HEADER IMMUNE SYSTEM 10-DEC-16 5U72
TITLE STRUCTURE OF HUMAN MR1-5OH-DCF 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: A, C;
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: B, D;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: MAIT T-CELL RECEPTOR BETA CHAIN;
COMPND 15 CHAIN: G, E;
COMPND 16 ENGINEERED: YES;
COMPND 17 MOL_ID: 4;
COMPND 18 MOLECULE: BETA-2-MICROGLOBULIN;
COMPND 19 CHAIN: H, F;
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_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: TRAV/TRAC;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET30;
SOURCE 21 MOL_ID: 3;
SOURCE 22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 23 ORGANISM_COMMON: HUMAN;
SOURCE 24 ORGANISM_TAXID: 9606;
SOURCE 25 GENE: TRBV/TRBC;
SOURCE 26 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 27 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 28 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 29 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 30 EXPRESSION_SYSTEM_PLASMID: PET30;
SOURCE 31 MOL_ID: 4;
SOURCE 32 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 33 ORGANISM_COMMON: HUMAN;
SOURCE 34 ORGANISM_TAXID: 9606;
SOURCE 35 GENE: B2M, CDABP0092, HDCMA22P;
SOURCE 36 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 37 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 38 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 39 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 40 EXPRESSION_SYSTEM_PLASMID: PET30
KEYWDS T-CELL RECEPTOR, IMMUNOLOGY, MHC-LIKE MOLECULE, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR A.N.KELLER,J.ROSSJOHN
REVDAT 6 04-OCT-23 5U72 1 REMARK
REVDAT 5 01-JAN-20 5U72 1 REMARK
REVDAT 4 17-JAN-18 5U72 1 REMARK
REVDAT 3 22-NOV-17 5U72 1 REMARK
REVDAT 2 13-SEP-17 5U72 1 REMARK
REVDAT 1 08-FEB-17 5U72 0
JRNL AUTH A.N.KELLER,J.ROSSJOHN
JRNL TITL T-CELL RECEPTOR COMPLEX
JRNL REF NAT.IMMUNOL. 2017
JRNL REFN ESSN 1529-2916
JRNL DOI 10.1038/NI.3679
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.82
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 69597
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.173
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.960
REMARK 3 FREE R VALUE TEST SET COUNT : 3455
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 36.8187 - 7.2920 0.99 2791 129 0.1572 0.1732
REMARK 3 2 7.2920 - 5.7952 0.99 2717 137 0.1684 0.2230
REMARK 3 3 5.7952 - 5.0648 0.99 2673 157 0.1481 0.1912
REMARK 3 4 5.0648 - 4.6027 0.99 2683 139 0.1251 0.1815
REMARK 3 5 4.6027 - 4.2733 0.99 2656 138 0.1189 0.1465
REMARK 3 6 4.2733 - 4.0217 0.99 2651 164 0.1361 0.1757
REMARK 3 7 4.0217 - 3.8205 0.99 2670 129 0.1524 0.1996
REMARK 3 8 3.8205 - 3.6543 0.99 2641 138 0.1593 0.2176
REMARK 3 9 3.6543 - 3.5138 0.99 2662 143 0.1610 0.2400
REMARK 3 10 3.5138 - 3.3926 0.99 2641 134 0.1724 0.2172
REMARK 3 11 3.3926 - 3.2866 0.99 2627 152 0.1805 0.2394
REMARK 3 12 3.2866 - 3.1927 0.99 2644 147 0.1952 0.2990
REMARK 3 13 3.1927 - 3.1087 0.99 2641 133 0.2028 0.2605
REMARK 3 14 3.1087 - 3.0329 0.99 2616 130 0.2055 0.2809
REMARK 3 15 3.0329 - 2.9640 0.99 2639 152 0.2087 0.2751
REMARK 3 16 2.9640 - 2.9009 0.99 2646 118 0.2087 0.3117
REMARK 3 17 2.9009 - 2.8429 0.99 2645 142 0.2168 0.3056
REMARK 3 18 2.8429 - 2.7893 0.98 2588 140 0.2247 0.3079
REMARK 3 19 2.7893 - 2.7395 0.99 2639 132 0.2384 0.3207
REMARK 3 20 2.7395 - 2.6931 0.98 2660 126 0.2291 0.3413
REMARK 3 21 2.6931 - 2.6496 0.98 2640 128 0.2450 0.3625
REMARK 3 22 2.6496 - 2.6089 0.98 2570 132 0.2451 0.3014
REMARK 3 23 2.6089 - 2.5705 0.98 2617 149 0.2361 0.3159
REMARK 3 24 2.5705 - 2.5343 0.98 2618 131 0.2393 0.3008
REMARK 3 25 2.5343 - 2.5001 0.97 2567 135 0.2564 0.3566
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.340
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.570
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 39.07
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.68
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 : 0.006 13158
REMARK 3 ANGLE : 0.971 17856
REMARK 3 CHIRALITY : 0.040 1891
REMARK 3 PLANARITY : 0.004 2334
REMARK 3 DIHEDRAL : 13.994 4703
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 45
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 0 THROUGH 83 )
REMARK 3 ORIGIN FOR THE GROUP (A): -46.9823 38.8212 191.6751
REMARK 3 T TENSOR
REMARK 3 T11: 0.3818 T22: 0.4014
REMARK 3 T33: 0.4173 T12: 0.1012
REMARK 3 T13: -0.0575 T23: -0.0373
REMARK 3 L TENSOR
REMARK 3 L11: 1.6961 L22: 1.8134
REMARK 3 L33: 1.4798 L12: -0.0146
REMARK 3 L13: -0.3827 L23: -0.7187
REMARK 3 S TENSOR
REMARK 3 S11: -0.0206 S12: -0.1695 S13: 0.3405
REMARK 3 S21: 0.2377 S22: -0.0067 S23: 0.2174
REMARK 3 S31: -0.1129 S32: -0.1913 S33: 0.0233
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 84 THROUGH 171 )
REMARK 3 ORIGIN FOR THE GROUP (A): -36.0460 40.3510 181.3430
REMARK 3 T TENSOR
REMARK 3 T11: 0.2919 T22: 0.2827
REMARK 3 T33: 0.3429 T12: 0.0429
REMARK 3 T13: -0.0302 T23: 0.0354
REMARK 3 L TENSOR
REMARK 3 L11: 2.3920 L22: 3.2327
REMARK 3 L33: 1.1110 L12: 0.5447
REMARK 3 L13: 0.1306 L23: -0.3375
REMARK 3 S TENSOR
REMARK 3 S11: -0.0213 S12: 0.0386 S13: 0.1984
REMARK 3 S21: -0.1435 S22: -0.0086 S23: -0.2966
REMARK 3 S31: -0.1756 S32: 0.0875 S33: 0.0280
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 172 THROUGH 269 )
REMARK 3 ORIGIN FOR THE GROUP (A): -63.7944 40.0470 161.9077
REMARK 3 T TENSOR
REMARK 3 T11: 0.3047 T22: 0.4778
REMARK 3 T33: 0.4546 T12: -0.1010
REMARK 3 T13: -0.1087 T23: 0.1450
REMARK 3 L TENSOR
REMARK 3 L11: 1.2455 L22: 1.6732
REMARK 3 L33: 1.7478 L12: 0.0790
REMARK 3 L13: -0.0516 L23: 0.1761
REMARK 3 S TENSOR
REMARK 3 S11: -0.0929 S12: 0.2493 S13: 0.3725
REMARK 3 S21: -0.2178 S22: 0.0103 S23: 0.0705
REMARK 3 S31: -0.3060 S32: 0.0893 S33: 0.0100
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 13 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.2421 12.0019 196.3699
REMARK 3 T TENSOR
REMARK 3 T11: 0.3986 T22: 0.1835
REMARK 3 T33: 0.2334 T12: -0.0050
REMARK 3 T13: 0.0136 T23: 0.0099
REMARK 3 L TENSOR
REMARK 3 L11: 1.4508 L22: 4.0949
REMARK 3 L33: 4.1031 L12: -0.4605
REMARK 3 L13: -0.1299 L23: -0.4771
REMARK 3 S TENSOR
REMARK 3 S11: 0.0728 S12: -0.7009 S13: -0.7576
REMARK 3 S21: -0.0336 S22: 0.1185 S23: 0.2006
REMARK 3 S31: 0.6387 S32: -0.3426 S33: -0.0901
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 14 THROUGH 52 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.2898 21.9927 193.4681
REMARK 3 T TENSOR
REMARK 3 T11: 0.3353 T22: 0.1561
REMARK 3 T33: 0.3341 T12: 0.0196
REMARK 3 T13: -0.0801 T23: -0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 2.9877 L22: 1.9197
REMARK 3 L33: 1.3471 L12: -1.6684
REMARK 3 L13: 0.0160 L23: -0.7864
REMARK 3 S TENSOR
REMARK 3 S11: 0.0553 S12: -0.0907 S13: -0.0375
REMARK 3 S21: -0.0959 S22: 0.1923 S23: 0.0450
REMARK 3 S31: -0.0500 S32: -0.0756 S33: -0.2114
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 53 THROUGH 108 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.9856 20.7495 192.4516
REMARK 3 T TENSOR
REMARK 3 T11: 0.2919 T22: 0.1915
REMARK 3 T33: 0.2593 T12: 0.0347
REMARK 3 T13: -0.0218 T23: -0.0243
REMARK 3 L TENSOR
REMARK 3 L11: 3.8436 L22: 2.7140
REMARK 3 L33: 2.0678 L12: -1.2764
REMARK 3 L13: 0.6764 L23: -0.5315
REMARK 3 S TENSOR
REMARK 3 S11: 0.0757 S12: 0.0972 S13: 0.1995
REMARK 3 S21: -0.0907 S22: -0.0261 S23: -0.1286
REMARK 3 S31: -0.1168 S32: 0.0127 S33: -0.0360
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 109 THROUGH 135 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.5815 7.9800 216.9499
REMARK 3 T TENSOR
REMARK 3 T11: 0.4949 T22: 0.1523
REMARK 3 T33: 0.2742 T12: 0.0427
REMARK 3 T13: -0.0302 T23: -0.0570
REMARK 3 L TENSOR
REMARK 3 L11: 1.6930 L22: 1.8248
REMARK 3 L33: 0.9888 L12: -0.1210
REMARK 3 L13: 0.4278 L23: 0.2681
REMARK 3 S TENSOR
REMARK 3 S11: 0.1368 S12: -0.0905 S13: -0.0371
REMARK 3 S21: 0.5520 S22: 0.0975 S23: -0.2223
REMARK 3 S31: -0.0023 S32: 0.2686 S33: -0.3437
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 136 THROUGH 175 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.7282 8.7581 211.3914
REMARK 3 T TENSOR
REMARK 3 T11: 0.3378 T22: 0.1994
REMARK 3 T33: 0.2984 T12: 0.0637
REMARK 3 T13: 0.0102 T23: -0.0371
REMARK 3 L TENSOR
REMARK 3 L11: 4.5312 L22: 2.8663
REMARK 3 L33: 5.2862 L12: 0.9167
REMARK 3 L13: -0.8556 L23: -0.2290
REMARK 3 S TENSOR
REMARK 3 S11: 0.0594 S12: 0.5779 S13: -0.0646
REMARK 3 S21: 0.1868 S22: 0.0693 S23: 0.1200
REMARK 3 S31: 0.2365 S32: -0.3465 S33: -0.1454
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 176 THROUGH 185 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.5623 -2.6426 224.7945
REMARK 3 T TENSOR
REMARK 3 T11: 0.9829 T22: 0.2932
REMARK 3 T33: 0.5600 T12: 0.0517
REMARK 3 T13: 0.0692 T23: 0.0226
REMARK 3 L TENSOR
REMARK 3 L11: 2.0604 L22: 0.6274
REMARK 3 L33: 2.3648 L12: -1.0897
REMARK 3 L13: -2.0777 L23: 1.2263
REMARK 3 S TENSOR
REMARK 3 S11: -0.6329 S12: -0.3552 S13: -0.6740
REMARK 3 S21: 1.2192 S22: 0.0393 S23: -0.5169
REMARK 3 S31: 0.8808 S32: -0.1635 S33: 0.3546
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 186 THROUGH 200 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.6965 -1.9232 212.1162
REMARK 3 T TENSOR
REMARK 3 T11: 0.5659 T22: 0.2704
REMARK 3 T33: 0.4936 T12: 0.0317
REMARK 3 T13: 0.0253 T23: -0.0155
REMARK 3 L TENSOR
REMARK 3 L11: 8.0037 L22: 4.7365
REMARK 3 L33: 6.1775 L12: 1.1911
REMARK 3 L13: 2.3851 L23: 0.7495
REMARK 3 S TENSOR
REMARK 3 S11: 0.4080 S12: 0.3495 S13: -0.7016
REMARK 3 S21: 0.6123 S22: -0.2296 S23: -0.2699
REMARK 3 S31: 0.9947 S32: 0.2921 S33: 0.0022
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 2 THROUGH 73 )
REMARK 3 ORIGIN FOR THE GROUP (A): -30.6372 29.8333 212.1807
REMARK 3 T TENSOR
REMARK 3 T11: 0.4222 T22: 0.4237
REMARK 3 T33: 0.3119 T12: 0.1086
REMARK 3 T13: -0.0367 T23: -0.1392
REMARK 3 L TENSOR
REMARK 3 L11: 3.2559 L22: 1.9942
REMARK 3 L33: 2.7145 L12: 0.0343
REMARK 3 L13: 0.0509 L23: -1.7542
REMARK 3 S TENSOR
REMARK 3 S11: 0.0405 S12: -0.4179 S13: 0.3469
REMARK 3 S21: 0.3910 S22: -0.1104 S23: 0.0770
REMARK 3 S31: -0.3926 S32: -0.3635 S33: 0.0798
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 74 THROUGH 109 )
REMARK 3 ORIGIN FOR THE GROUP (A): -28.7176 28.1327 209.8648
REMARK 3 T TENSOR
REMARK 3 T11: 0.3747 T22: 0.4733
REMARK 3 T33: 0.3176 T12: 0.0539
REMARK 3 T13: -0.0876 T23: -0.0617
REMARK 3 L TENSOR
REMARK 3 L11: 1.7638 L22: 3.5456
REMARK 3 L33: 3.6379 L12: 0.6831
REMARK 3 L13: -2.1273 L23: -2.8126
REMARK 3 S TENSOR
REMARK 3 S11: -0.0015 S12: -0.1381 S13: 0.1588
REMARK 3 S21: -0.0072 S22: 0.1623 S23: 0.1495
REMARK 3 S31: -0.0265 S32: -0.5895 S33: -0.1592
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 110 THROUGH 124 )
REMARK 3 ORIGIN FOR THE GROUP (A): -22.4223 15.8123 227.5024
REMARK 3 T TENSOR
REMARK 3 T11: 0.3569 T22: 0.4709
REMARK 3 T33: 0.2723 T12: -0.0647
REMARK 3 T13: -0.0320 T23: -0.0297
REMARK 3 L TENSOR
REMARK 3 L11: 2.6458 L22: 3.6665
REMARK 3 L33: 7.6553 L12: -2.6827
REMARK 3 L13: 1.8876 L23: -3.6715
REMARK 3 S TENSOR
REMARK 3 S11: 0.0189 S12: -0.3344 S13: -0.1779
REMARK 3 S21: -0.5101 S22: 0.3535 S23: 0.4286
REMARK 3 S31: 1.1391 S32: -1.4732 S33: -0.4040
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 125 THROUGH 202 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.1233 15.5991 220.1365
REMARK 3 T TENSOR
REMARK 3 T11: 0.3063 T22: 0.1754
REMARK 3 T33: 0.2090 T12: 0.0410
REMARK 3 T13: -0.0054 T23: -0.0235
REMARK 3 L TENSOR
REMARK 3 L11: 4.0076 L22: 2.1298
REMARK 3 L33: 2.6323 L12: 0.1731
REMARK 3 L13: -0.8205 L23: 0.1651
REMARK 3 S TENSOR
REMARK 3 S11: 0.1281 S12: 0.3271 S13: -0.1429
REMARK 3 S21: 0.1631 S22: -0.0824 S23: 0.0631
REMARK 3 S31: -0.0624 S32: -0.2651 S33: -0.0475
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 203 THROUGH 244 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.2062 22.0597 230.6919
REMARK 3 T TENSOR
REMARK 3 T11: 0.3978 T22: 0.2713
REMARK 3 T33: 0.3187 T12: 0.0058
REMARK 3 T13: -0.0405 T23: -0.0962
REMARK 3 L TENSOR
REMARK 3 L11: 3.9140 L22: 0.2437
REMARK 3 L33: 2.7358 L12: -0.1847
REMARK 3 L13: -2.0607 L23: -0.3306
REMARK 3 S TENSOR
REMARK 3 S11: 0.3055 S12: -0.0067 S13: 0.2578
REMARK 3 S21: 0.1351 S22: -0.0851 S23: -0.0643
REMARK 3 S31: -0.1864 S32: -0.1522 S33: -0.1637
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 19 )
REMARK 3 ORIGIN FOR THE GROUP (A): -66.7842 49.4032 175.8222
REMARK 3 T TENSOR
REMARK 3 T11: 0.3416 T22: 0.5094
REMARK 3 T33: 0.9141 T12: 0.1174
REMARK 3 T13: -0.1108 T23: 0.0453
REMARK 3 L TENSOR
REMARK 3 L11: 1.0450 L22: 0.9682
REMARK 3 L33: 2.9737 L12: -0.9372
REMARK 3 L13: -0.3909 L23: -0.2774
REMARK 3 S TENSOR
REMARK 3 S11: -0.3560 S12: 0.0258 S13: 0.8782
REMARK 3 S21: -0.6505 S22: -0.1669 S23: 0.7278
REMARK 3 S31: -0.5020 S32: -0.6339 S33: 0.4068
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 20 THROUGH 41 )
REMARK 3 ORIGIN FOR THE GROUP (A): -64.1166 51.2300 182.8449
REMARK 3 T TENSOR
REMARK 3 T11: 0.4472 T22: 0.6448
REMARK 3 T33: 0.7741 T12: 0.1675
REMARK 3 T13: -0.1012 T23: -0.1726
REMARK 3 L TENSOR
REMARK 3 L11: 4.1981 L22: 0.4113
REMARK 3 L33: 2.2530 L12: -0.9479
REMARK 3 L13: 1.8934 L23: -0.9571
REMARK 3 S TENSOR
REMARK 3 S11: -0.5153 S12: -0.3464 S13: 1.0242
REMARK 3 S21: 0.0372 S22: -0.0314 S23: 0.5052
REMARK 3 S31: -0.7002 S32: -0.4680 S33: 0.4571
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 42 THROUGH 51 )
REMARK 3 ORIGIN FOR THE GROUP (A): -73.5430 51.4563 188.7510
REMARK 3 T TENSOR
REMARK 3 T11: 0.5618 T22: 1.1267
REMARK 3 T33: 1.1316 T12: 0.2428
REMARK 3 T13: 0.0733 T23: -0.1164
REMARK 3 L TENSOR
REMARK 3 L11: 2.5893 L22: 0.0467
REMARK 3 L33: 0.3452 L12: -0.3140
REMARK 3 L13: 0.2979 L23: -0.0737
REMARK 3 S TENSOR
REMARK 3 S11: -0.0038 S12: -0.5965 S13: -0.2256
REMARK 3 S21: 0.4373 S22: -0.3557 S23: 0.9549
REMARK 3 S31: -0.3992 S32: -0.5585 S33: 0.4307
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 52 THROUGH 61 )
REMARK 3 ORIGIN FOR THE GROUP (A): -51.2131 45.9519 182.0355
REMARK 3 T TENSOR
REMARK 3 T11: 0.4575 T22: 0.4638
REMARK 3 T33: 0.4926 T12: 0.0513
REMARK 3 T13: -0.1045 T23: -0.0251
REMARK 3 L TENSOR
REMARK 3 L11: 4.6852 L22: 1.2432
REMARK 3 L33: 0.7931 L12: 0.5423
REMARK 3 L13: -1.4392 L23: -0.1758
REMARK 3 S TENSOR
REMARK 3 S11: -0.1571 S12: 0.1183 S13: -0.3613
REMARK 3 S21: -0.0348 S22: -0.0009 S23: -0.2533
REMARK 3 S31: -0.3312 S32: -0.2053 S33: 0.1872
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 62 THROUGH 71 )
REMARK 3 ORIGIN FOR THE GROUP (A): -67.1262 46.1143 182.9966
REMARK 3 T TENSOR
REMARK 3 T11: 0.3627 T22: 0.5932
REMARK 3 T33: 0.6394 T12: 0.1737
REMARK 3 T13: -0.0388 T23: -0.0907
REMARK 3 L TENSOR
REMARK 3 L11: 2.2202 L22: 1.5585
REMARK 3 L33: 2.5757 L12: -1.8762
REMARK 3 L13: 1.5603 L23: -1.2940
REMARK 3 S TENSOR
REMARK 3 S11: -0.5166 S12: -0.9465 S13: -0.2203
REMARK 3 S21: 0.5791 S22: 0.2550 S23: 0.6971
REMARK 3 S31: -0.1972 S32: -0.6059 S33: 0.2313
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 72 THROUGH 77 )
REMARK 3 ORIGIN FOR THE GROUP (A): -82.9900 53.2182 177.1502
REMARK 3 T TENSOR
REMARK 3 T11: 0.4814 T22: 1.2228
REMARK 3 T33: 1.3774 T12: 0.1372
REMARK 3 T13: -0.1148 T23: 0.2846
REMARK 3 L TENSOR
REMARK 3 L11: 0.0163 L22: 0.4370
REMARK 3 L33: 2.1724 L12: -0.0856
REMARK 3 L13: -0.1840 L23: 0.9767
REMARK 3 S TENSOR
REMARK 3 S11: 0.6797 S12: 0.3461 S13: -0.8150
REMARK 3 S21: -0.3805 S22: 0.2002 S23: 0.0881
REMARK 3 S31: -0.4357 S32: -1.3163 S33: -0.8558
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 78 THROUGH 97 )
REMARK 3 ORIGIN FOR THE GROUP (A): -67.0557 58.4173 179.9557
REMARK 3 T TENSOR
REMARK 3 T11: 0.6727 T22: 0.5579
REMARK 3 T33: 1.1342 T12: 0.1766
REMARK 3 T13: -0.2189 T23: -0.1094
REMARK 3 L TENSOR
REMARK 3 L11: 1.6279 L22: 2.5101
REMARK 3 L33: 0.6694 L12: 1.2290
REMARK 3 L13: -0.5059 L23: -1.0953
REMARK 3 S TENSOR
REMARK 3 S11: -0.3081 S12: -0.3119 S13: 1.1754
REMARK 3 S21: -0.0992 S22: 0.0330 S23: 0.6615
REMARK 3 S31: -0.6528 S32: -0.6150 S33: 0.2407
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 0 THROUGH 84 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.6874 25.4236 255.0706
REMARK 3 T TENSOR
REMARK 3 T11: 0.2378 T22: 0.3730
REMARK 3 T33: 0.2890 T12: 0.0070
REMARK 3 T13: 0.0048 T23: 0.0409
REMARK 3 L TENSOR
REMARK 3 L11: 1.6413 L22: 3.0478
REMARK 3 L33: 2.1351 L12: -0.1238
REMARK 3 L13: -0.1719 L23: -0.0885
REMARK 3 S TENSOR
REMARK 3 S11: 0.0384 S12: -0.3360 S13: 0.0468
REMARK 3 S21: 0.2424 S22: -0.2219 S23: -0.2917
REMARK 3 S31: -0.1506 S32: 0.0452 S33: 0.1575
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 85 THROUGH 171 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.8376 18.4123 244.6836
REMARK 3 T TENSOR
REMARK 3 T11: 0.2675 T22: 0.3322
REMARK 3 T33: 0.2057 T12: 0.0197
REMARK 3 T13: 0.0404 T23: 0.0327
REMARK 3 L TENSOR
REMARK 3 L11: 1.8629 L22: 2.5908
REMARK 3 L33: 1.7561 L12: -0.4237
REMARK 3 L13: 0.1036 L23: 1.2436
REMARK 3 S TENSOR
REMARK 3 S11: -0.0230 S12: -0.1164 S13: -0.1098
REMARK 3 S21: -0.1792 S22: -0.2125 S23: 0.0182
REMARK 3 S31: 0.0179 S32: -0.1900 S33: 0.2235
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 172 THROUGH 195 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.6419 37.8066 227.7572
REMARK 3 T TENSOR
REMARK 3 T11: 0.3585 T22: 0.2127
REMARK 3 T33: 0.3569 T12: -0.0661
REMARK 3 T13: 0.0082 T23: 0.0338
REMARK 3 L TENSOR
REMARK 3 L11: 3.0852 L22: 2.0279
REMARK 3 L33: 2.3648 L12: -0.7018
REMARK 3 L13: -0.7172 L23: -0.3785
REMARK 3 S TENSOR
REMARK 3 S11: 0.2963 S12: 0.0249 S13: 0.1253
REMARK 3 S21: -0.1253 S22: -0.1752 S23: -0.4618
REMARK 3 S31: -0.2504 S32: 0.3241 S33: -0.0669
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 196 THROUGH 216 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.6105 34.2432 224.9752
REMARK 3 T TENSOR
REMARK 3 T11: 0.3525 T22: 0.2443
REMARK 3 T33: 0.3827 T12: -0.0019
REMARK 3 T13: 0.0666 T23: 0.0492
REMARK 3 L TENSOR
REMARK 3 L11: 3.2350 L22: 3.2708
REMARK 3 L33: 3.3705 L12: -0.2349
REMARK 3 L13: -0.5585 L23: 1.1322
REMARK 3 S TENSOR
REMARK 3 S11: -0.0231 S12: 0.3065 S13: -0.1297
REMARK 3 S21: -0.2015 S22: 0.1775 S23: 0.0215
REMARK 3 S31: 0.1787 S32: -0.0282 S33: -0.0744
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 217 THROUGH 245 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.7611 30.7510 226.8929
REMARK 3 T TENSOR
REMARK 3 T11: 0.2762 T22: 0.2299
REMARK 3 T33: 0.3637 T12: 0.0337
REMARK 3 T13: 0.0137 T23: 0.0162
REMARK 3 L TENSOR
REMARK 3 L11: 2.1585 L22: 3.6811
REMARK 3 L33: 4.2111 L12: 0.7485
REMARK 3 L13: -0.9835 L23: 0.4232
REMARK 3 S TENSOR
REMARK 3 S11: -0.1330 S12: 0.0970 S13: -0.0903
REMARK 3 S21: 0.2650 S22: 0.1532 S23: -0.3680
REMARK 3 S31: 0.4093 S32: 0.2520 S33: 0.0337
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 246 THROUGH 269 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.9715 36.3315 216.4939
REMARK 3 T TENSOR
REMARK 3 T11: 0.3475 T22: 0.2126
REMARK 3 T33: 0.2589 T12: -0.0569
REMARK 3 T13: 0.0557 T23: 0.0088
REMARK 3 L TENSOR
REMARK 3 L11: 4.5647 L22: 6.7599
REMARK 3 L33: 0.4294 L12: -3.6724
REMARK 3 L13: 0.2938 L23: 0.4197
REMARK 3 S TENSOR
REMARK 3 S11: 0.2087 S12: 0.8681 S13: -0.2550
REMARK 3 S21: -0.5041 S22: -0.3656 S23: -0.3881
REMARK 3 S31: 0.2760 S32: -0.4031 S33: 0.1437
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 52 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.3744 25.7784 257.2194
REMARK 3 T TENSOR
REMARK 3 T11: 0.2398 T22: 0.3852
REMARK 3 T33: 0.2702 T12: 0.0237
REMARK 3 T13: -0.0038 T23: -0.0775
REMARK 3 L TENSOR
REMARK 3 L11: 2.2965 L22: 1.4940
REMARK 3 L33: 1.8119 L12: -0.1690
REMARK 3 L13: -0.6758 L23: 0.1272
REMARK 3 S TENSOR
REMARK 3 S11: -0.0741 S12: 0.0886 S13: 0.0826
REMARK 3 S21: -0.0794 S22: 0.0951 S23: 0.1510
REMARK 3 S31: -0.0412 S32: -0.3268 S33: -0.0199
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 53 THROUGH 75 )
REMARK 3 ORIGIN FOR THE GROUP (A): -25.7323 22.3905 249.0281
REMARK 3 T TENSOR
REMARK 3 T11: 0.2621 T22: 0.4716
REMARK 3 T33: 0.2642 T12: -0.0042
REMARK 3 T13: -0.0146 T23: -0.0847
REMARK 3 L TENSOR
REMARK 3 L11: 6.2662 L22: 4.1096
REMARK 3 L33: 5.2455 L12: 2.0657
REMARK 3 L13: -2.5370 L23: -1.2029
REMARK 3 S TENSOR
REMARK 3 S11: 0.2609 S12: 0.5440 S13: 0.1049
REMARK 3 S21: 0.0632 S22: -0.0031 S23: 0.4820
REMARK 3 S31: 0.1755 S32: -0.5127 S33: -0.2338
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 76 THROUGH 91 )
REMARK 3 ORIGIN FOR THE GROUP (A): -30.1928 20.2978 259.7798
REMARK 3 T TENSOR
REMARK 3 T11: 0.3520 T22: 0.5257
REMARK 3 T33: 0.3013 T12: -0.0136
REMARK 3 T13: 0.0105 T23: -0.0762
REMARK 3 L TENSOR
REMARK 3 L11: 3.0005 L22: 1.0571
REMARK 3 L33: 1.9161 L12: 0.6861
REMARK 3 L13: -0.8026 L23: -1.2570
REMARK 3 S TENSOR
REMARK 3 S11: -0.2757 S12: 0.0189 S13: 0.0305
REMARK 3 S21: -0.1563 S22: 0.1979 S23: 0.3095
REMARK 3 S31: 0.2889 S32: -0.4088 S33: 0.0397
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 92 THROUGH 135 )
REMARK 3 ORIGIN FOR THE GROUP (A): -39.8852 23.7161 270.3307
REMARK 3 T TENSOR
REMARK 3 T11: 0.2888 T22: 0.5257
REMARK 3 T33: 0.3025 T12: 0.0156
REMARK 3 T13: -0.0308 T23: -0.0473
REMARK 3 L TENSOR
REMARK 3 L11: 4.2042 L22: 0.9277
REMARK 3 L33: 1.7882 L12: 0.2357
REMARK 3 L13: -2.1432 L23: -0.5112
REMARK 3 S TENSOR
REMARK 3 S11: -0.0095 S12: -0.1427 S13: 0.0676
REMARK 3 S21: 0.1088 S22: 0.1761 S23: 0.2742
REMARK 3 S31: 0.0989 S32: -0.2292 S33: -0.1263
REMARK 3 TLS GROUP : 33
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 136 THROUGH 150 )
REMARK 3 ORIGIN FOR THE GROUP (A): -49.0123 30.2782 273.4842
REMARK 3 T TENSOR
REMARK 3 T11: 0.4787 T22: 0.5537
REMARK 3 T33: 0.6393 T12: -0.0398
REMARK 3 T13: 0.0236 T23: 0.0752
REMARK 3 L TENSOR
REMARK 3 L11: 7.6427 L22: 5.9650
REMARK 3 L33: 5.8590 L12: 1.3075
REMARK 3 L13: 1.9006 L23: 2.6195
REMARK 3 S TENSOR
REMARK 3 S11: -0.1657 S12: 1.0414 S13: 0.8532
REMARK 3 S21: -0.3023 S22: 0.3563 S23: -0.5063
REMARK 3 S31: -1.5082 S32: 0.0224 S33: -0.3361
REMARK 3 TLS GROUP : 34
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 151 THROUGH 175 )
REMARK 3 ORIGIN FOR THE GROUP (A): -46.8606 19.4908 274.5438
REMARK 3 T TENSOR
REMARK 3 T11: 0.3282 T22: 0.4496
REMARK 3 T33: 0.3851 T12: 0.0318
REMARK 3 T13: 0.0577 T23: 0.0220
REMARK 3 L TENSOR
REMARK 3 L11: 4.2951 L22: 4.1300
REMARK 3 L33: 5.4143 L12: 2.5280
REMARK 3 L13: 1.1053 L23: 1.0542
REMARK 3 S TENSOR
REMARK 3 S11: -0.0000 S12: 0.2909 S13: 0.0617
REMARK 3 S21: -0.1339 S22: 0.0244 S23: 0.0844
REMARK 3 S31: 0.2824 S32: -0.4184 S33: -0.0835
REMARK 3 TLS GROUP : 35
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 176 THROUGH 200 )
REMARK 3 ORIGIN FOR THE GROUP (A): -57.4948 30.2011 279.6763
REMARK 3 T TENSOR
REMARK 3 T11: 0.3936 T22: 0.7621
REMARK 3 T33: 0.7812 T12: 0.1225
REMARK 3 T13: 0.0857 T23: 0.0337
REMARK 3 L TENSOR
REMARK 3 L11: 3.2847 L22: 4.0216
REMARK 3 L33: 4.5965 L12: 1.9326
REMARK 3 L13: 0.0038 L23: 1.9181
REMARK 3 S TENSOR
REMARK 3 S11: -0.2939 S12: -0.1757 S13: 1.2283
REMARK 3 S21: 0.0882 S22: -0.1058 S23: 0.6584
REMARK 3 S31: -0.1252 S32: -0.9976 S33: 0.3985
REMARK 3 TLS GROUP : 36
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 2 THROUGH 94 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.4295 24.1103 276.0098
REMARK 3 T TENSOR
REMARK 3 T11: 0.3093 T22: 0.4442
REMARK 3 T33: 0.2241 T12: 0.0449
REMARK 3 T13: -0.0437 T23: -0.0324
REMARK 3 L TENSOR
REMARK 3 L11: 3.6378 L22: 1.4907
REMARK 3 L33: 3.3350 L12: 0.0654
REMARK 3 L13: -1.3557 L23: 0.3550
REMARK 3 S TENSOR
REMARK 3 S11: -0.0663 S12: -0.4301 S13: -0.0133
REMARK 3 S21: 0.2367 S22: 0.0058 S23: -0.0618
REMARK 3 S31: 0.0072 S32: 0.4578 S33: 0.0820
REMARK 3 TLS GROUP : 37
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 95 THROUGH 124 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.9796 24.2376 277.5385
REMARK 3 T TENSOR
REMARK 3 T11: 0.2906 T22: 0.2973
REMARK 3 T33: 0.2987 T12: 0.0010
REMARK 3 T13: 0.0232 T23: -0.0103
REMARK 3 L TENSOR
REMARK 3 L11: 2.5399 L22: 0.9424
REMARK 3 L33: 3.3474 L12: -0.4890
REMARK 3 L13: -1.5020 L23: 0.4678
REMARK 3 S TENSOR
REMARK 3 S11: 0.0654 S12: -0.2767 S13: 0.0995
REMARK 3 S21: 0.0957 S22: 0.0759 S23: 0.0548
REMARK 3 S31: -0.1570 S32: 0.1115 S33: -0.2174
REMARK 3 TLS GROUP : 38
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 125 THROUGH 203 )
REMARK 3 ORIGIN FOR THE GROUP (A): -42.8195 18.1068 283.1847
REMARK 3 T TENSOR
REMARK 3 T11: 0.3472 T22: 0.3891
REMARK 3 T33: 0.3977 T12: -0.0518
REMARK 3 T13: 0.0280 T23: 0.0684
REMARK 3 L TENSOR
REMARK 3 L11: 3.8316 L22: 2.1274
REMARK 3 L33: 3.2849 L12: -0.0714
REMARK 3 L13: 1.2975 L23: 0.2738
REMARK 3 S TENSOR
REMARK 3 S11: 0.1723 S12: -0.1139 S13: -0.7112
REMARK 3 S21: 0.0891 S22: 0.2672 S23: 0.1767
REMARK 3 S31: 0.4006 S32: -0.4862 S33: -0.3782
REMARK 3 TLS GROUP : 39
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 204 THROUGH 244 )
REMARK 3 ORIGIN FOR THE GROUP (A): -34.2101 15.2733 293.8095
REMARK 3 T TENSOR
REMARK 3 T11: 0.5494 T22: 0.5952
REMARK 3 T33: 0.4835 T12: -0.0545
REMARK 3 T13: -0.0681 T23: 0.3663
REMARK 3 L TENSOR
REMARK 3 L11: 1.7062 L22: 2.6299
REMARK 3 L33: 2.5984 L12: -0.8263
REMARK 3 L13: -1.7591 L23: -0.4247
REMARK 3 S TENSOR
REMARK 3 S11: 0.4013 S12: -0.8750 S13: -0.8020
REMARK 3 S21: 0.6467 S22: 0.4144 S23: 0.0294
REMARK 3 S31: 0.5056 S32: -0.1606 S33: -0.1125
REMARK 3 TLS GROUP : 40
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 1 THROUGH 19 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.9719 29.5593 239.2207
REMARK 3 T TENSOR
REMARK 3 T11: 0.2827 T22: 0.2680
REMARK 3 T33: 0.3681 T12: -0.0551
REMARK 3 T13: -0.0406 T23: 0.0712
REMARK 3 L TENSOR
REMARK 3 L11: 2.0411 L22: 1.9642
REMARK 3 L33: 1.7385 L12: -0.7993
REMARK 3 L13: -0.0961 L23: -0.0056
REMARK 3 S TENSOR
REMARK 3 S11: 0.1430 S12: -0.2429 S13: 0.1408
REMARK 3 S21: 0.0925 S22: -0.3706 S23: -0.2707
REMARK 3 S31: -0.3726 S32: 0.3685 S33: 0.2744
REMARK 3 TLS GROUP : 41
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 20 THROUGH 41 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.9869 27.2337 246.5338
REMARK 3 T TENSOR
REMARK 3 T11: 0.3521 T22: 0.4014
REMARK 3 T33: 0.3496 T12: 0.0200
REMARK 3 T13: -0.0984 T23: 0.0504
REMARK 3 L TENSOR
REMARK 3 L11: 2.8894 L22: 1.7164
REMARK 3 L33: 1.4290 L12: 1.3753
REMARK 3 L13: -0.2213 L23: -0.2533
REMARK 3 S TENSOR
REMARK 3 S11: -0.1653 S12: -0.5425 S13: 0.1211
REMARK 3 S21: 0.3255 S22: -0.0104 S23: -0.2965
REMARK 3 S31: -0.2996 S32: 0.1879 S33: 0.2083
REMARK 3 TLS GROUP : 42
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 42 THROUGH 51 )
REMARK 3 ORIGIN FOR THE GROUP (A): 36.7808 33.3286 252.5890
REMARK 3 T TENSOR
REMARK 3 T11: 0.6615 T22: 0.5742
REMARK 3 T33: 0.6110 T12: -0.0206
REMARK 3 T13: -0.2269 T23: 0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 3.7016 L22: 2.2403
REMARK 3 L33: 1.9260 L12: 0.7250
REMARK 3 L13: 0.2327 L23: -0.0137
REMARK 3 S TENSOR
REMARK 3 S11: -0.2779 S12: -1.1189 S13: 0.7471
REMARK 3 S21: 1.4790 S22: 0.1814 S23: -0.8707
REMARK 3 S31: -0.0301 S32: 0.4520 S33: -0.0017
REMARK 3 TLS GROUP : 43
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 52 THROUGH 61 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.4250 22.9269 245.6569
REMARK 3 T TENSOR
REMARK 3 T11: 0.3866 T22: 0.3468
REMARK 3 T33: 0.2872 T12: -0.0059
REMARK 3 T13: 0.0282 T23: 0.1062
REMARK 3 L TENSOR
REMARK 3 L11: 2.5229 L22: 3.7879
REMARK 3 L33: 1.3395 L12: 1.3955
REMARK 3 L13: 0.1227 L23: 1.2940
REMARK 3 S TENSOR
REMARK 3 S11: -0.2194 S12: -0.0946 S13: -0.1777
REMARK 3 S21: -0.1277 S22: 0.4220 S23: 0.0372
REMARK 3 S31: 0.1933 S32: -0.1438 S33: -0.1062
REMARK 3 TLS GROUP : 44
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 62 THROUGH 77 )
REMARK 3 ORIGIN FOR THE GROUP (A): 34.4753 34.1353 244.3554
REMARK 3 T TENSOR
REMARK 3 T11: 0.4388 T22: 0.4813
REMARK 3 T33: 0.5712 T12: -0.1085
REMARK 3 T13: -0.1500 T23: 0.0686
REMARK 3 L TENSOR
REMARK 3 L11: 5.1279 L22: 2.4136
REMARK 3 L33: 1.7768 L12: 1.4830
REMARK 3 L13: 0.8105 L23: 0.0412
REMARK 3 S TENSOR
REMARK 3 S11: -0.1743 S12: -0.4965 S13: 0.1114
REMARK 3 S21: 0.1457 S22: 0.0451 S23: -0.5282
REMARK 3 S31: -0.5218 S32: 0.3173 S33: 0.2322
REMARK 3 TLS GROUP : 45
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 78 THROUGH 97 )
REMARK 3 ORIGIN FOR THE GROUP (A): 36.1773 23.0298 244.1924
REMARK 3 T TENSOR
REMARK 3 T11: 0.2696 T22: 0.4064
REMARK 3 T33: 0.6298 T12: -0.0315
REMARK 3 T13: -0.0799 T23: 0.1816
REMARK 3 L TENSOR
REMARK 3 L11: 2.2338 L22: 5.0587
REMARK 3 L33: 0.6427 L12: 1.3856
REMARK 3 L13: -0.7776 L23: 0.0081
REMARK 3 S TENSOR
REMARK 3 S11: 0.1628 S12: -0.5241 S13: -0.2663
REMARK 3 S21: 0.7164 S22: -0.4829 S23: -1.3368
REMARK 3 S31: -0.2771 S32: 0.4021 S33: 0.2653
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 4
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN C
REMARK 3 ATOM PAIRS NUMBER : 2345
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN B
REMARK 3 SELECTION : CHAIN D
REMARK 3 ATOM PAIRS NUMBER : 1790
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 3
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN E
REMARK 3 SELECTION : CHAIN G
REMARK 3 ATOM PAIRS NUMBER : 2224
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 4
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN F
REMARK 3 SELECTION : CHAIN H
REMARK 3 ATOM PAIRS NUMBER : 903
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5U72 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-DEC-16.
REMARK 100 THE DEPOSITION ID IS D_1000225164.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-JUN-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 : AIMLESS 0.5.9
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 69625
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 36.815
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.07600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.56
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.46200
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 (%): 55.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
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 106.54500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.80000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 106.54500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 34.80000
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: 9120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36400 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 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 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: 9060 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 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 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 HIS A 17
REMARK 465 GLY A 18
REMARK 465 LYS A 189
REMARK 465 GLU A 190
REMARK 465 THR A 191
REMARK 465 PHE A 192
REMARK 465 PRO A 193
REMARK 465 GLY A 194
REMARK 465 VAL A 195
REMARK 465 THR A 196
REMARK 465 VAL A 222
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 ASP G 245
REMARK 465 ASP H 98
REMARK 465 MET H 99
REMARK 465 HIS C 17
REMARK 465 GLY C 18
REMARK 465 VAL C 222
REMARK 465 GLN C 223
REMARK 465 PRO C 248
REMARK 465 GLN C 249
REMARK 465 SER C 250
REMARK 465 PRO C 270
REMARK 465 SER D 126
REMARK 465 SER D 127
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 ASP F 98
REMARK 465 MET F 99
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 ARG A 79 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 82 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 188 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 216 CG CD CE NZ
REMARK 470 GLU A 219 CG CD OE1 OE2
REMARK 470 GLU A 220 CG CD OE1 OE2
REMARK 470 ILE A 221 CG1 CG2 CD1
REMARK 470 GLN A 223 CG CD OE1 NE2
REMARK 470 GLU A 224 CG CD OE1 OE2
REMARK 470 LEU A 246 CG CD1 CD2
REMARK 470 ASP A 247 CG OD1 OD2
REMARK 470 GLN A 249 CG CD OE1 NE2
REMARK 470 LEU A 253 CG CD1 CD2
REMARK 470 ILE B 4 CD1
REMARK 470 ARG B 122 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 147 CG CD CE NZ
REMARK 470 ASP B 148 CG OD1 OD2
REMARK 470 TRP G 96 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP G 96 CZ3 CH2
REMARK 470 GLU G 99 CG CD OE1 OE2
REMARK 470 GLU G 133 CG CD OE1 OE2
REMARK 470 LYS H 19 CG CD CE NZ
REMARK 470 LYS H 41 CG CD CE NZ
REMARK 470 GLU H 74 CG CD OE1 OE2
REMARK 470 LYS H 75 CG CD CE NZ
REMARK 470 GLN H 89 CG CD OE1 NE2
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 GLU C 224 CG CD OE1 OE2
REMARK 470 LEU C 253 CG CD1 CD2
REMARK 470 ILE D 4 CD1
REMARK 470 ARG D 122 CG CD NE CZ NH1 NH2
REMARK 470 ASP D 123 CG OD1 OD2
REMARK 470 LYS D 125 CG CD CE NZ
REMARK 470 ASP D 128 CG OD1 OD2
REMARK 470 LYS D 129 CG CD CE NZ
REMARK 470 LYS D 147 CG CD CE NZ
REMARK 470 ASP D 148 CG OD1 OD2
REMARK 470 GLU E 108 CG CD OE1 OE2
REMARK 470 GLU E 133 CG CD OE1 OE2
REMARK 470 LYS F 19 CG CD CE NZ
REMARK 470 LYS F 75 CG CD CE NZ
REMARK 470 GLN F 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 O TYR G 64 O HOH G 301 2.00
REMARK 500 O LEU C 246 O HOH C 401 2.02
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 LEU C 246 CA - CB - CG ANGL. DEV. = 16.1 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 29 -123.07 51.60
REMARK 500 PHE A 119 -59.74 -129.60
REMARK 500 ASN A 217 -113.37 55.71
REMARK 500 GLN B 2 -70.43 -94.25
REMARK 500 VAL B 50 -26.89 -140.28
REMARK 500 LYS B 57 75.14 -151.40
REMARK 500 ILE G 46 -61.44 -92.63
REMARK 500 SER G 87 -179.67 -174.39
REMARK 500 HIS G 168 -34.10 -134.81
REMARK 500 PRO H 32 -165.68 -75.28
REMARK 500 LYS H 48 41.48 -77.09
REMARK 500 TRP H 60 -3.09 77.79
REMARK 500 ASP C 29 -125.54 51.24
REMARK 500 PHE C 119 -59.80 -131.48
REMARK 500 THR C 191 -105.48 -92.43
REMARK 500 ASN C 217 8.81 57.30
REMARK 500 GLN D 2 -70.98 -94.89
REMARK 500 ASP D 115 57.98 -149.17
REMARK 500 LYS D 129 168.33 75.77
REMARK 500 ILE E 46 -64.32 -92.91
REMARK 500 SER E 87 -179.85 -175.08
REMARK 500 HIS E 168 -34.87 -131.91
REMARK 500 PRO F 32 -165.93 -74.34
REMARK 500 LYS F 48 48.35 -78.47
REMARK 500 TRP F 60 -4.51 78.53
REMARK 500 ASP F 96 -166.42 -108.39
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7ZV C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT F 101
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: 5U1R RELATED DB: PDB
REMARK 900 RELATED ID: 5U6Q RELATED DB: PDB
REMARK 900 RELATED ID: 5U2V RELATED DB: PDB
DBREF 5U72 A 1 270 UNP Q95460 HMR1_HUMAN 23 292
DBREF 5U72 B 1 203 PDB 5U72 5U72 1 203
DBREF 5U72 G 1 245 PDB 5U72 5U72 1 245
DBREF 5U72 H 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 5U72 C 1 270 UNP Q95460 HMR1_HUMAN 23 292
DBREF 5U72 D 1 203 PDB 5U72 5U72 1 203
DBREF 5U72 E 1 245 PDB 5U72 5U72 1 245
DBREF 5U72 F 1 99 UNP P61769 B2MG_HUMAN 21 119
SEQADV 5U72 MET A 0 UNP Q95460 INITIATING METHIONINE
SEQADV 5U72 SER A 261 UNP Q95460 CYS 283 CONFLICT
SEQADV 5U72 MET C 0 UNP Q95460 INITIATING METHIONINE
SEQADV 5U72 SER C 261 UNP Q95460 CYS 283 CONFLICT
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 99 ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG HIS
SEQRES 2 H 99 PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS TYR
SEQRES 3 H 99 VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP LEU
SEQRES 4 H 99 LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS SER
SEQRES 5 H 99 ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU LEU
SEQRES 6 H 99 TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU TYR
SEQRES 7 H 99 ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO LYS
SEQRES 8 H 99 ILE VAL LYS TRP ASP ARG ASP MET
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 99 ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG HIS
SEQRES 2 F 99 PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS TYR
SEQRES 3 F 99 VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP LEU
SEQRES 4 F 99 LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS SER
SEQRES 5 F 99 ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU LEU
SEQRES 6 F 99 TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU TYR
SEQRES 7 F 99 ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO LYS
SEQRES 8 F 99 ILE VAL LYS TRP ASP ARG ASP MET
HET ACT A 301 4
HET ACT A 302 4
HET GOL A 303 6
HET 7ZV C 301 20
HET DMS C 302 4
HET ACT F 101 4
HETNAM ACT ACETATE ION
HETNAM GOL GLYCEROL
HETNAM 7ZV 5-HYDROXYDICLOFENAC
HETNAM DMS DIMETHYL SULFOXIDE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN 7ZV 2-[2-[[2,6-BIS(CHLORANYL)PHENYL]AMINO]-5-OXIDANYL-
HETSYN 2 7ZV PHENYL]ETHANOIC ACID
FORMUL 9 ACT 3(C2 H3 O2 1-)
FORMUL 11 GOL C3 H8 O3
FORMUL 12 7ZV C14 H11 CL2 N O3
FORMUL 13 DMS C2 H6 O S
FORMUL 15 HOH *437(H2 O)
HELIX 1 AA1 ALA A 47 GLU A 52 1 6
HELIX 2 AA2 ALA A 55 ASN A 85 1 31
HELIX 3 AA3 ASP A 133 ALA A 145 1 13
HELIX 4 AA4 ASN A 146 GLU A 159 1 14
HELIX 5 AA5 GLU A 159 GLY A 172 1 14
HELIX 6 AA6 GLY A 172 GLN A 177 1 6
HELIX 7 AA7 GLN B 79 SER B 83 5 5
HELIX 8 AA8 ALA G 82 THR G 86 5 5
HELIX 9 AA9 ASP G 117 VAL G 121 5 5
HELIX 10 AB1 SER G 132 GLN G 140 1 9
HELIX 11 AB2 ALA G 199 GLN G 203 1 5
HELIX 12 AB3 ALA C 47 GLU C 52 1 6
HELIX 13 AB4 ALA C 55 ASN C 85 1 31
HELIX 14 AB5 ASP C 133 ALA C 145 1 13
HELIX 15 AB6 ASN C 146 GLU C 159 1 14
HELIX 16 AB7 GLU C 159 GLY C 172 1 14
HELIX 17 AB8 GLY C 172 GLN C 177 1 6
HELIX 18 AB9 GLN D 79 SER D 83 5 5
HELIX 19 AC1 ARG D 162 ASP D 165 5 4
HELIX 20 AC2 ALA E 82 THR E 86 5 5
HELIX 21 AC3 ASP E 117 VAL E 121 5 5
HELIX 22 AC4 SER E 132 GLN E 140 1 9
HELIX 23 AC5 ALA E 199 GLN E 203 1 5
SHEET 1 AA1 8 GLU A 44 PRO A 45 0
SHEET 2 AA1 8 HIS A 31 ASP A 37 -1 N THR A 35 O GLU A 44
SHEET 3 AA1 8 PHE A 22 VAL A 28 -1 N SER A 24 O TYR A 36
SHEET 4 AA1 8 HIS A 3 VAL A 12 -1 N LEU A 10 O ILE A 23
SHEET 5 AA1 8 THR A 91 LEU A 100 -1 O LEU A 100 N HIS A 3
SHEET 6 AA1 8 THR A 106 TYR A 114 -1 O ALA A 113 N GLN A 93
SHEET 7 AA1 8 GLN A 117 ASN A 123 -1 O PHE A 122 N LEU A 110
SHEET 8 AA1 8 SER A 128 ALA A 131 -1 O SER A 128 N ASN A 123
SHEET 1 AA2 4 LEU A 183 ASN A 187 0
SHEET 2 AA2 4 LEU A 198 PHE A 205 -1 O PHE A 199 N ASN A 187
SHEET 3 AA2 4 TYR A 238 ILE A 244 -1 O ALA A 240 N ALA A 202
SHEET 4 AA2 4 ASP A 226 TYR A 227 -1 N ASP A 226 O SER A 243
SHEET 1 AA3 4 LEU A 183 ASN A 187 0
SHEET 2 AA3 4 LEU A 198 PHE A 205 -1 O PHE A 199 N ASN A 187
SHEET 3 AA3 4 TYR A 238 ILE A 244 -1 O ALA A 240 N ALA A 202
SHEET 4 AA3 4 LEU A 231 PRO A 232 -1 N LEU A 231 O GLN A 239
SHEET 1 AA4 4 GLU A 219 GLU A 220 0
SHEET 2 AA4 4 TYR A 211 LYS A 216 -1 N LYS A 216 O GLU A 219
SHEET 3 AA4 4 TYR A 254 HIS A 260 -1 O HIS A 257 N THR A 213
SHEET 4 AA4 4 VAL A 263 GLN A 268 -1 O LEU A 267 N CYS A 256
SHEET 1 AA5 5 ASN B 3 ASP B 5 0
SHEET 2 AA5 5 VAL B 18 GLN B 25 -1 O THR B 23 N ASP B 5
SHEET 3 AA5 5 TYR B 70 LEU B 75 -1 O LEU B 75 N VAL B 18
SHEET 4 AA5 5 PHE B 60 SER B 65 -1 N SER B 61 O LEU B 74
SHEET 5 AA5 5 GLY B 53 LYS B 57 -1 N GLU B 55 O SER B 62
SHEET 1 AA6 5 GLU B 9 THR B 13 0
SHEET 2 AA6 5 THR B 103 LYS B 108 1 O ILE B 106 N MET B 10
SHEET 3 AA6 5 ALA B 84 LYS B 91 -1 N ALA B 84 O LEU B 105
SHEET 4 AA6 5 LEU B 32 GLN B 37 -1 N PHE B 33 O ALA B 89
SHEET 5 AA6 5 THR B 44 ASN B 49 -1 O ASN B 49 N LEU B 32
SHEET 1 AA7 4 GLU B 9 THR B 13 0
SHEET 2 AA7 4 THR B 103 LYS B 108 1 O ILE B 106 N MET B 10
SHEET 3 AA7 4 ALA B 84 LYS B 91 -1 N ALA B 84 O LEU B 105
SHEET 4 AA7 4 LEU B 97 TRP B 99 -1 O ILE B 98 N VAL B 90
SHEET 1 AA8 4 ALA B 117 GLN B 120 0
SHEET 2 AA8 4 SER B 130 THR B 135 -1 O LEU B 133 N TYR B 119
SHEET 3 AA8 4 PHE B 166 SER B 175 -1 O ALA B 173 N CYS B 132
SHEET 4 AA8 4 TYR B 152 ILE B 153 -1 N TYR B 152 O TRP B 174
SHEET 1 AA9 4 ALA B 117 GLN B 120 0
SHEET 2 AA9 4 SER B 130 THR B 135 -1 O LEU B 133 N TYR B 119
SHEET 3 AA9 4 PHE B 166 SER B 175 -1 O ALA B 173 N CYS B 132
SHEET 4 AA9 4 CYS B 157 MET B 161 -1 N MET B 161 O PHE B 166
SHEET 1 AB1 4 VAL G 4 THR G 7 0
SHEET 2 AB1 4 MET G 19 GLN G 25 -1 O ALA G 24 N THR G 5
SHEET 3 AB1 4 PHE G 74 LEU G 78 -1 O LEU G 76 N LEU G 21
SHEET 4 AB1 4 TYR G 64 ARG G 68 -1 N ASN G 65 O ARG G 77
SHEET 1 AB2 6 PHE G 10 LYS G 14 0
SHEET 2 AB2 6 SER G 110 LEU G 115 1 O LEU G 115 N LEU G 13
SHEET 3 AB2 6 SER G 87 SER G 94 -1 N SER G 87 O LEU G 112
SHEET 4 AB2 6 SER G 31 GLN G 37 -1 N TYR G 33 O ALA G 92
SHEET 5 AB2 6 ARG G 44 SER G 51 -1 O ILE G 46 N TRP G 34
SHEET 6 AB2 6 THR G 54 LYS G 57 -1 O ASP G 56 N TYR G 48
SHEET 1 AB3 4 PHE G 10 LYS G 14 0
SHEET 2 AB3 4 SER G 110 LEU G 115 1 O LEU G 115 N LEU G 13
SHEET 3 AB3 4 SER G 87 SER G 94 -1 N SER G 87 O LEU G 112
SHEET 4 AB3 4 PHE G 105 PHE G 106 -1 O PHE G 105 N SER G 93
SHEET 1 AB4 4 GLU G 125 PHE G 129 0
SHEET 2 AB4 4 LYS G 141 PHE G 151 -1 O VAL G 145 N PHE G 129
SHEET 3 AB4 4 TYR G 189 SER G 198 -1 O VAL G 197 N ALA G 142
SHEET 4 AB4 4 VAL G 171 THR G 173 -1 N CYS G 172 O ARG G 194
SHEET 1 AB5 4 GLU G 125 PHE G 129 0
SHEET 2 AB5 4 LYS G 141 PHE G 151 -1 O VAL G 145 N PHE G 129
SHEET 3 AB5 4 TYR G 189 SER G 198 -1 O VAL G 197 N ALA G 142
SHEET 4 AB5 4 LEU G 178 LYS G 179 -1 N LEU G 178 O ALA G 190
SHEET 1 AB6 4 LYS G 165 VAL G 167 0
SHEET 2 AB6 4 VAL G 156 VAL G 162 -1 N VAL G 162 O LYS G 165
SHEET 3 AB6 4 HIS G 208 PHE G 215 -1 O GLN G 212 N SER G 159
SHEET 4 AB6 4 GLN G 234 TRP G 241 -1 O ALA G 240 N PHE G 209
SHEET 1 AB7 4 LYS H 6 SER H 11 0
SHEET 2 AB7 4 ASN H 21 PHE H 30 -1 O ASN H 24 N TYR H 10
SHEET 3 AB7 4 PHE H 62 PHE H 70 -1 O PHE H 70 N ASN H 21
SHEET 4 AB7 4 GLU H 50 HIS H 51 -1 N GLU H 50 O TYR H 67
SHEET 1 AB8 4 LYS H 6 SER H 11 0
SHEET 2 AB8 4 ASN H 21 PHE H 30 -1 O ASN H 24 N TYR H 10
SHEET 3 AB8 4 PHE H 62 PHE H 70 -1 O PHE H 70 N ASN H 21
SHEET 4 AB8 4 SER H 55 PHE H 56 -1 N SER H 55 O TYR H 63
SHEET 1 AB9 4 GLU H 44 ARG H 45 0
SHEET 2 AB9 4 GLU H 36 LYS H 41 -1 N LYS H 41 O GLU H 44
SHEET 3 AB9 4 TYR H 78 ASN H 83 -1 O ALA H 79 N LEU H 40
SHEET 4 AB9 4 LYS H 91 LYS H 94 -1 O LYS H 91 N VAL H 82
SHEET 1 AC1 8 GLU C 44 PRO C 45 0
SHEET 2 AC1 8 HIS C 31 ASP C 37 -1 N THR C 35 O GLU C 44
SHEET 3 AC1 8 PHE C 22 VAL C 28 -1 N SER C 24 O TYR C 36
SHEET 4 AC1 8 HIS C 3 VAL C 12 -1 N PHE C 8 O VAL C 25
SHEET 5 AC1 8 THR C 91 LEU C 100 -1 O ILE C 96 N TYR C 7
SHEET 6 AC1 8 THR C 106 TYR C 114 -1 O GLN C 111 N MET C 95
SHEET 7 AC1 8 GLN C 117 ASN C 123 -1 O PHE C 122 N LEU C 110
SHEET 8 AC1 8 SER C 128 ALA C 131 -1 O LEU C 130 N ILE C 121
SHEET 1 AC2 4 LEU C 183 GLU C 190 0
SHEET 2 AC2 4 THR C 196 PHE C 205 -1 O PHE C 199 N ASN C 187
SHEET 3 AC2 4 TYR C 238 LEU C 246 -1 O ALA C 240 N ALA C 202
SHEET 4 AC2 4 ASP C 226 TYR C 227 -1 N ASP C 226 O SER C 243
SHEET 1 AC3 4 LEU C 183 GLU C 190 0
SHEET 2 AC3 4 THR C 196 PHE C 205 -1 O PHE C 199 N ASN C 187
SHEET 3 AC3 4 TYR C 238 LEU C 246 -1 O ALA C 240 N ALA C 202
SHEET 4 AC3 4 LEU C 231 PRO C 232 -1 N LEU C 231 O GLN C 239
SHEET 1 AC4 4 GLU C 219 GLU C 220 0
SHEET 2 AC4 4 TYR C 211 LYS C 216 -1 N LYS C 216 O GLU C 219
SHEET 3 AC4 4 TYR C 254 HIS C 260 -1 O HIS C 257 N THR C 213
SHEET 4 AC4 4 VAL C 263 GLN C 268 -1 O LEU C 267 N CYS C 256
SHEET 1 AC5 5 ASN D 3 ASP D 5 0
SHEET 2 AC5 5 VAL D 18 GLN D 25 -1 O THR D 23 N ASP D 5
SHEET 3 AC5 5 TYR D 70 LEU D 75 -1 O SER D 71 N CYS D 22
SHEET 4 AC5 5 PHE D 60 SER D 65 -1 N SER D 61 O LEU D 74
SHEET 5 AC5 5 GLY D 53 LYS D 57 -1 N LYS D 57 O PHE D 60
SHEET 1 AC6 5 GLU D 9 THR D 13 0
SHEET 2 AC6 5 THR D 103 LYS D 108 1 O ILE D 106 N MET D 10
SHEET 3 AC6 5 ALA D 84 LYS D 91 -1 N ALA D 84 O LEU D 105
SHEET 4 AC6 5 LEU D 32 GLN D 37 -1 N PHE D 33 O ALA D 89
SHEET 5 AC6 5 THR D 44 ASN D 49 -1 O ASN D 49 N LEU D 32
SHEET 1 AC7 4 GLU D 9 THR D 13 0
SHEET 2 AC7 4 THR D 103 LYS D 108 1 O ILE D 106 N MET D 10
SHEET 3 AC7 4 ALA D 84 LYS D 91 -1 N ALA D 84 O LEU D 105
SHEET 4 AC7 4 LEU D 97 TRP D 99 -1 O ILE D 98 N VAL D 90
SHEET 1 AC8 4 ALA D 117 LEU D 121 0
SHEET 2 AC8 4 SER D 130 THR D 135 -1 O LEU D 133 N TYR D 119
SHEET 3 AC8 4 PHE D 166 SER D 175 -1 O ALA D 173 N CYS D 132
SHEET 4 AC8 4 VAL D 151 ILE D 153 -1 N TYR D 152 O TRP D 174
SHEET 1 AC9 4 ALA D 117 LEU D 121 0
SHEET 2 AC9 4 SER D 130 THR D 135 -1 O LEU D 133 N TYR D 119
SHEET 3 AC9 4 PHE D 166 SER D 175 -1 O ALA D 173 N CYS D 132
SHEET 4 AC9 4 CYS D 157 MET D 161 -1 N CYS D 157 O SER D 170
SHEET 1 AD1 4 VAL E 4 THR E 7 0
SHEET 2 AD1 4 MET E 19 GLN E 25 -1 O ALA E 24 N THR E 5
SHEET 3 AD1 4 PHE E 74 LEU E 78 -1 O LEU E 78 N MET E 19
SHEET 4 AD1 4 TYR E 64 ARG E 68 -1 N ASN E 65 O ARG E 77
SHEET 1 AD2 6 PHE E 10 LYS E 14 0
SHEET 2 AD2 6 SER E 110 LEU E 115 1 O LEU E 115 N LEU E 13
SHEET 3 AD2 6 SER E 87 SER E 94 -1 N SER E 87 O LEU E 112
SHEET 4 AD2 6 SER E 31 GLN E 37 -1 N GLN E 37 O VAL E 88
SHEET 5 AD2 6 ARG E 44 SER E 51 -1 O ILE E 46 N TRP E 34
SHEET 6 AD2 6 THR E 54 LYS E 57 -1 O ASP E 56 N TYR E 48
SHEET 1 AD3 4 PHE E 10 LYS E 14 0
SHEET 2 AD3 4 SER E 110 LEU E 115 1 O LEU E 115 N LEU E 13
SHEET 3 AD3 4 SER E 87 SER E 94 -1 N SER E 87 O LEU E 112
SHEET 4 AD3 4 PHE E 105 PHE E 106 -1 O PHE E 105 N SER E 93
SHEET 1 AD4 4 GLU E 125 PHE E 129 0
SHEET 2 AD4 4 LYS E 141 PHE E 151 -1 O VAL E 145 N PHE E 129
SHEET 3 AD4 4 TYR E 189 SER E 198 -1 O TYR E 189 N PHE E 151
SHEET 4 AD4 4 VAL E 171 THR E 173 -1 N CYS E 172 O ARG E 194
SHEET 1 AD5 4 GLU E 125 PHE E 129 0
SHEET 2 AD5 4 LYS E 141 PHE E 151 -1 O VAL E 145 N PHE E 129
SHEET 3 AD5 4 TYR E 189 SER E 198 -1 O TYR E 189 N PHE E 151
SHEET 4 AD5 4 LEU E 178 LYS E 179 -1 N LEU E 178 O ALA E 190
SHEET 1 AD6 4 LYS E 165 VAL E 167 0
SHEET 2 AD6 4 VAL E 156 VAL E 162 -1 N VAL E 162 O LYS E 165
SHEET 3 AD6 4 HIS E 208 PHE E 215 -1 O ARG E 210 N TRP E 161
SHEET 4 AD6 4 GLN E 234 TRP E 241 -1 O GLN E 234 N PHE E 215
SHEET 1 AD7 4 LYS F 6 SER F 11 0
SHEET 2 AD7 4 ASN F 21 PHE F 30 -1 O SER F 28 N LYS F 6
SHEET 3 AD7 4 PHE F 62 PHE F 70 -1 O PHE F 70 N ASN F 21
SHEET 4 AD7 4 GLU F 50 HIS F 51 -1 N GLU F 50 O TYR F 67
SHEET 1 AD8 4 LYS F 6 SER F 11 0
SHEET 2 AD8 4 ASN F 21 PHE F 30 -1 O SER F 28 N LYS F 6
SHEET 3 AD8 4 PHE F 62 PHE F 70 -1 O PHE F 70 N ASN F 21
SHEET 4 AD8 4 SER F 55 PHE F 56 -1 N SER F 55 O TYR F 63
SHEET 1 AD9 4 GLU F 44 ARG F 45 0
SHEET 2 AD9 4 ILE F 35 LYS F 41 -1 N LYS F 41 O GLU F 44
SHEET 3 AD9 4 TYR F 78 HIS F 84 -1 O ARG F 81 N ASP F 38
SHEET 4 AD9 4 LYS F 91 LYS F 94 -1 O LYS F 91 N VAL F 82
SSBOND 1 CYS A 98 CYS A 161 1555 1555 2.04
SSBOND 2 CYS A 200 CYS A 256 1555 1555 2.03
SSBOND 3 CYS B 22 CYS B 88 1555 1555 2.02
SSBOND 4 CYS B 132 CYS B 182 1555 1555 2.03
SSBOND 5 CYS B 157 CYS G 172 1555 1555 2.03
SSBOND 6 CYS G 23 CYS G 91 1555 1555 2.01
SSBOND 7 CYS G 146 CYS G 211 1555 1555 2.00
SSBOND 8 CYS H 25 CYS H 80 1555 1555 2.03
SSBOND 9 CYS C 98 CYS C 161 1555 1555 2.04
SSBOND 10 CYS C 200 CYS C 256 1555 1555 2.03
SSBOND 11 CYS D 22 CYS D 88 1555 1555 2.02
SSBOND 12 CYS D 132 CYS D 182 1555 1555 2.03
SSBOND 13 CYS D 157 CYS E 172 1555 1555 2.03
SSBOND 14 CYS E 23 CYS E 91 1555 1555 2.03
SSBOND 15 CYS E 146 CYS E 211 1555 1555 2.02
SSBOND 16 CYS F 25 CYS F 80 1555 1555 2.04
CISPEP 1 TYR A 206 PRO A 207 0 1.61
CISPEP 2 THR G 7 PRO G 8 0 -1.53
CISPEP 3 TYR G 152 PRO G 153 0 -0.86
CISPEP 4 HIS H 31 PRO H 32 0 0.45
CISPEP 5 TYR C 206 PRO C 207 0 1.52
CISPEP 6 THR E 7 PRO E 8 0 -2.55
CISPEP 7 TYR E 152 PRO E 153 0 0.88
CISPEP 8 HIS F 31 PRO F 32 0 1.61
SITE 1 AC1 4 GLU A 160 TRP A 164 ARG A 167 SER B 93
SITE 1 AC2 5 THR A 2 SER A 4 ASP A 29 GLU A 99
SITE 2 AC2 5 HOH A 410
SITE 1 AC3 4 GLN A 64 ARG A 67 THR G 55 ASP G 56
SITE 1 AC4 14 TYR C 7 ARG C 9 SER C 24 LYS C 43
SITE 2 AC4 14 TYR C 62 LEU C 65 LEU C 66 TRP C 69
SITE 3 AC4 14 TRP C 156 TRP C 164 HOH C 415 HOH C 439
SITE 4 AC4 14 TYR D 95 GLU E 99
SITE 1 AC5 6 GLU C 160 ALA C 163 TRP C 164 ARG C 167
SITE 2 AC5 6 SER D 27 SER D 93
SITE 1 AC6 3 LYS F 6 ILE F 7 LYS F 91
CRYST1 213.090 69.600 142.370 90.00 103.72 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 0.004693 0.000000 0.001146 0.00000
SCALE2 0.000000 0.014368 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007230 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
