HEADER IMMUNE SYSTEM 07-JUN-16 5KD7
TITLE CRYSTAL STRUCTURE OF MURINE MHC-I H-2DD IN COMPLEX WITH MURINE BETA2-
TITLE 2 MICROGLOBULIN AND A VARIANT OF PEPTIDE (PV9) OF HIV GP120 MN ISOLATE
TITLE 3 (IGPGRAFYV)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: H-2 CLASS I HISTOCOMPATIBILITY ANTIGEN, D-D ALPHA CHAIN;
COMPND 3 CHAIN: A, C, F, I;
COMPND 4 SYNONYM: H-2D(D);
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: BETA-2-MICROGLOBULIN;
COMPND 8 CHAIN: B, D, G, J;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 3;
COMPND 11 MOLECULE: PEPTIDE (PV9) OF HIV GP120 MN ISOLATE (IGPGRAFYV);
COMPND 12 CHAIN: P, E, H, K;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: H2-D1;
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: PET21-B;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 13 ORGANISM_COMMON: MOUSE;
SOURCE 14 ORGANISM_TAXID: 10090;
SOURCE 15 GENE: B2M;
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: PET3A;
SOURCE 21 MOL_ID: 3;
SOURCE 22 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 GROUP M
SOURCE 23 SUBTYPE B (ISOLATE MN);
SOURCE 24 ORGANISM_TAXID: 11696;
SOURCE 25 EXPRESSION_SYSTEM: SYNTHETIC CONSTRUCT;
SOURCE 26 EXPRESSION_SYSTEM_TAXID: 32630
KEYWDS MAJOR HISTOMPATIBILITY COMPLEX CLASS I, MHC-I, H2-DD, H-2DD, HIV
KEYWDS 2 PEPTIDE, PVI10, PV9, GLYCOPROTEIN, IMMUNE RESPONSE, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR J.JIANG,K.NATARAJAN,D.MARGULIES
REVDAT 5 27-SEP-23 5KD7 1 REMARK
REVDAT 4 19-FEB-20 5KD7 1 SOURCE REMARK
REVDAT 3 28-FEB-18 5KD7 1 JRNL
REVDAT 2 07-FEB-18 5KD7 1 JRNL
REVDAT 1 11-OCT-17 5KD7 0
JRNL AUTH B.F.FREY,J.JIANG,Y.SUI,L.F.BOYD,B.YU,G.TATSUNO,R.BILLESKOV,
JRNL AUTH 2 S.SOLAYMANI-MOHAMMADI,P.W.BERMAN,D.H.MARGULIES,J.A.BERZOFSKY
JRNL TITL EFFECTS OF CROSS-PRESENTATION, ANTIGEN PROCESSING, AND
JRNL TITL 2 PEPTIDE BINDING IN HIV EVASION OF T CELL IMMUNITY.
JRNL REF J. IMMUNOL. V. 200 1853 2018
JRNL REFN ESSN 1550-6606
JRNL PMID 29374075
JRNL DOI 10.4049/JIMMUNOL.1701523
REMARK 2
REMARK 2 RESOLUTION. 2.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
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) : 2.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.72
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 72716
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.770
REMARK 3 FREE R VALUE TEST SET COUNT : 2011
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 42.7264 - 5.6596 0.99 5089 150 0.1588 0.2031
REMARK 3 2 5.6596 - 4.4938 0.99 5164 142 0.1406 0.1683
REMARK 3 3 4.4938 - 3.9262 0.99 5073 146 0.1497 0.1814
REMARK 3 4 3.9262 - 3.5674 0.99 5124 135 0.1815 0.2281
REMARK 3 5 3.5674 - 3.3118 0.99 5095 154 0.2066 0.2745
REMARK 3 6 3.3118 - 3.1166 0.98 5084 146 0.2177 0.2525
REMARK 3 7 3.1166 - 2.9606 0.98 5060 138 0.2446 0.3115
REMARK 3 8 2.9606 - 2.8317 0.98 5043 147 0.2414 0.2919
REMARK 3 9 2.8317 - 2.7227 0.97 5033 144 0.2372 0.3084
REMARK 3 10 2.7227 - 2.6288 0.97 5051 142 0.2449 0.3279
REMARK 3 11 2.6288 - 2.5466 0.97 4960 156 0.2542 0.3496
REMARK 3 12 2.5466 - 2.4738 0.97 4998 136 0.2572 0.3363
REMARK 3 13 2.4738 - 2.4087 0.97 4999 131 0.2760 0.3304
REMARK 3 14 2.4087 - 2.3499 0.96 4932 144 0.2910 0.3247
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) : 0.320
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.390
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 12810
REMARK 3 ANGLE : 0.777 17388
REMARK 3 CHIRALITY : 0.045 1764
REMARK 3 PLANARITY : 0.005 2267
REMARK 3 DIHEDRAL : 14.720 7589
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 57
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 56 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.1357 51.7749 1.1833
REMARK 3 T TENSOR
REMARK 3 T11: 0.4196 T22: 0.3787
REMARK 3 T33: 0.2292 T12: 0.1601
REMARK 3 T13: -0.0697 T23: 0.0388
REMARK 3 L TENSOR
REMARK 3 L11: 2.8384 L22: 8.6234
REMARK 3 L33: 2.4521 L12: 1.8308
REMARK 3 L13: 0.1231 L23: -0.7488
REMARK 3 S TENSOR
REMARK 3 S11: -0.1054 S12: -0.0591 S13: -0.1361
REMARK 3 S21: 0.3769 S22: -0.1852 S23: -0.6806
REMARK 3 S31: 0.2070 S32: 0.4090 S33: 0.2655
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 57 THROUGH 137 )
REMARK 3 ORIGIN FOR THE GROUP (A): -31.5739 59.8191 -3.0158
REMARK 3 T TENSOR
REMARK 3 T11: 0.3359 T22: 0.3660
REMARK 3 T33: 0.1584 T12: 0.1551
REMARK 3 T13: -0.0395 T23: 0.0052
REMARK 3 L TENSOR
REMARK 3 L11: 2.1061 L22: 3.1158
REMARK 3 L33: 2.7611 L12: -0.0214
REMARK 3 L13: 0.3272 L23: -0.5328
REMARK 3 S TENSOR
REMARK 3 S11: -0.1039 S12: -0.0303 S13: 0.0677
REMARK 3 S21: 0.2730 S22: 0.0166 S23: -0.0244
REMARK 3 S31: -0.0913 S32: -0.2871 S33: 0.0865
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 138 THROUGH 162 )
REMARK 3 ORIGIN FOR THE GROUP (A): -39.7456 62.0837 -9.9292
REMARK 3 T TENSOR
REMARK 3 T11: 0.3103 T22: 0.5596
REMARK 3 T33: 0.2783 T12: 0.1716
REMARK 3 T13: 0.0005 T23: 0.0345
REMARK 3 L TENSOR
REMARK 3 L11: 4.1668 L22: 7.4601
REMARK 3 L33: 4.2422 L12: 0.4126
REMARK 3 L13: 1.6470 L23: -1.3860
REMARK 3 S TENSOR
REMARK 3 S11: 0.1269 S12: 0.2891 S13: 0.2881
REMARK 3 S21: 0.0703 S22: 0.0971 S23: 0.7111
REMARK 3 S31: -0.0177 S32: -0.9130 S33: -0.1196
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 163 THROUGH 219 )
REMARK 3 ORIGIN FOR THE GROUP (A): -30.9304 40.4585 20.7882
REMARK 3 T TENSOR
REMARK 3 T11: 0.2215 T22: 0.3839
REMARK 3 T33: 0.2681 T12: -0.0504
REMARK 3 T13: 0.0021 T23: -0.0308
REMARK 3 L TENSOR
REMARK 3 L11: 1.2004 L22: 1.6967
REMARK 3 L33: 2.6780 L12: 0.2323
REMARK 3 L13: -0.3869 L23: -0.4656
REMARK 3 S TENSOR
REMARK 3 S11: 0.0140 S12: -0.2666 S13: 0.0199
REMARK 3 S21: -0.3109 S22: -0.3413 S23: 0.2447
REMARK 3 S31: 0.7763 S32: -0.9583 S33: 0.2990
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 220 THROUGH 274 )
REMARK 3 ORIGIN FOR THE GROUP (A): -34.7691 40.8101 31.7793
REMARK 3 T TENSOR
REMARK 3 T11: 0.3184 T22: 0.8026
REMARK 3 T33: 0.3257 T12: -0.2435
REMARK 3 T13: 0.0293 T23: -0.0453
REMARK 3 L TENSOR
REMARK 3 L11: 0.3907 L22: 0.8006
REMARK 3 L33: 4.0356 L12: 0.4987
REMARK 3 L13: -0.8058 L23: -0.5213
REMARK 3 S TENSOR
REMARK 3 S11: 0.1337 S12: -0.3797 S13: 0.0709
REMARK 3 S21: 0.1091 S22: -0.2946 S23: 0.4418
REMARK 3 S31: 0.7587 S32: -1.4441 S33: 0.0722
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 19 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.1815 50.5243 25.2497
REMARK 3 T TENSOR
REMARK 3 T11: 0.2672 T22: 0.1293
REMARK 3 T33: 0.1128 T12: 0.0157
REMARK 3 T13: -0.0335 T23: -0.0118
REMARK 3 L TENSOR
REMARK 3 L11: 2.3869 L22: 1.5371
REMARK 3 L33: 2.0481 L12: 1.5726
REMARK 3 L13: -0.9093 L23: 0.3251
REMARK 3 S TENSOR
REMARK 3 S11: -0.0578 S12: -0.0180 S13: -0.0102
REMARK 3 S21: 0.0759 S22: 0.0135 S23: 0.1161
REMARK 3 S31: -0.2864 S32: -0.2363 S33: 0.0332
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 20 THROUGH 51 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.3575 55.9237 20.4376
REMARK 3 T TENSOR
REMARK 3 T11: 0.3315 T22: 0.2307
REMARK 3 T33: 0.2507 T12: 0.0078
REMARK 3 T13: 0.0373 T23: 0.0508
REMARK 3 L TENSOR
REMARK 3 L11: 1.7521 L22: 2.9272
REMARK 3 L33: 3.8393 L12: -1.8505
REMARK 3 L13: 2.4287 L23: -2.6638
REMARK 3 S TENSOR
REMARK 3 S11: -0.0490 S12: 0.2314 S13: 0.1273
REMARK 3 S21: -0.3838 S22: -0.2472 S23: -0.1677
REMARK 3 S31: -0.6313 S32: 0.5649 S33: 0.2834
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 52 THROUGH 77 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.3639 52.3341 19.1814
REMARK 3 T TENSOR
REMARK 3 T11: 0.2805 T22: 0.1547
REMARK 3 T33: 0.2709 T12: 0.0169
REMARK 3 T13: 0.0549 T23: 0.0272
REMARK 3 L TENSOR
REMARK 3 L11: 8.8246 L22: 5.8497
REMARK 3 L33: 6.8864 L12: -5.2101
REMARK 3 L13: 6.9198 L23: -4.0914
REMARK 3 S TENSOR
REMARK 3 S11: 0.4986 S12: 0.2077 S13: -0.2782
REMARK 3 S21: -1.0400 S22: -0.2757 S23: 0.0060
REMARK 3 S31: 0.3111 S32: -0.1139 S33: -0.1624
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 78 THROUGH 99 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.3223 59.2387 27.9204
REMARK 3 T TENSOR
REMARK 3 T11: 0.4529 T22: 0.1679
REMARK 3 T33: 0.2526 T12: -0.0385
REMARK 3 T13: -0.0331 T23: 0.0033
REMARK 3 L TENSOR
REMARK 3 L11: 2.0285 L22: 5.4898
REMARK 3 L33: 3.6520 L12: -1.3874
REMARK 3 L13: 1.2697 L23: -3.0707
REMARK 3 S TENSOR
REMARK 3 S11: -0.0927 S12: -0.1585 S13: 0.2783
REMARK 3 S21: 0.1688 S22: -0.2592 S23: -0.2253
REMARK 3 S31: -0.8848 S32: -0.1032 S33: 0.3358
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'P' AND (RESID 1 THROUGH 9 )
REMARK 3 ORIGIN FOR THE GROUP (A): -30.2706 59.4644 -9.6049
REMARK 3 T TENSOR
REMARK 3 T11: 0.2225 T22: 0.3228
REMARK 3 T33: 0.2657 T12: 0.1102
REMARK 3 T13: -0.0259 T23: -0.0386
REMARK 3 L TENSOR
REMARK 3 L11: 2.2085 L22: 3.9994
REMARK 3 L33: 3.5656 L12: 2.4145
REMARK 3 L13: 0.0501 L23: -2.1426
REMARK 3 S TENSOR
REMARK 3 S11: 0.0467 S12: 0.1478 S13: 0.1632
REMARK 3 S21: 0.0228 S22: -0.1366 S23: 0.1431
REMARK 3 S31: -0.2075 S32: -0.1057 S33: 0.0835
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 2 THROUGH 56 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.5996 90.2229 41.9664
REMARK 3 T TENSOR
REMARK 3 T11: 0.5002 T22: 0.1817
REMARK 3 T33: 0.3245 T12: -0.1112
REMARK 3 T13: -0.1136 T23: 0.0135
REMARK 3 L TENSOR
REMARK 3 L11: 1.7684 L22: 6.0273
REMARK 3 L33: 1.3574 L12: -0.8089
REMARK 3 L13: -0.4423 L23: -0.4694
REMARK 3 S TENSOR
REMARK 3 S11: -0.0491 S12: 0.2078 S13: 0.1482
REMARK 3 S21: -0.4223 S22: -0.1207 S23: -0.1748
REMARK 3 S31: -0.5623 S32: 0.3710 S33: 0.1091
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 57 THROUGH 162 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.9793 81.2217 49.1688
REMARK 3 T TENSOR
REMARK 3 T11: 0.2257 T22: 0.1942
REMARK 3 T33: 0.2307 T12: -0.0371
REMARK 3 T13: -0.1168 T23: -0.0090
REMARK 3 L TENSOR
REMARK 3 L11: 2.3310 L22: 3.3765
REMARK 3 L33: 2.8842 L12: 0.3493
REMARK 3 L13: -0.9109 L23: 0.1486
REMARK 3 S TENSOR
REMARK 3 S11: -0.0242 S12: -0.0209 S13: 0.0836
REMARK 3 S21: -0.1618 S22: -0.1521 S23: 0.3402
REMARK 3 S31: -0.2718 S32: -0.3124 S33: 0.1626
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 163 THROUGH 219 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.1444 99.8249 23.1664
REMARK 3 T TENSOR
REMARK 3 T11: 0.2708 T22: 0.1527
REMARK 3 T33: 0.2852 T12: 0.0369
REMARK 3 T13: -0.0270 T23: -0.0686
REMARK 3 L TENSOR
REMARK 3 L11: 2.1863 L22: 1.8102
REMARK 3 L33: 5.3452 L12: -0.2265
REMARK 3 L13: -0.3173 L23: -1.0699
REMARK 3 S TENSOR
REMARK 3 S11: 0.0204 S12: 0.4237 S13: -0.1360
REMARK 3 S21: 0.0566 S22: -0.0666 S23: -0.0477
REMARK 3 S31: -0.0844 S32: -0.0976 S33: 0.0273
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 220 THROUGH 240 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.1420 93.4736 15.7225
REMARK 3 T TENSOR
REMARK 3 T11: 0.4228 T22: 0.6596
REMARK 3 T33: 0.5241 T12: -0.0364
REMARK 3 T13: -0.1443 T23: -0.1555
REMARK 3 L TENSOR
REMARK 3 L11: 1.9796 L22: 3.9357
REMARK 3 L33: 3.0739 L12: -2.5027
REMARK 3 L13: 1.1549 L23: -2.3974
REMARK 3 S TENSOR
REMARK 3 S11: 0.3048 S12: 0.4776 S13: -0.5841
REMARK 3 S21: -0.7050 S22: -0.0214 S23: 0.8172
REMARK 3 S31: 0.3715 S32: -0.8361 S33: -0.2076
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 241 THROUGH 274 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.5550 100.4888 10.4243
REMARK 3 T TENSOR
REMARK 3 T11: 0.5480 T22: 0.7117
REMARK 3 T33: 0.3109 T12: 0.1972
REMARK 3 T13: -0.0627 T23: -0.0658
REMARK 3 L TENSOR
REMARK 3 L11: 1.7657 L22: 2.3060
REMARK 3 L33: 3.2356 L12: -0.3878
REMARK 3 L13: -1.0472 L23: 1.3929
REMARK 3 S TENSOR
REMARK 3 S11: 0.4317 S12: 1.3247 S13: -0.3019
REMARK 3 S21: -0.7425 S22: -0.4679 S23: 0.3927
REMARK 3 S31: -0.3339 S32: -0.9659 S33: 0.0336
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 0 THROUGH 5 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.4226 72.5528 28.1125
REMARK 3 T TENSOR
REMARK 3 T11: 0.9573 T22: 0.3360
REMARK 3 T33: 0.4367 T12: -0.0779
REMARK 3 T13: -0.0455 T23: -0.1883
REMARK 3 L TENSOR
REMARK 3 L11: 6.3147 L22: 5.4440
REMARK 3 L33: 5.3464 L12: 5.8633
REMARK 3 L13: -5.8106 L23: -5.3954
REMARK 3 S TENSOR
REMARK 3 S11: -0.1492 S12: -0.0535 S13: -0.6965
REMARK 3 S21: -0.0195 S22: -0.2114 S23: -0.2943
REMARK 3 S31: 1.2617 S32: -0.0077 S33: 0.3405
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 6 THROUGH 19 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.1148 95.4372 16.0995
REMARK 3 T TENSOR
REMARK 3 T11: 0.4370 T22: 0.3107
REMARK 3 T33: 0.4037 T12: -0.0469
REMARK 3 T13: -0.0059 T23: 0.0287
REMARK 3 L TENSOR
REMARK 3 L11: 4.4076 L22: 6.9245
REMARK 3 L33: 4.5946 L12: 5.5400
REMARK 3 L13: -4.5110 L23: -5.6470
REMARK 3 S TENSOR
REMARK 3 S11: 0.3313 S12: 0.4438 S13: 0.5580
REMARK 3 S21: 0.0288 S22: 0.3064 S23: 0.8842
REMARK 3 S31: -0.3194 S32: -0.0499 S33: -0.6744
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 20 THROUGH 35 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.9491 84.7215 25.5140
REMARK 3 T TENSOR
REMARK 3 T11: 0.4419 T22: 0.1608
REMARK 3 T33: 0.2556 T12: 0.0222
REMARK 3 T13: -0.0846 T23: -0.0463
REMARK 3 L TENSOR
REMARK 3 L11: 3.1772 L22: 6.6137
REMARK 3 L33: 7.6432 L12: 3.3724
REMARK 3 L13: -3.5501 L23: -6.5625
REMARK 3 S TENSOR
REMARK 3 S11: 0.1224 S12: -0.0567 S13: -0.0369
REMARK 3 S21: -0.0267 S22: 0.0414 S23: -0.0171
REMARK 3 S31: 0.2979 S32: 0.2872 S33: -0.1833
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 36 THROUGH 41 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.2748 82.8291 20.4169
REMARK 3 T TENSOR
REMARK 3 T11: 0.5688 T22: 0.5407
REMARK 3 T33: 0.4917 T12: 0.3643
REMARK 3 T13: -0.0777 T23: -0.0288
REMARK 3 L TENSOR
REMARK 3 L11: 7.8924 L22: 2.6396
REMARK 3 L33: 7.2866 L12: 4.2730
REMARK 3 L13: -7.2374 L23: -3.4809
REMARK 3 S TENSOR
REMARK 3 S11: -0.3669 S12: -0.1710 S13: -0.6278
REMARK 3 S21: -0.0349 S22: -0.3590 S23: -0.4882
REMARK 3 S31: 0.5374 S32: 0.4356 S33: 0.6754
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 42 THROUGH 52 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.4779 86.8462 22.0098
REMARK 3 T TENSOR
REMARK 3 T11: 0.5450 T22: 0.8420
REMARK 3 T33: 0.6047 T12: 0.1995
REMARK 3 T13: -0.0363 T23: -0.1219
REMARK 3 L TENSOR
REMARK 3 L11: 4.4395 L22: 3.9200
REMARK 3 L33: 4.4508 L12: -0.1543
REMARK 3 L13: -4.4313 L23: 0.4876
REMARK 3 S TENSOR
REMARK 3 S11: 0.5431 S12: -0.5982 S13: 0.1945
REMARK 3 S21: 0.3028 S22: 0.0475 S23: -0.9732
REMARK 3 S31: 0.0146 S32: 0.8706 S33: -0.5682
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 53 THROUGH 61 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.0100 83.6870 34.9442
REMARK 3 T TENSOR
REMARK 3 T11: 0.5076 T22: 0.2756
REMARK 3 T33: 0.3083 T12: -0.0532
REMARK 3 T13: -0.1074 T23: 0.0651
REMARK 3 L TENSOR
REMARK 3 L11: 3.0274 L22: 6.2123
REMARK 3 L33: 2.4153 L12: 2.1352
REMARK 3 L13: 2.4122 L23: 0.1815
REMARK 3 S TENSOR
REMARK 3 S11: -0.1089 S12: 1.0310 S13: 1.1097
REMARK 3 S21: -0.3952 S22: 0.5241 S23: 0.5876
REMARK 3 S31: -1.2093 S32: -0.0506 S33: -0.3750
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 62 THROUGH 77 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.3948 91.2263 18.8787
REMARK 3 T TENSOR
REMARK 3 T11: 0.2525 T22: 0.3640
REMARK 3 T33: 0.2988 T12: 0.0747
REMARK 3 T13: -0.0437 T23: -0.0942
REMARK 3 L TENSOR
REMARK 3 L11: 5.5984 L22: 4.5541
REMARK 3 L33: 7.9189 L12: 2.8068
REMARK 3 L13: -5.0008 L23: -2.9125
REMARK 3 S TENSOR
REMARK 3 S11: 0.2653 S12: 0.3902 S13: -0.1082
REMARK 3 S21: -0.1773 S22: -0.1714 S23: -0.5067
REMARK 3 S31: -0.1641 S32: 0.1913 S33: -0.1472
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 78 THROUGH 83 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.2565 81.6288 18.1567
REMARK 3 T TENSOR
REMARK 3 T11: 0.6556 T22: 0.3058
REMARK 3 T33: 0.4646 T12: 0.3468
REMARK 3 T13: 0.0535 T23: -0.0059
REMARK 3 L TENSOR
REMARK 3 L11: 3.7587 L22: 6.9475
REMARK 3 L33: 4.5182 L12: 4.7724
REMARK 3 L13: -3.6040 L23: -4.1110
REMARK 3 S TENSOR
REMARK 3 S11: 0.1648 S12: -0.0723 S13: -0.5799
REMARK 3 S21: -0.2103 S22: -0.1221 S23: -0.8945
REMARK 3 S31: 0.4701 S32: 0.3816 S33: 0.1353
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 84 THROUGH 90 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.1114 71.6916 21.8692
REMARK 3 T TENSOR
REMARK 3 T11: 1.1101 T22: 0.3230
REMARK 3 T33: 0.6689 T12: 0.2825
REMARK 3 T13: 0.0380 T23: -0.0722
REMARK 3 L TENSOR
REMARK 3 L11: 3.3124 L22: 2.4470
REMARK 3 L33: 1.4738 L12: -1.2606
REMARK 3 L13: -1.8654 L23: 0.7935
REMARK 3 S TENSOR
REMARK 3 S11: 0.0651 S12: 0.3616 S13: -0.1990
REMARK 3 S21: -0.7283 S22: -0.2935 S23: 0.1308
REMARK 3 S31: 0.0377 S32: -0.0898 S33: 0.1830
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 91 THROUGH 99 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.8018 87.7054 11.2880
REMARK 3 T TENSOR
REMARK 3 T11: 0.5151 T22: 0.3294
REMARK 3 T33: 0.3003 T12: 0.1505
REMARK 3 T13: -0.0635 T23: -0.1253
REMARK 3 L TENSOR
REMARK 3 L11: 8.3182 L22: 2.7007
REMARK 3 L33: 6.5886 L12: 4.4282
REMARK 3 L13: -3.9098 L23: -3.3556
REMARK 3 S TENSOR
REMARK 3 S11: 0.2879 S12: 0.5106 S13: -0.1548
REMARK 3 S21: -1.0773 S22: 0.0108 S23: 0.0436
REMARK 3 S31: 0.3673 S32: 0.1554 S33: -0.2995
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 1 THROUGH 9 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.5249 82.5839 53.8081
REMARK 3 T TENSOR
REMARK 3 T11: 0.3052 T22: 0.1889
REMARK 3 T33: 0.3750 T12: -0.0527
REMARK 3 T13: -0.1188 T23: -0.0361
REMARK 3 L TENSOR
REMARK 3 L11: 0.2054 L22: 0.5144
REMARK 3 L33: 1.3532 L12: -0.1924
REMARK 3 L13: 0.1042 L23: -0.7606
REMARK 3 S TENSOR
REMARK 3 S11: -0.1327 S12: 0.0024 S13: 0.3990
REMARK 3 S21: 0.3176 S22: -0.1597 S23: 0.0199
REMARK 3 S31: -0.3125 S32: 0.1734 S33: 0.2638
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 2 THROUGH 174 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.0719 53.0604 91.6796
REMARK 3 T TENSOR
REMARK 3 T11: 0.3346 T22: 0.4503
REMARK 3 T33: 0.2290 T12: 0.1807
REMARK 3 T13: 0.0993 T23: 0.0270
REMARK 3 L TENSOR
REMARK 3 L11: 1.6498 L22: 3.0280
REMARK 3 L33: 3.1829 L12: -0.0342
REMARK 3 L13: -0.2243 L23: -0.6254
REMARK 3 S TENSOR
REMARK 3 S11: -0.1102 S12: 0.0769 S13: -0.1065
REMARK 3 S21: -0.2141 S22: -0.0988 S23: -0.4011
REMARK 3 S31: 0.6172 S32: 0.4069 S33: 0.1570
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 175 THROUGH 276 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.3100 49.2969 57.7870
REMARK 3 T TENSOR
REMARK 3 T11: 0.1496 T22: 0.4691
REMARK 3 T33: 0.2908 T12: 0.0408
REMARK 3 T13: -0.0282 T23: -0.0535
REMARK 3 L TENSOR
REMARK 3 L11: 1.9208 L22: 1.6293
REMARK 3 L33: 3.0513 L12: -0.1841
REMARK 3 L13: -0.0778 L23: 0.0340
REMARK 3 S TENSOR
REMARK 3 S11: -0.0604 S12: -0.4116 S13: 0.1103
REMARK 3 S21: 0.2712 S22: 0.1350 S23: -0.2869
REMARK 3 S31: 0.0360 S32: 1.0111 S33: 0.0093
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 0 THROUGH 11 )
REMARK 3 ORIGIN FOR THE GROUP (A): -22.4970 54.8358 68.0182
REMARK 3 T TENSOR
REMARK 3 T11: 0.4462 T22: 0.3656
REMARK 3 T33: 0.3655 T12: -0.0016
REMARK 3 T13: 0.0071 T23: -0.0131
REMARK 3 L TENSOR
REMARK 3 L11: 5.3455 L22: 6.2157
REMARK 3 L33: 5.2397 L12: -5.8024
REMARK 3 L13: -5.2994 L23: 5.7356
REMARK 3 S TENSOR
REMARK 3 S11: -0.2232 S12: -0.4629 S13: 0.1590
REMARK 3 S21: 0.4251 S22: 0.4503 S23: 0.0244
REMARK 3 S31: -0.3138 S32: 0.1605 S33: -0.2001
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 12 THROUGH 19 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.8649 35.6135 56.0209
REMARK 3 T TENSOR
REMARK 3 T11: 0.5954 T22: 0.2913
REMARK 3 T33: 0.3156 T12: 0.2238
REMARK 3 T13: 0.0307 T23: 0.0299
REMARK 3 L TENSOR
REMARK 3 L11: 5.1577 L22: 3.1821
REMARK 3 L33: 8.7427 L12: 3.7762
REMARK 3 L13: 4.6037 L23: 4.1290
REMARK 3 S TENSOR
REMARK 3 S11: 0.4536 S12: 0.6550 S13: -0.6591
REMARK 3 S21: -0.3186 S22: 0.2515 S23: -0.6380
REMARK 3 S31: 0.7542 S32: 0.4339 S33: -0.6407
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 20 THROUGH 30 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.9061 45.7988 66.2713
REMARK 3 T TENSOR
REMARK 3 T11: 0.3434 T22: 0.3335
REMARK 3 T33: 0.1533 T12: -0.0059
REMARK 3 T13: 0.0882 T23: 0.0465
REMARK 3 L TENSOR
REMARK 3 L11: 4.8919 L22: 5.3194
REMARK 3 L33: 8.3096 L12: -4.3098
REMARK 3 L13: -3.9845 L23: 6.2981
REMARK 3 S TENSOR
REMARK 3 S11: -0.3401 S12: 0.0390 S13: -0.0053
REMARK 3 S21: -0.0495 S22: 0.2444 S23: -0.1636
REMARK 3 S31: 0.5402 S32: 0.1364 S33: 0.0654
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 31 THROUGH 41 )
REMARK 3 ORIGIN FOR THE GROUP (A): -29.0548 47.8578 69.0799
REMARK 3 T TENSOR
REMARK 3 T11: 0.5019 T22: 0.5746
REMARK 3 T33: 0.2272 T12: -0.2227
REMARK 3 T13: 0.1148 T23: 0.0572
REMARK 3 L TENSOR
REMARK 3 L11: 0.8720 L22: 9.4649
REMARK 3 L33: 5.1207 L12: -1.1857
REMARK 3 L13: -0.9043 L23: 6.9741
REMARK 3 S TENSOR
REMARK 3 S11: -0.0237 S12: -0.0530 S13: -0.0501
REMARK 3 S21: 0.1261 S22: -0.1704 S23: 0.4171
REMARK 3 S31: 0.3804 S32: -0.5775 S33: 0.1933
REMARK 3 TLS GROUP : 33
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 42 THROUGH 51 )
REMARK 3 ORIGIN FOR THE GROUP (A): -28.3577 37.7690 64.0255
REMARK 3 T TENSOR
REMARK 3 T11: 0.6065 T22: 0.6436
REMARK 3 T33: 0.3739 T12: -0.4003
REMARK 3 T13: 0.1232 T23: 0.0101
REMARK 3 L TENSOR
REMARK 3 L11: 5.1985 L22: 2.1043
REMARK 3 L33: 7.3917 L12: 1.9819
REMARK 3 L13: 3.0037 L23: 1.0128
REMARK 3 S TENSOR
REMARK 3 S11: 0.2443 S12: -0.5723 S13: -0.6025
REMARK 3 S21: 0.3591 S22: -0.1445 S23: 0.0012
REMARK 3 S31: 0.7148 S32: -0.5530 S33: -0.0907
REMARK 3 TLS GROUP : 34
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 52 THROUGH 61 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.1236 53.3414 79.5171
REMARK 3 T TENSOR
REMARK 3 T11: 0.3015 T22: 0.3970
REMARK 3 T33: 0.1629 T12: 0.0538
REMARK 3 T13: 0.0136 T23: -0.0101
REMARK 3 L TENSOR
REMARK 3 L11: 6.9238 L22: 7.0950
REMARK 3 L33: 5.8055 L12: -6.4025
REMARK 3 L13: -1.1076 L23: 3.5923
REMARK 3 S TENSOR
REMARK 3 S11: 0.0219 S12: -0.4009 S13: 0.0503
REMARK 3 S21: 0.1023 S22: -0.0361 S23: -0.2085
REMARK 3 S31: 0.9263 S32: 0.1513 S33: 0.0576
REMARK 3 TLS GROUP : 35
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 62 THROUGH 90 )
REMARK 3 ORIGIN FOR THE GROUP (A): -25.0775 45.2018 62.6529
REMARK 3 T TENSOR
REMARK 3 T11: 0.2859 T22: 0.4059
REMARK 3 T33: 0.2264 T12: -0.1207
REMARK 3 T13: 0.1018 T23: 0.0423
REMARK 3 L TENSOR
REMARK 3 L11: 1.7995 L22: 4.4587
REMARK 3 L33: 5.2263 L12: -0.1178
REMARK 3 L13: 0.5213 L23: 2.6451
REMARK 3 S TENSOR
REMARK 3 S11: 0.0158 S12: -0.0204 S13: -0.0959
REMARK 3 S21: -0.0521 S22: -0.2665 S23: 0.2806
REMARK 3 S31: 0.6643 S32: -0.6264 S33: 0.2262
REMARK 3 TLS GROUP : 36
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 91 THROUGH 99 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.0577 47.6569 54.9619
REMARK 3 T TENSOR
REMARK 3 T11: 0.2433 T22: 0.4120
REMARK 3 T33: 0.2201 T12: -0.0545
REMARK 3 T13: -0.0265 T23: 0.1163
REMARK 3 L TENSOR
REMARK 3 L11: 3.0946 L22: 3.7849
REMARK 3 L33: 6.9004 L12: -1.7171
REMARK 3 L13: -3.5205 L23: 1.0009
REMARK 3 S TENSOR
REMARK 3 S11: 0.0337 S12: 0.0850 S13: 0.4332
REMARK 3 S21: -0.3941 S22: -0.1730 S23: -0.3033
REMARK 3 S31: 0.1686 S32: 0.3534 S33: 0.0898
REMARK 3 TLS GROUP : 37
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 9 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.4783 55.3461 98.5191
REMARK 3 T TENSOR
REMARK 3 T11: 0.2579 T22: 0.5305
REMARK 3 T33: 0.2792 T12: 0.1551
REMARK 3 T13: 0.0093 T23: 0.1165
REMARK 3 L TENSOR
REMARK 3 L11: 2.2516 L22: 1.1945
REMARK 3 L33: 5.6298 L12: 0.5100
REMARK 3 L13: -1.9428 L23: 1.6212
REMARK 3 S TENSOR
REMARK 3 S11: -0.3907 S12: -0.0620 S13: -0.0241
REMARK 3 S21: -0.0181 S22: 0.1777 S23: 0.1565
REMARK 3 S31: 0.0740 S32: 0.1481 S33: 0.2322
REMARK 3 TLS GROUP : 38
REMARK 3 SELECTION: CHAIN 'I' AND (RESID 2 THROUGH 37 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.0109 88.1113 77.1688
REMARK 3 T TENSOR
REMARK 3 T11: 1.2802 T22: 0.5441
REMARK 3 T33: 0.0078 T12: -0.5785
REMARK 3 T13: -0.2011 T23: -0.4917
REMARK 3 L TENSOR
REMARK 3 L11: 0.3291 L22: 0.8702
REMARK 3 L33: 0.9711 L12: 0.0166
REMARK 3 L13: -0.0906 L23: 0.3632
REMARK 3 S TENSOR
REMARK 3 S11: 0.0936 S12: -0.2259 S13: 0.2114
REMARK 3 S21: -0.0147 S22: 0.2027 S23: -0.2116
REMARK 3 S31: -0.8924 S32: 0.7247 S33: -0.0554
REMARK 3 TLS GROUP : 39
REMARK 3 SELECTION: CHAIN 'I' AND (RESID 38 THROUGH 56 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.1852 99.6531 74.2108
REMARK 3 T TENSOR
REMARK 3 T11: 1.8061 T22: 0.6390
REMARK 3 T33: 0.5559 T12: -0.8298
REMARK 3 T13: 0.0069 T23: -0.1964
REMARK 3 L TENSOR
REMARK 3 L11: 3.0065 L22: 3.1374
REMARK 3 L33: 1.3281 L12: 1.7037
REMARK 3 L13: 0.6516 L23: 0.9036
REMARK 3 S TENSOR
REMARK 3 S11: -0.1803 S12: 0.0496 S13: 0.4839
REMARK 3 S21: -0.1698 S22: 0.1595 S23: -0.2312
REMARK 3 S31: -0.5552 S32: 0.4157 S33: 0.0022
REMARK 3 TLS GROUP : 40
REMARK 3 SELECTION: CHAIN 'I' AND (RESID 57 THROUGH 118 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.5254 81.7856 71.1945
REMARK 3 T TENSOR
REMARK 3 T11: 0.6707 T22: 0.6282
REMARK 3 T33: 0.2330 T12: -0.3345
REMARK 3 T13: -0.0056 T23: -0.1097
REMARK 3 L TENSOR
REMARK 3 L11: 3.0451 L22: 1.9206
REMARK 3 L33: 0.7232 L12: 0.7860
REMARK 3 L13: 0.1660 L23: 0.0735
REMARK 3 S TENSOR
REMARK 3 S11: -0.1622 S12: -0.1686 S13: 0.1116
REMARK 3 S21: -0.2067 S22: 0.2414 S23: -0.1598
REMARK 3 S31: -1.0972 S32: 0.8753 S33: -0.0562
REMARK 3 TLS GROUP : 41
REMARK 3 SELECTION: CHAIN 'I' AND (RESID 119 THROUGH 162 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.8979 70.2286 68.0736
REMARK 3 T TENSOR
REMARK 3 T11: 0.3434 T22: 0.5858
REMARK 3 T33: 0.2786 T12: -0.0293
REMARK 3 T13: -0.0235 T23: -0.0680
REMARK 3 L TENSOR
REMARK 3 L11: 4.4065 L22: 3.6372
REMARK 3 L33: 5.6909 L12: 0.0139
REMARK 3 L13: -0.4416 L23: 1.5983
REMARK 3 S TENSOR
REMARK 3 S11: -0.2151 S12: 0.2702 S13: -0.2647
REMARK 3 S21: -0.2628 S22: 0.4307 S23: -0.3204
REMARK 3 S31: 0.3565 S32: 1.7019 S33: -0.1398
REMARK 3 TLS GROUP : 42
REMARK 3 SELECTION: CHAIN 'I' AND (RESID 163 THROUGH 198 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.1653 91.5526 85.9048
REMARK 3 T TENSOR
REMARK 3 T11: 0.7793 T22: 1.3992
REMARK 3 T33: 1.0472 T12: -0.5034
REMARK 3 T13: -0.1515 T23: -0.2457
REMARK 3 L TENSOR
REMARK 3 L11: 0.4574 L22: 0.4899
REMARK 3 L33: 6.7160 L12: -0.3338
REMARK 3 L13: 0.5980 L23: 0.7887
REMARK 3 S TENSOR
REMARK 3 S11: -0.5817 S12: 0.8028 S13: 0.1430
REMARK 3 S21: -0.2556 S22: 0.7837 S23: -0.4280
REMARK 3 S31: -0.2799 S32: 0.4786 S33: -0.1191
REMARK 3 TLS GROUP : 43
REMARK 3 SELECTION: CHAIN 'I' AND (RESID 199 THROUGH 219 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.0426 85.2033 101.9139
REMARK 3 T TENSOR
REMARK 3 T11: 0.5823 T22: 0.9199
REMARK 3 T33: 1.3609 T12: 0.2137
REMARK 3 T13: -0.2054 T23: -0.4930
REMARK 3 L TENSOR
REMARK 3 L11: 3.7379 L22: 1.6262
REMARK 3 L33: 3.5628 L12: -1.1567
REMARK 3 L13: 0.4301 L23: 1.1636
REMARK 3 S TENSOR
REMARK 3 S11: -0.7933 S12: 0.0279 S13: 0.0379
REMARK 3 S21: 0.1514 S22: 0.2541 S23: -0.3246
REMARK 3 S31: 0.5287 S32: 0.1849 S33: 0.4845
REMARK 3 TLS GROUP : 44
REMARK 3 SELECTION: CHAIN 'I' AND (RESID 220 THROUGH 240 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.6659 82.8040 100.5770
REMARK 3 T TENSOR
REMARK 3 T11: 0.7788 T22: 0.9431
REMARK 3 T33: 0.8153 T12: -0.2695
REMARK 3 T13: -0.0107 T23: -0.2330
REMARK 3 L TENSOR
REMARK 3 L11: 3.9868 L22: 0.1298
REMARK 3 L33: 3.2182 L12: -0.4065
REMARK 3 L13: 2.4088 L23: -0.6196
REMARK 3 S TENSOR
REMARK 3 S11: -0.2758 S12: 0.2776 S13: -0.2279
REMARK 3 S21: -0.0720 S22: 0.1828 S23: 0.2558
REMARK 3 S31: 0.5186 S32: -0.3168 S33: 0.0583
REMARK 3 TLS GROUP : 45
REMARK 3 SELECTION: CHAIN 'I' AND (RESID 241 THROUGH 252 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.7452 82.8878 107.8655
REMARK 3 T TENSOR
REMARK 3 T11: 0.6532 T22: 1.1816
REMARK 3 T33: 0.9967 T12: -0.0870
REMARK 3 T13: -0.2545 T23: -0.4359
REMARK 3 L TENSOR
REMARK 3 L11: 1.9472 L22: 1.1949
REMARK 3 L33: 4.9580 L12: 0.1444
REMARK 3 L13: -0.1934 L23: -0.3097
REMARK 3 S TENSOR
REMARK 3 S11: 0.0398 S12: -0.3520 S13: -0.4372
REMARK 3 S21: 0.3250 S22: 0.0313 S23: -0.4842
REMARK 3 S31: 0.3066 S32: 0.5258 S33: -0.1743
REMARK 3 TLS GROUP : 46
REMARK 3 SELECTION: CHAIN 'I' AND (RESID 253 THROUGH 275 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.4985 84.1923 107.4869
REMARK 3 T TENSOR
REMARK 3 T11: 0.7633 T22: 1.0539
REMARK 3 T33: 1.1370 T12: 0.2333
REMARK 3 T13: -0.1685 T23: -0.1549
REMARK 3 L TENSOR
REMARK 3 L11: 3.1018 L22: 1.9285
REMARK 3 L33: 2.6575 L12: 1.2270
REMARK 3 L13: -2.6229 L23: -0.2513
REMARK 3 S TENSOR
REMARK 3 S11: -0.0859 S12: -0.2033 S13: 0.1341
REMARK 3 S21: 0.1982 S22: -0.2503 S23: -0.4391
REMARK 3 S31: 0.5234 S32: 0.8270 S33: 0.3185
REMARK 3 TLS GROUP : 47
REMARK 3 SELECTION: CHAIN 'J' AND (RESID 0 THROUGH 5 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.1413 74.8537 90.1580
REMARK 3 T TENSOR
REMARK 3 T11: 0.3900 T22: 0.3629
REMARK 3 T33: 0.3132 T12: 0.0125
REMARK 3 T13: -0.0551 T23: -0.0052
REMARK 3 L TENSOR
REMARK 3 L11: 3.5157 L22: 2.3197
REMARK 3 L33: 3.4296 L12: -1.3091
REMARK 3 L13: -3.2472 L23: 0.3225
REMARK 3 S TENSOR
REMARK 3 S11: -0.1789 S12: 0.4436 S13: -0.6870
REMARK 3 S21: -0.0382 S22: 0.3989 S23: -0.0215
REMARK 3 S31: 0.5135 S32: -0.1327 S33: -0.1977
REMARK 3 TLS GROUP : 48
REMARK 3 SELECTION: CHAIN 'J' AND (RESID 6 THROUGH 11 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.0489 87.8793 100.8439
REMARK 3 T TENSOR
REMARK 3 T11: 0.5424 T22: 0.9776
REMARK 3 T33: 0.4813 T12: -0.1838
REMARK 3 T13: -0.0427 T23: -0.1722
REMARK 3 L TENSOR
REMARK 3 L11: 7.4362 L22: 3.6274
REMARK 3 L33: 7.7213 L12: 2.0799
REMARK 3 L13: 7.5756 L23: 2.0426
REMARK 3 S TENSOR
REMARK 3 S11: 0.1654 S12: -0.0775 S13: 0.0315
REMARK 3 S21: 0.4950 S22: 0.5443 S23: -1.5913
REMARK 3 S31: -0.1515 S32: 1.3474 S33: -0.6708
REMARK 3 TLS GROUP : 49
REMARK 3 SELECTION: CHAIN 'J' AND (RESID 12 THROUGH 30 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.7408 95.1755 101.5028
REMARK 3 T TENSOR
REMARK 3 T11: 1.0733 T22: 1.1034
REMARK 3 T33: 0.7316 T12: -0.3687
REMARK 3 T13: -0.1453 T23: -0.5506
REMARK 3 L TENSOR
REMARK 3 L11: 1.0421 L22: 0.6995
REMARK 3 L33: 3.3723 L12: 0.4403
REMARK 3 L13: 1.5657 L23: 1.4047
REMARK 3 S TENSOR
REMARK 3 S11: 0.2646 S12: -0.7092 S13: 0.5965
REMARK 3 S21: 1.0308 S22: 0.0876 S23: -0.6638
REMARK 3 S31: -0.6436 S32: 0.4429 S33: -0.1429
REMARK 3 TLS GROUP : 50
REMARK 3 SELECTION: CHAIN 'J' AND (RESID 31 THROUGH 41 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.5570 88.4989 94.5376
REMARK 3 T TENSOR
REMARK 3 T11: 0.7351 T22: 0.6319
REMARK 3 T33: 0.3472 T12: 0.0663
REMARK 3 T13: -0.1582 T23: -0.2302
REMARK 3 L TENSOR
REMARK 3 L11: 1.6296 L22: 2.6239
REMARK 3 L33: 2.4716 L12: 1.9281
REMARK 3 L13: 1.3165 L23: 2.2416
REMARK 3 S TENSOR
REMARK 3 S11: -0.0337 S12: -0.4434 S13: 0.7064
REMARK 3 S21: 0.2091 S22: -0.3648 S23: 0.5074
REMARK 3 S31: -0.7569 S32: -0.6376 S33: 0.5021
REMARK 3 TLS GROUP : 51
REMARK 3 SELECTION: CHAIN 'J' AND (RESID 42 THROUGH 51 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.3289 98.8101 99.6737
REMARK 3 T TENSOR
REMARK 3 T11: 1.1065 T22: 0.7811
REMARK 3 T33: 0.7937 T12: 0.0014
REMARK 3 T13: -0.1412 T23: -0.3651
REMARK 3 L TENSOR
REMARK 3 L11: 1.8623 L22: 1.4351
REMARK 3 L33: 2.4129 L12: -1.0028
REMARK 3 L13: -2.0966 L23: 0.9051
REMARK 3 S TENSOR
REMARK 3 S11: 0.0186 S12: -0.2001 S13: 0.7585
REMARK 3 S21: -0.0803 S22: 0.1419 S23: 0.2314
REMARK 3 S31: -1.0044 S32: -0.3189 S33: -0.1981
REMARK 3 TLS GROUP : 52
REMARK 3 SELECTION: CHAIN 'J' AND (RESID 52 THROUGH 61 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.2796 83.3897 84.1302
REMARK 3 T TENSOR
REMARK 3 T11: 0.4133 T22: 0.5572
REMARK 3 T33: 0.4253 T12: -0.2464
REMARK 3 T13: 0.0940 T23: -0.1168
REMARK 3 L TENSOR
REMARK 3 L11: 3.6990 L22: 7.8509
REMARK 3 L33: 9.6076 L12: 5.0691
REMARK 3 L13: 1.5290 L23: 4.9459
REMARK 3 S TENSOR
REMARK 3 S11: 0.4075 S12: -0.2769 S13: 0.5619
REMARK 3 S21: 0.3491 S22: 0.1278 S23: -0.8675
REMARK 3 S31: -0.6393 S32: 0.7803 S33: -0.4952
REMARK 3 TLS GROUP : 53
REMARK 3 SELECTION: CHAIN 'J' AND (RESID 62 THROUGH 71 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.1234 94.4395 95.2590
REMARK 3 T TENSOR
REMARK 3 T11: 1.1810 T22: 0.7107
REMARK 3 T33: 0.5282 T12: -0.2220
REMARK 3 T13: -0.0797 T23: -0.2651
REMARK 3 L TENSOR
REMARK 3 L11: 1.0101 L22: 8.2115
REMARK 3 L33: 4.7382 L12: 2.5565
REMARK 3 L13: 2.0023 L23: 6.2350
REMARK 3 S TENSOR
REMARK 3 S11: -0.2355 S12: -0.3765 S13: 0.7803
REMARK 3 S21: -0.5777 S22: -0.0081 S23: -0.1756
REMARK 3 S31: -1.3363 S32: 0.0020 S33: 0.2505
REMARK 3 TLS GROUP : 54
REMARK 3 SELECTION: CHAIN 'J' AND (RESID 72 THROUGH 77 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.4820 99.3060 113.9113
REMARK 3 T TENSOR
REMARK 3 T11: 1.1447 T22: 1.2235
REMARK 3 T33: 0.8456 T12: 0.1015
REMARK 3 T13: -0.0843 T23: -0.5951
REMARK 3 L TENSOR
REMARK 3 L11: 2.8773 L22: 6.5549
REMARK 3 L33: 2.3113 L12: 4.3344
REMARK 3 L13: 2.5440 L23: 3.8726
REMARK 3 S TENSOR
REMARK 3 S11: -0.1368 S12: -0.2635 S13: 0.3560
REMARK 3 S21: 0.2528 S22: -0.0724 S23: 0.1175
REMARK 3 S31: -0.4149 S32: 0.1933 S33: 0.1566
REMARK 3 TLS GROUP : 55
REMARK 3 SELECTION: CHAIN 'J' AND (RESID 78 THROUGH 90 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.6687 84.6473 99.5355
REMARK 3 T TENSOR
REMARK 3 T11: 0.6573 T22: 0.7967
REMARK 3 T33: 0.4053 T12: -0.0532
REMARK 3 T13: -0.0409 T23: -0.1782
REMARK 3 L TENSOR
REMARK 3 L11: 5.4977 L22: 2.0050
REMARK 3 L33: 4.8521 L12: 3.5677
REMARK 3 L13: 3.1404 L23: 7.0311
REMARK 3 S TENSOR
REMARK 3 S11: 0.2182 S12: -0.7733 S13: 0.5121
REMARK 3 S21: 0.8990 S22: -0.6057 S23: 0.3403
REMARK 3 S31: -0.0501 S32: -0.5065 S33: 0.3454
REMARK 3 TLS GROUP : 56
REMARK 3 SELECTION: CHAIN 'J' AND (RESID 91 THROUGH 99 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.9355 88.5359 107.8420
REMARK 3 T TENSOR
REMARK 3 T11: 0.7605 T22: 1.0332
REMARK 3 T33: 0.4504 T12: -0.0220
REMARK 3 T13: -0.0217 T23: -0.2826
REMARK 3 L TENSOR
REMARK 3 L11: 2.3420 L22: 2.0840
REMARK 3 L33: 1.8445 L12: -1.3692
REMARK 3 L13: -0.5325 L23: -1.1757
REMARK 3 S TENSOR
REMARK 3 S11: 0.2921 S12: -0.4001 S13: -0.0298
REMARK 3 S21: 0.2860 S22: 0.1156 S23: -0.7303
REMARK 3 S31: -0.0919 S32: 0.4409 S33: -0.3413
REMARK 3 TLS GROUP : 57
REMARK 3 SELECTION: CHAIN 'K' AND (RESID 1 THROUGH 9 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.4527 80.3900 65.1374
REMARK 3 T TENSOR
REMARK 3 T11: 0.5570 T22: 0.6316
REMARK 3 T33: 0.2506 T12: -0.3470
REMARK 3 T13: -0.0161 T23: 0.0673
REMARK 3 L TENSOR
REMARK 3 L11: 1.7530 L22: 0.4931
REMARK 3 L33: 2.0742 L12: -0.8830
REMARK 3 L13: 0.5208 L23: 0.0437
REMARK 3 S TENSOR
REMARK 3 S11: 0.0308 S12: -0.3708 S13: 0.0309
REMARK 3 S21: 0.5018 S22: -0.2949 S23: -0.1569
REMARK 3 S31: -0.7038 S32: 0.4127 S33: 0.1997
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 5KD7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUN-16.
REMARK 100 THE DEPOSITION ID IS D_1000222028.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-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 : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0333
REMARK 200 MONOCHROMATOR : SI 100
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 72767
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350
REMARK 200 RESOLUTION RANGE LOW (A) : 74.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.05500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.43
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.77100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
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: 3ECB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG 20000, 0.1M MES BUFFER, PH
REMARK 280 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4830 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, P
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4300 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19230 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, E
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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, 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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4360 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J, K
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 GLY A 275
REMARK 465 LYS A 276
REMARK 465 MET B 0
REMARK 465 GLY C 275
REMARK 465 LYS C 276
REMARK 465 GLY I 107
REMARK 465 PRO I 195
REMARK 465 GLU I 196
REMARK 465 GLY I 265
REMARK 465 LEU I 266
REMARK 465 PRO I 267
REMARK 465 GLU I 268
REMARK 465 PRO I 269
REMARK 465 LYS I 276
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 ASP A 106 CG OD1 OD2
REMARK 470 ILE B 1 CG1 CG2 CD1
REMARK 470 MET D 0 CG SD CE
REMARK 470 SER D 52 OG
REMARK 470 ASP D 53 CB CG OD1 OD2
REMARK 470 GLU F 222 CG CD OE1 OE2
REMARK 470 ILE G 1 CG1 CG2 CD1
REMARK 470 ARG I 44 CG CD NE CZ NH1 NH2
REMARK 470 GLU I 104 CG CD OE1 OE2
REMARK 470 ASP I 106 CG OD1 OD2
REMARK 470 ARG I 108 CG CD NE CZ NH1 NH2
REMARK 470 ARG I 181 CG CD NE CZ NH1 NH2
REMARK 470 HIS I 192 CG ND1 CD2 CE1 NE2
REMARK 470 ARG I 193 CG CD NE CZ NH1 NH2
REMARK 470 ARG I 194 CG CD NE CZ NH1 NH2
REMARK 470 ASP I 198 CG OD1 OD2
REMARK 470 VAL I 199 CG1 CG2
REMARK 470 GLU I 222 CG CD OE1 OE2
REMARK 470 GLU I 223 CG CD OE1 OE2
REMARK 470 LEU I 224 CG CD1 CD2
REMARK 470 GLN I 226 CG CD OE1 NE2
REMARK 470 GLU I 227 CG CD OE1 OE2
REMARK 470 GLU I 229 CG CD OE1 OE2
REMARK 470 LYS I 253 CG CD CE NZ
REMARK 470 GLU I 254 CG CD OE1 OE2
REMARK 470 LYS I 256 CG CD CE NZ
REMARK 470 GLU I 264 CG CD OE1 OE2
REMARK 470 LEU I 270 CG CD1 CD2
REMARK 470 LEU I 272 CG CD1 CD2
REMARK 470 ARG I 273 CG CD NE CZ NH1 NH2
REMARK 470 ARG J 12 CG CD NE CZ NH1 NH2
REMARK 470 GLU J 69 CG CD OE1 OE2
REMARK 470 ARG J 97 CG CD NE CZ NH1 NH2
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 OE1 GLU C 55 NH1 ARG C 170 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NH2 ARG A 273 OE1 GLU C 53 1445 2.16
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 A 230 CA - CB - CG ANGL. DEV. = 14.4 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 ARG A 14 71.18 -152.65
REMARK 500 ASP A 29 -91.18 57.99
REMARK 500 ASN A 30 23.22 -143.60
REMARK 500 ASN A 42 76.59 58.41
REMARK 500 TRP A 114 81.58 -164.34
REMARK 500 TYR A 123 -70.59 -110.80
REMARK 500 ALA A 136 -73.67 -61.00
REMARK 500 PRO A 210 -169.26 -76.86
REMARK 500 ASN A 220 13.20 56.86
REMARK 500 LEU A 224 59.42 -119.02
REMARK 500 GLN A 255 7.13 -66.05
REMARK 500 GLN B 2 101.02 59.82
REMARK 500 GLN B 29 30.93 72.27
REMARK 500 MET B 54 158.50 87.82
REMARK 500 LYS B 58 -39.94 -36.96
REMARK 500 TRP B 60 -7.71 83.53
REMARK 500 ASP C 29 -105.62 52.63
REMARK 500 ASN C 42 86.67 57.70
REMARK 500 TRP C 114 90.52 -167.85
REMARK 500 TYR C 123 -72.91 -113.67
REMARK 500 ALA C 136 -76.26 -67.15
REMARK 500 ASP C 198 -169.93 -114.96
REMARK 500 LEU C 224 40.30 -159.76
REMARK 500 GLN C 226 -88.37 -65.00
REMARK 500 ASP D 53 35.98 78.59
REMARK 500 SER D 55 -158.47 -163.83
REMARK 500 TRP D 60 -4.78 73.24
REMARK 500 ASP D 98 4.83 -69.61
REMARK 500 ARG E 5 -74.67 -63.20
REMARK 500 ALA E 6 -23.00 76.73
REMARK 500 ASP F 29 -100.99 56.67
REMARK 500 PHE F 33 -23.32 -149.89
REMARK 500 ASP F 106 -25.36 137.55
REMARK 500 TRP F 114 90.11 -163.30
REMARK 500 TYR F 123 -73.32 -104.20
REMARK 500 LEU F 219 -95.95 -98.68
REMARK 500 ASN F 220 61.79 -110.78
REMARK 500 LEU F 224 52.15 -103.62
REMARK 500 ASP G 53 152.90 69.21
REMARK 500 TRP G 60 -22.72 86.06
REMARK 500 ARG H 5 -71.42 -63.03
REMARK 500 ALA H 6 -21.63 72.17
REMARK 500 ARG I 14 77.66 -150.45
REMARK 500 ASP I 29 -103.86 55.41
REMARK 500 PHE I 33 -19.77 -142.23
REMARK 500 ASN I 42 80.71 54.76
REMARK 500 TRP I 114 89.34 -162.06
REMARK 500 TYR I 123 -72.66 -110.98
REMARK 500 ALA I 136 -72.13 -81.25
REMARK 500 ASP I 198 -145.94 -168.56
REMARK 500
REMARK 500 THIS ENTRY HAS 59 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 VAL J 9 TYR J 10 -144.56
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 EDO A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO F 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO F 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL F 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO I 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide GOL F 301 and CYS F
REMARK 800 121
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5KD4 RELATED DB: PDB
DBREF 5KD7 A 2 276 UNP P01900 HA12_MOUSE 26 300
DBREF 5KD7 B 1 99 UNP P01887 B2MG_MOUSE 21 119
DBREF 5KD7 P 1 9 PDB 5KD7 5KD7 1 9
DBREF 5KD7 C 2 276 UNP P01900 HA12_MOUSE 26 300
DBREF 5KD7 D 1 99 UNP P01887 B2MG_MOUSE 21 119
DBREF 5KD7 E 1 9 PDB 5KD7 5KD7 1 9
DBREF 5KD7 F 2 276 UNP P01900 HA12_MOUSE 26 300
DBREF 5KD7 G 1 99 UNP P01887 B2MG_MOUSE 21 119
DBREF 5KD7 H 1 9 PDB 5KD7 5KD7 1 9
DBREF 5KD7 I 2 276 UNP P01900 HA12_MOUSE 26 300
DBREF 5KD7 J 1 99 UNP P01887 B2MG_MOUSE 21 119
DBREF 5KD7 K 1 9 PDB 5KD7 5KD7 1 9
SEQADV 5KD7 MET B 0 UNP P01887 INITIATING METHIONINE
SEQADV 5KD7 MET D 0 UNP P01887 INITIATING METHIONINE
SEQADV 5KD7 MET G 0 UNP P01887 INITIATING METHIONINE
SEQADV 5KD7 MET J 0 UNP P01887 INITIATING METHIONINE
SEQRES 1 A 275 SER HIS SER LEU ARG TYR PHE VAL THR ALA VAL SER ARG
SEQRES 2 A 275 PRO GLY PHE GLY GLU PRO ARG TYR MET GLU VAL GLY TYR
SEQRES 3 A 275 VAL ASP ASN THR GLU PHE VAL ARG PHE ASP SER ASP ALA
SEQRES 4 A 275 GLU ASN PRO ARG TYR GLU PRO ARG ALA ARG TRP ILE GLU
SEQRES 5 A 275 GLN GLU GLY PRO GLU TYR TRP GLU ARG GLU THR ARG ARG
SEQRES 6 A 275 ALA LYS GLY ASN GLU GLN SER PHE ARG VAL ASP LEU ARG
SEQRES 7 A 275 THR ALA LEU ARG TYR TYR ASN GLN SER ALA GLY GLY SER
SEQRES 8 A 275 HIS THR LEU GLN TRP MET ALA GLY CYS ASP VAL GLU SER
SEQRES 9 A 275 ASP GLY ARG LEU LEU ARG GLY TYR TRP GLN PHE ALA TYR
SEQRES 10 A 275 ASP GLY CYS ASP TYR ILE ALA LEU ASN GLU ASP LEU LYS
SEQRES 11 A 275 THR TRP THR ALA ALA ASP MET ALA ALA GLN ILE THR ARG
SEQRES 12 A 275 ARG LYS TRP GLU GLN ALA GLY ALA ALA GLU ARG ASP ARG
SEQRES 13 A 275 ALA TYR LEU GLU GLY GLU CYS VAL GLU TRP LEU ARG ARG
SEQRES 14 A 275 TYR LEU LYS ASN GLY ASN ALA THR LEU LEU ARG THR ASP
SEQRES 15 A 275 PRO PRO LYS ALA HIS VAL THR HIS HIS ARG ARG PRO GLU
SEQRES 16 A 275 GLY ASP VAL THR LEU ARG CYS TRP ALA LEU GLY PHE TYR
SEQRES 17 A 275 PRO ALA ASP ILE THR LEU THR TRP GLN LEU ASN GLY GLU
SEQRES 18 A 275 GLU LEU THR GLN GLU MET GLU LEU VAL GLU THR ARG PRO
SEQRES 19 A 275 ALA GLY ASP GLY THR PHE GLN LYS TRP ALA SER VAL VAL
SEQRES 20 A 275 VAL PRO LEU GLY LYS GLU GLN LYS TYR THR CYS HIS VAL
SEQRES 21 A 275 GLU HIS GLU GLY LEU PRO GLU PRO LEU THR LEU ARG TRP
SEQRES 22 A 275 GLY LYS
SEQRES 1 B 100 MET ILE GLN LYS THR PRO GLN ILE GLN VAL TYR SER ARG
SEQRES 2 B 100 HIS PRO PRO GLU ASN GLY LYS PRO ASN ILE LEU ASN CYS
SEQRES 3 B 100 TYR VAL THR GLN PHE HIS PRO PRO HIS ILE GLU ILE GLN
SEQRES 4 B 100 MET LEU LYS ASN GLY LYS LYS ILE PRO LYS VAL GLU MET
SEQRES 5 B 100 SER ASP MET SER PHE SER LYS ASP TRP SER PHE TYR ILE
SEQRES 6 B 100 LEU ALA HIS THR GLU PHE THR PRO THR GLU THR ASP THR
SEQRES 7 B 100 TYR ALA CYS ARG VAL LYS HIS ALA SER MET ALA GLU PRO
SEQRES 8 B 100 LYS THR VAL TYR TRP ASP ARG ASP MET
SEQRES 1 P 9 ILE GLY PRO GLY ARG ALA PHE TYR VAL
SEQRES 1 C 275 SER HIS SER LEU ARG TYR PHE VAL THR ALA VAL SER ARG
SEQRES 2 C 275 PRO GLY PHE GLY GLU PRO ARG TYR MET GLU VAL GLY TYR
SEQRES 3 C 275 VAL ASP ASN THR GLU PHE VAL ARG PHE ASP SER ASP ALA
SEQRES 4 C 275 GLU ASN PRO ARG TYR GLU PRO ARG ALA ARG TRP ILE GLU
SEQRES 5 C 275 GLN GLU GLY PRO GLU TYR TRP GLU ARG GLU THR ARG ARG
SEQRES 6 C 275 ALA LYS GLY ASN GLU GLN SER PHE ARG VAL ASP LEU ARG
SEQRES 7 C 275 THR ALA LEU ARG TYR TYR ASN GLN SER ALA GLY GLY SER
SEQRES 8 C 275 HIS THR LEU GLN TRP MET ALA GLY CYS ASP VAL GLU SER
SEQRES 9 C 275 ASP GLY ARG LEU LEU ARG GLY TYR TRP GLN PHE ALA TYR
SEQRES 10 C 275 ASP GLY CYS ASP TYR ILE ALA LEU ASN GLU ASP LEU LYS
SEQRES 11 C 275 THR TRP THR ALA ALA ASP MET ALA ALA GLN ILE THR ARG
SEQRES 12 C 275 ARG LYS TRP GLU GLN ALA GLY ALA ALA GLU ARG ASP ARG
SEQRES 13 C 275 ALA TYR LEU GLU GLY GLU CYS VAL GLU TRP LEU ARG ARG
SEQRES 14 C 275 TYR LEU LYS ASN GLY ASN ALA THR LEU LEU ARG THR ASP
SEQRES 15 C 275 PRO PRO LYS ALA HIS VAL THR HIS HIS ARG ARG PRO GLU
SEQRES 16 C 275 GLY ASP VAL THR LEU ARG CYS TRP ALA LEU GLY PHE TYR
SEQRES 17 C 275 PRO ALA ASP ILE THR LEU THR TRP GLN LEU ASN GLY GLU
SEQRES 18 C 275 GLU LEU THR GLN GLU MET GLU LEU VAL GLU THR ARG PRO
SEQRES 19 C 275 ALA GLY ASP GLY THR PHE GLN LYS TRP ALA SER VAL VAL
SEQRES 20 C 275 VAL PRO LEU GLY LYS GLU GLN LYS TYR THR CYS HIS VAL
SEQRES 21 C 275 GLU HIS GLU GLY LEU PRO GLU PRO LEU THR LEU ARG TRP
SEQRES 22 C 275 GLY LYS
SEQRES 1 D 100 MET ILE GLN LYS THR PRO GLN ILE GLN VAL TYR SER ARG
SEQRES 2 D 100 HIS PRO PRO GLU ASN GLY LYS PRO ASN ILE LEU ASN CYS
SEQRES 3 D 100 TYR VAL THR GLN PHE HIS PRO PRO HIS ILE GLU ILE GLN
SEQRES 4 D 100 MET LEU LYS ASN GLY LYS LYS ILE PRO LYS VAL GLU MET
SEQRES 5 D 100 SER ASP MET SER PHE SER LYS ASP TRP SER PHE TYR ILE
SEQRES 6 D 100 LEU ALA HIS THR GLU PHE THR PRO THR GLU THR ASP THR
SEQRES 7 D 100 TYR ALA CYS ARG VAL LYS HIS ALA SER MET ALA GLU PRO
SEQRES 8 D 100 LYS THR VAL TYR TRP ASP ARG ASP MET
SEQRES 1 E 9 ILE GLY PRO GLY ARG ALA PHE TYR VAL
SEQRES 1 F 275 SER HIS SER LEU ARG TYR PHE VAL THR ALA VAL SER ARG
SEQRES 2 F 275 PRO GLY PHE GLY GLU PRO ARG TYR MET GLU VAL GLY TYR
SEQRES 3 F 275 VAL ASP ASN THR GLU PHE VAL ARG PHE ASP SER ASP ALA
SEQRES 4 F 275 GLU ASN PRO ARG TYR GLU PRO ARG ALA ARG TRP ILE GLU
SEQRES 5 F 275 GLN GLU GLY PRO GLU TYR TRP GLU ARG GLU THR ARG ARG
SEQRES 6 F 275 ALA LYS GLY ASN GLU GLN SER PHE ARG VAL ASP LEU ARG
SEQRES 7 F 275 THR ALA LEU ARG TYR TYR ASN GLN SER ALA GLY GLY SER
SEQRES 8 F 275 HIS THR LEU GLN TRP MET ALA GLY CYS ASP VAL GLU SER
SEQRES 9 F 275 ASP GLY ARG LEU LEU ARG GLY TYR TRP GLN PHE ALA TYR
SEQRES 10 F 275 ASP GLY CYS ASP TYR ILE ALA LEU ASN GLU ASP LEU LYS
SEQRES 11 F 275 THR TRP THR ALA ALA ASP MET ALA ALA GLN ILE THR ARG
SEQRES 12 F 275 ARG LYS TRP GLU GLN ALA GLY ALA ALA GLU ARG ASP ARG
SEQRES 13 F 275 ALA TYR LEU GLU GLY GLU CYS VAL GLU TRP LEU ARG ARG
SEQRES 14 F 275 TYR LEU LYS ASN GLY ASN ALA THR LEU LEU ARG THR ASP
SEQRES 15 F 275 PRO PRO LYS ALA HIS VAL THR HIS HIS ARG ARG PRO GLU
SEQRES 16 F 275 GLY ASP VAL THR LEU ARG CYS TRP ALA LEU GLY PHE TYR
SEQRES 17 F 275 PRO ALA ASP ILE THR LEU THR TRP GLN LEU ASN GLY GLU
SEQRES 18 F 275 GLU LEU THR GLN GLU MET GLU LEU VAL GLU THR ARG PRO
SEQRES 19 F 275 ALA GLY ASP GLY THR PHE GLN LYS TRP ALA SER VAL VAL
SEQRES 20 F 275 VAL PRO LEU GLY LYS GLU GLN LYS TYR THR CYS HIS VAL
SEQRES 21 F 275 GLU HIS GLU GLY LEU PRO GLU PRO LEU THR LEU ARG TRP
SEQRES 22 F 275 GLY LYS
SEQRES 1 G 100 MET ILE GLN LYS THR PRO GLN ILE GLN VAL TYR SER ARG
SEQRES 2 G 100 HIS PRO PRO GLU ASN GLY LYS PRO ASN ILE LEU ASN CYS
SEQRES 3 G 100 TYR VAL THR GLN PHE HIS PRO PRO HIS ILE GLU ILE GLN
SEQRES 4 G 100 MET LEU LYS ASN GLY LYS LYS ILE PRO LYS VAL GLU MET
SEQRES 5 G 100 SER ASP MET SER PHE SER LYS ASP TRP SER PHE TYR ILE
SEQRES 6 G 100 LEU ALA HIS THR GLU PHE THR PRO THR GLU THR ASP THR
SEQRES 7 G 100 TYR ALA CYS ARG VAL LYS HIS ALA SER MET ALA GLU PRO
SEQRES 8 G 100 LYS THR VAL TYR TRP ASP ARG ASP MET
SEQRES 1 H 9 ILE GLY PRO GLY ARG ALA PHE TYR VAL
SEQRES 1 I 275 SER HIS SER LEU ARG TYR PHE VAL THR ALA VAL SER ARG
SEQRES 2 I 275 PRO GLY PHE GLY GLU PRO ARG TYR MET GLU VAL GLY TYR
SEQRES 3 I 275 VAL ASP ASN THR GLU PHE VAL ARG PHE ASP SER ASP ALA
SEQRES 4 I 275 GLU ASN PRO ARG TYR GLU PRO ARG ALA ARG TRP ILE GLU
SEQRES 5 I 275 GLN GLU GLY PRO GLU TYR TRP GLU ARG GLU THR ARG ARG
SEQRES 6 I 275 ALA LYS GLY ASN GLU GLN SER PHE ARG VAL ASP LEU ARG
SEQRES 7 I 275 THR ALA LEU ARG TYR TYR ASN GLN SER ALA GLY GLY SER
SEQRES 8 I 275 HIS THR LEU GLN TRP MET ALA GLY CYS ASP VAL GLU SER
SEQRES 9 I 275 ASP GLY ARG LEU LEU ARG GLY TYR TRP GLN PHE ALA TYR
SEQRES 10 I 275 ASP GLY CYS ASP TYR ILE ALA LEU ASN GLU ASP LEU LYS
SEQRES 11 I 275 THR TRP THR ALA ALA ASP MET ALA ALA GLN ILE THR ARG
SEQRES 12 I 275 ARG LYS TRP GLU GLN ALA GLY ALA ALA GLU ARG ASP ARG
SEQRES 13 I 275 ALA TYR LEU GLU GLY GLU CYS VAL GLU TRP LEU ARG ARG
SEQRES 14 I 275 TYR LEU LYS ASN GLY ASN ALA THR LEU LEU ARG THR ASP
SEQRES 15 I 275 PRO PRO LYS ALA HIS VAL THR HIS HIS ARG ARG PRO GLU
SEQRES 16 I 275 GLY ASP VAL THR LEU ARG CYS TRP ALA LEU GLY PHE TYR
SEQRES 17 I 275 PRO ALA ASP ILE THR LEU THR TRP GLN LEU ASN GLY GLU
SEQRES 18 I 275 GLU LEU THR GLN GLU MET GLU LEU VAL GLU THR ARG PRO
SEQRES 19 I 275 ALA GLY ASP GLY THR PHE GLN LYS TRP ALA SER VAL VAL
SEQRES 20 I 275 VAL PRO LEU GLY LYS GLU GLN LYS TYR THR CYS HIS VAL
SEQRES 21 I 275 GLU HIS GLU GLY LEU PRO GLU PRO LEU THR LEU ARG TRP
SEQRES 22 I 275 GLY LYS
SEQRES 1 J 100 MET ILE GLN LYS THR PRO GLN ILE GLN VAL TYR SER ARG
SEQRES 2 J 100 HIS PRO PRO GLU ASN GLY LYS PRO ASN ILE LEU ASN CYS
SEQRES 3 J 100 TYR VAL THR GLN PHE HIS PRO PRO HIS ILE GLU ILE GLN
SEQRES 4 J 100 MET LEU LYS ASN GLY LYS LYS ILE PRO LYS VAL GLU MET
SEQRES 5 J 100 SER ASP MET SER PHE SER LYS ASP TRP SER PHE TYR ILE
SEQRES 6 J 100 LEU ALA HIS THR GLU PHE THR PRO THR GLU THR ASP THR
SEQRES 7 J 100 TYR ALA CYS ARG VAL LYS HIS ALA SER MET ALA GLU PRO
SEQRES 8 J 100 LYS THR VAL TYR TRP ASP ARG ASP MET
SEQRES 1 K 9 ILE GLY PRO GLY ARG ALA PHE TYR VAL
HET EDO A 301 4
HET EDO B 101 4
HET EDO B 102 4
HET EDO D 101 4
HET GOL F 301 6
HET EDO F 302 4
HET EDO F 303 4
HET GOL F 304 6
HET EDO I 301 4
HETNAM EDO 1,2-ETHANEDIOL
HETNAM GOL GLYCEROL
HETSYN EDO ETHYLENE GLYCOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 13 EDO 7(C2 H6 O2)
FORMUL 17 GOL 2(C3 H8 O3)
FORMUL 22 HOH *220(H2 O)
HELIX 1 AA1 ALA A 49 GLU A 55 5 7
HELIX 2 AA2 GLY A 56 ASN A 86 1 31
HELIX 3 AA3 ASP A 137 ALA A 150 1 14
HELIX 4 AA4 GLY A 151 GLY A 162 1 12
HELIX 5 AA5 GLY A 162 GLY A 175 1 14
HELIX 6 AA6 GLY A 175 LEU A 180 1 6
HELIX 7 AA7 LYS A 253 GLN A 255 5 3
HELIX 8 AA8 ALA C 49 GLU C 53 5 5
HELIX 9 AA9 GLY C 56 ASN C 86 1 31
HELIX 10 AB1 ASP C 137 ALA C 150 1 14
HELIX 11 AB2 GLY C 151 GLY C 162 1 12
HELIX 12 AB3 GLY C 162 GLY C 175 1 14
HELIX 13 AB4 GLY C 175 LEU C 180 1 6
HELIX 14 AB5 LYS C 253 GLN C 255 5 3
HELIX 15 AB6 TRP F 51 GLU F 55 5 5
HELIX 16 AB7 GLY F 56 ASN F 86 1 31
HELIX 17 AB8 ASP F 137 ALA F 150 1 14
HELIX 18 AB9 GLY F 151 GLY F 162 1 12
HELIX 19 AC1 GLY F 162 GLY F 175 1 14
HELIX 20 AC2 GLY F 175 LEU F 180 1 6
HELIX 21 AC3 LYS F 253 TYR F 257 5 5
HELIX 22 AC4 ALA I 49 GLU I 55 5 7
HELIX 23 AC5 GLY I 56 ASN I 86 1 31
HELIX 24 AC6 ASP I 137 GLY I 151 1 15
HELIX 25 AC7 GLY I 151 GLY I 162 1 12
HELIX 26 AC8 GLY I 162 GLY I 175 1 14
HELIX 27 AC9 GLY I 175 LEU I 180 1 6
SHEET 1 AA1 8 GLU A 46 PRO A 47 0
SHEET 2 AA1 8 THR A 31 ASP A 37 -1 N ARG A 35 O GLU A 46
SHEET 3 AA1 8 ARG A 21 VAL A 28 -1 N GLU A 24 O PHE A 36
SHEET 4 AA1 8 HIS A 3 VAL A 12 -1 N ARG A 6 O TYR A 27
SHEET 5 AA1 8 THR A 94 VAL A 103 -1 O VAL A 103 N HIS A 3
SHEET 6 AA1 8 LEU A 109 TYR A 118 -1 O LEU A 110 N ASP A 102
SHEET 7 AA1 8 CYS A 121 LEU A 126 -1 O ILE A 124 N PHE A 116
SHEET 8 AA1 8 TRP A 133 ALA A 135 -1 O THR A 134 N ALA A 125
SHEET 1 AA2 4 LYS A 186 ARG A 193 0
SHEET 2 AA2 4 VAL A 199 PHE A 208 -1 O TRP A 204 N HIS A 188
SHEET 3 AA2 4 PHE A 241 VAL A 249 -1 O VAL A 249 N VAL A 199
SHEET 4 AA2 4 GLU A 229 LEU A 230 -1 N GLU A 229 O SER A 246
SHEET 1 AA3 4 LYS A 186 ARG A 193 0
SHEET 2 AA3 4 VAL A 199 PHE A 208 -1 O TRP A 204 N HIS A 188
SHEET 3 AA3 4 PHE A 241 VAL A 249 -1 O VAL A 249 N VAL A 199
SHEET 4 AA3 4 ARG A 234 PRO A 235 -1 N ARG A 234 O GLN A 242
SHEET 1 AA4 4 GLU A 222 GLU A 223 0
SHEET 2 AA4 4 THR A 214 LEU A 219 -1 N LEU A 219 O GLU A 222
SHEET 3 AA4 4 TYR A 257 GLU A 262 -1 O THR A 258 N GLN A 218
SHEET 4 AA4 4 LEU A 270 LEU A 272 -1 O LEU A 272 N CYS A 259
SHEET 1 AA5 4 GLN B 6 SER B 11 0
SHEET 2 AA5 4 ASN B 21 PHE B 30 -1 O TYR B 26 N GLN B 8
SHEET 3 AA5 4 PHE B 62 PHE B 70 -1 O ALA B 66 N CYS B 25
SHEET 4 AA5 4 GLU B 50 MET B 51 -1 N GLU B 50 O HIS B 67
SHEET 1 AA6 4 GLN B 6 SER B 11 0
SHEET 2 AA6 4 ASN B 21 PHE B 30 -1 O TYR B 26 N GLN B 8
SHEET 3 AA6 4 PHE B 62 PHE B 70 -1 O ALA B 66 N CYS B 25
SHEET 4 AA6 4 SER B 55 PHE B 56 -1 N SER B 55 O TYR B 63
SHEET 1 AA7 4 LYS B 44 LYS B 45 0
SHEET 2 AA7 4 GLU B 36 LYS B 41 -1 N LYS B 41 O LYS B 44
SHEET 3 AA7 4 TYR B 78 LYS B 83 -1 O ALA B 79 N LEU B 40
SHEET 4 AA7 4 LYS B 91 TYR B 94 -1 O LYS B 91 N VAL B 82
SHEET 1 AA8 8 GLU C 46 PRO C 47 0
SHEET 2 AA8 8 THR C 31 ASP C 37 -1 N ARG C 35 O GLU C 46
SHEET 3 AA8 8 ARG C 21 VAL C 28 -1 N GLU C 24 O PHE C 36
SHEET 4 AA8 8 HIS C 3 VAL C 12 -1 N PHE C 8 O VAL C 25
SHEET 5 AA8 8 THR C 94 VAL C 103 -1 O ALA C 99 N TYR C 7
SHEET 6 AA8 8 LEU C 109 TYR C 118 -1 O ARG C 111 N ASP C 102
SHEET 7 AA8 8 CYS C 121 LEU C 126 -1 O ILE C 124 N PHE C 116
SHEET 8 AA8 8 TRP C 133 ALA C 135 -1 O THR C 134 N ALA C 125
SHEET 1 AA9 4 LYS C 186 ARG C 193 0
SHEET 2 AA9 4 ASP C 198 PHE C 208 -1 O TRP C 204 N HIS C 188
SHEET 3 AA9 4 PHE C 241 PRO C 250 -1 O VAL C 249 N VAL C 199
SHEET 4 AA9 4 GLU C 229 LEU C 230 -1 N GLU C 229 O SER C 246
SHEET 1 AB1 4 LYS C 186 ARG C 193 0
SHEET 2 AB1 4 ASP C 198 PHE C 208 -1 O TRP C 204 N HIS C 188
SHEET 3 AB1 4 PHE C 241 PRO C 250 -1 O VAL C 249 N VAL C 199
SHEET 4 AB1 4 ARG C 234 PRO C 235 -1 N ARG C 234 O GLN C 242
SHEET 1 AB2 3 THR C 214 LEU C 219 0
SHEET 2 AB2 3 TYR C 257 GLU C 262 -1 O HIS C 260 N THR C 216
SHEET 3 AB2 3 LEU C 270 ARG C 273 -1 O LEU C 272 N CYS C 259
SHEET 1 AB3 4 GLN D 6 SER D 11 0
SHEET 2 AB3 4 ASN D 21 PHE D 30 -1 O ASN D 24 N TYR D 10
SHEET 3 AB3 4 PHE D 62 PHE D 70 -1 O ALA D 66 N CYS D 25
SHEET 4 AB3 4 GLU D 50 PHE D 56 -1 N SER D 55 O TYR D 63
SHEET 1 AB4 4 LYS D 44 LYS D 45 0
SHEET 2 AB4 4 GLU D 36 LYS D 41 -1 N LYS D 41 O LYS D 44
SHEET 3 AB4 4 TYR D 78 LYS D 83 -1 O ALA D 79 N LEU D 40
SHEET 4 AB4 4 LYS D 91 TYR D 94 -1 O LYS D 91 N VAL D 82
SHEET 1 AB5 8 GLU F 46 PRO F 47 0
SHEET 2 AB5 8 THR F 31 ASP F 37 -1 N ARG F 35 O GLU F 46
SHEET 3 AB5 8 ARG F 21 VAL F 28 -1 N GLU F 24 O PHE F 36
SHEET 4 AB5 8 HIS F 3 VAL F 12 -1 N PHE F 8 O VAL F 25
SHEET 5 AB5 8 THR F 94 GLU F 104 -1 O LEU F 95 N ALA F 11
SHEET 6 AB5 8 ARG F 108 TYR F 118 -1 O LEU F 110 N ASP F 102
SHEET 7 AB5 8 CYS F 121 LEU F 126 -1 O TYR F 123 N PHE F 116
SHEET 8 AB5 8 TRP F 133 ALA F 135 -1 O THR F 134 N ALA F 125
SHEET 1 AB6 4 LYS F 186 ARG F 193 0
SHEET 2 AB6 4 ASP F 198 PHE F 208 -1 O TRP F 204 N HIS F 188
SHEET 3 AB6 4 PHE F 241 PRO F 250 -1 O ALA F 245 N CYS F 203
SHEET 4 AB6 4 GLU F 229 LEU F 230 -1 N GLU F 229 O SER F 246
SHEET 1 AB7 4 LYS F 186 ARG F 193 0
SHEET 2 AB7 4 ASP F 198 PHE F 208 -1 O TRP F 204 N HIS F 188
SHEET 3 AB7 4 PHE F 241 PRO F 250 -1 O ALA F 245 N CYS F 203
SHEET 4 AB7 4 ARG F 234 PRO F 235 -1 N ARG F 234 O GLN F 242
SHEET 1 AB8 3 THR F 214 GLN F 218 0
SHEET 2 AB8 3 THR F 258 GLU F 262 -1 O HIS F 260 N THR F 216
SHEET 3 AB8 3 LEU F 270 LEU F 272 -1 O LEU F 272 N CYS F 259
SHEET 1 AB9 4 GLN G 6 SER G 11 0
SHEET 2 AB9 4 ASN G 21 PHE G 30 -1 O ASN G 24 N TYR G 10
SHEET 3 AB9 4 PHE G 62 PHE G 70 -1 O THR G 68 N LEU G 23
SHEET 4 AB9 4 SER G 55 PHE G 56 -1 N SER G 55 O TYR G 63
SHEET 1 AC1 4 LYS G 44 LYS G 45 0
SHEET 2 AC1 4 GLU G 36 LYS G 41 -1 N LYS G 41 O LYS G 44
SHEET 3 AC1 4 TYR G 78 LYS G 83 -1 O ARG G 81 N GLN G 38
SHEET 4 AC1 4 LYS G 91 TYR G 94 -1 O LYS G 91 N VAL G 82
SHEET 1 AC2 8 TYR I 45 PRO I 47 0
SHEET 2 AC2 8 THR I 31 ASP I 37 -1 N ARG I 35 O GLU I 46
SHEET 3 AC2 8 ARG I 21 VAL I 28 -1 N VAL I 28 O THR I 31
SHEET 4 AC2 8 HIS I 3 VAL I 12 -1 N ARG I 6 O TYR I 27
SHEET 5 AC2 8 THR I 94 VAL I 103 -1 O TRP I 97 N VAL I 9
SHEET 6 AC2 8 LEU I 109 TYR I 118 -1 O ARG I 111 N ASP I 102
SHEET 7 AC2 8 CYS I 121 LEU I 126 -1 O CYS I 121 N TYR I 118
SHEET 8 AC2 8 TRP I 133 ALA I 135 -1 O THR I 134 N ALA I 125
SHEET 1 AC3 4 LYS I 186 ARG I 193 0
SHEET 2 AC3 4 VAL I 199 PHE I 208 -1 O TRP I 204 N HIS I 188
SHEET 3 AC3 4 PHE I 241 VAL I 249 -1 O ALA I 245 N CYS I 203
SHEET 4 AC3 4 ARG I 234 PRO I 235 -1 N ARG I 234 O GLN I 242
SHEET 1 AC4 4 GLU I 222 GLU I 223 0
SHEET 2 AC4 4 THR I 214 LEU I 219 -1 N LEU I 219 O GLU I 222
SHEET 3 AC4 4 TYR I 257 GLU I 262 -1 O HIS I 260 N THR I 216
SHEET 4 AC4 4 THR I 271 LEU I 272 -1 O LEU I 272 N CYS I 259
SHEET 1 AC5 4 GLN J 6 SER J 11 0
SHEET 2 AC5 4 ASN J 21 PHE J 30 -1 O THR J 28 N GLN J 6
SHEET 3 AC5 4 PHE J 62 PHE J 70 -1 O PHE J 70 N ASN J 21
SHEET 4 AC5 4 GLU J 50 MET J 51 -1 N GLU J 50 O HIS J 67
SHEET 1 AC6 4 GLN J 6 SER J 11 0
SHEET 2 AC6 4 ASN J 21 PHE J 30 -1 O THR J 28 N GLN J 6
SHEET 3 AC6 4 PHE J 62 PHE J 70 -1 O PHE J 70 N ASN J 21
SHEET 4 AC6 4 SER J 55 PHE J 56 -1 N SER J 55 O TYR J 63
SHEET 1 AC7 4 LYS J 44 LYS J 45 0
SHEET 2 AC7 4 GLU J 36 LYS J 41 -1 N LYS J 41 O LYS J 44
SHEET 3 AC7 4 TYR J 78 LYS J 83 -1 O ALA J 79 N LEU J 40
SHEET 4 AC7 4 LYS J 91 TYR J 94 -1 O LYS J 91 N VAL J 82
SSBOND 1 CYS A 101 CYS A 164 1555 1555 2.04
SSBOND 2 CYS A 203 CYS A 259 1555 1555 2.02
SSBOND 3 CYS B 25 CYS B 80 1555 1555 2.03
SSBOND 4 CYS C 101 CYS C 164 1555 1555 2.05
SSBOND 5 CYS C 203 CYS C 259 1555 1555 2.02
SSBOND 6 CYS D 25 CYS D 80 1555 1555 2.03
SSBOND 7 CYS F 101 CYS F 164 1555 1555 2.04
SSBOND 8 CYS F 203 CYS F 259 1555 1555 2.02
SSBOND 9 CYS G 25 CYS G 80 1555 1555 2.03
SSBOND 10 CYS I 101 CYS I 164 1555 1555 2.04
SSBOND 11 CYS I 203 CYS I 259 1555 1555 2.03
SSBOND 12 CYS J 25 CYS J 80 1555 1555 2.03
LINK SG CYS F 121 O1 GOL F 301 1555 1555 1.47
CISPEP 1 TYR A 209 PRO A 210 0 0.04
CISPEP 2 HIS B 31 PRO B 32 0 5.45
CISPEP 3 TYR C 209 PRO C 210 0 -2.41
CISPEP 4 HIS D 31 PRO D 32 0 6.96
CISPEP 5 TYR F 209 PRO F 210 0 1.20
CISPEP 6 HIS G 31 PRO G 32 0 4.35
CISPEP 7 TYR I 209 PRO I 210 0 5.83
CISPEP 8 HIS J 31 PRO J 32 0 3.10
SITE 1 AC1 8 HIS A 188 TRP A 204 LEU A 206 GLN A 242
SITE 2 AC1 8 HOH A 403 SER B 11 PRO B 14 HOH B 210
SITE 1 AC2 8 LEU B 40 ASN B 42 GLY B 43 THR B 77
SITE 2 AC2 8 ALA B 79 TYR B 94 PRO F 195 GLU F 196
SITE 1 AC3 7 ASP B 76 THR B 77 TYR B 78 TRP B 95
SITE 2 AC3 7 ARG B 97 HOH B 220 ARG F 193
SITE 1 AC4 2 CYS C 121 ILE D 1
SITE 1 AC5 4 LYS F 146 HOH F 402 TYR H 8 TYR P 8
SITE 1 AC6 5 VAL A 76 THR A 80 ARG A 83 LYS F 146
SITE 2 AC6 5 GLN F 149
SITE 1 AC7 5 ALA F 236 GLY F 237 ASP F 238 ARG G 12
SITE 2 AC7 5 ILE G 22
SITE 1 AC8 4 TYR E 8 LYS I 146 HOH I 401 TYR K 8
SITE 1 AC9 9 ALA F 117 TYR F 118 ASP F 119 GLY F 120
SITE 2 AC9 9 ASP F 122 TYR F 123 ASN I 86 GLN I 87
SITE 3 AC9 9 SER I 88
CRYST1 51.420 75.360 120.030 93.52 87.14 96.50 P 1 4
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 0.019448 0.002215 -0.000849 0.00000
SCALE2 0.000000 0.013355 0.000750 0.00000
SCALE3 0.000000 0.000000 0.008355 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
