HEADER PROTEIN BINDING/SIGNALING PROTEIN 14-JAN-11 3QBV
TITLE STRUCTURE OF DESIGNED ORTHOGONAL INTERACTION BETWEEN CDC42 AND
TITLE 2 NUCLEOTIDE EXCHANGE DOMAINS OF INTERSECTIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CELL DIVISION CONTROL PROTEIN 42 HOMOLOG;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: UNP RESIDUES 1-178;
COMPND 5 SYNONYM: G25K GTP-BINDING PROTEIN;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: INTERSECTIN-1;
COMPND 10 CHAIN: B, D;
COMPND 11 FRAGMENT: DH AND PH DOMAINS (UNP RESIDUES 1229-1571);
COMPND 12 SYNONYM: SH3 DOMAIN-CONTAINING PROTEIN 1A, SH3P17;
COMPND 13 ENGINEERED: YES;
COMPND 14 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CDC42;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA2;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGKC006;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: ITSN1, ITSN, SH3D1A;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: ROSETTA2;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PGKI009
KEYWDS COMPUTATIONALLY DESIGNED, ORTHOGONAL INTERACTION, GTPASE, NUCLEOTIDE
KEYWDS 2 EXCHANGE, CELL MEMBRANE, GTP-BINDING, LIPOPROTEIN, MEMBRANE,
KEYWDS 3 METHYLATION, NUCLEOTIDE-BINDING, PRENYLATION, CELL JUNCTION, CELL
KEYWDS 4 PROJECTION, ENDOCYTOSIS, PHOSPHOPROTEIN, SH3 DOMAIN, SYNAPSE,
KEYWDS 5 SYNAPTOSOME, PROTEIN BINDING-SIGNALING PROTEIN COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR G.T.KAPP,A.REMENYI,W.A.LIM,T.KORTEMME
REVDAT 5 13-SEP-23 3QBV 1 REMARK SEQADV
REVDAT 4 25-APR-12 3QBV 1 JRNL
REVDAT 3 18-APR-12 3QBV 1 JRNL
REVDAT 2 21-MAR-12 3QBV 1 JRNL
REVDAT 1 08-FEB-12 3QBV 0
JRNL AUTH G.T.KAPP,S.LIU,A.STEIN,D.T.WONG,A.REMENYI,B.J.YEH,
JRNL AUTH 2 J.S.FRASER,J.TAUNTON,W.A.LIM,T.KORTEMME
JRNL TITL CONTROL OF PROTEIN SIGNALING USING A COMPUTATIONALLY
JRNL TITL 2 DESIGNED GTPASE/GEF ORTHOGONAL PAIR.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 109 5277 2012
JRNL REFN ISSN 0027-8424
JRNL PMID 22403064
JRNL DOI 10.1073/PNAS.1114487109
REMARK 2
REMARK 2 RESOLUTION. 2.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_847
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) : 2.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.85
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 35295
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.246
REMARK 3 R VALUE (WORKING SET) : 0.241
REMARK 3 FREE R VALUE : 0.284
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.910
REMARK 3 FREE R VALUE TEST SET COUNT : 3499
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 45.8543 - 7.7368 0.99 1331 132 0.2209 0.2394
REMARK 3 2 7.7368 - 6.1456 1.00 1314 135 0.2843 0.2898
REMARK 3 3 6.1456 - 5.3701 1.00 1268 166 0.3019 0.3826
REMARK 3 4 5.3701 - 4.8797 1.00 1295 131 0.2170 0.2765
REMARK 3 5 4.8797 - 4.5303 1.00 1269 146 0.2173 0.2152
REMARK 3 6 4.5303 - 4.2634 1.00 1259 165 0.2122 0.2676
REMARK 3 7 4.2634 - 4.0500 1.00 1285 140 0.2121 0.2460
REMARK 3 8 4.0500 - 3.8738 1.00 1253 153 0.2122 0.2544
REMARK 3 9 3.8738 - 3.7248 1.00 1278 160 0.2244 0.2704
REMARK 3 10 3.7248 - 3.5963 1.00 1260 148 0.2370 0.2725
REMARK 3 11 3.5963 - 3.4839 1.00 1254 143 0.2188 0.2501
REMARK 3 12 3.4839 - 3.3843 1.00 1301 119 0.2510 0.3031
REMARK 3 13 3.3843 - 3.2953 1.00 1284 146 0.2453 0.3045
REMARK 3 14 3.2953 - 3.2149 1.00 1247 165 0.2622 0.3321
REMARK 3 15 3.2149 - 3.1418 1.00 1278 125 0.2514 0.3110
REMARK 3 16 3.1418 - 3.0750 1.00 1268 138 0.2429 0.2952
REMARK 3 17 3.0750 - 3.0135 1.00 1270 140 0.2556 0.3499
REMARK 3 18 3.0135 - 2.9566 1.00 1250 138 0.2448 0.3314
REMARK 3 19 2.9566 - 2.9038 1.00 1304 149 0.2662 0.3082
REMARK 3 20 2.9038 - 2.8546 1.00 1242 111 0.2634 0.3779
REMARK 3 21 2.8546 - 2.8086 1.00 1302 141 0.2678 0.2902
REMARK 3 22 2.8086 - 2.7654 0.99 1271 115 0.2809 0.3736
REMARK 3 23 2.7654 - 2.7247 1.00 1277 140 0.3077 0.3519
REMARK 3 24 2.7247 - 2.6863 0.97 1229 129 0.2723 0.3342
REMARK 3 25 2.6863 - 2.6500 0.95 1207 124 0.3050 0.3203
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.98
REMARK 3 K_SOL : 0.32
REMARK 3 B_SOL : 43.11
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.900
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.880
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -5.73780
REMARK 3 B22 (A**2) : -5.07010
REMARK 3 B33 (A**2) : 10.80790
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.13870
REMARK 3 B23 (A**2) : 0.00000
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 7070
REMARK 3 ANGLE : 1.001 9625
REMARK 3 CHIRALITY : 0.065 1139
REMARK 3 PLANARITY : 0.005 1246
REMARK 3 DIHEDRAL : 15.216 2466
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 30
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 1:24)
REMARK 3 ORIGIN FOR THE GROUP (A): 33.4851 13.9413 30.2990
REMARK 3 T TENSOR
REMARK 3 T11: 0.3369 T22: 0.3290
REMARK 3 T33: 0.1948 T12: 0.0270
REMARK 3 T13: -0.0558 T23: -0.1322
REMARK 3 L TENSOR
REMARK 3 L11: 0.0295 L22: 0.0211
REMARK 3 L33: 0.1035 L12: 0.0042
REMARK 3 L13: -0.0209 L23: -0.0167
REMARK 3 S TENSOR
REMARK 3 S11: -0.1042 S12: 0.0022 S13: 0.0463
REMARK 3 S21: -0.0577 S22: 0.0106 S23: -0.0330
REMARK 3 S31: -0.0000 S32: -0.0748 S33: -0.0911
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 25:40)
REMARK 3 ORIGIN FOR THE GROUP (A): 32.5340 14.5417 39.6208
REMARK 3 T TENSOR
REMARK 3 T11: 0.2661 T22: 0.3719
REMARK 3 T33: 0.6092 T12: -0.0573
REMARK 3 T13: 0.1120 T23: -0.0820
REMARK 3 L TENSOR
REMARK 3 L11: 0.0081 L22: 0.0108
REMARK 3 L33: 0.0034 L12: 0.0025
REMARK 3 L13: 0.0051 L23: -0.0043
REMARK 3 S TENSOR
REMARK 3 S11: -0.0033 S12: -0.0161 S13: 0.0313
REMARK 3 S21: 0.0862 S22: 0.0615 S23: 0.0207
REMARK 3 S31: 0.0759 S32: 0.0009 S33: 0.0001
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 41:56)
REMARK 3 ORIGIN FOR THE GROUP (A): 27.4901 25.4752 27.6550
REMARK 3 T TENSOR
REMARK 3 T11: 0.2524 T22: 0.2960
REMARK 3 T33: 0.2637 T12: 0.0034
REMARK 3 T13: 0.0190 T23: 0.0146
REMARK 3 L TENSOR
REMARK 3 L11: 0.1457 L22: 0.0141
REMARK 3 L33: 0.1256 L12: -0.0423
REMARK 3 L13: 0.1339 L23: -0.0363
REMARK 3 S TENSOR
REMARK 3 S11: -0.1379 S12: 0.0170 S13: 0.1575
REMARK 3 S21: -0.0135 S22: -0.0743 S23: 0.0363
REMARK 3 S31: -0.0593 S32: -0.0095 S33: -0.0157
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 57:86)
REMARK 3 ORIGIN FOR THE GROUP (A): 32.4800 5.2086 25.2115
REMARK 3 T TENSOR
REMARK 3 T11: 0.2679 T22: 0.2746
REMARK 3 T33: 0.1429 T12: -0.1069
REMARK 3 T13: 0.0649 T23: -0.1777
REMARK 3 L TENSOR
REMARK 3 L11: 0.0116 L22: 0.0139
REMARK 3 L33: 0.0394 L12: -0.0077
REMARK 3 L13: -0.0124 L23: 0.0123
REMARK 3 S TENSOR
REMARK 3 S11: -0.0314 S12: 0.0559 S13: -0.0005
REMARK 3 S21: -0.0653 S22: -0.0486 S23: -0.0243
REMARK 3 S31: -0.0044 S32: -0.0306 S33: -0.1095
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 87:122)
REMARK 3 ORIGIN FOR THE GROUP (A): 41.0028 8.0992 21.9921
REMARK 3 T TENSOR
REMARK 3 T11: 0.2954 T22: 0.3483
REMARK 3 T33: 0.0834 T12: -0.0814
REMARK 3 T13: 0.1372 T23: -0.1262
REMARK 3 L TENSOR
REMARK 3 L11: 0.0135 L22: 0.1506
REMARK 3 L33: 0.1125 L12: -0.0288
REMARK 3 L13: -0.0360 L23: 0.0231
REMARK 3 S TENSOR
REMARK 3 S11: -0.0449 S12: 0.0604 S13: 0.0073
REMARK 3 S21: -0.0157 S22: 0.0762 S23: -0.1408
REMARK 3 S31: 0.0487 S32: 0.1146 S33: -0.1505
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 123:164)
REMARK 3 ORIGIN FOR THE GROUP (A): 49.6747 12.4509 25.0645
REMARK 3 T TENSOR
REMARK 3 T11: 0.2967 T22: 0.4181
REMARK 3 T33: 0.5330 T12: -0.0279
REMARK 3 T13: 0.0594 T23: -0.1538
REMARK 3 L TENSOR
REMARK 3 L11: 0.0200 L22: 0.0178
REMARK 3 L33: 0.0093 L12: 0.0131
REMARK 3 L13: -0.0025 L23: -0.0106
REMARK 3 S TENSOR
REMARK 3 S11: -0.1126 S12: 0.0790 S13: 0.0165
REMARK 3 S21: 0.1317 S22: 0.0039 S23: -0.4527
REMARK 3 S31: -0.1223 S32: 0.1179 S33: -0.0009
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 165:178)
REMARK 3 ORIGIN FOR THE GROUP (A): 34.9177 23.1221 23.0368
REMARK 3 T TENSOR
REMARK 3 T11: 0.1966 T22: 0.1997
REMARK 3 T33: 0.1421 T12: -0.0486
REMARK 3 T13: 0.0271 T23: 0.0073
REMARK 3 L TENSOR
REMARK 3 L11: 0.0017 L22: 0.0027
REMARK 3 L33: 0.0075 L12: -0.0031
REMARK 3 L13: 0.0010 L23: -0.0043
REMARK 3 S TENSOR
REMARK 3 S11: -0.0230 S12: 0.1018 S13: 0.0770
REMARK 3 S21: -0.0197 S22: 0.0527 S23: -0.0064
REMARK 3 S31: -0.0068 S32: -0.0049 S33: -0.0000
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 1229:1439)
REMARK 3 ORIGIN FOR THE GROUP (A): 19.5672 1.3225 36.9501
REMARK 3 T TENSOR
REMARK 3 T11: 0.0726 T22: -0.1008
REMARK 3 T33: 0.0372 T12: -0.0291
REMARK 3 T13: -0.0172 T23: -0.1594
REMARK 3 L TENSOR
REMARK 3 L11: 0.2096 L22: 0.0797
REMARK 3 L33: 0.3439 L12: -0.0482
REMARK 3 L13: 0.0562 L23: 0.0547
REMARK 3 S TENSOR
REMARK 3 S11: 0.2401 S12: 0.0880 S13: -0.1340
REMARK 3 S21: 0.0504 S22: 0.2055 S23: 0.0762
REMARK 3 S31: -0.0511 S32: -0.3263 S33: 0.1807
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 1440:1462)
REMARK 3 ORIGIN FOR THE GROUP (A): 16.1875 -20.3899 9.4201
REMARK 3 T TENSOR
REMARK 3 T11: 0.4196 T22: 0.4397
REMARK 3 T33: 0.8431 T12: 0.1246
REMARK 3 T13: -0.3115 T23: -0.4385
REMARK 3 L TENSOR
REMARK 3 L11: 0.0520 L22: 0.0494
REMARK 3 L33: 0.0589 L12: 0.0020
REMARK 3 L13: -0.0260 L23: -0.0459
REMARK 3 S TENSOR
REMARK 3 S11: 0.0563 S12: 0.0484 S13: -0.0572
REMARK 3 S21: -0.0149 S22: -0.0444 S23: 0.0669
REMARK 3 S31: 0.0336 S32: -0.0239 S33: 0.0423
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 1463:1490)
REMARK 3 ORIGIN FOR THE GROUP (A): 24.8308 -12.3171 0.8437
REMARK 3 T TENSOR
REMARK 3 T11: 0.4975 T22: 0.9291
REMARK 3 T33: 0.5551 T12: 0.0192
REMARK 3 T13: 0.0092 T23: -0.5178
REMARK 3 L TENSOR
REMARK 3 L11: 0.1040 L22: 0.0101
REMARK 3 L33: 0.1350 L12: 0.0244
REMARK 3 L13: -0.0528 L23: 0.0152
REMARK 3 S TENSOR
REMARK 3 S11: 0.0807 S12: 0.0839 S13: 0.0389
REMARK 3 S21: -0.0880 S22: 0.0145 S23: 0.0014
REMARK 3 S31: -0.0190 S32: 0.0092 S33: 0.0509
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 1491:1578)
REMARK 3 ORIGIN FOR THE GROUP (A): 28.0636 -16.5362 2.5799
REMARK 3 T TENSOR
REMARK 3 T11: 0.3980 T22: 0.7191
REMARK 3 T33: 0.4480 T12: 0.1955
REMARK 3 T13: -0.0268 T23: -0.3928
REMARK 3 L TENSOR
REMARK 3 L11: 0.1395 L22: 0.1612
REMARK 3 L33: 0.1329 L12: 0.0899
REMARK 3 L13: 0.0887 L23: 0.1356
REMARK 3 S TENSOR
REMARK 3 S11: -0.0950 S12: 0.1375 S13: -0.0847
REMARK 3 S21: -0.0923 S22: -0.0325 S23: 0.0281
REMARK 3 S31: 0.0959 S32: -0.0347 S33: 0.0081
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 1:24)
REMARK 3 ORIGIN FOR THE GROUP (A): -20.2530 -30.9073 30.3482
REMARK 3 T TENSOR
REMARK 3 T11: 0.3740 T22: 0.3419
REMARK 3 T33: 0.1392 T12: 0.0653
REMARK 3 T13: 0.0109 T23: 0.2046
REMARK 3 L TENSOR
REMARK 3 L11: 0.0133 L22: 0.0679
REMARK 3 L33: 0.0119 L12: 0.0045
REMARK 3 L13: -0.0013 L23: -0.0280
REMARK 3 S TENSOR
REMARK 3 S11: -0.0884 S12: -0.0155 S13: -0.0273
REMARK 3 S21: -0.0113 S22: 0.0019 S23: -0.0161
REMARK 3 S31: -0.0340 S32: 0.0248 S33: -0.1310
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 25:40)
REMARK 3 ORIGIN FOR THE GROUP (A): -19.1881 -31.3785 39.6810
REMARK 3 T TENSOR
REMARK 3 T11: 0.2789 T22: 0.3931
REMARK 3 T33: 0.6750 T12: -0.0749
REMARK 3 T13: -0.1280 T23: -0.0272
REMARK 3 L TENSOR
REMARK 3 L11: 0.0101 L22: 0.0128
REMARK 3 L33: 0.0049 L12: -0.0041
REMARK 3 L13: 0.0010 L23: 0.0053
REMARK 3 S TENSOR
REMARK 3 S11: -0.0337 S12: -0.0190 S13: -0.0237
REMARK 3 S21: 0.1001 S22: -0.0121 S23: 0.0721
REMARK 3 S31: 0.0417 S32: 0.0043 S33: -0.0001
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 41:56)
REMARK 3 ORIGIN FOR THE GROUP (A): -14.2579 -42.4356 27.6758
REMARK 3 T TENSOR
REMARK 3 T11: 0.2422 T22: 0.2041
REMARK 3 T33: 0.2026 T12: 0.0548
REMARK 3 T13: 0.0221 T23: 0.0159
REMARK 3 L TENSOR
REMARK 3 L11: 0.0018 L22: 0.0051
REMARK 3 L33: -0.0009 L12: -0.0050
REMARK 3 L13: -0.0005 L23: 0.0026
REMARK 3 S TENSOR
REMARK 3 S11: -0.0512 S12: 0.0574 S13: -0.1222
REMARK 3 S21: -0.0139 S22: -0.0946 S23: -0.0393
REMARK 3 S31: 0.1152 S32: -0.0087 S33: -0.0001
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 57:86)
REMARK 3 ORIGIN FOR THE GROUP (A): -19.1312 -22.1453 25.2072
REMARK 3 T TENSOR
REMARK 3 T11: 0.1943 T22: 0.2468
REMARK 3 T33: 0.1565 T12: -0.0545
REMARK 3 T13: -0.0146 T23: 0.2753
REMARK 3 L TENSOR
REMARK 3 L11: 0.1307 L22: 0.0199
REMARK 3 L33: 0.0330 L12: 0.0102
REMARK 3 L13: 0.0133 L23: -0.0247
REMARK 3 S TENSOR
REMARK 3 S11: -0.1295 S12: 0.0718 S13: 0.0586
REMARK 3 S21: -0.0989 S22: -0.0752 S23: -0.0724
REMARK 3 S31: 0.1462 S32: 0.0621 S33: -0.3852
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 87:122)
REMARK 3 ORIGIN FOR THE GROUP (A): -27.6896 -25.1853 21.8366
REMARK 3 T TENSOR
REMARK 3 T11: 0.3523 T22: 0.4321
REMARK 3 T33: 0.1768 T12: -0.0254
REMARK 3 T13: -0.1497 T23: 0.2187
REMARK 3 L TENSOR
REMARK 3 L11: 0.2541 L22: 0.6134
REMARK 3 L33: 0.6487 L12: -0.3922
REMARK 3 L13: -0.2638 L23: 0.4141
REMARK 3 S TENSOR
REMARK 3 S11: -0.1275 S12: 0.0927 S13: -0.0372
REMARK 3 S21: -0.0515 S22: -0.0042 S23: 0.2160
REMARK 3 S31: 0.0052 S32: -0.1282 S33: -0.3285
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 123:138)
REMARK 3 ORIGIN FOR THE GROUP (A): -44.6287 -21.6557 31.5241
REMARK 3 T TENSOR
REMARK 3 T11: 0.2213 T22: 0.3632
REMARK 3 T33: 0.6820 T12: 0.0412
REMARK 3 T13: -0.0201 T23: 0.1529
REMARK 3 L TENSOR
REMARK 3 L11: 0.0029 L22: 0.0049
REMARK 3 L33: 0.0037 L12: 0.0014
REMARK 3 L13: -0.0016 L23: -0.0046
REMARK 3 S TENSOR
REMARK 3 S11: 0.0310 S12: -0.0210 S13: 0.0258
REMARK 3 S21: -0.0239 S22: 0.0118 S23: -0.0065
REMARK 3 S31: 0.0192 S32: -0.0120 S33: -0.0001
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 139:149)
REMARK 3 ORIGIN FOR THE GROUP (A): -35.4820 -30.7058 15.8447
REMARK 3 T TENSOR
REMARK 3 T11: 0.6229 T22: 0.7112
REMARK 3 T33: 0.6475 T12: -0.0487
REMARK 3 T13: -0.3034 T23: 0.0130
REMARK 3 L TENSOR
REMARK 3 L11: 0.0011 L22: -0.0003
REMARK 3 L33: 0.0019 L12: 0.0007
REMARK 3 L13: 0.0011 L23: 0.0005
REMARK 3 S TENSOR
REMARK 3 S11: -0.0331 S12: 0.0074 S13: -0.0456
REMARK 3 S21: 0.0157 S22: -0.0226 S23: 0.0500
REMARK 3 S31: 0.0237 S32: -0.0348 S33: 0.0000
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 150:178)
REMARK 3 ORIGIN FOR THE GROUP (A): -26.2455 -37.9150 25.4111
REMARK 3 T TENSOR
REMARK 3 T11: 0.2372 T22: 0.2123
REMARK 3 T33: 0.1620 T12: -0.0045
REMARK 3 T13: -0.0050 T23: 0.0533
REMARK 3 L TENSOR
REMARK 3 L11: 0.1321 L22: 0.0094
REMARK 3 L33: 0.0177 L12: 0.0167
REMARK 3 L13: -0.0023 L23: 0.0073
REMARK 3 S TENSOR
REMARK 3 S11: -0.0555 S12: 0.2340 S13: -0.1736
REMARK 3 S21: 0.0358 S22: 0.0831 S23: 0.1887
REMARK 3 S31: 0.1180 S32: -0.0411 S33: 0.0079
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 1229:1262)
REMARK 3 ORIGIN FOR THE GROUP (A): -13.0776 -23.3471 48.1075
REMARK 3 T TENSOR
REMARK 3 T11: 0.2181 T22: 0.1851
REMARK 3 T33: 0.3064 T12: -0.0413
REMARK 3 T13: -0.0128 T23: 0.0757
REMARK 3 L TENSOR
REMARK 3 L11: 0.0193 L22: 0.0048
REMARK 3 L33: 0.0283 L12: 0.0147
REMARK 3 L13: 0.0183 L23: 0.0153
REMARK 3 S TENSOR
REMARK 3 S11: 0.0378 S12: -0.0402 S13: -0.0749
REMARK 3 S21: 0.1452 S22: -0.0747 S23: 0.1272
REMARK 3 S31: 0.0649 S32: 0.0442 S33: -0.0001
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 1263:1284)
REMARK 3 ORIGIN FOR THE GROUP (A): 9.4830 -22.3870 27.3266
REMARK 3 T TENSOR
REMARK 3 T11: 0.2068 T22: 0.2297
REMARK 3 T33: 0.3133 T12: -0.0660
REMARK 3 T13: -0.1217 T23: -0.0353
REMARK 3 L TENSOR
REMARK 3 L11: 0.2094 L22: 0.0020
REMARK 3 L33: 0.3789 L12: -0.0159
REMARK 3 L13: -0.2809 L23: 0.0228
REMARK 3 S TENSOR
REMARK 3 S11: 0.0996 S12: -0.1093 S13: 0.0586
REMARK 3 S21: -0.0091 S22: 0.0971 S23: -0.1381
REMARK 3 S31: -0.1108 S32: 0.0044 S33: 0.1136
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 1285:1326)
REMARK 3 ORIGIN FOR THE GROUP (A): -7.3307 -14.8010 50.2779
REMARK 3 T TENSOR
REMARK 3 T11: 0.1858 T22: 0.1975
REMARK 3 T33: 0.1996 T12: -0.0283
REMARK 3 T13: 0.0139 T23: 0.0363
REMARK 3 L TENSOR
REMARK 3 L11: 0.0230 L22: 0.0551
REMARK 3 L33: 0.0376 L12: -0.0150
REMARK 3 L13: 0.0095 L23: -0.0387
REMARK 3 S TENSOR
REMARK 3 S11: 0.0457 S12: -0.1010 S13: 0.0092
REMARK 3 S21: 0.2323 S22: 0.0044 S23: -0.1099
REMARK 3 S31: 0.0019 S32: 0.1662 S33: -0.0025
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 1327:1349)
REMARK 3 ORIGIN FOR THE GROUP (A): -0.8129 -17.8947 24.2489
REMARK 3 T TENSOR
REMARK 3 T11: 0.3311 T22: 0.2783
REMARK 3 T33: 0.2745 T12: 0.0208
REMARK 3 T13: -0.0716 T23: 0.1013
REMARK 3 L TENSOR
REMARK 3 L11: 0.0160 L22: 0.0113
REMARK 3 L33: 0.0036 L12: -0.0017
REMARK 3 L13: 0.0044 L23: 0.0089
REMARK 3 S TENSOR
REMARK 3 S11: 0.1011 S12: 0.1485 S13: 0.0342
REMARK 3 S21: -0.0023 S22: 0.0863 S23: 0.2109
REMARK 3 S31: 0.0344 S32: -0.0114 S33: 0.0004
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 1350:1370)
REMARK 3 ORIGIN FOR THE GROUP (A): 3.4735 -34.7305 28.2886
REMARK 3 T TENSOR
REMARK 3 T11: 0.2515 T22: 0.1354
REMARK 3 T33: 0.2144 T12: 0.0688
REMARK 3 T13: 0.0255 T23: 0.0186
REMARK 3 L TENSOR
REMARK 3 L11: 0.0608 L22: 0.0200
REMARK 3 L33: 0.0412 L12: 0.0346
REMARK 3 L13: 0.0119 L23: 0.0144
REMARK 3 S TENSOR
REMARK 3 S11: -0.0083 S12: 0.0435 S13: -0.1824
REMARK 3 S21: -0.0416 S22: 0.0772 S23: -0.0636
REMARK 3 S31: 0.0285 S32: 0.0247 S33: 0.0000
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 1371:1402)
REMARK 3 ORIGIN FOR THE GROUP (A): -15.9459 -17.2343 41.1177
REMARK 3 T TENSOR
REMARK 3 T11: 0.1210 T22: 0.1526
REMARK 3 T33: 0.1946 T12: 0.0257
REMARK 3 T13: -0.0051 T23: 0.0166
REMARK 3 L TENSOR
REMARK 3 L11: 0.0453 L22: 0.0112
REMARK 3 L33: 0.0246 L12: -0.0234
REMARK 3 L13: 0.0357 L23: -0.0195
REMARK 3 S TENSOR
REMARK 3 S11: -0.0430 S12: 0.0602 S13: -0.0261
REMARK 3 S21: 0.0899 S22: -0.0490 S23: 0.0528
REMARK 3 S31: -0.0062 S32: 0.0741 S33: -0.0000
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 1403:1439)
REMARK 3 ORIGIN FOR THE GROUP (A): -10.2543 -6.9831 28.2300
REMARK 3 T TENSOR
REMARK 3 T11: 0.2360 T22: 0.1421
REMARK 3 T33: 0.3368 T12: -0.0112
REMARK 3 T13: 0.0433 T23: 0.1757
REMARK 3 L TENSOR
REMARK 3 L11: 0.1000 L22: 0.0023
REMARK 3 L33: 0.1412 L12: 0.0291
REMARK 3 L13: 0.0103 L23: 0.0070
REMARK 3 S TENSOR
REMARK 3 S11: 0.0079 S12: 0.1280 S13: 0.1441
REMARK 3 S21: 0.0415 S22: -0.0405 S23: -0.0205
REMARK 3 S31: -0.2179 S32: 0.0904 S33: -0.0835
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 1440:1479)
REMARK 3 ORIGIN FOR THE GROUP (A): -6.7646 -0.2799 8.3955
REMARK 3 T TENSOR
REMARK 3 T11: 0.7532 T22: 0.6480
REMARK 3 T33: 0.6529 T12: -0.0193
REMARK 3 T13: 0.0798 T23: 0.2588
REMARK 3 L TENSOR
REMARK 3 L11: 0.0085 L22: 0.0081
REMARK 3 L33: 0.0087 L12: -0.0000
REMARK 3 L13: 0.0112 L23: -0.0036
REMARK 3 S TENSOR
REMARK 3 S11: -0.0655 S12: 0.0277 S13: 0.0135
REMARK 3 S21: 0.0142 S22: -0.0154 S23: 0.0539
REMARK 3 S31: -0.0958 S32: -0.0187 S33: -0.0001
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 1480:1492)
REMARK 3 ORIGIN FOR THE GROUP (A): -9.4366 -0.2831 4.2034
REMARK 3 T TENSOR
REMARK 3 T11: 0.8355 T22: 0.7580
REMARK 3 T33: 0.4322 T12: 0.1056
REMARK 3 T13: 0.1284 T23: 0.1242
REMARK 3 L TENSOR
REMARK 3 L11: -0.0004 L22: 0.0050
REMARK 3 L33: 0.0052 L12: -0.0008
REMARK 3 L13: 0.0004 L23: -0.0058
REMARK 3 S TENSOR
REMARK 3 S11: 0.0057 S12: 0.0462 S13: 0.0047
REMARK 3 S21: 0.0166 S22: -0.0344 S23: 0.0044
REMARK 3 S31: -0.0050 S32: 0.0201 S33: 0.0001
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 1493:1562)
REMARK 3 ORIGIN FOR THE GROUP (A): -10.1235 -2.7253 1.3589
REMARK 3 T TENSOR
REMARK 3 T11: 0.9464 T22: 0.6963
REMARK 3 T33: 0.6382 T12: 0.1170
REMARK 3 T13: -0.2256 T23: 0.2184
REMARK 3 L TENSOR
REMARK 3 L11: 0.0004 L22: 0.0001
REMARK 3 L33: 0.0042 L12: 0.0009
REMARK 3 L13: 0.0033 L23: 0.0026
REMARK 3 S TENSOR
REMARK 3 S11: -0.0295 S12: 0.0372 S13: -0.0287
REMARK 3 S21: -0.0628 S22: 0.0526 S23: 0.0462
REMARK 3 S31: 0.1542 S32: 0.0337 S33: -0.0088
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 1563:1579)
REMARK 3 ORIGIN FOR THE GROUP (A): -19.3654 8.1135 12.0119
REMARK 3 T TENSOR
REMARK 3 T11: 1.1777 T22: 1.2870
REMARK 3 T33: 1.3021 T12: 0.2160
REMARK 3 T13: -0.0362 T23: 0.2481
REMARK 3 L TENSOR
REMARK 3 L11: 0.0046 L22: 0.0282
REMARK 3 L33: 0.0073 L12: 0.0079
REMARK 3 L13: 0.0058 L23: 0.0130
REMARK 3 S TENSOR
REMARK 3 S11: 0.0639 S12: -0.0021 S13: 0.0050
REMARK 3 S21: -0.0019 S22: 0.0245 S23: 0.0074
REMARK 3 S31: -0.0292 S32: -0.0029 S33: 0.0001
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 2
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'B' AND (RESSEQ 1229:1443 OR RESSEQ
REMARK 3 1450:1469 OR RESSEQ 1562:1578 )
REMARK 3 SELECTION : CHAIN 'D' AND (RESSEQ 1229:1443 OR RESSEQ
REMARK 3 1450:1469 OR RESSEQ 1562:1578 )
REMARK 3 ATOM PAIRS NUMBER : 1822
REMARK 3 RMSD : 0.024
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'A' AND (RESSEQ 1:29 OR RESSEQ
REMARK 3 31:178 )
REMARK 3 SELECTION : CHAIN 'C' AND (RESSEQ 1:29 OR RESSEQ
REMARK 3 31:178 )
REMARK 3 ATOM PAIRS NUMBER : 1270
REMARK 3 RMSD : 0.020
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3QBV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JAN-11.
REMARK 100 THE DEPOSITION ID IS D_1000063448.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-SEP-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.115872
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35386
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.650
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.41200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1KI1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM TRIS PH 7.5, 25% PEG 3350, 150MM
REMARK 280 AMMONIUM SULFATE, AND 1MM DTT, TEMPERATURE 295K, VAPOR DIFFUSION,
REMARK 280 HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 40.03100
REMARK 290 SMTRY3 2 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2820 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24270 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3010 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23530 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER A 30
REMARK 465 LEU B 1445
REMARK 465 SER B 1446
REMARK 465 GLU B 1447
REMARK 465 ASN B 1475
REMARK 465 LYS B 1476
REMARK 465 PRO B 1495
REMARK 465 LEU B 1496
REMARK 465 GLY B 1497
REMARK 465 SER B 1498
REMARK 465 SER B 1499
REMARK 465 GLY B 1500
REMARK 465 THR B 1501
REMARK 465 ASP B 1502
REMARK 465 LYS B 1503
REMARK 465 VAL B 1504
REMARK 465 LYS B 1514
REMARK 465 MET B 1515
REMARK 465 TYR B 1516
REMARK 465 LYS B 1517
REMARK 465 THR B 1518
REMARK 465 PRO B 1519
REMARK 465 LEU B 1529
REMARK 465 PRO B 1530
REMARK 465 THR B 1531
REMARK 465 PRO B 1533
REMARK 465 SER B 1534
REMARK 465 GLY B 1535
REMARK 465 ASP B 1536
REMARK 465 GLU B 1537
REMARK 465 PRO B 1538
REMARK 465 HIS B 1544
REMARK 465 ILE B 1545
REMARK 465 THR B 1550
REMARK 465 LEU B 1551
REMARK 465 ARG B 1552
REMARK 465 ALA B 1553
REMARK 465 GLU B 1554
REMARK 465 SER B 1555
REMARK 465 ILE B 1556
REMARK 465 ASN B 1557
REMARK 465 GLU B 1558
REMARK 465 ARG B 1559
REMARK 465 THR B 1560
REMARK 465 LYS B 1579
REMARK 465 SER C 30
REMARK 465 GLY D 1444
REMARK 465 LEU D 1445
REMARK 465 SER D 1446
REMARK 465 GLU D 1447
REMARK 465 GLN D 1448
REMARK 465 LEU D 1449
REMARK 465 TYR D 1470
REMARK 465 ALA D 1472
REMARK 465 LYS D 1473
REMARK 465 SER D 1474
REMARK 465 ASN D 1475
REMARK 465 LYS D 1476
REMARK 465 GLU D 1477
REMARK 465 LEU D 1478
REMARK 465 PRO D 1495
REMARK 465 LEU D 1496
REMARK 465 GLY D 1497
REMARK 465 SER D 1498
REMARK 465 SER D 1499
REMARK 465 GLY D 1500
REMARK 465 THR D 1501
REMARK 465 ASP D 1502
REMARK 465 LYS D 1508
REMARK 465 SER D 1509
REMARK 465 ASN D 1510
REMARK 465 TYR D 1516
REMARK 465 LYS D 1517
REMARK 465 THR D 1518
REMARK 465 PRO D 1519
REMARK 465 ASN D 1523
REMARK 465 GLU D 1524
REMARK 465 LYS D 1528
REMARK 465 LEU D 1529
REMARK 465 PRO D 1530
REMARK 465 THR D 1531
REMARK 465 ASP D 1532
REMARK 465 PRO D 1533
REMARK 465 SER D 1534
REMARK 465 GLY D 1535
REMARK 465 ASP D 1536
REMARK 465 GLU D 1537
REMARK 465 PRO D 1538
REMARK 465 ILE D 1542
REMARK 465 SER D 1543
REMARK 465 HIS D 1544
REMARK 465 ILE D 1545
REMARK 465 ASP D 1546
REMARK 465 ARG D 1547
REMARK 465 VAL D 1548
REMARK 465 TYR D 1549
REMARK 465 THR D 1550
REMARK 465 LEU D 1551
REMARK 465 ARG D 1552
REMARK 465 ALA D 1553
REMARK 465 GLU D 1554
REMARK 465 SER D 1555
REMARK 465 ILE D 1556
REMARK 465 ASN D 1557
REMARK 465 GLU D 1558
REMARK 465 ARG D 1559
REMARK 465 THR D 1560
REMARK 465 ALA D 1561
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 MET A 1 CG SD CE
REMARK 470 GLN A 2 CG CD OE1 NE2
REMARK 470 THR A 3 OG1 CG2
REMARK 470 LEU A 19 CG CD1 CD2
REMARK 470 LYS A 27 CG CD CE NZ
REMARK 470 PHE A 28 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 31 CG CD OE1 OE2
REMARK 470 TYR A 32 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 VAL A 33 CG1 CG2
REMARK 470 THR A 35 OG1 CG2
REMARK 470 VAL A 36 CG1 CG2
REMARK 470 THR A 43 OG1 CG2
REMARK 470 VAL A 77 CG1 CG2
REMARK 470 GLU A 91 CG CD OE1 OE2
REMARK 470 LYS A 107 CG CD CE NZ
REMARK 470 LEU A 112 CG CD1 CD2
REMARK 470 ILE A 126 CG1 CG2 CD1
REMARK 470 GLU A 127 CG CD OE1 OE2
REMARK 470 LYS A 128 CG CD CE NZ
REMARK 470 LYS A 131 CG CD CE NZ
REMARK 470 LYS A 133 CG CD CE NZ
REMARK 470 LYS A 135 CG CD CE NZ
REMARK 470 THR A 138 OG1 CG2
REMARK 470 GLU A 140 CG CD OE1 OE2
REMARK 470 LYS A 150 CG CD CE NZ
REMARK 470 LYS A 166 CG CD CE NZ
REMARK 470 GLU A 178 CG CD OE1 OE2
REMARK 470 ASP B1229 CG OD1 OD2
REMARK 470 GLU B1250 CG CD OE1 OE2
REMARK 470 LEU B1258 CG CD1 CD2
REMARK 470 ILE B1262 CG1 CG2 CD1
REMARK 470 LYS B1265 CG CD CE NZ
REMARK 470 GLU B1271 CG CD OE1 OE2
REMARK 470 GLU B1275 CG CD OE1 OE2
REMARK 470 LEU B1295 CG CD1 CD2
REMARK 470 LEU B1296 CG CD1 CD2
REMARK 470 LYS B1304 CG CD CE NZ
REMARK 470 MET B1305 CG SD CE
REMARK 470 GLU B1308 CG CD OE1 OE2
REMARK 470 LYS B1309 CG CD CE NZ
REMARK 470 MET B1310 CG SD CE
REMARK 470 VAL B1312 CG1 CG2
REMARK 470 LYS B1313 CG CD CE NZ
REMARK 470 ILE B1315 CG1 CG2 CD1
REMARK 470 LYS B1346 CG CD CE NZ
REMARK 470 ASP B1348 CG OD1 OD2
REMARK 470 GLU B1349 CG CD OE1 OE2
REMARK 470 LYS B1358 CG CD CE NZ
REMARK 470 ARG B1384 CG CD NE CZ NH1 NH2
REMARK 470 LYS B1390 CG CD CE NZ
REMARK 470 GLU B1394 CG CD OE1 OE2
REMARK 470 ASN B1399 CG OD1 ND2
REMARK 470 LYS B1407 CG CD CE NZ
REMARK 470 GLU B1411 CG CD OE1 OE2
REMARK 470 LEU B1416 CG CD1 CD2
REMARK 470 GLU B1428 CG CD OE1 OE2
REMARK 470 ASP B1431 CG OD1 OD2
REMARK 470 ARG B1432 CG CD NE CZ NH1 NH2
REMARK 470 HIS B1439 CG ND1 CD2 CE1 NE2
REMARK 470 GLN B1441 CG CD OE1 NE2
REMARK 470 CYS B1442 SG
REMARK 470 GLU B1443 CG CD OE1 OE2
REMARK 470 VAL B1450 CG1 CG2
REMARK 470 THR B1455 OG1 CG2
REMARK 470 ASN B1456 CG OD1 ND2
REMARK 470 LEU B1458 CG CD1 CD2
REMARK 470 LYS B1462 CG CD CE NZ
REMARK 470 LEU B1464 CG CD1 CD2
REMARK 470 HIS B1465 CG ND1 CD2 CE1 NE2
REMARK 470 SER B1466 OG
REMARK 470 LYS B1468 CG CD CE NZ
REMARK 470 LEU B1469 CG CD1 CD2
REMARK 470 TYR B1470 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B1471 CG CD CE NZ
REMARK 470 LYS B1473 CG CD CE NZ
REMARK 470 SER B1474 OG
REMARK 470 GLU B1477 CG CD OE1 OE2
REMARK 470 LEU B1478 CG CD1 CD2
REMARK 470 TYR B1479 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU B1482 CG CD1 CD2
REMARK 470 ASN B1484 CG OD1 ND2
REMARK 470 PHE B1486 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU B1488 CG CD1 CD2
REMARK 470 LEU B1489 CG CD1 CD2
REMARK 470 THR B1490 OG1 CG2
REMARK 470 GLN B1491 CG CD OE1 NE2
REMARK 470 ILE B1492 CG1 CG2 CD1
REMARK 470 LYS B1494 CG CD CE NZ
REMARK 470 SER B1506 OG
REMARK 470 PRO B1507 CG CD
REMARK 470 LYS B1508 CG CD CE NZ
REMARK 470 SER B1509 OG
REMARK 470 ASN B1510 CG OD1 ND2
REMARK 470 LEU B1511 CG CD1 CD2
REMARK 470 TYR B1513 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 PHE B1521 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN B1523 CG OD1 ND2
REMARK 470 GLU B1524 CG CD OE1 OE2
REMARK 470 VAL B1525 CG1 CG2
REMARK 470 LEU B1526 CG CD1 CD2
REMARK 470 VAL B1527 CG1 CG2
REMARK 470 LYS B1528 CG CD CE NZ
REMARK 470 ASP B1532 CG OD1 OD2
REMARK 470 ILE B1539 CG1 CG2 CD1
REMARK 470 HIS B1541 CG ND1 CD2 CE1 NE2
REMARK 470 ILE B1542 CG1 CG2 CD1
REMARK 470 ASP B1546 CG OD1 OD2
REMARK 470 ARG B1547 CG CD NE CZ NH1 NH2
REMARK 470 VAL B1548 CG1 CG2
REMARK 470 TYR B1549 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 TRP B1562 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B1562 CZ3 CH2
REMARK 470 VAL B1563 CG1 CG2
REMARK 470 GLN B1564 CG CD OE1 NE2
REMARK 470 LYS B1565 CG CD CE NZ
REMARK 470 ILE B1566 CG1 CG2 CD1
REMARK 470 LYS B1567 CG CD CE NZ
REMARK 470 SER B1570 OG
REMARK 470 GLU B1571 CG CD OE1 OE2
REMARK 470 LEU B1572 CG CD1 CD2
REMARK 470 TYR B1573 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ILE B1574 CG1 CG2 CD1
REMARK 470 GLU B1575 CG CD OE1 OE2
REMARK 470 THR B1576 OG1 CG2
REMARK 470 GLU B1577 CG CD OE1 OE2
REMARK 470 LYS B1578 CG CD CE NZ
REMARK 470 MET C 1 CG SD CE
REMARK 470 GLN C 2 CG CD OE1 NE2
REMARK 470 THR C 3 OG1 CG2
REMARK 470 LEU C 19 CG CD1 CD2
REMARK 470 LYS C 27 CG CD CE NZ
REMARK 470 PHE C 28 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU C 31 CG CD OE1 OE2
REMARK 470 TYR C 32 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 VAL C 33 CG1 CG2
REMARK 470 THR C 35 OG1 CG2
REMARK 470 THR C 43 OG1 CG2
REMARK 470 VAL C 77 CG1 CG2
REMARK 470 VAL C 85 CG1 CG2
REMARK 470 GLU C 95 CG CD OE1 OE2
REMARK 470 THR C 115 OG1 CG2
REMARK 470 LYS C 135 CG CD CE NZ
REMARK 470 THR C 138 OG1 CG2
REMARK 470 LYS C 144 CG CD CE NZ
REMARK 470 LEU C 145 CG CD1 CD2
REMARK 470 ASP C 148 CG OD1 OD2
REMARK 470 LYS C 150 CG CD CE NZ
REMARK 470 GLU C 178 CG CD OE1 OE2
REMARK 470 LEU D1258 CG CD1 CD2
REMARK 470 GLU D1271 CG CD OE1 OE2
REMARK 470 GLU D1275 CG CD OE1 OE2
REMARK 470 LYS D1276 CG CD CE NZ
REMARK 470 LYS D1286 CG CD CE NZ
REMARK 470 LEU D1295 CG CD1 CD2
REMARK 470 LEU D1296 CG CD1 CD2
REMARK 470 LYS D1304 CG CD CE NZ
REMARK 470 MET D1305 CG SD CE
REMARK 470 LYS D1309 CG CD CE NZ
REMARK 470 VAL D1312 CG1 CG2
REMARK 470 SER D1320 OG
REMARK 470 LYS D1346 CG CD CE NZ
REMARK 470 GLU D1349 CG CD OE1 OE2
REMARK 470 LYS D1358 CG CD CE NZ
REMARK 470 ASN D1399 CG OD1 ND2
REMARK 470 LYS D1407 CG CD CE NZ
REMARK 470 GLU D1426 CG CD OE1 OE2
REMARK 470 ARG D1432 CG CD NE CZ NH1 NH2
REMARK 470 GLU D1434 CG CD OE1 OE2
REMARK 470 VAL D1440 CG1 CG2
REMARK 470 GLN D1441 CG CD OE1 NE2
REMARK 470 CYS D1442 SG
REMARK 470 VAL D1450 CG1 CG2
REMARK 470 THR D1455 OG1 CG2
REMARK 470 ASN D1456 CG OD1 ND2
REMARK 470 LEU D1458 CG CD1 CD2
REMARK 470 LEU D1464 CG CD1 CD2
REMARK 470 LYS D1468 CG CD CE NZ
REMARK 470 LEU D1469 CG CD1 CD2
REMARK 470 LYS D1471 CG CD CE NZ
REMARK 470 PHE D1481 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU D1487 CG CD1 CD2
REMARK 470 THR D1490 OG1 CG2
REMARK 470 GLN D1491 CG CD OE1 NE2
REMARK 470 ILE D1492 CG1 CG2 CD1
REMARK 470 THR D1493 OG1 CG2
REMARK 470 LYS D1494 CG CD CE NZ
REMARK 470 LYS D1503 CG CD CE NZ
REMARK 470 VAL D1504 CG1 CG2
REMARK 470 PHE D1505 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER D1506 OG
REMARK 470 LEU D1511 CG CD1 CD2
REMARK 470 GLN D1512 CG CD OE1 NE2
REMARK 470 TYR D1513 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 MET D1515 CG SD CE
REMARK 470 PHE D1521 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL D1525 CG1 CG2
REMARK 470 LEU D1526 CG CD1 CD2
REMARK 470 VAL D1527 CG1 CG2
REMARK 470 ILE D1539 CG1 CG2 CD1
REMARK 470 PHE D1540 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 HIS D1541 CG ND1 CD2 CE1 NE2
REMARK 470 TRP D1562 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP D1562 CZ3 CH2
REMARK 470 GLN D1564 CG CD OE1 NE2
REMARK 470 LYS D1565 CG CD CE NZ
REMARK 470 ILE D1566 CG1 CG2 CD1
REMARK 470 LYS D1567 CG CD CE NZ
REMARK 470 SER D1570 OG
REMARK 470 GLU D1571 CG CD OE1 OE2
REMARK 470 LEU D1572 CG CD1 CD2
REMARK 470 TYR D1573 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ILE D1574 CG1 CG2 CD1
REMARK 470 GLU D1575 CG CD OE1 OE2
REMARK 470 GLU D1577 CG CD OE1 OE2
REMARK 470 LYS D1578 CG CD CE NZ
REMARK 470 LYS D1579 CG CD CE NZ
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 ASN A 26 -8.60 62.47
REMARK 500 ASN A 39 68.31 -159.02
REMARK 500 LYS A 96 -51.39 -135.48
REMARK 500 ASP A 118 -4.82 -55.84
REMARK 500 GLN A 162 -0.47 75.95
REMARK 500 VAL B1283 -121.67 44.30
REMARK 500 ASN B1284 31.72 -99.69
REMARK 500 CYS B1442 50.81 -101.71
REMARK 500 CYS B1457 14.44 -147.88
REMARK 500 PRO B1507 44.11 -94.86
REMARK 500 ASN B1510 136.33 -174.14
REMARK 500 ASN C 26 -8.44 63.03
REMARK 500 ASN C 39 68.12 -159.30
REMARK 500 LYS C 96 -51.19 -135.48
REMARK 500 ASP C 118 -4.39 -57.13
REMARK 500 GLN C 162 -1.54 76.01
REMARK 500 VAL D1283 -122.59 44.48
REMARK 500 CYS D1442 50.80 -101.39
REMARK 500 CYS D1457 14.36 -147.84
REMARK 500 VAL D1504 -12.68 70.76
REMARK 500 PHE D1505 34.25 -164.42
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 GDP A 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP C 200
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KI1 RELATED DB: PDB
DBREF 3QBV A 1 178 UNP P60953 CDC42_HUMAN 1 178
DBREF 3QBV B 1229 1579 UNP Q15811 ITSN1_HUMAN 1229 1579
DBREF 3QBV C 1 178 UNP P60953 CDC42_HUMAN 1 178
DBREF 3QBV D 1229 1579 UNP Q15811 ITSN1_HUMAN 1229 1579
SEQADV 3QBV ARG A 56 UNP P60953 PHE 56 ENGINEERED MUTATION
SEQADV 3QBV LYS A 163 UNP P60953 ARG 163 VARIANT
SEQADV 3QBV GLU B 1373 UNP Q15811 SER 1373 ENGINEERED MUTATION
SEQADV 3QBV ARG C 56 UNP P60953 PHE 56 ENGINEERED MUTATION
SEQADV 3QBV LYS C 163 UNP P60953 ARG 163 VARIANT
SEQADV 3QBV GLU D 1373 UNP Q15811 SER 1373 ENGINEERED MUTATION
SEQRES 1 A 178 MET GLN THR ILE LYS CYS VAL VAL VAL GLY ASP GLY ALA
SEQRES 2 A 178 VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR THR ASN
SEQRES 3 A 178 LYS PHE PRO SER GLU TYR VAL PRO THR VAL PHE ASP ASN
SEQRES 4 A 178 TYR ALA VAL THR VAL MET ILE GLY GLY GLU PRO TYR THR
SEQRES 5 A 178 LEU GLY LEU ARG ASP THR ALA GLY GLN GLU ASP TYR ASP
SEQRES 6 A 178 ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP VAL PHE
SEQRES 7 A 178 LEU VAL CYS PHE SER VAL VAL SER PRO SER SER PHE GLU
SEQRES 8 A 178 ASN VAL LYS GLU LYS TRP VAL PRO GLU ILE THR HIS HIS
SEQRES 9 A 178 CYS PRO LYS THR PRO PHE LEU LEU VAL GLY THR GLN ILE
SEQRES 10 A 178 ASP LEU ARG ASP ASP PRO SER THR ILE GLU LYS LEU ALA
SEQRES 11 A 178 LYS ASN LYS GLN LYS PRO ILE THR PRO GLU THR ALA GLU
SEQRES 12 A 178 LYS LEU ALA ARG ASP LEU LYS ALA VAL LYS TYR VAL GLU
SEQRES 13 A 178 CYS SER ALA LEU THR GLN LYS GLY LEU LYS ASN VAL PHE
SEQRES 14 A 178 ASP GLU ALA ILE LEU ALA ALA LEU GLU
SEQRES 1 B 351 ASP MET LEU THR PRO THR GLU ARG LYS ARG GLN GLY TYR
SEQRES 2 B 351 ILE HIS GLU LEU ILE VAL THR GLU GLU ASN TYR VAL ASN
SEQRES 3 B 351 ASP LEU GLN LEU VAL THR GLU ILE PHE GLN LYS PRO LEU
SEQRES 4 B 351 MET GLU SER GLU LEU LEU THR GLU LYS GLU VAL ALA MET
SEQRES 5 B 351 ILE PHE VAL ASN TRP LYS GLU LEU ILE MET CYS ASN ILE
SEQRES 6 B 351 LYS LEU LEU LYS ALA LEU ARG VAL ARG LYS LYS MET SER
SEQRES 7 B 351 GLY GLU LYS MET PRO VAL LYS MET ILE GLY ASP ILE LEU
SEQRES 8 B 351 SER ALA GLN LEU PRO HIS MET GLN PRO TYR ILE ARG PHE
SEQRES 9 B 351 CYS SER ARG GLN LEU ASN GLY ALA ALA LEU ILE GLN GLN
SEQRES 10 B 351 LYS THR ASP GLU ALA PRO ASP PHE LYS GLU PHE VAL LYS
SEQRES 11 B 351 ARG LEU ALA MET ASP PRO ARG CYS LYS GLY MET PRO LEU
SEQRES 12 B 351 SER GLU PHE ILE LEU LYS PRO MET GLN ARG VAL THR ARG
SEQRES 13 B 351 TYR PRO LEU ILE ILE LYS ASN ILE LEU GLU ASN THR PRO
SEQRES 14 B 351 GLU ASN HIS PRO ASP HIS SER HIS LEU LYS HIS ALA LEU
SEQRES 15 B 351 GLU LYS ALA GLU GLU LEU CYS SER GLN VAL ASN GLU GLY
SEQRES 16 B 351 VAL ARG GLU LYS GLU ASN SER ASP ARG LEU GLU TRP ILE
SEQRES 17 B 351 GLN ALA HIS VAL GLN CYS GLU GLY LEU SER GLU GLN LEU
SEQRES 18 B 351 VAL PHE ASN SER VAL THR ASN CYS LEU GLY PRO ARG LYS
SEQRES 19 B 351 PHE LEU HIS SER GLY LYS LEU TYR LYS ALA LYS SER ASN
SEQRES 20 B 351 LYS GLU LEU TYR GLY PHE LEU PHE ASN ASP PHE LEU LEU
SEQRES 21 B 351 LEU THR GLN ILE THR LYS PRO LEU GLY SER SER GLY THR
SEQRES 22 B 351 ASP LYS VAL PHE SER PRO LYS SER ASN LEU GLN TYR LYS
SEQRES 23 B 351 MET TYR LYS THR PRO ILE PHE LEU ASN GLU VAL LEU VAL
SEQRES 24 B 351 LYS LEU PRO THR ASP PRO SER GLY ASP GLU PRO ILE PHE
SEQRES 25 B 351 HIS ILE SER HIS ILE ASP ARG VAL TYR THR LEU ARG ALA
SEQRES 26 B 351 GLU SER ILE ASN GLU ARG THR ALA TRP VAL GLN LYS ILE
SEQRES 27 B 351 LYS ALA ALA SER GLU LEU TYR ILE GLU THR GLU LYS LYS
SEQRES 1 C 178 MET GLN THR ILE LYS CYS VAL VAL VAL GLY ASP GLY ALA
SEQRES 2 C 178 VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR THR ASN
SEQRES 3 C 178 LYS PHE PRO SER GLU TYR VAL PRO THR VAL PHE ASP ASN
SEQRES 4 C 178 TYR ALA VAL THR VAL MET ILE GLY GLY GLU PRO TYR THR
SEQRES 5 C 178 LEU GLY LEU ARG ASP THR ALA GLY GLN GLU ASP TYR ASP
SEQRES 6 C 178 ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP VAL PHE
SEQRES 7 C 178 LEU VAL CYS PHE SER VAL VAL SER PRO SER SER PHE GLU
SEQRES 8 C 178 ASN VAL LYS GLU LYS TRP VAL PRO GLU ILE THR HIS HIS
SEQRES 9 C 178 CYS PRO LYS THR PRO PHE LEU LEU VAL GLY THR GLN ILE
SEQRES 10 C 178 ASP LEU ARG ASP ASP PRO SER THR ILE GLU LYS LEU ALA
SEQRES 11 C 178 LYS ASN LYS GLN LYS PRO ILE THR PRO GLU THR ALA GLU
SEQRES 12 C 178 LYS LEU ALA ARG ASP LEU LYS ALA VAL LYS TYR VAL GLU
SEQRES 13 C 178 CYS SER ALA LEU THR GLN LYS GLY LEU LYS ASN VAL PHE
SEQRES 14 C 178 ASP GLU ALA ILE LEU ALA ALA LEU GLU
SEQRES 1 D 351 ASP MET LEU THR PRO THR GLU ARG LYS ARG GLN GLY TYR
SEQRES 2 D 351 ILE HIS GLU LEU ILE VAL THR GLU GLU ASN TYR VAL ASN
SEQRES 3 D 351 ASP LEU GLN LEU VAL THR GLU ILE PHE GLN LYS PRO LEU
SEQRES 4 D 351 MET GLU SER GLU LEU LEU THR GLU LYS GLU VAL ALA MET
SEQRES 5 D 351 ILE PHE VAL ASN TRP LYS GLU LEU ILE MET CYS ASN ILE
SEQRES 6 D 351 LYS LEU LEU LYS ALA LEU ARG VAL ARG LYS LYS MET SER
SEQRES 7 D 351 GLY GLU LYS MET PRO VAL LYS MET ILE GLY ASP ILE LEU
SEQRES 8 D 351 SER ALA GLN LEU PRO HIS MET GLN PRO TYR ILE ARG PHE
SEQRES 9 D 351 CYS SER ARG GLN LEU ASN GLY ALA ALA LEU ILE GLN GLN
SEQRES 10 D 351 LYS THR ASP GLU ALA PRO ASP PHE LYS GLU PHE VAL LYS
SEQRES 11 D 351 ARG LEU ALA MET ASP PRO ARG CYS LYS GLY MET PRO LEU
SEQRES 12 D 351 SER GLU PHE ILE LEU LYS PRO MET GLN ARG VAL THR ARG
SEQRES 13 D 351 TYR PRO LEU ILE ILE LYS ASN ILE LEU GLU ASN THR PRO
SEQRES 14 D 351 GLU ASN HIS PRO ASP HIS SER HIS LEU LYS HIS ALA LEU
SEQRES 15 D 351 GLU LYS ALA GLU GLU LEU CYS SER GLN VAL ASN GLU GLY
SEQRES 16 D 351 VAL ARG GLU LYS GLU ASN SER ASP ARG LEU GLU TRP ILE
SEQRES 17 D 351 GLN ALA HIS VAL GLN CYS GLU GLY LEU SER GLU GLN LEU
SEQRES 18 D 351 VAL PHE ASN SER VAL THR ASN CYS LEU GLY PRO ARG LYS
SEQRES 19 D 351 PHE LEU HIS SER GLY LYS LEU TYR LYS ALA LYS SER ASN
SEQRES 20 D 351 LYS GLU LEU TYR GLY PHE LEU PHE ASN ASP PHE LEU LEU
SEQRES 21 D 351 LEU THR GLN ILE THR LYS PRO LEU GLY SER SER GLY THR
SEQRES 22 D 351 ASP LYS VAL PHE SER PRO LYS SER ASN LEU GLN TYR LYS
SEQRES 23 D 351 MET TYR LYS THR PRO ILE PHE LEU ASN GLU VAL LEU VAL
SEQRES 24 D 351 LYS LEU PRO THR ASP PRO SER GLY ASP GLU PRO ILE PHE
SEQRES 25 D 351 HIS ILE SER HIS ILE ASP ARG VAL TYR THR LEU ARG ALA
SEQRES 26 D 351 GLU SER ILE ASN GLU ARG THR ALA TRP VAL GLN LYS ILE
SEQRES 27 D 351 LYS ALA ALA SER GLU LEU TYR ILE GLU THR GLU LYS LYS
HET GDP A 200 28
HET GDP C 200 28
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
FORMUL 5 GDP 2(C10 H15 N5 O11 P2)
FORMUL 7 HOH *115(H2 O)
HELIX 1 1 GLY A 15 THR A 25 1 11
HELIX 2 2 LEU A 67 TYR A 72 5 6
HELIX 3 3 SER A 86 LYS A 96 1 11
HELIX 4 4 LYS A 96 CYS A 105 1 10
HELIX 5 5 GLN A 116 ARG A 120 5 5
HELIX 6 6 ASP A 122 ASN A 132 1 11
HELIX 7 7 THR A 138 LEU A 149 1 12
HELIX 8 8 GLY A 164 GLU A 178 1 15
HELIX 9 9 THR B 1232 PHE B 1263 1 32
HELIX 10 10 PHE B 1263 SER B 1270 1 8
HELIX 11 11 THR B 1274 VAL B 1283 1 10
HELIX 12 12 ASN B 1284 GLY B 1307 1 24
HELIX 13 13 ILE B 1315 LEU B 1323 1 9
HELIX 14 14 PRO B 1324 MET B 1326 5 3
HELIX 15 15 GLN B 1327 ALA B 1350 1 24
HELIX 16 16 ALA B 1350 ALA B 1361 1 12
HELIX 17 17 MET B 1362 LYS B 1367 5 6
HELIX 18 18 PRO B 1370 ILE B 1375 1 6
HELIX 19 19 LEU B 1376 ASN B 1395 1 20
HELIX 20 20 ASP B 1402 VAL B 1440 1 39
HELIX 21 21 TRP B 1562 THR B 1576 1 15
HELIX 22 22 GLY C 15 THR C 25 1 11
HELIX 23 23 LEU C 67 TYR C 72 5 6
HELIX 24 24 SER C 86 LYS C 96 1 11
HELIX 25 25 LYS C 96 CYS C 105 1 10
HELIX 26 26 GLN C 116 ARG C 120 5 5
HELIX 27 27 ASP C 122 ASN C 132 1 11
HELIX 28 28 THR C 138 LEU C 149 1 12
HELIX 29 29 GLY C 164 GLU C 178 1 15
HELIX 30 30 THR D 1232 PHE D 1263 1 32
HELIX 31 31 PHE D 1263 SER D 1270 1 8
HELIX 32 32 THR D 1274 VAL D 1283 1 10
HELIX 33 33 ASN D 1284 GLY D 1307 1 24
HELIX 34 34 ILE D 1315 LEU D 1323 1 9
HELIX 35 35 PRO D 1324 MET D 1326 5 3
HELIX 36 36 GLN D 1327 ALA D 1350 1 24
HELIX 37 37 ALA D 1350 ALA D 1361 1 12
HELIX 38 38 MET D 1362 LYS D 1367 5 6
HELIX 39 39 PRO D 1370 ILE D 1375 1 6
HELIX 40 40 LEU D 1376 ASN D 1395 1 20
HELIX 41 41 ASP D 1402 HIS D 1439 1 38
HELIX 42 42 VAL D 1563 THR D 1576 1 14
HELIX 43 43 GLU D 1577 LYS D 1579 5 3
SHEET 1 A 6 ALA A 41 ILE A 46 0
SHEET 2 A 6 GLU A 49 ASP A 57 -1 O TYR A 51 N VAL A 44
SHEET 3 A 6 THR A 3 GLY A 10 1 N ILE A 4 O GLY A 54
SHEET 4 A 6 VAL A 77 SER A 83 1 O CYS A 81 N VAL A 9
SHEET 5 A 6 PHE A 110 THR A 115 1 O VAL A 113 N VAL A 80
SHEET 6 A 6 TYR A 154 GLU A 156 1 O VAL A 155 N GLY A 114
SHEET 1 B 3 PHE B1463 GLY B1467 0
SHEET 2 B 3 TYR B1479 PHE B1483 -1 O LEU B1482 N HIS B1465
SHEET 3 B 3 LEU B1487 THR B1490 -1 O THR B1490 N TYR B1479
SHEET 1 C 2 ILE B1492 THR B1493 0
SHEET 2 C 2 LEU B1511 GLN B1512 -1 O LEU B1511 N THR B1493
SHEET 1 D 2 VAL B1525 VAL B1527 0
SHEET 2 D 2 PHE B1540 ILE B1542 -1 O PHE B1540 N VAL B1527
SHEET 1 E 6 ALA C 41 ILE C 46 0
SHEET 2 E 6 GLU C 49 ASP C 57 -1 O TYR C 51 N VAL C 44
SHEET 3 E 6 THR C 3 VAL C 9 1 N ILE C 4 O GLY C 54
SHEET 4 E 6 VAL C 77 SER C 83 1 O CYS C 81 N VAL C 9
SHEET 5 E 6 PHE C 110 THR C 115 1 O VAL C 113 N VAL C 80
SHEET 6 E 6 TYR C 154 GLU C 156 1 O VAL C 155 N GLY C 114
SHEET 1 F 5 VAL D1440 GLN D1441 0
SHEET 2 F 5 GLN D1512 LYS D1514 1 O GLN D1512 N GLN D1441
SHEET 3 F 5 LEU D1487 GLN D1491 -1 N GLN D1491 O TYR D1513
SHEET 4 F 5 GLY D1480 PHE D1483 -1 N PHE D1481 O LEU D1488
SHEET 5 F 5 PHE D1463 GLY D1467 -1 N LEU D1464 O LEU D1482
SITE 1 AC1 15 GLY A 12 ALA A 13 VAL A 14 GLY A 15
SITE 2 AC1 15 LYS A 16 THR A 17 CYS A 18 GLN A 116
SITE 3 AC1 15 ASP A 118 SER A 158 ALA A 159 LEU A 160
SITE 4 AC1 15 HOH A 189 HOH A 190 HOH A 197
SITE 1 AC2 17 GLY C 12 ALA C 13 VAL C 14 GLY C 15
SITE 2 AC2 17 LYS C 16 THR C 17 CYS C 18 VAL C 33
SITE 3 AC2 17 GLN C 116 ASP C 118 LEU C 119 SER C 158
SITE 4 AC2 17 ALA C 159 LEU C 160 HOH C 187 HOH C 190
SITE 5 AC2 17 HOH C 192
CRYST1 85.460 80.062 94.591 90.00 108.23 90.00 P 1 21 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 0.011701 0.000000 0.003854 0.00000
SCALE2 0.000000 0.012490 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011130 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
