HEADER TRANSFERASE/CAMP BINDING PROTEIN 05-MAY-16 5JR7
TITLE CRYSTAL STRUCTURE OF AN ACRDYS HETERODIMER [RIA(92-365):C] OF PKA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: PKA C-ALPHA;
COMPND 5 EC: 2.7.11.11;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE TYPE I-ALPHA REGULATORY
COMPND 9 SUBUNIT;
COMPND 10 CHAIN: B, D;
COMPND 11 FRAGMENT: UNP RESIDUES 92-366;
COMPND 12 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: PRKACA, PKACA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 10 ORGANISM_COMMON: BOVINE;
SOURCE 11 ORGANISM_TAXID: 9913;
SOURCE 12 GENE: PRKAR1A;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 83333
KEYWDS PKA SIGNALING, RIA SUBUNIT, DISEASE MUTATIONS, DYSFUNCTIONAL ACRDYS
KEYWDS 2 MUTANT, TRANSFERASE-CAMP BINDING PROTEIN COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.G.H.BRUYSTENS,J.WU,S.S.TAYLOR
REVDAT 3 25-DEC-19 5JR7 1 REMARK
REVDAT 2 27-SEP-17 5JR7 1 REMARK
REVDAT 1 15-MAR-17 5JR7 0
JRNL AUTH J.G.BRUYSTENS,J.WU,A.FORTEZZO,J.DEL RIO,C.NIELSEN,
JRNL AUTH 2 D.K.BLUMENTHAL,R.ROCK,E.STEFAN,S.S.TAYLOR
JRNL TITL STRUCTURE OF A PKA RI ALPHA RECURRENT ACRODYSOSTOSIS MUTANT
JRNL TITL 2 EXPLAINS DEFECTIVE CAMP-DEPENDENT ACTIVATION.
JRNL REF J. MOL. BIOL. V. 428 4890 2016
JRNL REFN ESSN 1089-8638
JRNL PMID 27825928
JRNL DOI 10.1016/J.JMB.2016.10.033
REMARK 2
REMARK 2 RESOLUTION. 3.56 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.7_650
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.56
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.11
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 15043
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.269
REMARK 3 R VALUE (WORKING SET) : 0.266
REMARK 3 FREE R VALUE : 0.322
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090
REMARK 3 FREE R VALUE TEST SET COUNT : 765
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 49.1104 - 6.0846 0.99 2902 164 0.2182 0.2558
REMARK 3 2 6.0846 - 4.8309 0.99 2890 165 0.2729 0.3065
REMARK 3 3 4.8309 - 4.2206 0.97 2841 159 0.2472 0.3636
REMARK 3 4 4.2206 - 3.8349 0.95 2814 132 0.3044 0.3902
REMARK 3 5 3.8349 - 3.5601 0.97 2831 145 0.3668 0.4017
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.83
REMARK 3 K_SOL : 0.29
REMARK 3 B_SOL : 74.42
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.580
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 38.870
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) : -2.77090
REMARK 3 B22 (A**2) : 9.79920
REMARK 3 B33 (A**2) : -7.02830
REMARK 3 B12 (A**2) : 0.19230
REMARK 3 B13 (A**2) : -5.50600
REMARK 3 B23 (A**2) : -8.11560
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 : 0.009 9971
REMARK 3 ANGLE : 1.738 13489
REMARK 3 CHIRALITY : 0.126 1452
REMARK 3 PLANARITY : 0.007 1728
REMARK 3 DIHEDRAL : 18.060 3690
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 28
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 13:42)
REMARK 3 ORIGIN FOR THE GROUP (A): 3.9034 -27.6877 7.3914
REMARK 3 T TENSOR
REMARK 3 T11: 1.0376 T22: 0.7090
REMARK 3 T33: 0.7414 T12: 0.3876
REMARK 3 T13: -0.5277 T23: 0.0386
REMARK 3 L TENSOR
REMARK 3 L11: 0.4474 L22: 1.0834
REMARK 3 L33: 0.1717 L12: 0.6758
REMARK 3 L13: 0.2791 L23: 0.4273
REMARK 3 S TENSOR
REMARK 3 S11: -0.1312 S12: 0.1517 S13: 0.0424
REMARK 3 S21: -0.2797 S22: -0.0996 S23: 1.0231
REMARK 3 S31: -0.7287 S32: 0.2020 S33: -0.2464
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 43:160)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.5287 -34.0081 22.8319
REMARK 3 T TENSOR
REMARK 3 T11: -0.1526 T22: 0.1565
REMARK 3 T33: 0.1094 T12: -0.2077
REMARK 3 T13: -0.0679 T23: -0.0660
REMARK 3 L TENSOR
REMARK 3 L11: 0.8913 L22: 2.1089
REMARK 3 L33: 1.5391 L12: 0.2773
REMARK 3 L13: -0.5017 L23: -1.2796
REMARK 3 S TENSOR
REMARK 3 S11: 0.2159 S12: 0.3762 S13: 0.0412
REMARK 3 S21: 0.1167 S22: 0.6353 S23: 1.1316
REMARK 3 S31: -0.4117 S32: -0.7722 S33: 1.2926
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 161:272)
REMARK 3 ORIGIN FOR THE GROUP (A): 24.1035 -29.2162 24.2045
REMARK 3 T TENSOR
REMARK 3 T11: 0.0262 T22: 0.0763
REMARK 3 T33: 0.2784 T12: 0.0590
REMARK 3 T13: -0.0221 T23: -0.0160
REMARK 3 L TENSOR
REMARK 3 L11: 1.6014 L22: 0.5674
REMARK 3 L33: 0.4822 L12: -0.1732
REMARK 3 L13: -0.2607 L23: -0.0083
REMARK 3 S TENSOR
REMARK 3 S11: -0.4420 S12: 0.4585 S13: 0.0280
REMARK 3 S21: 0.0860 S22: 0.2258 S23: 0.1113
REMARK 3 S31: -0.0362 S32: 0.0110 S33: -0.6903
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 273:316)
REMARK 3 ORIGIN FOR THE GROUP (A): 26.8355 -36.8915 11.6878
REMARK 3 T TENSOR
REMARK 3 T11: 0.2958 T22: 0.4997
REMARK 3 T33: -0.1383 T12: -0.0460
REMARK 3 T13: 0.0342 T23: 0.0018
REMARK 3 L TENSOR
REMARK 3 L11: 0.5038 L22: 0.1653
REMARK 3 L33: 0.3782 L12: -0.2816
REMARK 3 L13: -0.1362 L23: 0.1241
REMARK 3 S TENSOR
REMARK 3 S11: 0.2068 S12: 0.5073 S13: 0.2140
REMARK 3 S21: -0.3566 S22: -0.1880 S23: -0.0173
REMARK 3 S31: -0.0624 S32: -0.0368 S33: 0.0436
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 317:350)
REMARK 3 ORIGIN FOR THE GROUP (A): -2.1268 -32.0910 30.4277
REMARK 3 T TENSOR
REMARK 3 T11: 0.5101 T22: 1.0478
REMARK 3 T33: 0.8655 T12: 0.3463
REMARK 3 T13: -0.0606 T23: -0.0549
REMARK 3 L TENSOR
REMARK 3 L11: 0.8419 L22: 0.4270
REMARK 3 L33: 0.6821 L12: 0.3994
REMARK 3 L13: -0.1475 L23: -0.3658
REMARK 3 S TENSOR
REMARK 3 S11: 0.1351 S12: 0.5949 S13: 0.7383
REMARK 3 S21: -0.2215 S22: -0.1008 S23: 0.4572
REMARK 3 S31: -0.4587 S32: -0.6267 S33: -0.3561
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 92:119)
REMARK 3 ORIGIN FOR THE GROUP (A): 18.0362 -9.9505 31.1525
REMARK 3 T TENSOR
REMARK 3 T11: 0.1015 T22: 0.2225
REMARK 3 T33: 0.7415 T12: 0.4872
REMARK 3 T13: -0.2105 T23: 0.1389
REMARK 3 L TENSOR
REMARK 3 L11: 0.3378 L22: 0.9895
REMARK 3 L33: 0.8094 L12: -0.0093
REMARK 3 L13: 0.0073 L23: 0.5829
REMARK 3 S TENSOR
REMARK 3 S11: 0.0755 S12: -0.1233 S13: 0.1177
REMARK 3 S21: 0.5675 S22: 0.2795 S23: 0.0963
REMARK 3 S31: 0.2427 S32: -0.2493 S33: -0.3918
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 120:151)
REMARK 3 ORIGIN FOR THE GROUP (A): 33.6984 -4.0625 35.8501
REMARK 3 T TENSOR
REMARK 3 T11: 0.4690 T22: 0.2896
REMARK 3 T33: 0.9319 T12: -0.0776
REMARK 3 T13: 0.0565 T23: -0.1855
REMARK 3 L TENSOR
REMARK 3 L11: 0.0346 L22: 0.0087
REMARK 3 L33: 0.2104 L12: -0.0146
REMARK 3 L13: 0.0533 L23: -0.0189
REMARK 3 S TENSOR
REMARK 3 S11: -0.1677 S12: 0.3230 S13: -0.1030
REMARK 3 S21: 0.0297 S22: 0.2109 S23: -0.2583
REMARK 3 S31: 0.3606 S32: 0.5006 S33: -0.0099
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 152:198)
REMARK 3 ORIGIN FOR THE GROUP (A): 23.2745 -11.4575 51.5686
REMARK 3 T TENSOR
REMARK 3 T11: 1.7642 T22: 0.3564
REMARK 3 T33: 0.0778 T12: 0.2687
REMARK 3 T13: -0.3005 T23: 0.4760
REMARK 3 L TENSOR
REMARK 3 L11: 0.7246 L22: 0.0936
REMARK 3 L33: 0.4487 L12: 0.1483
REMARK 3 L13: -0.2065 L23: -0.1825
REMARK 3 S TENSOR
REMARK 3 S11: -0.1104 S12: -0.4721 S13: -0.2561
REMARK 3 S21: 0.2042 S22: -0.0602 S23: -0.0402
REMARK 3 S31: -0.1240 S32: 0.0212 S33: -0.4670
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 199:211)
REMARK 3 ORIGIN FOR THE GROUP (A): 19.9886 -16.3603 40.2100
REMARK 3 T TENSOR
REMARK 3 T11: 1.1529 T22: 0.1308
REMARK 3 T33: 0.4867 T12: 0.2179
REMARK 3 T13: 0.0633 T23: -0.0974
REMARK 3 L TENSOR
REMARK 3 L11: 0.0540 L22: 0.0642
REMARK 3 L33: 0.0300 L12: -0.0428
REMARK 3 L13: -0.0184 L23: -0.0079
REMARK 3 S TENSOR
REMARK 3 S11: -0.0237 S12: -0.1027 S13: -0.0137
REMARK 3 S21: 0.0266 S22: 0.0273 S23: 0.0633
REMARK 3 S31: 0.0527 S32: 0.0536 S33: -0.0418
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 212:225)
REMARK 3 ORIGIN FOR THE GROUP (A): 24.3038 -6.0799 51.3862
REMARK 3 T TENSOR
REMARK 3 T11: 1.3689 T22: 0.5323
REMARK 3 T33: 0.3883 T12: 0.2775
REMARK 3 T13: 0.2823 T23: -0.1069
REMARK 3 L TENSOR
REMARK 3 L11: 0.0691 L22: 0.0799
REMARK 3 L33: 0.2341 L12: -0.0263
REMARK 3 L13: -0.0765 L23: 0.1268
REMARK 3 S TENSOR
REMARK 3 S11: -0.0008 S12: -0.1313 S13: -0.0782
REMARK 3 S21: 0.3274 S22: 0.1999 S23: -0.0759
REMARK 3 S31: 0.1930 S32: 0.1663 S33: 0.1465
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 226:251)
REMARK 3 ORIGIN FOR THE GROUP (A): 26.0830 -4.0966 19.2413
REMARK 3 T TENSOR
REMARK 3 T11: 0.7085 T22: -0.5967
REMARK 3 T33: 0.3093 T12: -0.0907
REMARK 3 T13: -0.0126 T23: -0.2759
REMARK 3 L TENSOR
REMARK 3 L11: 0.2014 L22: 0.2749
REMARK 3 L33: 0.3243 L12: -0.1194
REMARK 3 L13: -0.0011 L23: 0.2542
REMARK 3 S TENSOR
REMARK 3 S11: -0.2733 S12: -0.0505 S13: 0.1383
REMARK 3 S21: 0.2806 S22: -0.1526 S23: 0.3860
REMARK 3 S31: 0.1285 S32: -0.0981 S33: -1.0262
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 252:302)
REMARK 3 ORIGIN FOR THE GROUP (A): 41.8508 -4.7476 11.1379
REMARK 3 T TENSOR
REMARK 3 T11: 0.1157 T22: 0.2259
REMARK 3 T33: 0.6225 T12: -0.2348
REMARK 3 T13: -0.1448 T23: 0.0357
REMARK 3 L TENSOR
REMARK 3 L11: 0.4575 L22: 0.5720
REMARK 3 L33: 0.2726 L12: -0.0706
REMARK 3 L13: -0.3192 L23: 0.0325
REMARK 3 S TENSOR
REMARK 3 S11: 0.0768 S12: 0.2949 S13: 0.1851
REMARK 3 S21: -0.0167 S22: -0.0342 S23: 0.2377
REMARK 3 S31: -0.0264 S32: -0.4242 S33: 0.0877
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 303:310)
REMARK 3 ORIGIN FOR THE GROUP (A): 64.9295 3.5707 6.1012
REMARK 3 T TENSOR
REMARK 3 T11: 1.1608 T22: 0.7767
REMARK 3 T33: 0.9995 T12: -0.3473
REMARK 3 T13: 0.2759 T23: 0.2593
REMARK 3 L TENSOR
REMARK 3 L11: 0.0113 L22: 0.0008
REMARK 3 L33: 0.0476 L12: 0.0012
REMARK 3 L13: 0.0236 L23: 0.0036
REMARK 3 S TENSOR
REMARK 3 S11: -0.0407 S12: 0.0240 S13: 0.0580
REMARK 3 S21: -0.0038 S22: -0.0386 S23: -0.0301
REMARK 3 S31: -0.0828 S32: 0.0829 S33: -0.0829
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 311:358)
REMARK 3 ORIGIN FOR THE GROUP (A): 45.5217 -4.7372 8.9958
REMARK 3 T TENSOR
REMARK 3 T11: 0.3541 T22: 0.5496
REMARK 3 T33: 0.1466 T12: -0.2225
REMARK 3 T13: 0.1300 T23: 0.0057
REMARK 3 L TENSOR
REMARK 3 L11: 0.6708 L22: 0.6493
REMARK 3 L33: 0.9160 L12: 0.3402
REMARK 3 L13: 0.2295 L23: -0.3261
REMARK 3 S TENSOR
REMARK 3 S11: -0.0962 S12: -0.2577 S13: -0.0732
REMARK 3 S21: -0.2652 S22: -0.0601 S23: -0.1814
REMARK 3 S31: 0.1331 S32: 0.4839 S33: -1.4128
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 13:42)
REMARK 3 ORIGIN FOR THE GROUP (A): 12.0725 -26.0599 52.3278
REMARK 3 T TENSOR
REMARK 3 T11: 1.3016 T22: 0.7978
REMARK 3 T33: 0.9180 T12: 0.1446
REMARK 3 T13: 0.3949 T23: 0.3763
REMARK 3 L TENSOR
REMARK 3 L11: 0.2029 L22: 0.6467
REMARK 3 L33: 0.1262 L12: 0.2299
REMARK 3 L13: 0.0046 L23: 0.2221
REMARK 3 S TENSOR
REMARK 3 S11: -0.1441 S12: -0.0546 S13: -0.5064
REMARK 3 S21: -0.1000 S22: -0.2291 S23: -0.9723
REMARK 3 S31: 0.6411 S32: 0.0796 S33: 0.0410
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 43:160)
REMARK 3 ORIGIN FOR THE GROUP (A): 9.8039 -26.2273 69.2516
REMARK 3 T TENSOR
REMARK 3 T11: -0.3634 T22: 0.3603
REMARK 3 T33: 0.4111 T12: -0.0378
REMARK 3 T13: 0.3609 T23: 0.1764
REMARK 3 L TENSOR
REMARK 3 L11: 0.3565 L22: 0.4343
REMARK 3 L33: 0.5294 L12: -0.1023
REMARK 3 L13: 0.1862 L23: 0.2355
REMARK 3 S TENSOR
REMARK 3 S11: 0.2595 S12: 0.4534 S13: -0.1161
REMARK 3 S21: -0.4964 S22: -0.0446 S23: -0.9369
REMARK 3 S31: 0.4608 S32: 1.2138 S33: 0.0695
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 161:272)
REMARK 3 ORIGIN FOR THE GROUP (A): -7.7009 -31.2328 68.7736
REMARK 3 T TENSOR
REMARK 3 T11: 0.3038 T22: -0.4725
REMARK 3 T33: 0.0854 T12: -0.1126
REMARK 3 T13: 0.1061 T23: 0.3638
REMARK 3 L TENSOR
REMARK 3 L11: 0.4904 L22: 0.6809
REMARK 3 L33: 0.8564 L12: -0.1813
REMARK 3 L13: 0.5313 L23: -0.6067
REMARK 3 S TENSOR
REMARK 3 S11: 0.3847 S12: 0.3933 S13: 0.4649
REMARK 3 S21: -0.6786 S22: -0.4617 S23: 0.2584
REMARK 3 S31: 0.4585 S32: 0.6875 S33: -0.1212
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 273:316)
REMARK 3 ORIGIN FOR THE GROUP (A): -10.5619 -19.3045 60.3148
REMARK 3 T TENSOR
REMARK 3 T11: 0.4706 T22: 0.2756
REMARK 3 T33: -0.2357 T12: 0.0167
REMARK 3 T13: 0.1742 T23: 0.1878
REMARK 3 L TENSOR
REMARK 3 L11: 0.2138 L22: 0.5275
REMARK 3 L33: 0.4143 L12: -0.0689
REMARK 3 L13: -0.1707 L23: -0.2919
REMARK 3 S TENSOR
REMARK 3 S11: 0.2464 S12: 0.3547 S13: 0.0242
REMARK 3 S21: -0.2967 S22: -0.2993 S23: -0.1963
REMARK 3 S31: 0.1690 S32: -0.0510 S33: -0.3981
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 317:350)
REMARK 3 ORIGIN FOR THE GROUP (A): 18.6622 -30.8973 75.2235
REMARK 3 T TENSOR
REMARK 3 T11: 0.8131 T22: 1.2597
REMARK 3 T33: 1.2533 T12: 0.0175
REMARK 3 T13: 0.2052 T23: -0.1690
REMARK 3 L TENSOR
REMARK 3 L11: 0.1103 L22: -0.0003
REMARK 3 L33: 0.0590 L12: -0.0073
REMARK 3 L13: -0.0476 L23: 0.0132
REMARK 3 S TENSOR
REMARK 3 S11: -0.0873 S12: 0.0017 S13: -0.1359
REMARK 3 S21: -0.6384 S22: -0.1243 S23: -0.9014
REMARK 3 S31: 0.1613 S32: -0.2430 S33: -0.0037
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 92:119)
REMARK 3 ORIGIN FOR THE GROUP (A): -1.9216 -51.6885 67.2419
REMARK 3 T TENSOR
REMARK 3 T11: 0.4534 T22: 0.4151
REMARK 3 T33: 0.6518 T12: 0.0455
REMARK 3 T13: 0.2527 T23: -0.0248
REMARK 3 L TENSOR
REMARK 3 L11: 0.3855 L22: 0.0568
REMARK 3 L33: 0.4643 L12: 0.0785
REMARK 3 L13: 0.2319 L23: -0.0748
REMARK 3 S TENSOR
REMARK 3 S11: -0.1422 S12: 0.1788 S13: -0.4129
REMARK 3 S21: -0.1256 S22: 0.0406 S23: -0.0228
REMARK 3 S31: 0.1971 S32: 0.4637 S33: 0.0593
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 120:151)
REMARK 3 ORIGIN FOR THE GROUP (A): -17.2913 -58.9977 69.7545
REMARK 3 T TENSOR
REMARK 3 T11: 1.2759 T22: 0.8218
REMARK 3 T33: 1.1448 T12: 0.0962
REMARK 3 T13: 0.2090 T23: -0.0823
REMARK 3 L TENSOR
REMARK 3 L11: 0.0757 L22: 0.2743
REMARK 3 L33: 0.0892 L12: 0.1176
REMARK 3 L13: -0.0491 L23: -0.1474
REMARK 3 S TENSOR
REMARK 3 S11: 0.0474 S12: -0.1827 S13: -0.5330
REMARK 3 S21: 0.2183 S22: -0.0967 S23: -0.0915
REMARK 3 S31: 0.6178 S32: -0.4990 S33: -0.0044
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 152:198)
REMARK 3 ORIGIN FOR THE GROUP (A): -6.7361 -58.7629 86.5012
REMARK 3 T TENSOR
REMARK 3 T11: 1.5200 T22: -0.0034
REMARK 3 T33: 0.7855 T12: 0.4938
REMARK 3 T13: -0.0744 T23: 0.1826
REMARK 3 L TENSOR
REMARK 3 L11: 0.6582 L22: 0.8522
REMARK 3 L33: 0.3846 L12: -0.0062
REMARK 3 L13: -0.0030 L23: -0.5737
REMARK 3 S TENSOR
REMARK 3 S11: 0.1026 S12: -0.4010 S13: -0.1866
REMARK 3 S21: 0.5234 S22: 0.0736 S23: -0.2939
REMARK 3 S31: -0.2353 S32: -0.0881 S33: 0.2567
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 199:211)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.4692 -49.5119 78.0923
REMARK 3 T TENSOR
REMARK 3 T11: 1.3104 T22: 0.5678
REMARK 3 T33: 0.4447 T12: 0.3908
REMARK 3 T13: -0.3396 T23: -0.1080
REMARK 3 L TENSOR
REMARK 3 L11: 0.0776 L22: 0.0811
REMARK 3 L33: 0.1485 L12: -0.0487
REMARK 3 L13: -0.0968 L23: 0.0247
REMARK 3 S TENSOR
REMARK 3 S11: -0.1084 S12: -0.0073 S13: 0.0061
REMARK 3 S21: -0.0214 S22: -0.0571 S23: 0.0310
REMARK 3 S31: 0.0780 S32: -0.0765 S33: -0.0486
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 212:225)
REMARK 3 ORIGIN FOR THE GROUP (A): -7.8314 -63.6345 84.2824
REMARK 3 T TENSOR
REMARK 3 T11: 0.7787 T22: 0.2670
REMARK 3 T33: 1.0625 T12: 0.5668
REMARK 3 T13: -0.1184 T23: 0.4093
REMARK 3 L TENSOR
REMARK 3 L11: 0.3238 L22: 0.6652
REMARK 3 L33: 0.1663 L12: -0.1674
REMARK 3 L13: -0.0420 L23: -0.0975
REMARK 3 S TENSOR
REMARK 3 S11: -0.0289 S12: -0.1049 S13: 0.0099
REMARK 3 S21: 0.1410 S22: -0.0628 S23: -0.0309
REMARK 3 S31: 0.1020 S32: 0.0311 S33: -0.3011
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 226:251)
REMARK 3 ORIGIN FOR THE GROUP (A): -10.1773 -52.1762 53.9812
REMARK 3 T TENSOR
REMARK 3 T11: 0.4692 T22: 0.2263
REMARK 3 T33: 0.5235 T12: 0.1280
REMARK 3 T13: 0.0335 T23: -0.3791
REMARK 3 L TENSOR
REMARK 3 L11: 0.5847 L22: 0.3444
REMARK 3 L33: 0.4428 L12: -0.1916
REMARK 3 L13: -0.0265 L23: 0.1281
REMARK 3 S TENSOR
REMARK 3 S11: -0.0363 S12: -0.2375 S13: 0.0683
REMARK 3 S21: 0.5561 S22: 0.2239 S23: -0.6055
REMARK 3 S31: 0.2783 S32: 0.2427 S33: 0.3173
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 252:302)
REMARK 3 ORIGIN FOR THE GROUP (A): -26.2017 -48.1234 46.8507
REMARK 3 T TENSOR
REMARK 3 T11: 0.5886 T22: 0.3193
REMARK 3 T33: 0.4421 T12: 0.0916
REMARK 3 T13: -0.0495 T23: 0.0390
REMARK 3 L TENSOR
REMARK 3 L11: 0.0485 L22: 0.2298
REMARK 3 L33: 0.5981 L12: -0.0897
REMARK 3 L13: 0.0456 L23: 0.0789
REMARK 3 S TENSOR
REMARK 3 S11: 0.1815 S12: 0.0468 S13: -0.1278
REMARK 3 S21: -0.1224 S22: -0.0445 S23: 0.1295
REMARK 3 S31: 0.6995 S32: -0.6096 S33: -0.0037
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 303:310)
REMARK 3 ORIGIN FOR THE GROUP (A): -50.1071 -54.2059 40.0630
REMARK 3 T TENSOR
REMARK 3 T11: 1.7312 T22: 1.0771
REMARK 3 T33: 1.3378 T12: -0.2532
REMARK 3 T13: 0.2094 T23: -0.0146
REMARK 3 L TENSOR
REMARK 3 L11: 0.1486 L22: 0.0752
REMARK 3 L33: 0.1234 L12: 0.1057
REMARK 3 L13: -0.1366 L23: -0.0971
REMARK 3 S TENSOR
REMARK 3 S11: -0.0389 S12: -0.0825 S13: -0.1101
REMARK 3 S21: 0.0513 S22: -0.0335 S23: -0.0267
REMARK 3 S31: 0.0340 S32: 0.0375 S33: -0.0211
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 311:357)
REMARK 3 ORIGIN FOR THE GROUP (A): -29.9429 -47.3138 45.0507
REMARK 3 T TENSOR
REMARK 3 T11: 0.4718 T22: -0.2608
REMARK 3 T33: 0.1622 T12: 0.1987
REMARK 3 T13: 0.0147 T23: 0.2047
REMARK 3 L TENSOR
REMARK 3 L11: 0.3756 L22: 0.3594
REMARK 3 L33: 0.6654 L12: 0.0903
REMARK 3 L13: 0.1230 L23: 0.0088
REMARK 3 S TENSOR
REMARK 3 S11: -0.0836 S12: -0.0400 S13: -0.4041
REMARK 3 S21: 0.0075 S22: 0.3668 S23: 0.1258
REMARK 3 S31: 0.2889 S32: -0.3776 S33: 0.3005
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 5JR7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAY-16.
REMARK 100 THE DEPOSITION ID IS D_1000221098.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-MAY-14
REMARK 200 TEMPERATURE (KELVIN) : 200
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : DOUBLE-CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15767
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.560
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.15500
REMARK 200 R SYM (I) : 0.10700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.56
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.49000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.100
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: 2QCS
REMARK 200
REMARK 200 REMARK: THERE ARE TWO MOLECULES PER ASYMMETRICAL UNIT
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM THIOCYANATE AND 20% PEG
REMARK 280 3350 WITH THE PROTEIN AT A FINAL CONCENTRATION OF 5 MG/ML IN A
REMARK 280 1.6 UL DROP, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
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
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: 4480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 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: 4580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 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 GLY A 1
REMARK 465 ASN A 2
REMARK 465 ALA A 3
REMARK 465 ALA A 4
REMARK 465 ALA A 5
REMARK 465 ALA A 6
REMARK 465 LYS A 7
REMARK 465 LYS A 8
REMARK 465 GLY A 9
REMARK 465 SER A 10
REMARK 465 GLU A 11
REMARK 465 GLN A 12
REMARK 465 GLY B 91
REMARK 465 PRO B 359
REMARK 465 CYS B 360
REMARK 465 SER B 361
REMARK 465 ASP B 362
REMARK 465 ILE B 363
REMARK 465 LEU B 364
REMARK 465 LYS B 365
REMARK 465 GLY C 1
REMARK 465 ASN C 2
REMARK 465 ALA C 3
REMARK 465 ALA C 4
REMARK 465 ALA C 5
REMARK 465 ALA C 6
REMARK 465 LYS C 7
REMARK 465 LYS C 8
REMARK 465 GLY C 9
REMARK 465 SER C 10
REMARK 465 GLU C 11
REMARK 465 GLN C 12
REMARK 465 GLY D 91
REMARK 465 GLY D 358
REMARK 465 PRO D 359
REMARK 465 CYS D 360
REMARK 465 SER D 361
REMARK 465 ASP D 362
REMARK 465 ILE D 363
REMARK 465 LEU D 364
REMARK 465 LYS D 365
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 13 CG CD OE1 OE2
REMARK 470 LYS A 16 CD CE NZ
REMARK 470 LYS A 21 CE NZ
REMARK 470 LYS A 28 CD CE NZ
REMARK 470 GLU A 31 CD OE1 OE2
REMARK 470 LYS A 81 CD CE NZ
REMARK 470 ARG A 93 CZ NH1 NH2
REMARK 470 LYS A 105 CD CE NZ
REMARK 470 LYS A 192 CE NZ
REMARK 470 LYS A 254 CG CD CE NZ
REMARK 470 ARG A 256 CD NE CZ NH1 NH2
REMARK 470 LYS A 309 CE NZ
REMARK 470 LYS A 317 CG CD CE NZ
REMARK 470 LYS A 319 CG CD CE NZ
REMARK 470 GLU A 331 CG CD OE1 OE2
REMARK 470 GLU A 333 CG CD OE1 OE2
REMARK 470 GLU A 334 CG CD OE1 OE2
REMARK 470 LYS A 345 CG CD CE NZ
REMARK 470 GLU B 101 OE1
REMARK 470 LYS B 114 CD CE NZ
REMARK 470 LYS B 121 CD CE NZ
REMARK 470 LYS B 128 CE NZ
REMARK 470 GLN B 177 CD OE1 NE2
REMARK 470 GLU B 270 OE2
REMARK 470 LYS B 279 CE NZ
REMARK 470 ARG B 303 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 304 CG CD NE CZ NH1 NH2
REMARK 470 SER B 305 OG
REMARK 470 GLU B 306 CG CD OE1 OE2
REMARK 470 ASN B 307 CB CG OD1 ND2
REMARK 470 ARG B 333 NH1 NH2
REMARK 470 GLU C 13 CG CD OE1 OE2
REMARK 470 LYS C 16 CD CE NZ
REMARK 470 LYS C 21 CE NZ
REMARK 470 LYS C 28 CD CE NZ
REMARK 470 GLU C 31 CD OE1 OE2
REMARK 470 LYS C 81 CD CE NZ
REMARK 470 ARG C 93 CZ NH1 NH2
REMARK 470 LYS C 105 CD CE NZ
REMARK 470 LYS C 192 CE NZ
REMARK 470 LYS C 254 CG CD CE NZ
REMARK 470 ARG C 256 CD NE CZ NH1 NH2
REMARK 470 LYS C 309 CE NZ
REMARK 470 LYS C 317 CG CD CE NZ
REMARK 470 PHE C 318 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS C 319 CG CD CE NZ
REMARK 470 GLU C 331 CG CD OE1 OE2
REMARK 470 GLU C 333 CG CD OE1 OE2
REMARK 470 GLU C 334 CG CD OE1 OE2
REMARK 470 LYS C 345 CG CD CE NZ
REMARK 470 GLU D 101 OE1 OE2
REMARK 470 GLU D 106 CD OE1 OE2
REMARK 470 LYS D 114 CD CE NZ
REMARK 470 LYS D 121 CD CE NZ
REMARK 470 LYS D 128 CE NZ
REMARK 470 GLN D 177 CD OE1 NE2
REMARK 470 GLU D 270 CD OE1 OE2
REMARK 470 LYS D 279 CE NZ
REMARK 470 ARG D 303 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 304 CG CD NE CZ NH1 NH2
REMARK 470 SER D 305 OG
REMARK 470 GLU D 306 CG CD OE1 OE2
REMARK 470 ASN D 307 CB CG OD1 ND2
REMARK 470 ARG D 333 NH1 NH2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 PHE A 318 CG CD1 CD2 CE1 CE2 CZ
REMARK 480 GLU B 245 CD
REMARK 480 GLU D 245 CD
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 OD1 ASP D 181 CZ3 TRP D 188 1.99
REMARK 500 OD1 ASP A 112 OH TYR A 117 2.03
REMARK 500 O PHE A 43 NH1 ARG A 45 2.05
REMARK 500 O SER B 249 OE2 GLU B 255 2.06
REMARK 500 O TPO A 197 OH TYR A 215 2.10
REMARK 500 O GLN A 39 OE1 GLN A 42 2.11
REMARK 500 O HIS C 87 N ASN C 90 2.11
REMARK 500 OD1 ASP D 181 CH2 TRP D 188 2.12
REMARK 500 OD2 ASP A 328 NH2 ARG B 92 2.13
REMARK 500 O THR B 264 OD1 ASP B 267 2.15
REMARK 500 ND2 ASN C 90 O ALA C 188 2.16
REMARK 500 O SER B 305 OE1 GLU B 308 2.16
REMARK 500 OE1 GLU D 275 OE1 GLN D 278 2.16
REMARK 500 O SER B 305 OE2 GLU B 308 2.17
REMARK 500 NZ LYS A 111 CD1 PHE A 350 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 LYS A 111 CE LYS A 111 NZ -0.175
REMARK 500 ARG B 333 NE ARG B 333 CZ 0.164
REMARK 500 TRP C 30 CB TRP C 30 CG -0.114
REMARK 500 ASP D 181 CB ASP D 181 CG -0.190
REMARK 500 TRP D 188 CZ3 TRP D 188 CH2 -0.113
REMARK 500 ARG D 333 NE ARG D 333 CZ 0.162
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 27 CB - CG - CD1 ANGL. DEV. = -29.6 DEGREES
REMARK 500 LYS A 111 CB - CA - C ANGL. DEV. = -13.1 DEGREES
REMARK 500 LEU A 116 CB - CG - CD1 ANGL. DEV. = -13.0 DEGREES
REMARK 500 ARG B 92 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 LEU B 126 CA - CB - CG ANGL. DEV. = -14.1 DEGREES
REMARK 500 ARG B 333 CD - NE - CZ ANGL. DEV. = -12.7 DEGREES
REMARK 500 LYS C 61 CD - CE - NZ ANGL. DEV. = -41.5 DEGREES
REMARK 500 LEU C 167 CB - CG - CD2 ANGL. DEV. = -17.4 DEGREES
REMARK 500 LEU C 227 CB - CG - CD1 ANGL. DEV. = -22.3 DEGREES
REMARK 500 ASP D 181 CB - CG - OD1 ANGL. DEV. = -21.3 DEGREES
REMARK 500 ASP D 181 CB - CG - OD2 ANGL. DEV. = 16.9 DEGREES
REMARK 500 ARG D 333 CD - NE - CZ ANGL. DEV. = -10.8 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 THR A 32 79.23 -117.50
REMARK 500 ILE A 46 -81.57 -104.12
REMARK 500 SEP A 139 142.26 -39.07
REMARK 500 ASP A 184 76.68 64.37
REMARK 500 ASN A 216 -169.79 -129.91
REMARK 500 LEU A 273 46.24 -82.71
REMARK 500 ASN B 185 42.68 39.44
REMARK 500 ASN B 186 -2.34 72.21
REMARK 500 SER B 256 0.39 -62.77
REMARK 500 ASP B 276 123.56 -39.82
REMARK 500 ASN B 307 65.41 -101.08
REMARK 500 GLU B 308 -90.63 -138.11
REMARK 500 SER B 319 -17.94 87.21
REMARK 500 LYS C 28 -75.04 -59.20
REMARK 500 ILE C 46 -76.98 -115.78
REMARK 500 PHE C 100 137.30 -177.70
REMARK 500 PHE C 110 -178.30 174.17
REMARK 500 ASP C 112 -168.78 -165.65
REMARK 500 ARG C 165 -21.93 72.48
REMARK 500 LYS C 168 150.34 175.82
REMARK 500 ASP C 184 86.07 54.89
REMARK 500 TRP C 196 -63.20 -133.88
REMARK 500 TPO C 197 127.65 -23.24
REMARK 500 SER C 212 -0.29 68.16
REMARK 500 ASN C 216 -169.08 -126.29
REMARK 500 TYR C 229 -73.65 -50.37
REMARK 500 LYS C 266 -72.32 -58.64
REMARK 500 CYS C 343 70.89 63.57
REMARK 500 GLU C 346 -60.61 -90.40
REMARK 500 GLU D 106 -7.48 -54.36
REMARK 500 PHE D 136 -57.23 -126.65
REMARK 500 ASN D 142 -71.28 -51.41
REMARK 500 ALA D 150 -7.33 -58.85
REMARK 500 ASN D 186 -6.58 66.03
REMARK 500 ALA D 189 -74.32 -91.87
REMARK 500 SER D 197 177.78 174.03
REMARK 500 PHE D 198 172.44 179.22
REMARK 500 SER D 252 -72.02 -72.80
REMARK 500 ARG D 304 -76.70 -101.06
REMARK 500 GLU D 308 -159.11 -133.69
REMARK 500 SER D 319 -10.26 78.78
REMARK 500 PRO D 332 -177.29 -60.68
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ALA B 189 13.71
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 ADP A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ADP C 400
DBREF 5JR7 A 1 350 UNP P05132 KAPCA_MOUSE 2 351
DBREF 5JR7 B 91 365 UNP P00514 KAP0_BOVIN 92 366
DBREF 5JR7 C 1 350 UNP P05132 KAPCA_MOUSE 2 351
DBREF 5JR7 D 91 365 UNP P00514 KAP0_BOVIN 92 366
SEQRES 1 A 350 GLY ASN ALA ALA ALA ALA LYS LYS GLY SER GLU GLN GLU
SEQRES 2 A 350 SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP PHE
SEQRES 3 A 350 LEU LYS LYS TRP GLU THR PRO SER GLN ASN THR ALA GLN
SEQRES 4 A 350 LEU ASP GLN PHE ASP ARG ILE LYS THR LEU GLY THR GLY
SEQRES 5 A 350 SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS GLU SER
SEQRES 6 A 350 GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN LYS
SEQRES 7 A 350 VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN GLU
SEQRES 8 A 350 LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU VAL
SEQRES 9 A 350 LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU TYR
SEQRES 10 A 350 MET VAL MET GLU TYR VAL ALA GLY GLY GLU MET PHE SER
SEQRES 11 A 350 HIS LEU ARG ARG ILE GLY ARG PHE SEP GLU PRO HIS ALA
SEQRES 12 A 350 ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE GLU TYR
SEQRES 13 A 350 LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU LYS PRO
SEQRES 14 A 350 GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE GLN VAL
SEQRES 15 A 350 THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY ARG THR
SEQRES 16 A 350 TRP TPO LEU CYS GLY THR PRO GLU TYR LEU ALA PRO GLU
SEQRES 17 A 350 ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL ASP TRP
SEQRES 18 A 350 TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA ALA GLY
SEQRES 19 A 350 TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN ILE TYR
SEQRES 20 A 350 GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO SER HIS
SEQRES 21 A 350 PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN LEU LEU
SEQRES 22 A 350 GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU LYS ASN
SEQRES 23 A 350 GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE ALA THR
SEQRES 24 A 350 THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL GLU ALA
SEQRES 25 A 350 PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP THR SER
SEQRES 26 A 350 ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG VAL SEP
SEQRES 27 A 350 ILE ASN GLU LYS CYS GLY LYS GLU PHE THR GLU PHE
SEQRES 1 B 275 GLY ARG ARG ARG ARG GLY ALA ILE SER ALA GLU VAL TYR
SEQRES 2 B 275 THR GLU GLU ASP ALA ALA SER TYR VAL ARG LYS VAL ILE
SEQRES 3 B 275 PRO LYS ASP TYR LYS THR MET ALA ALA LEU ALA LYS ALA
SEQRES 4 B 275 ILE GLU LYS ASN VAL LEU PHE SER HIS LEU ASP ASP ASN
SEQRES 5 B 275 GLU ARG SER ASP ILE PHE ASP ALA MET PHE PRO VAL SER
SEQRES 6 B 275 PHE ILE ALA GLY GLU THR VAL ILE GLN GLN GLY ASP GLU
SEQRES 7 B 275 GLY ASP ASN PHE TYR VAL ILE ASP GLN GLY GLU MET ASP
SEQRES 8 B 275 VAL TYR VAL ASN ASN GLU TRP ALA THR SER VAL GLY GLU
SEQRES 9 B 275 GLY GLY SER PHE GLY GLU LEU ALA LEU ILE TYR GLY THR
SEQRES 10 B 275 PRO ARG ALA ALA THR VAL LYS ALA LYS THR ASN VAL LYS
SEQRES 11 B 275 LEU TRP GLY ILE ASP ARG ASP SER TYR ARG ARG ILE LEU
SEQRES 12 B 275 MET GLY SER THR LEU ARG LYS ARG LYS MET TYR GLU GLU
SEQRES 13 B 275 PHE LEU SER LYS VAL SER ILE LEU GLU SER LEU ASP LYS
SEQRES 14 B 275 TRP GLU ARG LEU THR VAL ALA ASP ALA LEU GLU PRO VAL
SEQRES 15 B 275 GLN PHE GLU ASP GLY GLN LYS ILE VAL VAL GLN GLY GLU
SEQRES 16 B 275 PRO GLY ASP GLU PHE PHE ILE ILE LEU GLU GLY SER ALA
SEQRES 17 B 275 ALA VAL LEU GLN ARG ARG SER GLU ASN GLU GLU PHE VAL
SEQRES 18 B 275 GLU VAL GLY ARG LEU GLY PRO SER ASP TYR PHE GLY GLU
SEQRES 19 B 275 ILE ALA LEU LEU MET ASN ARG PRO ARG ALA ALA THR VAL
SEQRES 20 B 275 VAL ALA ARG GLY PRO LEU LYS CYS VAL LYS LEU ASP ARG
SEQRES 21 B 275 PRO ARG PHE GLU ARG VAL LEU GLY PRO CYS SER ASP ILE
SEQRES 22 B 275 LEU LYS
SEQRES 1 C 350 GLY ASN ALA ALA ALA ALA LYS LYS GLY SER GLU GLN GLU
SEQRES 2 C 350 SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP PHE
SEQRES 3 C 350 LEU LYS LYS TRP GLU THR PRO SER GLN ASN THR ALA GLN
SEQRES 4 C 350 LEU ASP GLN PHE ASP ARG ILE LYS THR LEU GLY THR GLY
SEQRES 5 C 350 SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS GLU SER
SEQRES 6 C 350 GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN LYS
SEQRES 7 C 350 VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN GLU
SEQRES 8 C 350 LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU VAL
SEQRES 9 C 350 LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU TYR
SEQRES 10 C 350 MET VAL MET GLU TYR VAL ALA GLY GLY GLU MET PHE SER
SEQRES 11 C 350 HIS LEU ARG ARG ILE GLY ARG PHE SEP GLU PRO HIS ALA
SEQRES 12 C 350 ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE GLU TYR
SEQRES 13 C 350 LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU LYS PRO
SEQRES 14 C 350 GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE GLN VAL
SEQRES 15 C 350 THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY ARG THR
SEQRES 16 C 350 TRP TPO LEU CYS GLY THR PRO GLU TYR LEU ALA PRO GLU
SEQRES 17 C 350 ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL ASP TRP
SEQRES 18 C 350 TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA ALA GLY
SEQRES 19 C 350 TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN ILE TYR
SEQRES 20 C 350 GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO SER HIS
SEQRES 21 C 350 PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN LEU LEU
SEQRES 22 C 350 GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU LYS ASN
SEQRES 23 C 350 GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE ALA THR
SEQRES 24 C 350 THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL GLU ALA
SEQRES 25 C 350 PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP THR SER
SEQRES 26 C 350 ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG VAL SEP
SEQRES 27 C 350 ILE ASN GLU LYS CYS GLY LYS GLU PHE THR GLU PHE
SEQRES 1 D 275 GLY ARG ARG ARG ARG GLY ALA ILE SER ALA GLU VAL TYR
SEQRES 2 D 275 THR GLU GLU ASP ALA ALA SER TYR VAL ARG LYS VAL ILE
SEQRES 3 D 275 PRO LYS ASP TYR LYS THR MET ALA ALA LEU ALA LYS ALA
SEQRES 4 D 275 ILE GLU LYS ASN VAL LEU PHE SER HIS LEU ASP ASP ASN
SEQRES 5 D 275 GLU ARG SER ASP ILE PHE ASP ALA MET PHE PRO VAL SER
SEQRES 6 D 275 PHE ILE ALA GLY GLU THR VAL ILE GLN GLN GLY ASP GLU
SEQRES 7 D 275 GLY ASP ASN PHE TYR VAL ILE ASP GLN GLY GLU MET ASP
SEQRES 8 D 275 VAL TYR VAL ASN ASN GLU TRP ALA THR SER VAL GLY GLU
SEQRES 9 D 275 GLY GLY SER PHE GLY GLU LEU ALA LEU ILE TYR GLY THR
SEQRES 10 D 275 PRO ARG ALA ALA THR VAL LYS ALA LYS THR ASN VAL LYS
SEQRES 11 D 275 LEU TRP GLY ILE ASP ARG ASP SER TYR ARG ARG ILE LEU
SEQRES 12 D 275 MET GLY SER THR LEU ARG LYS ARG LYS MET TYR GLU GLU
SEQRES 13 D 275 PHE LEU SER LYS VAL SER ILE LEU GLU SER LEU ASP LYS
SEQRES 14 D 275 TRP GLU ARG LEU THR VAL ALA ASP ALA LEU GLU PRO VAL
SEQRES 15 D 275 GLN PHE GLU ASP GLY GLN LYS ILE VAL VAL GLN GLY GLU
SEQRES 16 D 275 PRO GLY ASP GLU PHE PHE ILE ILE LEU GLU GLY SER ALA
SEQRES 17 D 275 ALA VAL LEU GLN ARG ARG SER GLU ASN GLU GLU PHE VAL
SEQRES 18 D 275 GLU VAL GLY ARG LEU GLY PRO SER ASP TYR PHE GLY GLU
SEQRES 19 D 275 ILE ALA LEU LEU MET ASN ARG PRO ARG ALA ALA THR VAL
SEQRES 20 D 275 VAL ALA ARG GLY PRO LEU LYS CYS VAL LYS LEU ASP ARG
SEQRES 21 D 275 PRO ARG PHE GLU ARG VAL LEU GLY PRO CYS SER ASP ILE
SEQRES 22 D 275 LEU LYS
MODRES 5JR7 SEP A 139 SER MODIFIED RESIDUE
MODRES 5JR7 TPO A 197 THR MODIFIED RESIDUE
MODRES 5JR7 SEP A 338 SER MODIFIED RESIDUE
MODRES 5JR7 SEP C 139 SER MODIFIED RESIDUE
MODRES 5JR7 TPO C 197 THR MODIFIED RESIDUE
MODRES 5JR7 SEP C 338 SER MODIFIED RESIDUE
HET SEP A 139 10
HET TPO A 197 11
HET SEP A 338 10
HET SEP C 139 10
HET TPO C 197 11
HET SEP C 338 10
HET ADP A 400 27
HET ADP C 400 27
HETNAM SEP PHOSPHOSERINE
HETNAM TPO PHOSPHOTHREONINE
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETSYN SEP PHOSPHONOSERINE
HETSYN TPO PHOSPHONOTHREONINE
FORMUL 1 SEP 4(C3 H8 N O6 P)
FORMUL 1 TPO 2(C4 H10 N O6 P)
FORMUL 5 ADP 2(C10 H15 N5 O10 P2)
HELIX 1 AA1 GLU A 13 THR A 32 1 20
HELIX 2 AA2 GLN A 39 ASP A 41 5 3
HELIX 3 AA3 LYS A 76 LEU A 82 1 7
HELIX 4 AA4 GLN A 84 VAL A 98 1 15
HELIX 5 AA5 GLU A 127 GLY A 136 1 10
HELIX 6 AA6 SEP A 139 LEU A 160 1 22
HELIX 7 AA7 LYS A 168 GLU A 170 5 3
HELIX 8 AA8 THR A 201 LEU A 205 5 5
HELIX 9 AA9 ALA A 206 LEU A 211 1 6
HELIX 10 AB1 ALA A 218 GLY A 234 1 17
HELIX 11 AB2 GLN A 242 GLY A 253 1 12
HELIX 12 AB3 SER A 262 LEU A 273 1 12
HELIX 13 AB4 VAL A 288 ASN A 293 1 6
HELIX 14 AB5 HIS A 294 ALA A 298 5 5
HELIX 15 AB6 ASP A 301 GLN A 307 1 7
HELIX 16 AB7 THR B 104 TYR B 111 1 8
HELIX 17 AB8 ASP B 119 GLU B 131 1 13
HELIX 18 AB9 ASN B 133 HIS B 138 1 6
HELIX 19 AC1 ASP B 140 MET B 151 1 12
HELIX 20 AC2 GLY B 199 ILE B 204 5 6
HELIX 21 AC3 ARG B 226 LYS B 250 1 25
HELIX 22 AC4 VAL B 251 GLU B 255 5 5
HELIX 23 AC5 ASP B 258 LEU B 269 1 12
HELIX 24 AC6 GLU B 324 MET B 329 1 6
HELIX 25 AC7 ARG B 350 LEU B 357 1 8
HELIX 26 AC8 VAL C 15 THR C 32 1 18
HELIX 27 AC9 GLN C 39 PHE C 43 5 5
HELIX 28 AD1 LYS C 76 LEU C 82 1 7
HELIX 29 AD2 GLN C 84 GLN C 96 1 13
HELIX 30 AD3 GLU C 127 GLY C 136 1 10
HELIX 31 AD4 SEP C 139 LEU C 160 1 22
HELIX 32 AD5 LYS C 168 GLU C 170 5 3
HELIX 33 AD6 THR C 201 LEU C 205 5 5
HELIX 34 AD7 ALA C 206 LEU C 211 1 6
HELIX 35 AD8 ALA C 218 GLY C 234 1 17
HELIX 36 AD9 GLN C 242 VAL C 251 1 10
HELIX 37 AE1 SER C 262 LEU C 273 1 12
HELIX 38 AE2 VAL C 288 ASN C 293 1 6
HELIX 39 AE3 HIS C 294 ALA C 298 5 5
HELIX 40 AE4 ASP C 301 GLN C 307 1 7
HELIX 41 AE5 THR D 104 ALA D 109 1 6
HELIX 42 AE6 ASP D 119 ALA D 124 1 6
HELIX 43 AE7 ALA D 124 GLU D 131 1 8
HELIX 44 AE8 ASN D 133 HIS D 138 1 6
HELIX 45 AE9 ASP D 140 MET D 151 1 12
HELIX 46 AF1 GLU D 200 TYR D 205 1 6
HELIX 47 AF2 ARG D 226 VAL D 251 1 26
HELIX 48 AF3 ASP D 258 ASP D 267 1 10
HELIX 49 AF4 GLU D 324 MET D 329 1 6
HELIX 50 AF5 ASP D 349 LEU D 357 1 9
SHEET 1 AA1 5 PHE A 43 THR A 51 0
SHEET 2 AA1 5 GLY A 55 HIS A 62 -1 O VAL A 57 N GLY A 50
SHEET 3 AA1 5 ASN A 67 ASP A 75 -1 O MET A 71 N MET A 58
SHEET 4 AA1 5 ASN A 115 GLU A 121 -1 O MET A 120 N ALA A 70
SHEET 5 AA1 5 LEU A 106 LYS A 111 -1 N GLU A 107 O VAL A 119
SHEET 1 AA2 2 LEU A 162 ILE A 163 0
SHEET 2 AA2 2 LYS A 189 ARG A 190 -1 O LYS A 189 N ILE A 163
SHEET 1 AA3 2 LEU A 172 ILE A 174 0
SHEET 2 AA3 2 ILE A 180 VAL A 182 -1 O GLN A 181 N LEU A 173
SHEET 1 AA4 2 CYS A 199 GLY A 200 0
SHEET 2 AA4 2 ILE B 98 SER B 99 -1 O ILE B 98 N GLY A 200
SHEET 1 AA5 4 PHE B 152 PHE B 156 0
SHEET 2 AA5 4 VAL B 219 ASP B 225 -1 O GLY B 223 N PHE B 152
SHEET 3 AA5 4 ASN B 171 GLN B 177 -1 N VAL B 174 O TRP B 222
SHEET 4 AA5 4 SER B 197 PHE B 198 -1 O PHE B 198 N TYR B 173
SHEET 1 AA6 4 THR B 161 ILE B 163 0
SHEET 2 AA6 4 THR B 212 ALA B 215 -1 O VAL B 213 N VAL B 162
SHEET 3 AA6 4 MET B 180 VAL B 184 -1 N ASP B 181 O LYS B 214
SHEET 4 AA6 4 GLU B 187 VAL B 192 -1 O GLU B 187 N VAL B 184
SHEET 1 AA7 4 GLU B 270 PHE B 274 0
SHEET 2 AA7 4 THR B 336 ASP B 349 -1 O LEU B 343 N PHE B 274
SHEET 3 AA7 4 GLU B 289 GLN B 302 -1 N LEU B 301 O THR B 336
SHEET 4 AA7 4 VAL B 311 LEU B 316 -1 O LEU B 316 N ALA B 298
SHEET 1 AA8 4 LYS B 279 VAL B 281 0
SHEET 2 AA8 4 THR B 336 ASP B 349 -1 O VAL B 337 N VAL B 281
SHEET 3 AA8 4 GLU B 289 GLN B 302 -1 N LEU B 301 O THR B 336
SHEET 4 AA8 4 TYR B 321 PHE B 322 -1 O PHE B 322 N PHE B 291
SHEET 1 AA9 2 PRO B 286 GLY B 287 0
SHEET 2 AA9 2 ARG B 331 PRO B 332 -1 O ARG B 331 N GLY B 287
SHEET 1 AB1 5 LYS C 47 THR C 51 0
SHEET 2 AB1 5 ARG C 56 HIS C 62 -1 O LEU C 59 N LYS C 47
SHEET 3 AB1 5 ASN C 67 ASP C 75 -1 O ILE C 73 N ARG C 56
SHEET 4 AB1 5 ASN C 115 GLU C 121 -1 O MET C 118 N LYS C 72
SHEET 5 AB1 5 LEU C 106 PHE C 110 -1 N PHE C 110 O TYR C 117
SHEET 1 AB2 2 LEU C 162 ILE C 163 0
SHEET 2 AB2 2 LYS C 189 ARG C 190 -1 O LYS C 189 N ILE C 163
SHEET 1 AB3 2 LEU C 172 ILE C 174 0
SHEET 2 AB3 2 ILE C 180 VAL C 182 -1 O GLN C 181 N LEU C 173
SHEET 1 AB4 2 CYS C 199 GLY C 200 0
SHEET 2 AB4 2 ILE D 98 SER D 99 -1 O ILE D 98 N GLY C 200
SHEET 1 AB5 3 VAL D 154 PHE D 156 0
SHEET 2 AB5 3 VAL D 219 ASP D 225 -1 O LEU D 221 N VAL D 154
SHEET 3 AB5 3 ASN D 171 ILE D 175 -1 N VAL D 174 O TRP D 222
SHEET 1 AB6 4 GLU D 160 ILE D 163 0
SHEET 2 AB6 4 THR D 212 ALA D 215 -1 O ALA D 215 N GLU D 160
SHEET 3 AB6 4 MET D 180 VAL D 184 -1 N ASP D 181 O LYS D 214
SHEET 4 AB6 4 GLU D 187 VAL D 192 -1 O ALA D 189 N VAL D 182
SHEET 1 AB7 4 GLU D 270 PHE D 274 0
SHEET 2 AB7 4 THR D 336 LYS D 347 -1 O CYS D 345 N VAL D 272
SHEET 3 AB7 4 PHE D 291 ARG D 303 -1 N LEU D 301 O THR D 336
SHEET 4 AB7 4 PHE D 310 LEU D 316 -1 O LEU D 316 N ALA D 298
SHEET 1 AB8 4 GLU D 270 PHE D 274 0
SHEET 2 AB8 4 THR D 336 LYS D 347 -1 O CYS D 345 N VAL D 272
SHEET 3 AB8 4 PHE D 291 ARG D 303 -1 N LEU D 301 O THR D 336
SHEET 4 AB8 4 TYR D 321 PHE D 322 -1 O PHE D 322 N PHE D 291
SHEET 1 AB9 2 PRO D 286 GLY D 287 0
SHEET 2 AB9 2 ARG D 331 PRO D 332 -1 O ARG D 331 N GLY D 287
LINK C PHE A 138 N SEP A 139 1555 1555 1.33
LINK C SEP A 139 N GLU A 140 1555 1555 1.34
LINK C TRP A 196 N TPO A 197 1555 1555 1.33
LINK C TPO A 197 N LEU A 198 1555 1555 1.32
LINK C VAL A 337 N SEP A 338 1555 1555 1.33
LINK C SEP A 338 N ILE A 339 1555 1555 1.32
LINK C PHE C 138 N SEP C 139 1555 1555 1.33
LINK C SEP C 139 N GLU C 140 1555 1555 1.33
LINK C TRP C 196 N TPO C 197 1555 1555 1.33
LINK C TPO C 197 N LEU C 198 1555 1555 1.33
LINK C VAL C 337 N SEP C 338 1555 1555 1.33
LINK C SEP C 338 N ILE C 339 1555 1555 1.33
SITE 1 AC1 16 GLY A 50 GLY A 52 GLY A 55 VAL A 57
SITE 2 AC1 16 ALA A 70 LYS A 72 MET A 120 GLU A 121
SITE 3 AC1 16 VAL A 123 GLU A 127 GLU A 170 ASN A 171
SITE 4 AC1 16 LEU A 173 THR A 183 ASP A 184 PHE A 327
SITE 1 AC2 13 GLY C 50 GLY C 52 GLY C 55 VAL C 57
SITE 2 AC2 13 ALA C 70 LYS C 72 GLU C 121 VAL C 123
SITE 3 AC2 13 GLU C 127 GLU C 170 LEU C 173 THR C 183
SITE 4 AC2 13 ASP C 184
CRYST1 60.146 66.790 87.932 101.76 89.37 105.27 P 1 2
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 0.016626 0.004539 0.000781 0.00000
SCALE2 0.000000 0.015520 0.003306 0.00000
SCALE3 0.000000 0.000000 0.011628 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
