898
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 78 THROUGH 90 )
REMARK 3 ORIGIN FOR THE GROUP (A): -63.0251 63.4879 184.3624
REMARK 3 T TENSOR
REMARK 3 T11: 0.6733 T22: 0.7202
REMARK 3 T33: 1.5942 T12: 0.2918
REMARK 3 T13: -0.3563 T23: -0.3532
REMARK 3 L TENSOR
REMARK 3 L11: 3.0475 L22: 1.9944
REMARK 3 L33: 2.1501 L12: 2.1284
REMARK 3 L13: 0.8901 L23: -0.3660
REMARK 3 S TENSOR
REMARK 3 S11: -0.6246 S12: -0.7037 S13: 0.3226
REMARK 3 S21: 0.5464 S22: 0.2564 S23: 0.0702
REMARK 3 S31: -0.8174 S32: -0.4815 S33: 0.2821
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 91 THROUGH 97 )
REMARK 3 ORIGIN FOR THE GROUP (A): -71.1077 59.0203 175.7554
REMARK 3 T TENSOR
REMARK 3 T11: 0.8110 T22: 0.9124
REMARK 3 T33: 1.1426 T12: 0.3753
REMARK 3 T13: -0.6150 T23: 0.0279
REMARK 3 L TENSOR
REMARK 3 L11: 5.8440 L22: 3.5456
REMARK 3 L33: 4.5131 L12: -0.1819
REMARK 3 L13: 1.3101 L23: -2.1733
REMARK 3 S TENSOR
REMARK 3 S11: 0.4590 S12: 0.3418 S13: -0.4572
REMARK 3 S21: -0.8489 S22: -0.2962 S23: 0.2509
REMARK 3 S31: 0.5547 S32: -0.3452 S33: -0.4152
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 0 THROUGH 133 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.7194 25.4653 251.8690
REMARK 3 T TENSOR
REMARK 3 T11: 0.2045 T22: 0.4965
REMARK 3 T33: 0.2037 T12: 0.0110
REMARK 3 T13: 0.0012 T23: 0.0378
REMARK 3 L TENSOR
REMARK 3 L11: 1.8839 L22: 4.0923
REMARK 3 L33: 1.9479 L12: -0.1053
REMARK 3 L13: 0.0523 L23: -0.0623
REMARK 3 S TENSOR
REMARK 3 S11: -0.1019 S12: -0.3983 S13: 0.0284
REMARK 3 S21: 0.0216 S22: -0.1147 S23: -0.2101
REMARK 3 S31: -0.0002 S32: 0.0104 S33: 0.1961
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 134 THROUGH 182 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.5571 29.2959 245.5382
REMARK 3 T TENSOR
REMARK 3 T11: 0.2533 T22: 0.2912
REMARK 3 T33: 0.1119 T12: 0.0386
REMARK 3 T13: -0.0457 T23: -0.0795
REMARK 3 L TENSOR
REMARK 3 L11: 2.7330 L22: 1.3058
REMARK 3 L33: 2.2648 L12: 0.5358
REMARK 3 L13: -0.8690 L23: -0.8248
REMARK 3 S TENSOR
REMARK 3 S11: -0.0592 S12: 0.0442 S13: 0.1701
REMARK 3 S21: 0.0857 S22: 0.0570 S23: 0.3623
REMARK 3 S31: -0.2409 S32: -0.3115 S33: 0.0166
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 183 THROUGH 269 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.4199 36.8185 223.6306
REMARK 3 T TENSOR
REMARK 3 T11: 0.2300 T22: 0.1979
REMARK 3 T33: 0.3098 T12: -0.0325
REMARK 3 T13: -0.0183 T23: -0.0224
REMARK 3 L TENSOR
REMARK 3 L11: 5.0772 L22: 6.1537
REMARK 3 L33: 6.4060 L12: -1.2541
REMARK 3 L13: -1.3967 L23: 0.1000
REMARK 3 S TENSOR
REMARK 3 S11: 0.1922 S12: 0.3836 S13: -0.1337
REMARK 3 S21: -0.1753 S22: 0.0210 S23: -0.6104
REMARK 3 S31: 0.4404 S32: 0.4834 S33: -0.1792
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 91 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.3940 27.5732 256.5746
REMARK 3 T TENSOR
REMARK 3 T11: 0.2823 T22: 0.4898
REMARK 3 T33: 0.2368 T12: 0.0605
REMARK 3 T13: -0.0555 T23: -0.1478
REMARK 3 L TENSOR
REMARK 3 L11: 4.9005 L22: 1.2241
REMARK 3 L33: 4.5049 L12: 0.2950
REMARK 3 L13: -1.7210 L23: -1.3667
REMARK 3 S TENSOR
REMARK 3 S11: -0.1667 S12: 0.1985 S13: -0.0508
REMARK 3 S21: -0.0645 S22: 0.0894 S23: 0.0736
REMARK 3 S31: 0.2108 S32: -0.3935 S33: 0.0908
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 92 THROUGH 135 )
REMARK 3 ORIGIN FOR THE GROUP (A): -39.1377 26.9971 273.0016
REMARK 3 T TENSOR
REMARK 3 T11: 0.4352 T22: 0.7091
REMARK 3 T33: 0.3928 T12: -0.0040
REMARK 3 T13: -0.0657 T23: 0.0631
REMARK 3 L TENSOR
REMARK 3 L11: 4.2384 L22: 0.7079
REMARK 3 L33: 4.6009 L12: 0.2569
REMARK 3 L13: -4.2317 L23: -0.5124
REMARK 3 S TENSOR
REMARK 3 S11: 0.0674 S12: -0.1094 S13: 0.1565
REMARK 3 S21: 0.2272 S22: 0.1464 S23: 0.3437
REMARK 3 S31: 0.3518 S32: -0.4847 S33: -0.0506
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 136 THROUGH 200 )
REMARK 3 ORIGIN FOR THE GROUP (A): -50.2436 29.4921 277.6374
REMARK 3 T TENSOR
REMARK 3 T11: 0.2700 T22: 0.6571
REMARK 3 T33: 0.4710 T12: -0.0423
REMARK 3 T13: 0.0507 T23: -0.0078
REMARK 3 L TENSOR
REMARK 3 L11: 9.6213 L22: 5.8546
REMARK 3 L33: 5.6887 L12: -0.7501
REMARK 3 L13: 0.3816 L23: -0.5814
REMARK 3 S TENSOR
REMARK 3 S11: 0.0925 S12: 0.2558 S13: 0.7286
REMARK 3 S21: -0.0556 S22: 0.0595 S23: 0.3730
REMARK 3 S31: -0.2455 S32: -0.8175 S33: 0.0438
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 2 THROUGH 14 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.5604 22.9055 283.7439
REMARK 3 T TENSOR
REMARK 3 T11: 0.4299 T22: 0.8038
REMARK 3 T33: 0.1076 T12: 0.0338
REMARK 3 T13: 0.0230 T23: 0.0668
REMARK 3 L TENSOR
REMARK 3 L11: 6.2274 L22: 2.6547
REMARK 3 L33: 2.6122 L12: 0.2299
REMARK 3 L13: -1.9088 L23: -2.3849
REMARK 3 S TENSOR
REMARK 3 S11: -0.2310 S12: -0.4241 S13: -0.3211
REMARK 3 S21: 0.5686 S22: -0.1486 S23: -0.1066
REMARK 3 S31: 1.0134 S32: 0.1508 S33: 0.4329
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 15 THROUGH 109 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.2741 27.1813 274.3274
REMARK 3 T TENSOR
REMARK 3 T11: 0.3382 T22: 0.5016
REMARK 3 T33: 0.2100 T12: 0.0925
REMARK 3 T13: -0.1077 T23: 0.0102
REMARK 3 L TENSOR
REMARK 3 L11: 3.4027 L22: 2.6190
REMARK 3 L33: 4.9945 L12: -0.1011
REMARK 3 L13: -1.9597 L23: 1.9991
REMARK 3 S TENSOR
REMARK 3 S11: -0.1609 S12: -0.3432 S13: 0.0391
REMARK 3 S21: 0.1804 S22: -0.0284 S23: -0.0381
REMARK 3 S31: -0.0691 S32: 0.4260 S33: 0.1847
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 110 THROUGH 124 )
REMARK 3 ORIGIN FOR THE GROUP (A): -22.8690 32.1681 292.0270
REMARK 3 T TENSOR
REMARK 3 T11: 0.4212 T22: 0.6677
REMARK 3 T33: 0.2174 T12: 0.0453
REMARK 3 T13: -0.0115 T23: -0.0525
REMARK 3 L TENSOR
REMARK 3 L11: 8.0777 L22: 4.7511
REMARK 3 L33: 5.7424 L12: -0.9670
REMARK 3 L13: -6.5040 L23: -0.7383
REMARK 3 S TENSOR
REMARK 3 S11: 0.0680 S12: -0.9757 S13: 0.5010
REMARK 3 S21: 0.3300 S22: 0.3303 S23: -0.0088
REMARK 3 S31: -0.4616 S32: 0.7727 S33: -0.3042
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 125 THROUGH 162 )
REMARK 3 ORIGIN FOR THE GROUP (A): -43.3594 20.3989 285.6057
REMARK 3 T TENSOR
REMARK 3 T11: 0.4159 T22: 0.5266
REMARK 3 T33: 0.3203 T12: -0.1014
REMARK 3 T13: -0.0746 T23: 0.0991
REMARK 3 L TENSOR
REMARK 3 L11: 8.5726 L22: 5.1230
REMARK 3 L33: 5.9358 L12: 2.1089
REMARK 3 L13: 3.6837 L23: 1.9535
REMARK 3 S TENSOR
REMARK 3 S11: 0.5894 S12: -0.7167 S13: -1.0521
REMARK 3 S21: 0.0804 S22: -0.0201 S23: 0.3704
REMARK 3 S31: 0.8734 S32: -0.9288 S33: -0.4711
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 163 THROUGH 188 )
REMARK 3 ORIGIN FOR THE GROUP (A): -35.7290 26.9102 283.9727
REMARK 3 T TENSOR
REMARK 3 T11: 0.3713 T22: 0.4195
REMARK 3 T33: 0.3608 T12: -0.0010
REMARK 3 T13: -0.0743 T23: 0.0257
REMARK 3 L TENSOR
REMARK 3 L11: 3.6056 L22: 6.3155
REMARK 3 L33: 5.2410 L12: -0.3660
REMARK 3 L13: 1.1827 L23: 0.8520
REMARK 3 S TENSOR
REMARK 3 S11: 0.2493 S12: -0.1170 S13: -0.6393
REMARK 3 S21: -0.1210 S22: 0.5580 S23: -0.2386
REMARK 3 S31: 0.2377 S32: 0.0947 S33: -0.5931
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 189 THROUGH 203 )
REMARK 3 ORIGIN FOR THE GROUP (A): -46.2992 16.8450 282.6415
REMARK 3 T TENSOR
REMARK 3 T11: 0.5426 T22: 0.6487
REMARK 3 T33: 0.5474 T12: -0.1971
REMARK 3 T13: -0.0713 T23: 0.2024
REMARK 3 L TENSOR
REMARK 3 L11: 5.7120 L22: 3.1172
REMARK 3 L33: 3.4220 L12: 0.8713
REMARK 3 L13: 3.4579 L23: 2.5085
REMARK 3 S TENSOR
REMARK 3 S11: 0.5534 S12: 0.1152 S13: -0.9474
REMARK 3 S21: 0.7499 S22: 0.3129 S23: 0.9113
REMARK 3 S31: 0.6090 S32: -0.4091 S33: -0.5325
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 204 THROUGH 225 )
REMARK 3 ORIGIN FOR THE GROUP (A): -31.3612 17.6140 293.1629
REMARK 3 T TENSOR
REMARK 3 T11: 0.6731 T22: 0.7181
REMARK 3 T33: 0.4092 T12: 0.0125
REMARK 3 T13: -0.0986 T23: 0.2232
REMARK 3 L TENSOR
REMARK 3 L11: 4.3004 L22: 3.6707
REMARK 3 L33: 4.2125 L12: -1.2534
REMARK 3 L13: -0.3485 L23: 0.0078
REMARK 3 S TENSOR
REMARK 3 S11: 0.6545 S12: -0.9116 S13: -0.9842
REMARK 3 S21: 0.2122 S22: -0.0051 S23: 0.0181
REMARK 3 S31: 0.8118 S32: 0.1502 S33: -0.6907
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 226 THROUGH 242 )
REMARK 3 ORIGIN FOR THE GROUP (A): -32.4472 20.7562 297.7737
REMARK 3 T TENSOR
REMARK 3 T11: 0.7246 T22: 0.8979
REMARK 3 T33: 0.3534 T12: 0.0963
REMARK 3 T13: -0.0999 T23: 0.2223
REMARK 3 L TENSOR
REMARK 3 L11: 5.0756 L22: 4.8022
REMARK 3 L33: 2.9806 L12: -1.2959
REMARK 3 L13: -0.5606 L23: -1.7952
REMARK 3 S TENSOR
REMARK 3 S11: 0.4204 S12: -1.1175 S13: -0.6954
REMARK 3 S21: 1.2603 S22: 0.3397 S23: 0.2564
REMARK 3 S31: 0.3057 S32: -0.1601 S33: -0.7323
REMARK 3 TLS GROUP : 33
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 0 THROUGH 19 )
REMARK 3 ORIGIN FOR THE GROUP (A): 31.6475 31.5378 240.6464
REMARK 3 T TENSOR
REMARK 3 T11: 0.1956 T22: 0.3888
REMARK 3 T33: 0.2893 T12: 0.0400
REMARK 3 T13: -0.0751 T23: 0.1026
REMARK 3 L TENSOR
REMARK 3 L11: 7.7854 L22: 7.2430
REMARK 3 L33: 4.2052 L12: 3.1387
REMARK 3 L13: 1.4279 L23: 2.1083
REMARK 3 S TENSOR
REMARK 3 S11: -0.0861 S12: -0.2152 S13: 0.0083
REMARK 3 S21: -0.2860 S22: -0.3976 S23: -0.5533
REMARK 3 S31: -0.4039 S32: 0.5302 S33: 0.4555
REMARK 3 TLS GROUP : 34
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 20 THROUGH 41 )
REMARK 3 ORIGIN FOR THE GROUP (A): 31.2070 30.5608 247.4374
REMARK 3 T TENSOR
REMARK 3 T11: 0.4201 T22: 0.5903
REMARK 3 T33: 0.3657 T12: -0.0170
REMARK 3 T13: -0.1520 T23: 0.1211
REMARK 3 L TENSOR
REMARK 3 L11: 6.3359 L22: 5.8300
REMARK 3 L33: 0.8702 L12: 5.4471
REMARK 3 L13: 0.3794 L23: 1.0144
REMARK 3 S TENSOR
REMARK 3 S11: 0.3861 S12: -0.8425 S13: -0.5661
REMARK 3 S21: 0.9642 S22: -0.5301 S23: -0.4754
REMARK 3 S31: -0.6078 S32: 0.3780 S33: 0.1844
REMARK 3 TLS GROUP : 35
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 42 THROUGH 51 )
REMARK 3 ORIGIN FOR THE GROUP (A): 37.9228 36.3122 253.5169
REMARK 3 T TENSOR
REMARK 3 T11: 0.8394 T22: 1.2986
REMARK 3 T33: 0.6052 T12: -0.0466
REMARK 3 T13: -0.3303 T23: 0.0666
REMARK 3 L TENSOR
REMARK 3 L11: 6.9141 L22: 7.9700
REMARK 3 L33: 0.3619 L12: 1.5548
REMARK 3 L13: 1.1897 L23: -0.8229
REMARK 3 S TENSOR
REMARK 3 S11: -0.2021 S12: -2.1909 S13: 0.1312
REMARK 3 S21: 2.1828 S22: 0.4156 S23: -0.2792
REMARK 3 S31: 0.7075 S32: 0.7916 S33: -0.1932
REMARK 3 TLS GROUP : 36
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 52 THROUGH 61 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.9325 26.3090 247.0236
REMARK 3 T TENSOR
REMARK 3 T11: 0.3006 T22: 0.4520
REMARK 3 T33: 0.2756 T12: -0.0695
REMARK 3 T13: 0.0595 T23: 0.1143
REMARK 3 L TENSOR
REMARK 3 L11: 8.8030 L22: 4.2424
REMARK 3 L33: 4.8279 L12: 5.9580
REMARK 3 L13: 5.2705 L23: 3.5069
REMARK 3 S TENSOR
REMARK 3 S11: 0.3450 S12: -0.6040 S13: 0.1520
REMARK 3 S21: 0.5536 S22: -0.6032 S23: -0.1108
REMARK 3 S31: 0.1882 S32: -0.4896 S33: 0.3402
REMARK 3 TLS GROUP : 37
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 62 THROUGH 77 )
REMARK 3 ORIGIN FOR THE GROUP (A): 35.8906 37.4211 245.1704
REMARK 3 T TENSOR
REMARK 3 T11: 0.5049 T22: 0.7184
REMARK 3 T33: 0.3848 T12: -0.1946
REMARK 3 T13: -0.2199 T23: 0.0314
REMARK 3 L TENSOR
REMARK 3 L11: 9.3641 L22: 7.7837
REMARK 3 L33: 2.9611 L12: 4.0634
REMARK 3 L13: 0.0025 L23: -0.7418
REMARK 3 S TENSOR
REMARK 3 S11: 0.1031 S12: -0.4508 S13: 0.5581
REMARK 3 S21: 0.3783 S22: -0.0764 S23: -0.3284
REMARK 3 S31: -0.8697 S32: 0.9370 S33: 0.0979
REMARK 3 TLS GROUP : 38
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 78 THROUGH 90 )
REMARK 3 ORIGIN FOR THE GROUP (A): 36.0679 23.2436 248.5824
REMARK 3 T TENSOR
REMARK 3 T11: 0.3601 T22: 0.6464
REMARK 3 T33: 0.7856 T12: 0.0756
REMARK 3 T13: -0.2883 T23: 0.3340
REMARK 3 L TENSOR
REMARK 3 L11: 1.9524 L22: 8.1574
REMARK 3 L33: 0.8933 L12: 1.7588
REMARK 3 L13: -1.1390 L23: -1.5815
REMARK 3 S TENSOR
REMARK 3 S11: -0.2192 S12: -0.1683 S13: 0.0195
REMARK 3 S21: 0.9440 S22: -0.0885 S23: -0.3083
REMARK 3 S31: -0.2704 S32: 0.4761 S33: -0.0240
REMARK 3 TLS GROUP : 39
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 91 THROUGH 99 )
REMARK 3 ORIGIN FOR THE GROUP (A): 40.2961 32.1671 238.1910
REMARK 3 T TENSOR
REMARK 3 T11: 0.1967 T22: 0.7184
REMARK 3 T33: 0.8903 T12: 0.1590
REMARK 3 T13: 0.1391 T23: 0.2103
REMARK 3 L TENSOR
REMARK 3 L11: 9.3118 L22: 3.7476
REMARK 3 L33: 2.0079 L12: -0.8411
REMARK 3 L13: -0.8279 L23: 0.1703
REMARK 3 S TENSOR
REMARK 3 S11: 0.3921 S12: 0.6106 S13: 0.8205
REMARK 3 S21: -0.4513 S22: -0.7078 S23: -0.3375
REMARK 3 S31: -0.1300 S32: 0.3187 S33: 0.1230
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5U1R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-DEC-16.
REMARK 100 THE DEPOSITION ID IS D_1000225137.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-MAR-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.953
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 0.3.11
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55497
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 48.995
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.78
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.74300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> 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: PHASER
REMARK 200 STARTING MODEL: 4L4T
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: BTP, PEG 3350, NAAC, PH 6.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 106.28550
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.82500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 106.28550
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 34.82500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, E, F
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, G, H
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 GLU C 190
REMARK 465 THR C 191
REMARK 465 PHE C 192
REMARK 465 PRO C 193
REMARK 465 GLY C 194
REMARK 465 VAL C 195
REMARK 465 THR C 196
REMARK 465 PRO C 270
REMARK 465 PRO D 200
REMARK 465 GLU D 201
REMARK 465 SER D 202
REMARK 465 SER D 203
REMARK 465 ASN E 1
REMARK 465 ASP E 245
REMARK 465 MET F 0
REMARK 465 ASP F 98
REMARK 465 MET F 99
REMARK 465 HIS A 17
REMARK 465 GLY A 18
REMARK 465 ASP A 247
REMARK 465 PRO A 248
REMARK 465 GLN A 249
REMARK 465 SER A 250
REMARK 465 SER A 251
REMARK 465 ASN A 252
REMARK 465 PRO A 270
REMARK 465 GLU B 201
REMARK 465 SER B 202
REMARK 465 SER B 203
REMARK 465 ASN G 1
REMARK 465 ARG G 243
REMARK 465 ALA G 244
REMARK 465 ASP G 245
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 HIS C 17 CG ND1 CD2 CE1 NE2
REMARK 470 GLU C 102 CG CD OE1 OE2
REMARK 470 LYS C 189 CG CD CE NZ
REMARK 470 LYS C 216 CG CD CE NZ
REMARK 470 GLU C 219 CG CD OE1 OE2
REMARK 470 GLU C 220 CG CD OE1 OE2
REMARK 470 VAL C 222 CG1 CG2
REMARK 470 LEU C 246 CG CD1 CD2
REMARK 470 LEU C 253 CG CD1 CD2
REMARK 470 LYS D 147 CG CD CE NZ
REMARK 470 ASP D 194 CG OD1 OD2
REMARK 470 LYS E 14 CG CD CE NZ
REMARK 470 GLU E 133 CG CD OE1 OE2
REMARK 470 LYS E 165 CG CD CE NZ
REMARK 470 ARG E 243 CG CD NE CZ NH1 NH2
REMARK 470 LYS F 19 CG CD CE NZ
REMARK 470 LYS F 41 CG CD CE NZ
REMARK 470 GLU F 44 CG CD OE1 OE2
REMARK 470 ARG F 45 CG CD NE CZ NH1 NH2
REMARK 470 LYS F 48 CG CD CE NZ
REMARK 470 GLU F 74 CG CD OE1 OE2
REMARK 470 LYS F 75 CG CD CE NZ
REMARK 470 GLU F 77 CG CD OE1 OE2
REMARK 470 GLN F 89 CG CD OE1 NE2
REMARK 470 LYS F 94 CG CD CE NZ
REMARK 470 LYS A 216 CG CD CE NZ
REMARK 470 GLU A 219 CG CD OE1 OE2
REMARK 470 LEU A 253 CG CD1 CD2
REMARK 470 ILE B 4 CD1
REMARK 470 LYS B 57 CG CD CE NZ
REMARK 470 GLN B 120 CG CD OE1 NE2
REMARK 470 ARG B 122 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 125 CG CD CE NZ
REMARK 470 ASP B 128 CG OD1 OD2
REMARK 470 GLN B 145 CG CD OE1 NE2
REMARK 470 LYS B 147 CG CD CE NZ
REMARK 470 ASP B 148 CG OD1 OD2
REMARK 470 ASN B 188 CG OD1 ND2
REMARK 470 LYS G 9 CG CD CE NZ
REMARK 470 LYS G 119 CG CD CE NZ
REMARK 470 GLU G 133 CG CD OE1 OE2
REMARK 470 LYS G 165 CG CD CE NZ
REMARK 470 GLU G 223 CG CD OE1 OE2
REMARK 470 LYS H 19 CG CD CE NZ
REMARK 470 LYS H 58 CG CD CE NZ
REMARK 470 LYS H 75 CG CD CE NZ
REMARK 470 GLN H 89 CG CD OE1 NE2
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 OG SER C 89 O HOH C 401 2.11
REMARK 500 NH2 ARG A 1 O ARG A 178 2.17
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 LYS C 78 CD - CE - NZ ANGL. DEV. = 17.8 DEGREES
REMARK 500 GLN E 176 CA - CB - CG ANGL. DEV. = 16.4 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 HIS C 17 -119.37 51.61
REMARK 500 ASP C 29 -115.47 55.91
REMARK 500 PHE C 119 -49.85 -131.91
REMARK 500 ASN C 146 79.09 -106.82
REMARK 500 GLU C 159 -57.15 -122.28
REMARK 500 GLU C 224 66.13 -158.00
REMARK 500 HIS C 260 117.35 -160.02
REMARK 500 ASP D 115 65.58 -156.89
REMARK 500 ASP D 179 56.57 -95.20
REMARK 500 ASP A 29 -121.54 57.13
REMARK 500 PHE A 119 -56.50 -129.48
REMARK 500 GLU A 219 -76.48 -114.12
REMARK 500 GLN B 2 -39.56 -130.19
REMARK 500 SER B 83 106.74 -59.37
REMARK 500 ASP B 92 -166.20 -79.83
REMARK 500 GLN B 112 -75.97 -3.12
REMARK 500 ASP B 115 64.01 -157.65
REMARK 500 SER B 126 30.79 -162.88
REMARK 500 SER B 127 -178.87 -64.68
REMARK 500 SER B 149 157.47 170.18
REMARK 500 ASP B 165 77.10 46.61
REMARK 500 ASP B 179 77.89 -100.57
REMARK 500 GLU G 79 -72.24 -58.16
REMARK 500 SER G 87 -179.39 -172.73
REMARK 500 HIS G 168 -31.19 -135.40
REMARK 500 PRO H 32 -169.38 -74.43
REMARK 500 TRP H 60 -4.76 75.08
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 NA E 301 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR E 47 OH
REMARK 620 2 PRO E 61 O 100.7
REMARK 620 3 TYR E 64 O 91.9 87.0
REMARK 620 4 HOH E 409 O 164.4 90.8 78.1
REMARK 620 5 HOH E 427 O 76.7 163.6 77.0 89.3
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 NA C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DIF C 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA E 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DIF A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5U16 RELATED DB: PDB
REMARK 900 RELATED ID: 5U17 RELATED DB: PDB
REMARK 900 RELATED ID: 5U6Q RELATED DB: PDB
REMARK 900 RELATED ID: 5U2V RELATED DB: PDB
DBREF 5U1R C 1 270 UNP Q95460 HMR1_HUMAN 23 292
DBREF 5U1R D 1 203 PDB 5U1R 5U1R 1 203
DBREF 5U1R E 1 245 PDB 5U1R 5U1R 1 245
DBREF 5U1R F 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 5U1R A 1 270 UNP Q95460 HMR1_HUMAN 23 292
DBREF 5U1R B 1 203 PDB 5U1R 5U1R 1 203
DBREF 5U1R G 1 245 PDB 5U1R 5U1R 1 245
DBREF 5U1R H 1 99 UNP P61769 B2MG_HUMAN 21 119
SEQADV 5U1R MET C 0 UNP Q95460 INITIATING METHIONINE
SEQADV 5U1R SER C 261 UNP Q95460 CYS 283 CONFLICT
SEQADV 5U1R MET F 0 UNP P61769 INITIATING METHIONINE
SEQADV 5U1R MET A 0 UNP Q95460 INITIATING METHIONINE
SEQADV 5U1R SER A 261 UNP Q95460 CYS 283 CONFLICT
SEQADV 5U1R MET H 0 UNP P61769 INITIATING METHIONINE
SEQRES 1 C 271 MET ARG THR HIS SER LEU ARG TYR PHE ARG LEU GLY VAL
SEQRES 2 C 271 SER ASP PRO ILE HIS GLY VAL PRO GLU PHE ILE SER VAL
SEQRES 3 C 271 GLY TYR VAL ASP SER HIS PRO ILE THR THR TYR ASP SER
SEQRES 4 C 271 VAL THR ARG GLN LYS GLU PRO ARG ALA PRO TRP MET ALA
SEQRES 5 C 271 GLU ASN LEU ALA PRO ASP HIS TRP GLU ARG TYR THR GLN
SEQRES 6 C 271 LEU LEU ARG GLY TRP GLN GLN MET PHE LYS VAL GLU LEU
SEQRES 7 C 271 LYS ARG LEU GLN ARG HIS TYR ASN HIS SER GLY SER HIS
SEQRES 8 C 271 THR TYR GLN ARG MET ILE GLY CYS GLU LEU LEU GLU ASP
SEQRES 9 C 271 GLY SER THR THR GLY PHE LEU GLN TYR ALA TYR ASP GLY
SEQRES 10 C 271 GLN ASP PHE LEU ILE PHE ASN LYS ASP THR LEU SER TRP
SEQRES 11 C 271 LEU ALA VAL ASP ASN VAL ALA HIS THR ILE LYS GLN ALA
SEQRES 12 C 271 TRP GLU ALA ASN GLN HIS GLU LEU LEU TYR GLN LYS ASN
SEQRES 13 C 271 TRP LEU GLU GLU GLU CYS ILE ALA TRP LEU LYS ARG PHE
SEQRES 14 C 271 LEU GLU TYR GLY LYS ASP THR LEU GLN ARG THR GLU PRO
SEQRES 15 C 271 PRO LEU VAL ARG VAL ASN ARG LYS GLU THR PHE PRO GLY
SEQRES 16 C 271 VAL THR ALA LEU PHE CYS LYS ALA HIS GLY PHE TYR PRO
SEQRES 17 C 271 PRO GLU ILE TYR MET THR TRP MET LYS ASN GLY GLU GLU
SEQRES 18 C 271 ILE VAL GLN GLU ILE ASP TYR GLY ASP ILE LEU PRO SER
SEQRES 19 C 271 GLY ASP GLY THR TYR GLN ALA TRP ALA SER ILE GLU LEU
SEQRES 20 C 271 ASP PRO GLN SER SER ASN LEU TYR SER CYS HIS VAL GLU
SEQRES 21 C 271 HIS SER GLY VAL HIS MET VAL LEU GLN VAL PRO
SEQRES 1 D 203 GLY GLN ASN ILE ASP GLN PRO THR GLU MET THR ALA THR
SEQRES 2 D 203 GLU GLY ALA ILE VAL GLN ILE ASN CYS THR TYR GLN THR
SEQRES 3 D 203 SER GLY PHE ASN GLY LEU PHE TRP TYR GLN GLN HIS ALA
SEQRES 4 D 203 GLY GLU ALA PRO THR PHE LEU SER TYR ASN VAL LEU ASP
SEQRES 5 D 203 GLY LEU GLU GLU LYS GLY ARG PHE SER SER PHE LEU SER
SEQRES 6 D 203 ARG SER LYS GLY TYR SER TYR LEU LEU LEU LYS GLU LEU
SEQRES 7 D 203 GLN MET LYS ASP SER ALA SER TYR LEU CYS ALA VAL LYS
SEQRES 8 D 203 ASP SER ASN TYR GLN LEU ILE TRP GLY ALA GLY THR LYS
SEQRES 9 D 203 LEU ILE ILE LYS PRO ASP ILE GLN ASN PRO ASP PRO ALA
SEQRES 10 D 203 VAL TYR GLN LEU ARG ASP SER LYS SER SER ASP LYS SER
SEQRES 11 D 203 VAL CYS LEU PHE THR ASP PHE ASP SER GLN THR ASN VAL
SEQRES 12 D 203 SER GLN SER LYS ASP SER ASP VAL TYR ILE THR ASP LYS
SEQRES 13 D 203 CYS VAL LEU ASP MET ARG SER MET ASP PHE LYS SER ASN
SEQRES 14 D 203 SER ALA VAL ALA TRP SER ASN LYS SER ASP PHE ALA CYS
SEQRES 15 D 203 ALA ASN ALA PHE ASN ASN SER ILE ILE PRO GLU ASP THR
SEQRES 16 D 203 PHE PHE PRO SER PRO GLU SER SER
SEQRES 1 E 245 ASN ALA GLY VAL THR GLN THR PRO LYS PHE GLN VAL LEU
SEQRES 2 E 245 LYS THR GLY GLN SER MET THR LEU GLN CYS ALA GLN ASP
SEQRES 3 E 245 MET ASN HIS ASN SER MET TYR TRP TYR ARG GLN ASP PRO
SEQRES 4 E 245 GLY MET GLY LEU ARG LEU ILE TYR TYR SER ALA SER GLU
SEQRES 5 E 245 GLY THR THR ASP LYS GLY GLU VAL PRO ASN GLY TYR ASN
SEQRES 6 E 245 VAL SER ARG LEU ASN LYS ARG GLU PHE SER LEU ARG LEU
SEQRES 7 E 245 GLU SER ALA ALA PRO SER GLN THR SER VAL TYR PHE CYS
SEQRES 8 E 245 ALA SER SER VAL TRP THR GLY GLU GLY SER GLY GLU LEU
SEQRES 9 E 245 PHE PHE GLY GLU GLY SER ARG LEU THR VAL LEU GLU ASP
SEQRES 10 E 245 LEU LYS ASN VAL PHE PRO PRO GLU VAL ALA VAL PHE GLU
SEQRES 11 E 245 PRO SER GLU ALA GLU ILE SER HIS THR GLN LYS ALA THR
SEQRES 12 E 245 LEU VAL CYS LEU ALA THR GLY PHE TYR PRO ASP HIS VAL
SEQRES 13 E 245 GLU LEU SER TRP TRP VAL ASN GLY LYS GLU VAL HIS SER
SEQRES 14 E 245 GLY VAL CYS THR ASP PRO GLN PRO LEU LYS GLU GLN PRO
SEQRES 15 E 245 ALA LEU ASN ASP SER ARG TYR ALA LEU SER SER ARG LEU
SEQRES 16 E 245 ARG VAL SER ALA THR PHE TRP GLN ASN PRO ARG ASN HIS
SEQRES 17 E 245 PHE ARG CYS GLN VAL GLN PHE TYR GLY LEU SER GLU ASN
SEQRES 18 E 245 ASP GLU TRP THR GLN ASP ARG ALA LYS PRO VAL THR GLN
SEQRES 19 E 245 ILE VAL SER ALA GLU ALA TRP GLY ARG ALA ASP
SEQRES 1 F 100 MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG
SEQRES 2 F 100 HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS
SEQRES 3 F 100 TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP
SEQRES 4 F 100 LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS
SEQRES 5 F 100 SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU
SEQRES 6 F 100 LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU
SEQRES 7 F 100 TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO
SEQRES 8 F 100 LYS ILE VAL LYS TRP ASP ARG ASP MET
SEQRES 1 A 271 MET ARG THR HIS SER LEU ARG TYR PHE ARG LEU GLY VAL
SEQRES 2 A 271 SER ASP PRO ILE HIS GLY VAL PRO GLU PHE ILE SER VAL
SEQRES 3 A 271 GLY TYR VAL ASP SER HIS PRO ILE THR THR TYR ASP SER
SEQRES 4 A 271 VAL THR ARG GLN LYS GLU PRO ARG ALA PRO TRP MET ALA
SEQRES 5 A 271 GLU ASN LEU ALA PRO ASP HIS TRP GLU ARG TYR THR GLN
SEQRES 6 A 271 LEU LEU ARG GLY TRP GLN GLN MET PHE LYS VAL GLU LEU
SEQRES 7 A 271 LYS ARG LEU GLN ARG HIS TYR ASN HIS SER GLY SER HIS
SEQRES 8 A 271 THR TYR GLN ARG MET ILE GLY CYS GLU LEU LEU GLU ASP
SEQRES 9 A 271 GLY SER THR THR GLY PHE LEU GLN TYR ALA TYR ASP GLY
SEQRES 10 A 271 GLN ASP PHE LEU ILE PHE ASN LYS ASP THR LEU SER TRP
SEQRES 11 A 271 LEU ALA VAL ASP ASN VAL ALA HIS THR ILE LYS GLN ALA
SEQRES 12 A 271 TRP GLU ALA ASN GLN HIS GLU LEU LEU TYR GLN LYS ASN
SEQRES 13 A 271 TRP LEU GLU GLU GLU CYS ILE ALA TRP LEU LYS ARG PHE
SEQRES 14 A 271 LEU GLU TYR GLY LYS ASP THR LEU GLN ARG THR GLU PRO
SEQRES 15 A 271 PRO LEU VAL ARG VAL ASN ARG LYS GLU THR PHE PRO GLY
SEQRES 16 A 271 VAL THR ALA LEU PHE CYS LYS ALA HIS GLY PHE TYR PRO
SEQRES 17 A 271 PRO GLU ILE TYR MET THR TRP MET LYS ASN GLY GLU GLU
SEQRES 18 A 271 ILE VAL GLN GLU ILE ASP TYR GLY ASP ILE LEU PRO SER
SEQRES 19 A 271 GLY ASP GLY THR TYR GLN ALA TRP ALA SER ILE GLU LEU
SEQRES 20 A 271 ASP PRO GLN SER SER ASN LEU TYR SER CYS HIS VAL GLU
SEQRES 21 A 271 HIS SER GLY VAL HIS MET VAL LEU GLN VAL PRO
SEQRES 1 B 203 GLY GLN ASN ILE ASP GLN PRO THR GLU MET THR ALA THR
SEQRES 2 B 203 GLU GLY ALA ILE VAL GLN ILE ASN CYS THR TYR GLN THR
SEQRES 3 B 203 SER GLY PHE ASN GLY LEU PHE TRP TYR GLN GLN HIS ALA
SEQRES 4 B 203 GLY GLU ALA PRO THR PHE LEU SER TYR ASN VAL LEU ASP
SEQRES 5 B 203 GLY LEU GLU GLU LYS GLY ARG PHE SER SER PHE LEU SER
SEQRES 6 B 203 ARG SER LYS GLY TYR SER TYR LEU LEU LEU LYS GLU LEU
SEQRES 7 B 203 GLN MET LYS ASP SER ALA SER TYR LEU CYS ALA VAL LYS
SEQRES 8 B 203 ASP SER ASN TYR GLN LEU ILE TRP GLY ALA GLY THR LYS
SEQRES 9 B 203 LEU ILE ILE LYS PRO ASP ILE GLN ASN PRO ASP PRO ALA
SEQRES 10 B 203 VAL TYR GLN LEU ARG ASP SER LYS SER SER ASP LYS SER
SEQRES 11 B 203 VAL CYS LEU PHE THR ASP PHE ASP SER GLN THR ASN VAL
SEQRES 12 B 203 SER GLN SER LYS ASP SER ASP VAL TYR ILE THR ASP LYS
SEQRES 13 B 203 CYS VAL LEU ASP MET ARG SER MET ASP PHE LYS SER ASN
SEQRES 14 B 203 SER ALA VAL ALA TRP SER ASN LYS SER ASP PHE ALA CYS
SEQRES 15 B 203 ALA ASN ALA PHE ASN ASN SER ILE ILE PRO GLU ASP THR
SEQRES 16 B 203 PHE PHE PRO SER PRO GLU SER SER
SEQRES 1 G 245 ASN ALA GLY VAL THR GLN THR PRO LYS PHE GLN VAL LEU
SEQRES 2 G 245 LYS THR GLY GLN SER MET THR LEU GLN CYS ALA GLN ASP
SEQRES 3 G 245 MET ASN HIS ASN SER MET TYR TRP TYR ARG GLN ASP PRO
SEQRES 4 G 245 GLY MET GLY LEU ARG LEU ILE TYR TYR SER ALA SER GLU
SEQRES 5 G 245 GLY THR THR ASP LYS GLY GLU VAL PRO ASN GLY TYR ASN
SEQRES 6 G 245 VAL SER ARG LEU ASN LYS ARG GLU PHE SER LEU ARG LEU
SEQRES 7 G 245 GLU SER ALA ALA PRO SER GLN THR SER VAL TYR PHE CYS
SEQRES 8 G 245 ALA SER SER VAL TRP THR GLY GLU GLY SER GLY GLU LEU
SEQRES 9 G 245 PHE PHE GLY GLU GLY SER ARG LEU THR VAL LEU GLU ASP
SEQRES 10 G 245 LEU LYS ASN VAL PHE PRO PRO GLU VAL ALA VAL PHE GLU
SEQRES 11 G 245 PRO SER GLU ALA GLU ILE SER HIS THR GLN LYS ALA THR
SEQRES 12 G 245 LEU VAL CYS LEU ALA THR GLY PHE TYR PRO ASP HIS VAL
SEQRES 13 G 245 GLU LEU SER TRP TRP VAL ASN GLY LYS GLU VAL HIS SER
SEQRES 14 G 245 GLY VAL CYS THR ASP PRO GLN PRO LEU LYS GLU GLN PRO
SEQRES 15 G 245 ALA LEU ASN ASP SER ARG TYR ALA LEU SER SER ARG LEU
SEQRES 16 G 245 ARG VAL SER ALA THR PHE TRP GLN ASN PRO ARG ASN HIS
SEQRES 17 G 245 PHE ARG CYS GLN VAL GLN PHE TYR GLY LEU SER GLU ASN
SEQRES 18 G 245 ASP GLU TRP THR GLN ASP ARG ALA LYS PRO VAL THR GLN
SEQRES 19 G 245 ILE VAL SER ALA GLU ALA TRP GLY ARG ALA ASP
SEQRES 1 H 100 MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG
SEQRES 2 H 100 HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS
SEQRES 3 H 100 TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP
SEQRES 4 H 100 LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS
SEQRES 5 H 100 SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU
SEQRES 6 H 100 LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU
SEQRES 7 H 100 TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO
SEQRES 8 H 100 LYS ILE VAL LYS TRP ASP ARG ASP MET
HET NA C 301 1
HET ACT C 302 4
HET GOL C 303 6
HET GOL C 304 6
HET DIF C 305 19
HET NA E 301 1
HET ACT A 301 4
HET GOL A 302 6
HET DIF A 303 19
HET ACT B 301 4
HETNAM NA SODIUM ION
HETNAM ACT ACETATE ION
HETNAM GOL GLYCEROL
HETNAM DIF 2-[2,6-DICHLOROPHENYL)AMINO]BENZENEACETIC ACID
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN DIF DICLOFENAC
FORMUL 9 NA 2(NA 1+)
FORMUL 10 ACT 3(C2 H3 O2 1-)
FORMUL 11 GOL 3(C3 H8 O3)
FORMUL 13 DIF 2(C14 H11 CL2 N O2)
FORMUL 19 HOH *172(H2 O)
HELIX 1 AA1 ALA C 47 GLU C 52 1 6
HELIX 2 AA2 ALA C 55 TYR C 84 1 30
HELIX 3 AA3 ASP C 133 GLU C 144 1 12
HELIX 4 AA4 ASN C 146 GLU C 159 1 14
HELIX 5 AA5 GLU C 159 GLY C 172 1 14
HELIX 6 AA6 GLY C 172 GLN C 177 1 6
HELIX 7 AA7 GLN D 79 SER D 83 5 5
HELIX 8 AA8 ALA D 181 ALA D 185 5 5
HELIX 9 AA9 ALA E 82 THR E 86 5 5
HELIX 10 AB1 ASP E 117 VAL E 121 5 5
HELIX 11 AB2 SER E 132 GLN E 140 1 9
HELIX 12 AB3 ALA E 199 GLN E 203 1 5
HELIX 13 AB4 ALA A 47 GLU A 52 1 6
HELIX 14 AB5 ALA A 55 ASN A 85 1 31
HELIX 15 AB6 ASP A 133 GLU A 144 1 12
HELIX 16 AB7 ASN A 146 GLU A 159 1 14
HELIX 17 AB8 GLU A 159 GLY A 172 1 14
HELIX 18 AB9 GLY A 172 GLN A 177 1 6
HELIX 19 AC1 GLN B 79 SER B 83 5 5
HELIX 20 AC2 ALA B 181 ALA B 185 5 5
HELIX 21 AC3 ALA G 82 THR G 86 5 5
HELIX 22 AC4 ASP G 117 VAL G 121 5 5
HELIX 23 AC5 SER G 132 GLN G 140 1 9
HELIX 24 AC6 ALA G 199 GLN G 203 1 5
SHEET 1 AA1 8 GLU C 44 PRO C 45 0
SHEET 2 AA1 8 HIS C 31 ASP C 37 -1 N THR C 35 O GLU C 44
SHEET 3 AA1 8 PHE C 22 VAL C 28 -1 N SER C 24 O TYR C 36
SHEET 4 AA1 8 HIS C 3 VAL C 12 -1 N LEU C 10 O ILE C 23
SHEET 5 AA1 8 THR C 91 LEU C 100 -1 O LEU C 100 N HIS C 3
SHEET 6 AA1 8 THR C 106 TYR C 114 -1 O ALA C 113 N GLN C 93
SHEET 7 AA1 8 GLN C 117 ASN C 123 -1 O LEU C 120 N TYR C 112
SHEET 8 AA1 8 SER C 128 ALA C 131 -1 O LEU C 130 N ILE C 121
SHEET 1 AA2 4 LEU C 183 ASN C 187 0
SHEET 2 AA2 4 LEU C 198 PHE C 205 -1 O LYS C 201 N ARG C 185
SHEET 3 AA2 4 TYR C 238 ILE C 244 -1 O ALA C 242 N CYS C 200
SHEET 4 AA2 4 ASP C 226 TYR C 227 -1 N ASP C 226 O SER C 243
SHEET 1 AA3 4 LEU C 183 ASN C 187 0
SHEET 2 AA3 4 LEU C 198 PHE C 205 -1 O LYS C 201 N ARG C 185
SHEET 3 AA3 4 TYR C 238 ILE C 244 -1 O ALA C 242 N CYS C 200
SHEET 4 AA3 4 LEU C 231 PRO C 232 -1 N LEU C 231 O GLN C 239
SHEET 1 AA4 4 GLU C 219 GLU C 220 0
SHEET 2 AA4 4 TYR C 211 LYS C 216 -1 N LYS C 216 O GLU C 219
SHEET 3 AA4 4 TYR C 254 HIS C 260 -1 O HIS C 257 N THR C 213
SHEET 4 AA4 4 VAL C 263 GLN C 268 -1 O MET C 265 N VAL C 258
SHEET 1 AA5 5 ASN D 3 ASP D 5 0
SHEET 2 AA5 5 VAL D 18 GLN D 25 -1 O GLN D 25 N ASN D 3
SHEET 3 AA5 5 TYR D 70 LEU D 75 -1 O SER D 71 N CYS D 22
SHEET 4 AA5 5 PHE D 60 SER D 65 -1 N SER D 61 O LEU D 74
SHEET 5 AA5 5 GLY D 53 LYS D 57 -1 N LYS D 57 O PHE D 60
SHEET 1 AA6 5 GLU D 9 THR D 13 0
SHEET 2 AA6 5 THR D 103 LYS D 108 1 O ILE D 106 N MET D 10
SHEET 3 AA6 5 SER D 85 LYS D 91 -1 N TYR D 86 O THR D 103
SHEET 4 AA6 5 LEU D 32 GLN D 37 -1 N GLN D 37 O SER D 85
SHEET 5 AA6 5 THR D 44 ASN D 49 -1 O ASN D 49 N LEU D 32
SHEET 1 AA7 4 GLU D 9 THR D 13 0
SHEET 2 AA7 4 THR D 103 LYS D 108 1 O ILE D 106 N MET D 10
SHEET 3 AA7 4 SER D 85 LYS D 91 -1 N TYR D 86 O THR D 103
SHEET 4 AA7 4 LEU D 97 TRP D 99 -1 O ILE D 98 N VAL D 90
SHEET 1 AA8 4 ALA D 117 GLN D 120 0
SHEET 2 AA8 4 SER D 130 THR D 135 -1 O LEU D 133 N TYR D 119
SHEET 3 AA8 4 PHE D 166 SER D 175 -1 O ALA D 173 N CYS D 132
SHEET 4 AA8 4 TYR D 152 ILE D 153 -1 N TYR D 152 O TRP D 174
SHEET 1 AA9 4 ALA D 117 GLN D 120 0
SHEET 2 AA9 4 SER D 130 THR D 135 -1 O LEU D 133 N TYR D 119
SHEET 3 AA9 4 PHE D 166 SER D 175 -1 O ALA D 173 N CYS D 132
SHEET 4 AA9 4 CYS D 157 MET D 161 -1 N MET D 161 O PHE D 166
SHEET 1 AB1 4 VAL E 4 THR E 7 0
SHEET 2 AB1 4 MET E 19 GLN E 25 -1 O ALA E 24 N THR E 5
SHEET 3 AB1 4 PHE E 74 LEU E 78 -1 O LEU E 78 N MET E 19
SHEET 4 AB1 4 TYR E 64 ARG E 68 -1 N SER E 67 O SER E 75
SHEET 1 AB2 6 PHE E 10 LYS E 14 0
SHEET 2 AB2 6 SER E 110 LEU E 115 1 O THR E 113 N LEU E 13
SHEET 3 AB2 6 SER E 87 SER E 94 -1 N TYR E 89 O SER E 110
SHEET 4 AB2 6 SER E 31 GLN E 37 -1 N GLN E 37 O VAL E 88
SHEET 5 AB2 6 ARG E 44 SER E 51 -1 O ILE E 46 N TRP E 34
SHEET 6 AB2 6 THR E 54 LYS E 57 -1 O ASP E 56 N TYR E 48
SHEET 1 AB3 4 PHE E 10 LYS E 14 0
SHEET 2 AB3 4 SER E 110 LEU E 115 1 O THR E 113 N LEU E 13
SHEET 3 AB3 4 SER E 87 SER E 94 -1 N TYR E 89 O SER E 110
SHEET 4 AB3 4 PHE E 105 PHE E 106 -1 O PHE E 105 N SER E 93
SHEET 1 AB4 4 GLU E 125 PHE E 129 0
SHEET 2 AB4 4 LYS E 141 PHE E 151 -1 O VAL E 145 N PHE E 129
SHEET 3 AB4 4 TYR E 189 SER E 198 -1 O VAL E 197 N ALA E 142
SHEET 4 AB4 4 VAL E 171 THR E 173 -1 N CYS E 172 O ARG E 194
SHEET 1 AB5 4 GLU E 125 PHE E 129 0
SHEET 2 AB5 4 LYS E 141 PHE E 151 -1 O VAL E 145 N PHE E 129
SHEET 3 AB5 4 TYR E 189 SER E 198 -1 O VAL E 197 N ALA E 142
SHEET 4 AB5 4 LEU E 178 LYS E 179 -1 N LEU E 178 O ALA E 190
SHEET 1 AB6 4 LYS E 165 VAL E 167 0
SHEET 2 AB6 4 VAL E 156 VAL E 162 -1 N VAL E 162 O LYS E 165
SHEET 3 AB6 4 HIS E 208 PHE E 215 -1 O ARG E 210 N TRP E 161
SHEET 4 AB6 4 GLN E 234 TRP E 241 -1 O ALA E 240 N PHE E 209
SHEET 1 AB7 4 LYS F 6 SER F 11 0
SHEET 2 AB7 4 ASN F 21 PHE F 30 -1 O ASN F 24 N TYR F 10
SHEET 3 AB7 4 PHE F 62 PHE F 70 -1 O PHE F 70 N ASN F 21
SHEET 4 AB7 4 GLU F 50 HIS F 51 -1 N GLU F 50 O TYR F 67
SHEET 1 AB8 4 LYS F 6 SER F 11 0
SHEET 2 AB8 4 ASN F 21 PHE F 30 -1 O ASN F 24 N TYR F 10
SHEET 3 AB8 4 PHE F 62 PHE F 70 -1 O PHE F 70 N ASN F 21
SHEET 4 AB8 4 SER F 55 PHE F 56 -1 N SER F 55 O TYR F 63
SHEET 1 AB9 4 GLU F 44 ARG F 45 0
SHEET 2 AB9 4 GLU F 36 LYS F 41 -1 N LYS F 41 O GLU F 44
SHEET 3 AB9 4 TYR F 78 ASN F 83 -1 O ALA F 79 N LEU F 40
SHEET 4 AB9 4 LYS F 91 LYS F 94 -1 O LYS F 91 N VAL F 82
SHEET 1 AC1 8 GLU A 44 PRO A 45 0
SHEET 2 AC1 8 HIS A 31 ASP A 37 -1 N THR A 35 O GLU A 44
SHEET 3 AC1 8 PHE A 22 VAL A 28 -1 N SER A 24 O TYR A 36
SHEET 4 AC1 8 HIS A 3 VAL A 12 -1 N ARG A 6 O TYR A 27
SHEET 5 AC1 8 THR A 91 LEU A 100 -1 O LEU A 100 N HIS A 3
SHEET 6 AC1 8 THR A 106 TYR A 114 -1 O ALA A 113 N GLN A 93
SHEET 7 AC1 8 GLN A 117 ASN A 123 -1 O LEU A 120 N TYR A 112
SHEET 8 AC1 8 SER A 128 ALA A 131 -1 O LEU A 130 N ILE A 121
SHEET 1 AC2 4 LEU A 183 PHE A 192 0
SHEET 2 AC2 4 VAL A 195 PHE A 205 -1 O PHE A 199 N ASN A 187
SHEET 3 AC2 4 TYR A 238 GLU A 245 -1 O ALA A 240 N ALA A 202
SHEET 4 AC2 4 ASP A 226 TYR A 227 -1 N ASP A 226 O SER A 243
SHEET 1 AC3 4 LEU A 183 PHE A 192 0
SHEET 2 AC3 4 VAL A 195 PHE A 205 -1 O PHE A 199 N ASN A 187
SHEET 3 AC3 4 TYR A 238 GLU A 245 -1 O ALA A 240 N ALA A 202
SHEET 4 AC3 4 LEU A 231 PRO A 232 -1 N LEU A 231 O GLN A 239
SHEET 1 AC4 4 GLU A 220 ILE A 221 0
SHEET 2 AC4 4 TYR A 211 LYS A 216 -1 N LYS A 216 O GLU A 220
SHEET 3 AC4 4 TYR A 254 HIS A 260 -1 O HIS A 257 N THR A 213
SHEET 4 AC4 4 VAL A 263 GLN A 268 -1 O LEU A 267 N CYS A 256
SHEET 1 AC5 5 ASN B 3 ASP B 5 0
SHEET 2 AC5 5 VAL B 18 GLN B 25 -1 O THR B 23 N ASP B 5
SHEET 3 AC5 5 TYR B 70 LEU B 75 -1 O SER B 71 N CYS B 22
SHEET 4 AC5 5 PHE B 60 SER B 65 -1 N SER B 61 O LEU B 74
SHEET 5 AC5 5 GLY B 53 LYS B 57 -1 N LYS B 57 O PHE B 60
SHEET 1 AC6 5 GLU B 9 THR B 13 0
SHEET 2 AC6 5 THR B 103 LYS B 108 1 O ILE B 106 N MET B 10
SHEET 3 AC6 5 ALA B 84 LYS B 91 -1 N ALA B 84 O LEU B 105
SHEET 4 AC6 5 LEU B 32 GLN B 37 -1 N PHE B 33 O ALA B 89
SHEET 5 AC6 5 THR B 44 ASN B 49 -1 O LEU B 46 N TRP B 34
SHEET 1 AC7 4 GLU B 9 THR B 13 0
SHEET 2 AC7 4 THR B 103 LYS B 108 1 O ILE B 106 N MET B 10
SHEET 3 AC7 4 ALA B 84 LYS B 91 -1 N ALA B 84 O LEU B 105
SHEET 4 AC7 4 LEU B 97 TRP B 99 -1 O ILE B 98 N VAL B 90
SHEET 1 AC8 4 ALA B 117 ARG B 122 0
SHEET 2 AC8 4 SER B 130 THR B 135 -1 O VAL B 131 N LEU B 121
SHEET 3 AC8 4 PHE B 166 TRP B 174 -1 O ALA B 173 N CYS B 132
SHEET 4 AC8 4 TYR B 152 ILE B 153 -1 N TYR B 152 O TRP B 174
SHEET 1 AC9 4 ALA B 117 ARG B 122 0
SHEET 2 AC9 4 SER B 130 THR B 135 -1 O VAL B 131 N LEU B 121
SHEET 3 AC9 4 PHE B 166 TRP B 174 -1 O ALA B 173 N CYS B 132
SHEET 4 AC9 4 CYS B 157 MET B 161 -1 N MET B 161 O PHE B 166
SHEET 1 AD1 4 VAL G 4 THR G 7 0
SHEET 2 AD1 4 MET G 19 GLN G 25 -1 O ALA G 24 N THR G 5
SHEET 3 AD1 4 PHE G 74 LEU G 78 -1 O LEU G 76 N LEU G 21
SHEET 4 AD1 4 TYR G 64 ARG G 68 -1 N ASN G 65 O ARG G 77
SHEET 1 AD2 6 PHE G 10 LYS G 14 0
SHEET 2 AD2 6 SER G 110 LEU G 115 1 O LEU G 115 N LEU G 13
SHEET 3 AD2 6 SER G 87 SER G 94 -1 N TYR G 89 O SER G 110
SHEET 4 AD2 6 SER G 31 GLN G 37 -1 N TYR G 35 O PHE G 90
SHEET 5 AD2 6 ARG G 44 SER G 51 -1 O ILE G 46 N TRP G 34
SHEET 6 AD2 6 THR G 54 LYS G 57 -1 O ASP G 56 N TYR G 48
SHEET 1 AD3 4 PHE G 10 LYS G 14 0
SHEET 2 AD3 4 SER G 110 LEU G 115 1 O LEU G 115 N LEU G 13
SHEET 3 AD3 4 SER G 87 SER G 94 -1 N TYR G 89 O SER G 110
SHEET 4 AD3 4 PHE G 105 PHE G 106 -1 O PHE G 105 N SER G 93
SHEET 1 AD4 4 GLU G 125 PHE G 129 0
SHEET 2 AD4 4 LYS G 141 PHE G 151 -1 O THR G 149 N GLU G 125
SHEET 3 AD4 4 TYR G 189 SER G 198 -1 O LEU G 195 N LEU G 144
SHEET 4 AD4 4 VAL G 171 THR G 173 -1 N CYS G 172 O ARG G 194
SHEET 1 AD5 4 GLU G 125 PHE G 129 0
SHEET 2 AD5 4 LYS G 141 PHE G 151 -1 O THR G 149 N GLU G 125
SHEET 3 AD5 4 TYR G 189 SER G 198 -1 O LEU G 195 N LEU G 144
SHEET 4 AD5 4 LEU G 178 LYS G 179 -1 N LEU G 178 O ALA G 190
SHEET 1 AD6 4 LYS G 165 VAL G 167 0
SHEET 2 AD6 4 VAL G 156 VAL G 162 -1 N VAL G 162 O LYS G 165
SHEET 3 AD6 4 HIS G 208 PHE G 215 -1 O GLN G 214 N GLU G 157
SHEET 4 AD6 4 GLN G 234 TRP G 241 -1 O GLN G 234 N PHE G 215
SHEET 1 AD7 4 LYS H 6 SER H 11 0
SHEET 2 AD7 4 ASN H 21 PHE H 30 -1 O ASN H 24 N TYR H 10
SHEET 3 AD7 4 PHE H 62 PHE H 70 -1 O LEU H 64 N VAL H 27
SHEET 4 AD7 4 GLU H 50 HIS H 51 -1 N GLU H 50 O TYR H 67
SHEET 1 AD8 4 LYS H 6 SER H 11 0
SHEET 2 AD8 4 ASN H 21 PHE H 30 -1 O ASN H 24 N TYR H 10
SHEET 3 AD8 4 PHE H 62 PHE H 70 -1 O LEU H 64 N VAL H 27
SHEET 4 AD8 4 SER H 55 PHE H 56 -1 N SER H 55 O TYR H 63
SHEET 1 AD9 4 GLU H 44 ARG H 45 0
SHEET 2 AD9 4 ILE H 35 LYS H 41 -1 N LYS H 41 O GLU H 44
SHEET 3 AD9 4 TYR H 78 HIS H 84 -1 O ARG H 81 N ASP H 38
SHEET 4 AD9 4 LYS H 91 LYS H 94 -1 O LYS H 91 N VAL H 82
SSBOND 1 CYS C 98 CYS C 161 1555 1555 2.03
SSBOND 2 CYS C 200 CYS C 256 1555 1555 2.03
SSBOND 3 CYS D 22 CYS D 88 1555 1555 2.03
SSBOND 4 CYS D 132 CYS D 182 1555 1555 2.03
SSBOND 5 CYS D 157 CYS E 172 1555 1555 2.03
SSBOND 6 CYS E 23 CYS E 91 1555 1555 2.03
SSBOND 7 CYS E 146 CYS E 211 1555 1555 2.03
SSBOND 8 CYS F 25 CYS F 80 1555 1555 2.03
SSBOND 9 CYS A 98 CYS A 161 1555 1555 2.04
SSBOND 10 CYS A 200 CYS A 256 1555 1555 2.03
SSBOND 11 CYS B 22 CYS B 88 1555 1555 2.03
SSBOND 12 CYS B 132 CYS B 182 1555 1555 2.03
SSBOND 13 CYS B 157 CYS G 172 1555 1555 2.03
SSBOND 14 CYS G 23 CYS G 91 1555 1555 2.03
SSBOND 15 CYS G 146 CYS G 211 1555 1555 2.03
SSBOND 16 CYS H 25 CYS H 80 1555 1555 2.04
LINK O PRO C 181 NA NA C 301 1555 1555 3.18
LINK OH TYR E 47 NA NA E 301 1555 1555 2.42
LINK O PRO E 61 NA NA E 301 1555 1555 2.48
LINK O TYR E 64 NA NA E 301 1555 1555 2.62
LINK NA NA E 301 O HOH E 409 1555 1555 2.46
LINK NA NA E 301 O HOH E 427 1555 1555 2.70
CISPEP 1 TYR C 206 PRO C 207 0 3.04
CISPEP 2 VAL C 222 GLN C 223 0 2.18
CISPEP 3 GLY D 1 GLN D 2 0 -2.03
CISPEP 4 THR E 7 PRO E 8 0 -3.33
CISPEP 5 THR E 15 GLY E 16 0 -6.47
CISPEP 6 TYR E 152 PRO E 153 0 -1.47
CISPEP 7 HIS F 31 PRO F 32 0 2.15
CISPEP 8 TYR A 206 PRO A 207 0 1.63
CISPEP 9 LYS B 125 SER B 126 0 -11.65
CISPEP 10 SER B 149 ASP B 150 0 -9.33
CISPEP 11 THR G 7 PRO G 8 0 -3.81
CISPEP 12 TYR G 152 PRO G 153 0 1.19
CISPEP 13 HIS H 31 PRO H 32 0 1.27
SITE 1 AC1 2 PRO C 181 LEU C 183
SITE 1 AC2 4 GLU C 160 TRP C 164 ARG C 167 SER D 93
SITE 1 AC3 2 ASP C 133 ASN C 134
SITE 1 AC4 4 ALA C 131 ASP C 133 ASN C 134 HIS C 137
SITE 1 AC5 10 TYR C 7 ARG C 9 SER C 24 LYS C 43
SITE 2 AC5 10 TYR C 62 LEU C 66 TRP C 156 TRP C 164
SITE 3 AC5 10 TYR D 95 GLU E 99
SITE 1 AC6 5 TYR E 47 PRO E 61 TYR E 64 HOH E 409
SITE 2 AC6 5 HOH E 427
SITE 1 AC7 5 ARG A 6 PHE A 8 ASP A 29 PHE H 56
SITE 2 AC7 5 TYR H 63
SITE 1 AC8 8 ILE A 210 TYR A 211 MET A 212 TYR A 227
SITE 2 AC8 8 GLY A 228 TRP A 241 ASN E 204 ARG E 206
SITE 1 AC9 8 TYR A 7 ARG A 9 SER A 24 TYR A 62
SITE 2 AC9 8 LEU A 66 TRP A 156 TYR B 95 GLU G 99
SITE 1 AD1 5 ASP B 52 GLY B 53 GLU B 55 GLN E 226
SITE 2 AD1 5 ARG E 228
CRYST1 212.571 69.650 142.850 90.00 103.38 90.00 C 1 2 1 8
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 0.004704 0.000000 0.001119 0.00000
SCALE2 0.000000 0.014358 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007196 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
