HEADER TRANSFERASE 24-FEB-12 4DWJ
TITLE CRYSTAL STRUCTURE OF THYMIDYLATE KINASE FROM STAPHYLOCOCCUS AUREUS IN
TITLE 2 COMPLEX WITH THYMIDINE MONOPHOSPHATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THYMIDYLATE KINASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 SYNONYM: DTMP KINASE;
COMPND 5 EC: 2.7.4.9;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS;
SOURCE 3 ORGANISM_TAXID: 158878;
SOURCE 4 STRAIN: MU50;
SOURCE 5 GENE: TMK, SAV0482;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) MAGIC;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS STRUCTURAL GENOMICS, PSI-BIOLOGY, MIDWEST CENTER FOR STRUCTURAL
KEYWDS 2 GENOMICS, MCSG, STRUCTURES OF MTB PROTEINS CONFERRING SUSCEPTIBILITY
KEYWDS 3 TO KNOWN MTB INHIBITORS, MTBI, THYMIDYLATE KINASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.V.FILIPPOVA,G.MINASOV,L.SHUVALOVA,O.KIRYUKHINA,R.JEDRZEJCZAK,
AUTHOR 2 G.BABNIGG,E.RUBIN,J.SACCHETTINI,A.JOACHIMIAK,W.F.ANDERSON,MIDWEST
AUTHOR 3 CENTER FOR STRUCTURAL GENOMICS (MCSG),STRUCTURES OF MTB PROTEINS
AUTHOR 4 CONFERRING SUSCEPTIBILITY TO KNOWN MTB INHIBITORS (MTBI)
REVDAT 5 13-SEP-23 4DWJ 1 REMARK SEQADV
REVDAT 4 15-NOV-17 4DWJ 1 REMARK
REVDAT 3 10-OCT-12 4DWJ 1 AUTHOR
REVDAT 2 11-APR-12 4DWJ 1 AUTHOR
REVDAT 1 07-MAR-12 4DWJ 0
JRNL AUTH E.V.FILIPPOVA,G.MINASOV,L.SHUVALOVA,O.KIRYUKHINA,
JRNL AUTH 2 R.JEDRZEJCZAK,A.JOACHIMIAK,W.F.ANDERSON,
JRNL AUTH 3 MIDWEST CENTER FOR STRUCTURAL GENOMICS (MCSG)
JRNL TITL CRYSTAL STRUCTURE OF THYMIDYLATE KINASE FROM STAPHYLOCOCCUS
JRNL TITL 2 AUREUS IN COMPLEX WITH THYMIDINE MONOPHOSPHATE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.74 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.74
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.7
REMARK 3 NUMBER OF REFLECTIONS : 37963
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2016
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.74
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.81
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2747
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.79
REMARK 3 BIN R VALUE (WORKING SET) : 0.2690
REMARK 3 BIN FREE R VALUE SET COUNT : 163
REMARK 3 BIN FREE R VALUE : 0.3390
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12722
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 120
REMARK 3 SOLVENT ATOMS : 75
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 71.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 57.26
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.15000
REMARK 3 B22 (A**2) : -4.26000
REMARK 3 B33 (A**2) : -1.82000
REMARK 3 B12 (A**2) : -0.26000
REMARK 3 B13 (A**2) : -0.55000
REMARK 3 B23 (A**2) : 3.12000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.444
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.347
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 36.772
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.931
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 13060 ; 0.012 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 8931 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 17632 ; 1.744 ; 1.981
REMARK 3 BOND ANGLES OTHERS (DEGREES): 21750 ; 1.108 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1575 ; 2.341 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 653 ;29.661 ;24.349
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2378 ;10.399 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 104 ;13.092 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1979 ; 0.101 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 14386 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2583 ; 0.004 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 16
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 123
REMARK 3 ORIGIN FOR THE GROUP (A): -1.2141 -39.8170 -17.0285
REMARK 3 T TENSOR
REMARK 3 T11: 0.0726 T22: 0.2564
REMARK 3 T33: 0.1630 T12: 0.0563
REMARK 3 T13: -0.0179 T23: -0.0407
REMARK 3 L TENSOR
REMARK 3 L11: 0.7807 L22: 5.1092
REMARK 3 L33: 1.3281 L12: -0.1352
REMARK 3 L13: -0.4867 L23: -0.8760
REMARK 3 S TENSOR
REMARK 3 S11: 0.0441 S12: 0.1750 S13: -0.1200
REMARK 3 S21: -0.3912 S22: -0.0225 S23: -0.0955
REMARK 3 S31: -0.0918 S32: -0.1257 S33: -0.0215
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 124 A 204
REMARK 3 ORIGIN FOR THE GROUP (A): 3.5849 -25.2842 -14.2611
REMARK 3 T TENSOR
REMARK 3 T11: 0.0623 T22: 0.2315
REMARK 3 T33: 0.2130 T12: 0.0249
REMARK 3 T13: 0.0303 T23: 0.0174
REMARK 3 L TENSOR
REMARK 3 L11: 1.0395 L22: 5.2354
REMARK 3 L33: 1.2275 L12: -0.2661
REMARK 3 L13: -0.5268 L23: -0.2008
REMARK 3 S TENSOR
REMARK 3 S11: 0.1974 S12: 0.1028 S13: 0.0560
REMARK 3 S21: -0.0848 S22: -0.1095 S23: -0.5370
REMARK 3 S31: -0.2468 S32: 0.0142 S33: -0.0879
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 2 B 125
REMARK 3 ORIGIN FOR THE GROUP (A): -1.1932 -62.8890 -0.2326
REMARK 3 T TENSOR
REMARK 3 T11: 0.0309 T22: 0.2519
REMARK 3 T33: 0.1626 T12: -0.0077
REMARK 3 T13: 0.0124 T23: -0.0259
REMARK 3 L TENSOR
REMARK 3 L11: 0.4759 L22: 3.2868
REMARK 3 L33: 1.4693 L12: 0.3176
REMARK 3 L13: 0.2711 L23: -0.8506
REMARK 3 S TENSOR
REMARK 3 S11: 0.0426 S12: -0.0996 S13: 0.0876
REMARK 3 S21: 0.2148 S22: 0.0054 S23: 0.0106
REMARK 3 S31: 0.0609 S32: -0.2879 S33: -0.0480
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 126 B 204
REMARK 3 ORIGIN FOR THE GROUP (A): 4.1135 -77.6545 -2.9188
REMARK 3 T TENSOR
REMARK 3 T11: 0.0692 T22: 0.1911
REMARK 3 T33: 0.2375 T12: -0.0159
REMARK 3 T13: -0.0330 T23: 0.0185
REMARK 3 L TENSOR
REMARK 3 L11: 0.0445 L22: 4.2317
REMARK 3 L33: 5.1977 L12: -0.2207
REMARK 3 L13: -0.1385 L23: 0.2910
REMARK 3 S TENSOR
REMARK 3 S11: 0.0421 S12: -0.0460 S13: -0.0085
REMARK 3 S21: 0.0657 S22: 0.0907 S23: -0.4186
REMARK 3 S31: 0.2613 S32: 0.1707 S33: -0.1328
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 2 C 134
REMARK 3 ORIGIN FOR THE GROUP (A): -29.9693 -83.5829 -1.3147
REMARK 3 T TENSOR
REMARK 3 T11: 0.0553 T22: 0.2026
REMARK 3 T33: 0.1214 T12: 0.0591
REMARK 3 T13: 0.0019 T23: -0.0153
REMARK 3 L TENSOR
REMARK 3 L11: 0.8604 L22: 2.7307
REMARK 3 L33: 1.3651 L12: 0.0013
REMARK 3 L13: 0.0971 L23: -0.6680
REMARK 3 S TENSOR
REMARK 3 S11: 0.1094 S12: 0.1681 S13: -0.0573
REMARK 3 S21: -0.2458 S22: -0.0574 S23: -0.0439
REMARK 3 S31: -0.0476 S32: -0.2698 S33: -0.0520
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 135 C 204
REMARK 3 ORIGIN FOR THE GROUP (A): -25.5613 -69.0831 1.9060
REMARK 3 T TENSOR
REMARK 3 T11: 0.0602 T22: 0.1275
REMARK 3 T33: 0.2050 T12: 0.0575
REMARK 3 T13: 0.0185 T23: 0.0307
REMARK 3 L TENSOR
REMARK 3 L11: 1.1235 L22: 3.1022
REMARK 3 L33: 2.8284 L12: -0.2532
REMARK 3 L13: -0.4249 L23: -0.0049
REMARK 3 S TENSOR
REMARK 3 S11: 0.0491 S12: 0.1334 S13: 0.1019
REMARK 3 S21: 0.0064 S22: -0.0340 S23: -0.2842
REMARK 3 S31: -0.2119 S32: -0.2365 S33: -0.0151
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 2 D 126
REMARK 3 ORIGIN FOR THE GROUP (A): -30.3370 -33.9013 15.7321
REMARK 3 T TENSOR
REMARK 3 T11: 0.0979 T22: 0.2556
REMARK 3 T33: 0.1688 T12: -0.0570
REMARK 3 T13: 0.0181 T23: -0.0571
REMARK 3 L TENSOR
REMARK 3 L11: 0.5297 L22: 5.0236
REMARK 3 L33: 0.8975 L12: 0.1160
REMARK 3 L13: 0.3352 L23: -0.7581
REMARK 3 S TENSOR
REMARK 3 S11: 0.0458 S12: -0.1475 S13: 0.1023
REMARK 3 S21: 0.4123 S22: -0.1703 S23: -0.1874
REMARK 3 S31: 0.1317 S32: -0.0390 S33: 0.1245
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 127 D 204
REMARK 3 ORIGIN FOR THE GROUP (A): -25.9367 -49.1077 12.4266
REMARK 3 T TENSOR
REMARK 3 T11: 0.0625 T22: 0.2292
REMARK 3 T33: 0.2086 T12: 0.0005
REMARK 3 T13: -0.0231 T23: 0.0380
REMARK 3 L TENSOR
REMARK 3 L11: 1.1040 L22: 4.7772
REMARK 3 L33: 0.5498 L12: 0.3411
REMARK 3 L13: 0.3506 L23: 0.0571
REMARK 3 S TENSOR
REMARK 3 S11: 0.2163 S12: -0.1312 S13: -0.0498
REMARK 3 S21: 0.1005 S22: -0.2219 S23: -0.5481
REMARK 3 S31: 0.1584 S32: 0.0575 S33: 0.0056
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 2 E 128
REMARK 3 ORIGIN FOR THE GROUP (A): -0.8140 -33.4485 30.9846
REMARK 3 T TENSOR
REMARK 3 T11: 0.0228 T22: 0.1790
REMARK 3 T33: 0.2000 T12: -0.0237
REMARK 3 T13: -0.0256 T23: -0.0217
REMARK 3 L TENSOR
REMARK 3 L11: 1.4117 L22: 3.9388
REMARK 3 L33: 3.9406 L12: 0.2297
REMARK 3 L13: -0.3355 L23: -0.9064
REMARK 3 S TENSOR
REMARK 3 S11: -0.0072 S12: 0.2452 S13: -0.2311
REMARK 3 S21: -0.0790 S22: 0.0941 S23: 0.4230
REMARK 3 S31: 0.0355 S32: -0.4313 S33: -0.0869
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 129 E 204
REMARK 3 ORIGIN FOR THE GROUP (A): 3.5360 -17.9875 33.8278
REMARK 3 T TENSOR
REMARK 3 T11: 0.3062 T22: 0.0839
REMARK 3 T33: 0.1006 T12: 0.0040
REMARK 3 T13: 0.0412 T23: 0.0125
REMARK 3 L TENSOR
REMARK 3 L11: 1.6486 L22: 4.3728
REMARK 3 L33: 8.4589 L12: -0.3401
REMARK 3 L13: 0.4067 L23: 1.0999
REMARK 3 S TENSOR
REMARK 3 S11: -0.1168 S12: 0.1049 S13: -0.0052
REMARK 3 S21: 0.1383 S22: 0.1122 S23: 0.0389
REMARK 3 S31: -1.4245 S32: -0.1876 S33: 0.0046
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 2 F 81
REMARK 3 ORIGIN FOR THE GROUP (A): -33.5620 -41.0304 -32.0139
REMARK 3 T TENSOR
REMARK 3 T11: 0.0240 T22: 0.2650
REMARK 3 T33: 0.3406 T12: -0.0250
REMARK 3 T13: -0.0098 T23: -0.0019
REMARK 3 L TENSOR
REMARK 3 L11: 1.6012 L22: 4.4099
REMARK 3 L33: 4.4174 L12: -0.4163
REMARK 3 L13: -0.0574 L23: -1.5331
REMARK 3 S TENSOR
REMARK 3 S11: -0.0955 S12: -0.2297 S13: 0.2643
REMARK 3 S21: -0.0741 S22: 0.4296 S23: 0.9136
REMARK 3 S31: -0.0146 S32: -0.6616 S33: -0.3340
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 82 F 204
REMARK 3 ORIGIN FOR THE GROUP (A): -25.0002 -49.5882 -34.5405
REMARK 3 T TENSOR
REMARK 3 T11: 0.1005 T22: 0.1168
REMARK 3 T33: 0.1315 T12: -0.0115
REMARK 3 T13: -0.0282 T23: 0.0179
REMARK 3 L TENSOR
REMARK 3 L11: 1.9466 L22: 3.6574
REMARK 3 L33: 5.2081 L12: 0.0581
REMARK 3 L13: -0.2948 L23: -0.5617
REMARK 3 S TENSOR
REMARK 3 S11: -0.0361 S12: -0.0094 S13: 0.1111
REMARK 3 S21: -0.1673 S22: 0.1905 S23: 0.0076
REMARK 3 S31: 0.6999 S32: -0.1199 S33: -0.1544
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 2 G 122
REMARK 3 ORIGIN FOR THE GROUP (A): 0.9469 -56.5791 47.6884
REMARK 3 T TENSOR
REMARK 3 T11: 0.3902 T22: 0.0932
REMARK 3 T33: 0.1607 T12: -0.0657
REMARK 3 T13: 0.0862 T23: -0.0158
REMARK 3 L TENSOR
REMARK 3 L11: 0.7980 L22: 5.2611
REMARK 3 L33: 4.8219 L12: 0.9380
REMARK 3 L13: 0.4915 L23: -1.6752
REMARK 3 S TENSOR
REMARK 3 S11: 0.2379 S12: -0.1047 S13: 0.2133
REMARK 3 S21: 0.7994 S22: -0.1511 S23: 0.1484
REMARK 3 S31: 0.4805 S32: 0.0081 S33: -0.0868
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 123 G 203
REMARK 3 ORIGIN FOR THE GROUP (A): 7.5011 -69.9814 45.2921
REMARK 3 T TENSOR
REMARK 3 T11: 0.7208 T22: 0.1345
REMARK 3 T33: 0.1297 T12: 0.0775
REMARK 3 T13: -0.0957 T23: 0.0450
REMARK 3 L TENSOR
REMARK 3 L11: 1.1286 L22: 6.0074
REMARK 3 L33: 4.4699 L12: 0.0983
REMARK 3 L13: 0.2993 L23: -0.1211
REMARK 3 S TENSOR
REMARK 3 S11: 0.4093 S12: 0.0310 S13: -0.0705
REMARK 3 S21: 0.5555 S22: -0.3097 S23: -0.7048
REMARK 3 S31: 1.2637 S32: 0.4804 S33: -0.0996
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 1 H 82
REMARK 3 ORIGIN FOR THE GROUP (A): -30.9320 -75.4135 44.7430
REMARK 3 T TENSOR
REMARK 3 T11: 0.4505 T22: 0.1302
REMARK 3 T33: 0.1473 T12: 0.0961
REMARK 3 T13: -0.1178 T23: 0.0167
REMARK 3 L TENSOR
REMARK 3 L11: 1.4705 L22: 4.4101
REMARK 3 L33: 4.2986 L12: -0.0558
REMARK 3 L13: -1.1455 L23: -0.9664
REMARK 3 S TENSOR
REMARK 3 S11: 0.2312 S12: 0.2189 S13: -0.1147
REMARK 3 S21: -0.8749 S22: -0.0427 S23: 0.4514
REMARK 3 S31: -0.4614 S32: -0.2826 S33: -0.1885
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 83 H 203
REMARK 3 ORIGIN FOR THE GROUP (A): -22.3565 -67.8545 49.3977
REMARK 3 T TENSOR
REMARK 3 T11: 0.4844 T22: 0.0985
REMARK 3 T33: 0.1359 T12: -0.0563
REMARK 3 T13: 0.0702 T23: 0.0434
REMARK 3 L TENSOR
REMARK 3 L11: 1.6317 L22: 6.8872
REMARK 3 L33: 4.1733 L12: -0.3705
REMARK 3 L13: -0.2794 L23: 0.4519
REMARK 3 S TENSOR
REMARK 3 S11: 0.3534 S12: -0.0209 S13: 0.0033
REMARK 3 S21: -0.7235 S22: -0.2971 S23: -0.6466
REMARK 3 S31: -0.8703 S32: 0.3203 S33: -0.0563
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4DWJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-12.
REMARK 100 THE DEPOSITION ID IS D_1000070871.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-NOV-11
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 : APS
REMARK 200 BEAMLINE : 21-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97886
REMARK 200 MONOCHROMATOR : SI-111 CHANNEL
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39979
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.740
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.2
REMARK 200 DATA REDUNDANCY : 1.900
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.2700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.41000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2CCJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MGCL2, 0.1 M HEPES, 25 %
REMARK 280 PEG3350, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 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: 3090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 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 350
REMARK 350 BIOMOLECULE: 3
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: 2560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, G
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2880 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -23
REMARK 465 HIS A -22
REMARK 465 HIS A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 SER A -16
REMARK 465 SER A -15
REMARK 465 GLY A -14
REMARK 465 VAL A -13
REMARK 465 ASP A -12
REMARK 465 LEU A -11
REMARK 465 GLY A -10
REMARK 465 THR A -9
REMARK 465 GLU A -8
REMARK 465 ASN A -7
REMARK 465 LEU A -6
REMARK 465 TYR A -5
REMARK 465 PHE A -4
REMARK 465 GLN A -3
REMARK 465 SER A -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
REMARK 465 MET A 1
REMARK 465 ASN A 173
REMARK 465 GLU A 174
REMARK 465 SER A 175
REMARK 465 ILE A 205
REMARK 465 MET B -23
REMARK 465 HIS B -22
REMARK 465 HIS B -21
REMARK 465 HIS B -20
REMARK 465 HIS B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 SER B -16
REMARK 465 SER B -15
REMARK 465 GLY B -14
REMARK 465 VAL B -13
REMARK 465 ASP B -12
REMARK 465 LEU B -11
REMARK 465 GLY B -10
REMARK 465 THR B -9
REMARK 465 GLU B -8
REMARK 465 ASN B -7
REMARK 465 LEU B -6
REMARK 465 TYR B -5
REMARK 465 PHE B -4
REMARK 465 GLN B -3
REMARK 465 SER B -2
REMARK 465 ASN B -1
REMARK 465 ALA B 0
REMARK 465 MET B 1
REMARK 465 ILE B 205
REMARK 465 MET C -23
REMARK 465 HIS C -22
REMARK 465 HIS C -21
REMARK 465 HIS C -20
REMARK 465 HIS C -19
REMARK 465 HIS C -18
REMARK 465 HIS C -17
REMARK 465 SER C -16
REMARK 465 SER C -15
REMARK 465 GLY C -14
REMARK 465 VAL C -13
REMARK 465 ASP C -12
REMARK 465 LEU C -11
REMARK 465 GLY C -10
REMARK 465 THR C -9
REMARK 465 GLU C -8
REMARK 465 ASN C -7
REMARK 465 LEU C -6
REMARK 465 TYR C -5
REMARK 465 PHE C -4
REMARK 465 GLN C -3
REMARK 465 SER C -2
REMARK 465 ASN C -1
REMARK 465 ALA C 0
REMARK 465 MET C 1
REMARK 465 ARG C 147
REMARK 465 ILE C 205
REMARK 465 MET D -23
REMARK 465 HIS D -22
REMARK 465 HIS D -21
REMARK 465 HIS D -20
REMARK 465 HIS D -19
REMARK 465 HIS D -18
REMARK 465 HIS D -17
REMARK 465 SER D -16
REMARK 465 SER D -15
REMARK 465 GLY D -14
REMARK 465 VAL D -13
REMARK 465 ASP D -12
REMARK 465 LEU D -11
REMARK 465 GLY D -10
REMARK 465 THR D -9
REMARK 465 GLU D -8
REMARK 465 ASN D -7
REMARK 465 LEU D -6
REMARK 465 TYR D -5
REMARK 465 PHE D -4
REMARK 465 GLN D -3
REMARK 465 SER D -2
REMARK 465 ASN D -1
REMARK 465 ALA D 0
REMARK 465 MET D 1
REMARK 465 ASN D 173
REMARK 465 GLU D 174
REMARK 465 SER D 175
REMARK 465 ILE D 205
REMARK 465 MET E -23
REMARK 465 HIS E -22
REMARK 465 HIS E -21
REMARK 465 HIS E -20
REMARK 465 HIS E -19
REMARK 465 HIS E -18
REMARK 465 HIS E -17
REMARK 465 SER E -16
REMARK 465 SER E -15
REMARK 465 GLY E -14
REMARK 465 VAL E -13
REMARK 465 ASP E -12
REMARK 465 LEU E -11
REMARK 465 GLY E -10
REMARK 465 THR E -9
REMARK 465 GLU E -8
REMARK 465 ASN E -7
REMARK 465 LEU E -6
REMARK 465 TYR E -5
REMARK 465 PHE E -4
REMARK 465 GLN E -3
REMARK 465 SER E -2
REMARK 465 ASN E -1
REMARK 465 ALA E 0
REMARK 465 MET E 1
REMARK 465 ASN E 173
REMARK 465 GLU E 174
REMARK 465 ILE E 205
REMARK 465 MET F -23
REMARK 465 HIS F -22
REMARK 465 HIS F -21
REMARK 465 HIS F -20
REMARK 465 HIS F -19
REMARK 465 HIS F -18
REMARK 465 HIS F -17
REMARK 465 SER F -16
REMARK 465 SER F -15
REMARK 465 GLY F -14
REMARK 465 VAL F -13
REMARK 465 ASP F -12
REMARK 465 LEU F -11
REMARK 465 GLY F -10
REMARK 465 THR F -9
REMARK 465 GLU F -8
REMARK 465 ASN F -7
REMARK 465 LEU F -6
REMARK 465 TYR F -5
REMARK 465 PHE F -4
REMARK 465 GLN F -3
REMARK 465 SER F -2
REMARK 465 ASN F -1
REMARK 465 ALA F 0
REMARK 465 MET F 1
REMARK 465 ASN F 173
REMARK 465 GLU F 174
REMARK 465 ILE F 205
REMARK 465 MET G -23
REMARK 465 HIS G -22
REMARK 465 HIS G -21
REMARK 465 HIS G -20
REMARK 465 HIS G -19
REMARK 465 HIS G -18
REMARK 465 HIS G -17
REMARK 465 SER G -16
REMARK 465 SER G -15
REMARK 465 GLY G -14
REMARK 465 VAL G -13
REMARK 465 ASP G -12
REMARK 465 LEU G -11
REMARK 465 GLY G -10
REMARK 465 THR G -9
REMARK 465 GLU G -8
REMARK 465 ASN G -7
REMARK 465 LEU G -6
REMARK 465 TYR G -5
REMARK 465 PHE G -4
REMARK 465 GLN G -3
REMARK 465 SER G -2
REMARK 465 ASN G -1
REMARK 465 ALA G 0
REMARK 465 MET G 1
REMARK 465 GLY G 85
REMARK 465 LYS G 144
REMARK 465 ASN G 145
REMARK 465 SER G 146
REMARK 465 ARG G 147
REMARK 465 ASP G 148
REMARK 465 GLN G 149
REMARK 465 ASN G 150
REMARK 465 ARG G 151
REMARK 465 ASN G 173
REMARK 465 GLU G 174
REMARK 465 SER G 175
REMARK 465 LYS G 204
REMARK 465 ILE G 205
REMARK 465 MET H -23
REMARK 465 HIS H -22
REMARK 465 HIS H -21
REMARK 465 HIS H -20
REMARK 465 HIS H -19
REMARK 465 HIS H -18
REMARK 465 HIS H -17
REMARK 465 SER H -16
REMARK 465 SER H -15
REMARK 465 GLY H -14
REMARK 465 VAL H -13
REMARK 465 ASP H -12
REMARK 465 LEU H -11
REMARK 465 GLY H -10
REMARK 465 THR H -9
REMARK 465 GLU H -8
REMARK 465 ASN H -7
REMARK 465 LEU H -6
REMARK 465 TYR H -5
REMARK 465 PHE H -4
REMARK 465 GLN H -3
REMARK 465 SER H -2
REMARK 465 ASN H -1
REMARK 465 ALA H 0
REMARK 465 ASN H 145
REMARK 465 SER H 146
REMARK 465 ARG H 147
REMARK 465 ASP H 148
REMARK 465 GLN H 149
REMARK 465 ASN H 150
REMARK 465 ARG H 151
REMARK 465 ASN H 173
REMARK 465 GLU H 174
REMARK 465 SER H 175
REMARK 465 GLN H 176
REMARK 465 LYS H 204
REMARK 465 ILE H 205
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 46 CD OE1 OE2
REMARK 470 ASP A 56 CG OD1 OD2
REMARK 470 ARG B 147 CD NE CZ NH1 NH2
REMARK 470 GLN B 154 CG CD OE1 NE2
REMARK 470 GLN C 154 CG CD OE1 NE2
REMARK 470 ILE C 171 CG2 CD1
REMARK 470 HIS C 172 CG ND1 CD2 CE1 NE2
REMARK 470 ASN C 173 OD1 ND2
REMARK 470 GLU C 174 CD OE1 OE2
REMARK 470 GLU D 46 CD OE1 OE2
REMARK 470 ASP D 56 CG OD1 OD2
REMARK 470 ARG E 147 CZ NH1 NH2
REMARK 470 ARG F 147 CZ NH1 NH2
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 ILE C 171 CB - CA - C ANGL. DEV. = -21.2 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 LYS A 77 -52.23 -130.96
REMARK 500 ARG A 92 148.96 81.72
REMARK 500 TYR A 93 -149.17 -166.51
REMARK 500 TYR A 103 -67.13 -96.98
REMARK 500 ASP B 56 13.95 57.16
REMARK 500 LYS B 77 -59.92 -126.01
REMARK 500 ARG B 92 144.35 80.16
REMARK 500 TYR B 93 -149.58 -161.88
REMARK 500 TYR B 103 -68.14 -94.07
REMARK 500 ASN B 121 54.25 36.14
REMARK 500 HIS B 172 53.52 -69.78
REMARK 500 LYS C 77 -54.96 -124.92
REMARK 500 ARG C 92 142.68 80.98
REMARK 500 TYR C 93 -141.25 -158.96
REMARK 500 TYR C 103 -68.04 -91.65
REMARK 500 ASN C 121 53.68 36.85
REMARK 500 HIS C 172 29.50 -79.13
REMARK 500 ASP D 56 24.75 49.27
REMARK 500 LYS D 77 -50.02 -128.20
REMARK 500 ARG D 92 147.17 81.70
REMARK 500 TYR D 93 -145.86 -166.23
REMARK 500 TYR D 100 -71.36 -74.87
REMARK 500 TYR D 103 -60.42 -96.26
REMARK 500 ASP E 56 19.39 55.88
REMARK 500 LYS E 77 -61.34 -131.53
REMARK 500 ARG E 92 149.14 83.72
REMARK 500 TYR E 93 -148.51 -166.40
REMARK 500 TYR E 103 -63.35 -93.69
REMARK 500 ASN E 121 54.65 35.22
REMARK 500 LYS F 77 -60.83 -125.82
REMARK 500 ARG F 92 147.53 82.23
REMARK 500 TYR F 93 -149.46 -165.58
REMARK 500 LYS G 77 -60.95 -133.49
REMARK 500 ARG G 92 147.32 80.65
REMARK 500 TYR G 93 -143.89 -163.11
REMARK 500 TYR G 103 -64.59 -92.13
REMARK 500 LYS H 77 -55.74 -128.35
REMARK 500 ARG H 92 147.48 82.18
REMARK 500 TYR H 93 -148.15 -165.55
REMARK 500 TYR H 103 -61.74 -94.28
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 TMP B 301
REMARK 610 TMP C 301
REMARK 610 TMP D 301
REMARK 610 TMP F 301
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TMP A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TMP B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TMP C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TMP D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TMP F 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TMP G 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TMP H 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2CCG RELATED DB: PDB
REMARK 900 RELATED ID: MCSG-APC105704 RELATED DB: TARGETTRACK
DBREF 4DWJ A 1 205 UNP P65248 KTHY_STAAM 1 205
DBREF 4DWJ B 1 205 UNP P65248 KTHY_STAAM 1 205
DBREF 4DWJ C 1 205 UNP P65248 KTHY_STAAM 1 205
DBREF 4DWJ D 1 205 UNP P65248 KTHY_STAAM 1 205
DBREF 4DWJ E 1 205 UNP P65248 KTHY_STAAM 1 205
DBREF 4DWJ F 1 205 UNP P65248 KTHY_STAAM 1 205
DBREF 4DWJ G 1 205 UNP P65248 KTHY_STAAM 1 205
DBREF 4DWJ H 1 205 UNP P65248 KTHY_STAAM 1 205
SEQADV 4DWJ MET A -23 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS A -22 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS A -21 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS A -20 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS A -19 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS A -18 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS A -17 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ SER A -16 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ SER A -15 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ GLY A -14 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ VAL A -13 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ ASP A -12 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ LEU A -11 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ GLY A -10 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ THR A -9 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ GLU A -8 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ ASN A -7 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ LEU A -6 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ TYR A -5 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ PHE A -4 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ GLN A -3 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ SER A -2 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ ASN A -1 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ ALA A 0 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ MET B -23 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS B -22 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS B -21 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS B -20 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS B -19 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS B -18 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS B -17 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ SER B -16 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ SER B -15 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ GLY B -14 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ VAL B -13 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ ASP B -12 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ LEU B -11 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ GLY B -10 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ THR B -9 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ GLU B -8 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ ASN B -7 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ LEU B -6 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ TYR B -5 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ PHE B -4 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ GLN B -3 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ SER B -2 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ ASN B -1 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ ALA B 0 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ MET C -23 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS C -22 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS C -21 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS C -20 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS C -19 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS C -18 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS C -17 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ SER C -16 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ SER C -15 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ GLY C -14 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ VAL C -13 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ ASP C -12 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ LEU C -11 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ GLY C -10 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ THR C -9 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ GLU C -8 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ ASN C -7 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ LEU C -6 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ TYR C -5 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ PHE C -4 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ GLN C -3 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ SER C -2 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ ASN C -1 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ ALA C 0 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ MET D -23 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS D -22 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS D -21 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS D -20 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS D -19 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS D -18 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS D -17 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ SER D -16 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ SER D -15 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ GLY D -14 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ VAL D -13 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ ASP D -12 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ LEU D -11 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ GLY D -10 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ THR D -9 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ GLU D -8 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ ASN D -7 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ LEU D -6 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ TYR D -5 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ PHE D -4 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ GLN D -3 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ SER D -2 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ ASN D -1 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ ALA D 0 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ MET E -23 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS E -22 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS E -21 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS E -20 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS E -19 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS E -18 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS E -17 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ SER E -16 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ SER E -15 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ GLY E -14 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ VAL E -13 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ ASP E -12 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ LEU E -11 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ GLY E -10 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ THR E -9 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ GLU E -8 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ ASN E -7 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ LEU E -6 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ TYR E -5 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ PHE E -4 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ GLN E -3 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ SER E -2 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ ASN E -1 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ ALA E 0 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ MET F -23 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS F -22 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS F -21 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS F -20 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS F -19 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS F -18 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS F -17 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ SER F -16 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ SER F -15 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ GLY F -14 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ VAL F -13 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ ASP F -12 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ LEU F -11 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ GLY F -10 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ THR F -9 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ GLU F -8 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ ASN F -7 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ LEU F -6 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ TYR F -5 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ PHE F -4 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ GLN F -3 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ SER F -2 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ ASN F -1 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ ALA F 0 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ MET G -23 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS G -22 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS G -21 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS G -20 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS G -19 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS G -18 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS G -17 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ SER G -16 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ SER G -15 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ GLY G -14 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ VAL G -13 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ ASP G -12 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ LEU G -11 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ GLY G -10 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ THR G -9 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ GLU G -8 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ ASN G -7 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ LEU G -6 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ TYR G -5 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ PHE G -4 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ GLN G -3 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ SER G -2 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ ASN G -1 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ ALA G 0 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ MET H -23 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS H -22 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS H -21 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS H -20 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS H -19 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS H -18 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ HIS H -17 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ SER H -16 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ SER H -15 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ GLY H -14 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ VAL H -13 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ ASP H -12 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ LEU H -11 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ GLY H -10 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ THR H -9 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ GLU H -8 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ ASN H -7 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ LEU H -6 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ TYR H -5 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ PHE H -4 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ GLN H -3 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ SER H -2 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ ASN H -1 UNP P65248 EXPRESSION TAG
SEQADV 4DWJ ALA H 0 UNP P65248 EXPRESSION TAG
SEQRES 1 A 229 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 229 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA MET SER
SEQRES 3 A 229 ALA PHE ILE THR PHE GLU GLY PRO GLU GLY SER GLY LYS
SEQRES 4 A 229 THR THR VAL ILE ASN GLU VAL TYR HIS ARG LEU VAL LYS
SEQRES 5 A 229 ASP TYR ASP VAL ILE MET THR ARG GLU PRO GLY GLY VAL
SEQRES 6 A 229 PRO THR GLY GLU GLU ILE ARG LYS ILE VAL LEU GLU GLY
SEQRES 7 A 229 ASN ASP MET ASP ILE ARG THR GLU ALA MET LEU PHE ALA
SEQRES 8 A 229 ALA SER ARG ARG GLU HIS LEU VAL LEU LYS VAL ILE PRO
SEQRES 9 A 229 ALA LEU LYS GLU GLY LYS VAL VAL LEU CYS ASP ARG TYR
SEQRES 10 A 229 ILE ASP SER SER LEU ALA TYR GLN GLY TYR ALA ARG GLY
SEQRES 11 A 229 ILE GLY VAL GLU GLU VAL ARG ALA LEU ASN GLU PHE ALA
SEQRES 12 A 229 ILE ASN GLY LEU TYR PRO ASP LEU THR ILE TYR LEU ASN
SEQRES 13 A 229 VAL SER ALA GLU VAL GLY ARG GLU ARG ILE ILE LYS ASN
SEQRES 14 A 229 SER ARG ASP GLN ASN ARG LEU ASP GLN GLU ASP LEU LYS
SEQRES 15 A 229 PHE HIS GLU LYS VAL ILE GLU GLY TYR GLN GLU ILE ILE
SEQRES 16 A 229 HIS ASN GLU SER GLN ARG PHE LYS SER VAL ASN ALA ASP
SEQRES 17 A 229 GLN PRO LEU GLU ASN VAL VAL GLU ASP THR TYR GLN THR
SEQRES 18 A 229 ILE ILE LYS TYR LEU GLU LYS ILE
SEQRES 1 B 229 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 B 229 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA MET SER
SEQRES 3 B 229 ALA PHE ILE THR PHE GLU GLY PRO GLU GLY SER GLY LYS
SEQRES 4 B 229 THR THR VAL ILE ASN GLU VAL TYR HIS ARG LEU VAL LYS
SEQRES 5 B 229 ASP TYR ASP VAL ILE MET THR ARG GLU PRO GLY GLY VAL
SEQRES 6 B 229 PRO THR GLY GLU GLU ILE ARG LYS ILE VAL LEU GLU GLY
SEQRES 7 B 229 ASN ASP MET ASP ILE ARG THR GLU ALA MET LEU PHE ALA
SEQRES 8 B 229 ALA SER ARG ARG GLU HIS LEU VAL LEU LYS VAL ILE PRO
SEQRES 9 B 229 ALA LEU LYS GLU GLY LYS VAL VAL LEU CYS ASP ARG TYR
SEQRES 10 B 229 ILE ASP SER SER LEU ALA TYR GLN GLY TYR ALA ARG GLY
SEQRES 11 B 229 ILE GLY VAL GLU GLU VAL ARG ALA LEU ASN GLU PHE ALA
SEQRES 12 B 229 ILE ASN GLY LEU TYR PRO ASP LEU THR ILE TYR LEU ASN
SEQRES 13 B 229 VAL SER ALA GLU VAL GLY ARG GLU ARG ILE ILE LYS ASN
SEQRES 14 B 229 SER ARG ASP GLN ASN ARG LEU ASP GLN GLU ASP LEU LYS
SEQRES 15 B 229 PHE HIS GLU LYS VAL ILE GLU GLY TYR GLN GLU ILE ILE
SEQRES 16 B 229 HIS ASN GLU SER GLN ARG PHE LYS SER VAL ASN ALA ASP
SEQRES 17 B 229 GLN PRO LEU GLU ASN VAL VAL GLU ASP THR TYR GLN THR
SEQRES 18 B 229 ILE ILE LYS TYR LEU GLU LYS ILE
SEQRES 1 C 229 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 C 229 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA MET SER
SEQRES 3 C 229 ALA PHE ILE THR PHE GLU GLY PRO GLU GLY SER GLY LYS
SEQRES 4 C 229 THR THR VAL ILE ASN GLU VAL TYR HIS ARG LEU VAL LYS
SEQRES 5 C 229 ASP TYR ASP VAL ILE MET THR ARG GLU PRO GLY GLY VAL
SEQRES 6 C 229 PRO THR GLY GLU GLU ILE ARG LYS ILE VAL LEU GLU GLY
SEQRES 7 C 229 ASN ASP MET ASP ILE ARG THR GLU ALA MET LEU PHE ALA
SEQRES 8 C 229 ALA SER ARG ARG GLU HIS LEU VAL LEU LYS VAL ILE PRO
SEQRES 9 C 229 ALA LEU LYS GLU GLY LYS VAL VAL LEU CYS ASP ARG TYR
SEQRES 10 C 229 ILE ASP SER SER LEU ALA TYR GLN GLY TYR ALA ARG GLY
SEQRES 11 C 229 ILE GLY VAL GLU GLU VAL ARG ALA LEU ASN GLU PHE ALA
SEQRES 12 C 229 ILE ASN GLY LEU TYR PRO ASP LEU THR ILE TYR LEU ASN
SEQRES 13 C 229 VAL SER ALA GLU VAL GLY ARG GLU ARG ILE ILE LYS ASN
SEQRES 14 C 229 SER ARG ASP GLN ASN ARG LEU ASP GLN GLU ASP LEU LYS
SEQRES 15 C 229 PHE HIS GLU LYS VAL ILE GLU GLY TYR GLN GLU ILE ILE
SEQRES 16 C 229 HIS ASN GLU SER GLN ARG PHE LYS SER VAL ASN ALA ASP
SEQRES 17 C 229 GLN PRO LEU GLU ASN VAL VAL GLU ASP THR TYR GLN THR
SEQRES 18 C 229 ILE ILE LYS TYR LEU GLU LYS ILE
SEQRES 1 D 229 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 D 229 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA MET SER
SEQRES 3 D 229 ALA PHE ILE THR PHE GLU GLY PRO GLU GLY SER GLY LYS
SEQRES 4 D 229 THR THR VAL ILE ASN GLU VAL TYR HIS ARG LEU VAL LYS
SEQRES 5 D 229 ASP TYR ASP VAL ILE MET THR ARG GLU PRO GLY GLY VAL
SEQRES 6 D 229 PRO THR GLY GLU GLU ILE ARG LYS ILE VAL LEU GLU GLY
SEQRES 7 D 229 ASN ASP MET ASP ILE ARG THR GLU ALA MET LEU PHE ALA
SEQRES 8 D 229 ALA SER ARG ARG GLU HIS LEU VAL LEU LYS VAL ILE PRO
SEQRES 9 D 229 ALA LEU LYS GLU GLY LYS VAL VAL LEU CYS ASP ARG TYR
SEQRES 10 D 229 ILE ASP SER SER LEU ALA TYR GLN GLY TYR ALA ARG GLY
SEQRES 11 D 229 ILE GLY VAL GLU GLU VAL ARG ALA LEU ASN GLU PHE ALA
SEQRES 12 D 229 ILE ASN GLY LEU TYR PRO ASP LEU THR ILE TYR LEU ASN
SEQRES 13 D 229 VAL SER ALA GLU VAL GLY ARG GLU ARG ILE ILE LYS ASN
SEQRES 14 D 229 SER ARG ASP GLN ASN ARG LEU ASP GLN GLU ASP LEU LYS
SEQRES 15 D 229 PHE HIS GLU LYS VAL ILE GLU GLY TYR GLN GLU ILE ILE
SEQRES 16 D 229 HIS ASN GLU SER GLN ARG PHE LYS SER VAL ASN ALA ASP
SEQRES 17 D 229 GLN PRO LEU GLU ASN VAL VAL GLU ASP THR TYR GLN THR
SEQRES 18 D 229 ILE ILE LYS TYR LEU GLU LYS ILE
SEQRES 1 E 229 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 E 229 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA MET SER
SEQRES 3 E 229 ALA PHE ILE THR PHE GLU GLY PRO GLU GLY SER GLY LYS
SEQRES 4 E 229 THR THR VAL ILE ASN GLU VAL TYR HIS ARG LEU VAL LYS
SEQRES 5 E 229 ASP TYR ASP VAL ILE MET THR ARG GLU PRO GLY GLY VAL
SEQRES 6 E 229 PRO THR GLY GLU GLU ILE ARG LYS ILE VAL LEU GLU GLY
SEQRES 7 E 229 ASN ASP MET ASP ILE ARG THR GLU ALA MET LEU PHE ALA
SEQRES 8 E 229 ALA SER ARG ARG GLU HIS LEU VAL LEU LYS VAL ILE PRO
SEQRES 9 E 229 ALA LEU LYS GLU GLY LYS VAL VAL LEU CYS ASP ARG TYR
SEQRES 10 E 229 ILE ASP SER SER LEU ALA TYR GLN GLY TYR ALA ARG GLY
SEQRES 11 E 229 ILE GLY VAL GLU GLU VAL ARG ALA LEU ASN GLU PHE ALA
SEQRES 12 E 229 ILE ASN GLY LEU TYR PRO ASP LEU THR ILE TYR LEU ASN
SEQRES 13 E 229 VAL SER ALA GLU VAL GLY ARG GLU ARG ILE ILE LYS ASN
SEQRES 14 E 229 SER ARG ASP GLN ASN ARG LEU ASP GLN GLU ASP LEU LYS
SEQRES 15 E 229 PHE HIS GLU LYS VAL ILE GLU GLY TYR GLN GLU ILE ILE
SEQRES 16 E 229 HIS ASN GLU SER GLN ARG PHE LYS SER VAL ASN ALA ASP
SEQRES 17 E 229 GLN PRO LEU GLU ASN VAL VAL GLU ASP THR TYR GLN THR
SEQRES 18 E 229 ILE ILE LYS TYR LEU GLU LYS ILE
SEQRES 1 F 229 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 F 229 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA MET SER
SEQRES 3 F 229 ALA PHE ILE THR PHE GLU GLY PRO GLU GLY SER GLY LYS
SEQRES 4 F 229 THR THR VAL ILE ASN GLU VAL TYR HIS ARG LEU VAL LYS
SEQRES 5 F 229 ASP TYR ASP VAL ILE MET THR ARG GLU PRO GLY GLY VAL
SEQRES 6 F 229 PRO THR GLY GLU GLU ILE ARG LYS ILE VAL LEU GLU GLY
SEQRES 7 F 229 ASN ASP MET ASP ILE ARG THR GLU ALA MET LEU PHE ALA
SEQRES 8 F 229 ALA SER ARG ARG GLU HIS LEU VAL LEU LYS VAL ILE PRO
SEQRES 9 F 229 ALA LEU LYS GLU GLY LYS VAL VAL LEU CYS ASP ARG TYR
SEQRES 10 F 229 ILE ASP SER SER LEU ALA TYR GLN GLY TYR ALA ARG GLY
SEQRES 11 F 229 ILE GLY VAL GLU GLU VAL ARG ALA LEU ASN GLU PHE ALA
SEQRES 12 F 229 ILE ASN GLY LEU TYR PRO ASP LEU THR ILE TYR LEU ASN
SEQRES 13 F 229 VAL SER ALA GLU VAL GLY ARG GLU ARG ILE ILE LYS ASN
SEQRES 14 F 229 SER ARG ASP GLN ASN ARG LEU ASP GLN GLU ASP LEU LYS
SEQRES 15 F 229 PHE HIS GLU LYS VAL ILE GLU GLY TYR GLN GLU ILE ILE
SEQRES 16 F 229 HIS ASN GLU SER GLN ARG PHE LYS SER VAL ASN ALA ASP
SEQRES 17 F 229 GLN PRO LEU GLU ASN VAL VAL GLU ASP THR TYR GLN THR
SEQRES 18 F 229 ILE ILE LYS TYR LEU GLU LYS ILE
SEQRES 1 G 229 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 G 229 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA MET SER
SEQRES 3 G 229 ALA PHE ILE THR PHE GLU GLY PRO GLU GLY SER GLY LYS
SEQRES 4 G 229 THR THR VAL ILE ASN GLU VAL TYR HIS ARG LEU VAL LYS
SEQRES 5 G 229 ASP TYR ASP VAL ILE MET THR ARG GLU PRO GLY GLY VAL
SEQRES 6 G 229 PRO THR GLY GLU GLU ILE ARG LYS ILE VAL LEU GLU GLY
SEQRES 7 G 229 ASN ASP MET ASP ILE ARG THR GLU ALA MET LEU PHE ALA
SEQRES 8 G 229 ALA SER ARG ARG GLU HIS LEU VAL LEU LYS VAL ILE PRO
SEQRES 9 G 229 ALA LEU LYS GLU GLY LYS VAL VAL LEU CYS ASP ARG TYR
SEQRES 10 G 229 ILE ASP SER SER LEU ALA TYR GLN GLY TYR ALA ARG GLY
SEQRES 11 G 229 ILE GLY VAL GLU GLU VAL ARG ALA LEU ASN GLU PHE ALA
SEQRES 12 G 229 ILE ASN GLY LEU TYR PRO ASP LEU THR ILE TYR LEU ASN
SEQRES 13 G 229 VAL SER ALA GLU VAL GLY ARG GLU ARG ILE ILE LYS ASN
SEQRES 14 G 229 SER ARG ASP GLN ASN ARG LEU ASP GLN GLU ASP LEU LYS
SEQRES 15 G 229 PHE HIS GLU LYS VAL ILE GLU GLY TYR GLN GLU ILE ILE
SEQRES 16 G 229 HIS ASN GLU SER GLN ARG PHE LYS SER VAL ASN ALA ASP
SEQRES 17 G 229 GLN PRO LEU GLU ASN VAL VAL GLU ASP THR TYR GLN THR
SEQRES 18 G 229 ILE ILE LYS TYR LEU GLU LYS ILE
SEQRES 1 H 229 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 H 229 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA MET SER
SEQRES 3 H 229 ALA PHE ILE THR PHE GLU GLY PRO GLU GLY SER GLY LYS
SEQRES 4 H 229 THR THR VAL ILE ASN GLU VAL TYR HIS ARG LEU VAL LYS
SEQRES 5 H 229 ASP TYR ASP VAL ILE MET THR ARG GLU PRO GLY GLY VAL
SEQRES 6 H 229 PRO THR GLY GLU GLU ILE ARG LYS ILE VAL LEU GLU GLY
SEQRES 7 H 229 ASN ASP MET ASP ILE ARG THR GLU ALA MET LEU PHE ALA
SEQRES 8 H 229 ALA SER ARG ARG GLU HIS LEU VAL LEU LYS VAL ILE PRO
SEQRES 9 H 229 ALA LEU LYS GLU GLY LYS VAL VAL LEU CYS ASP ARG TYR
SEQRES 10 H 229 ILE ASP SER SER LEU ALA TYR GLN GLY TYR ALA ARG GLY
SEQRES 11 H 229 ILE GLY VAL GLU GLU VAL ARG ALA LEU ASN GLU PHE ALA
SEQRES 12 H 229 ILE ASN GLY LEU TYR PRO ASP LEU THR ILE TYR LEU ASN
SEQRES 13 H 229 VAL SER ALA GLU VAL GLY ARG GLU ARG ILE ILE LYS ASN
SEQRES 14 H 229 SER ARG ASP GLN ASN ARG LEU ASP GLN GLU ASP LEU LYS
SEQRES 15 H 229 PHE HIS GLU LYS VAL ILE GLU GLY TYR GLN GLU ILE ILE
SEQRES 16 H 229 HIS ASN GLU SER GLN ARG PHE LYS SER VAL ASN ALA ASP
SEQRES 17 H 229 GLN PRO LEU GLU ASN VAL VAL GLU ASP THR TYR GLN THR
SEQRES 18 H 229 ILE ILE LYS TYR LEU GLU LYS ILE
HET TMP A 301 21
HET TMP B 301 14
HET TMP C 301 14
HET TMP D 301 20
HET TMP F 301 9
HET TMP G 301 21
HET TMP H 301 21
HETNAM TMP THYMIDINE-5'-PHOSPHATE
FORMUL 9 TMP 7(C10 H15 N2 O8 P)
FORMUL 16 HOH *75(H2 O)
HELIX 1 1 GLY A 14 LYS A 28 1 15
HELIX 2 2 VAL A 41 GLU A 53 1 13
HELIX 3 3 ASP A 58 LYS A 77 1 20
HELIX 4 4 LYS A 77 GLU A 84 1 8
HELIX 5 5 TYR A 93 GLN A 101 1 9
HELIX 6 6 GLY A 108 ASN A 121 1 14
HELIX 7 7 SER A 134 ASN A 145 1 12
HELIX 8 8 ASP A 153 HIS A 172 1 20
HELIX 9 9 PRO A 186 LYS A 204 1 19
HELIX 10 10 GLY B 14 TYR B 30 1 17
HELIX 11 11 VAL B 41 GLU B 53 1 13
HELIX 12 12 ASP B 58 LYS B 77 1 20
HELIX 13 13 LYS B 77 GLU B 84 1 8
HELIX 14 14 TYR B 93 GLN B 101 1 9
HELIX 15 15 GLY B 108 ASN B 121 1 14
HELIX 16 16 SER B 134 ASN B 145 1 12
HELIX 17 17 ASP B 153 HIS B 172 1 20
HELIX 18 18 PRO B 186 LYS B 204 1 19
HELIX 19 19 GLY C 14 TYR C 30 1 17
HELIX 20 20 VAL C 41 GLU C 53 1 13
HELIX 21 21 ASP C 58 LYS C 77 1 20
HELIX 22 22 LYS C 77 LYS C 83 1 7
HELIX 23 23 TYR C 93 GLN C 101 1 9
HELIX 24 24 GLY C 108 ASN C 121 1 14
HELIX 25 25 SER C 134 ASN C 145 1 12
HELIX 26 26 ASP C 153 HIS C 172 1 20
HELIX 27 27 PRO C 186 LYS C 204 1 19
HELIX 28 28 GLY D 14 LYS D 28 1 15
HELIX 29 29 VAL D 41 GLU D 53 1 13
HELIX 30 30 ASP D 58 LYS D 77 1 20
HELIX 31 31 LYS D 77 GLU D 84 1 8
HELIX 32 32 TYR D 93 GLN D 101 1 9
HELIX 33 33 GLY D 108 ASN D 121 1 14
HELIX 34 34 SER D 134 ASN D 145 1 12
HELIX 35 35 ASP D 153 HIS D 172 1 20
HELIX 36 36 PRO D 186 LYS D 204 1 19
HELIX 37 37 GLY E 14 LYS E 28 1 15
HELIX 38 38 VAL E 41 GLU E 53 1 13
HELIX 39 39 ASP E 58 LYS E 77 1 20
HELIX 40 40 LYS E 77 GLU E 84 1 8
HELIX 41 41 TYR E 93 GLN E 101 1 9
HELIX 42 42 GLY E 108 ASN E 121 1 14
HELIX 43 43 SER E 134 SER E 146 1 13
HELIX 44 44 ASP E 153 HIS E 172 1 20
HELIX 45 45 PRO E 186 LYS E 204 1 19
HELIX 46 46 GLY F 14 LYS F 28 1 15
HELIX 47 47 VAL F 41 GLU F 53 1 13
HELIX 48 48 ASP F 58 LYS F 77 1 20
HELIX 49 49 LYS F 77 GLU F 84 1 8
HELIX 50 50 TYR F 93 GLN F 101 1 9
HELIX 51 51 GLY F 108 ASN F 121 1 14
HELIX 52 52 SER F 134 ASN F 145 1 12
HELIX 53 53 ASP F 153 HIS F 172 1 20
HELIX 54 54 PRO F 186 LYS F 204 1 19
HELIX 55 55 GLY G 14 LYS G 28 1 15
HELIX 56 56 VAL G 41 GLU G 53 1 13
HELIX 57 57 ASP G 58 LYS G 77 1 20
HELIX 58 58 LYS G 77 GLU G 84 1 8
HELIX 59 59 TYR G 93 GLN G 101 1 9
HELIX 60 60 GLY G 108 ASN G 121 1 14
HELIX 61 61 SER G 134 ILE G 143 1 10
HELIX 62 62 ASP G 153 HIS G 172 1 20
HELIX 63 63 PRO G 186 GLU G 203 1 18
HELIX 64 64 GLY H 14 LYS H 28 1 15
HELIX 65 65 VAL H 41 GLU H 53 1 13
HELIX 66 66 ASP H 58 LYS H 77 1 20
HELIX 67 67 LYS H 77 GLU H 84 1 8
HELIX 68 68 TYR H 93 GLN H 101 1 9
HELIX 69 69 GLY H 108 ASN H 121 1 14
HELIX 70 70 SER H 134 LYS H 144 1 11
HELIX 71 71 ASP H 153 HIS H 172 1 20
HELIX 72 72 PRO H 186 GLU H 203 1 18
SHEET 1 A 5 VAL A 32 ARG A 36 0
SHEET 2 A 5 VAL A 87 ASP A 91 1 O LEU A 89 N ILE A 33
SHEET 3 A 5 ALA A 3 GLU A 8 1 N ILE A 5 O CYS A 90
SHEET 4 A 5 LEU A 127 ASN A 132 1 O ILE A 129 N GLU A 8
SHEET 5 A 5 PHE A 178 ASN A 182 1 O LYS A 179 N TYR A 130
SHEET 1 B 5 VAL B 32 ARG B 36 0
SHEET 2 B 5 VAL B 87 ASP B 91 1 O LEU B 89 N ILE B 33
SHEET 3 B 5 ALA B 3 GLU B 8 1 N ALA B 3 O VAL B 88
SHEET 4 B 5 LEU B 127 ASN B 132 1 O ILE B 129 N GLU B 8
SHEET 5 B 5 PHE B 178 ASN B 182 1 O VAL B 181 N ASN B 132
SHEET 1 C 5 VAL C 32 ARG C 36 0
SHEET 2 C 5 VAL C 87 ASP C 91 1 O LEU C 89 N ILE C 33
SHEET 3 C 5 ALA C 3 GLU C 8 1 N ILE C 5 O CYS C 90
SHEET 4 C 5 LEU C 127 ASN C 132 1 O ILE C 129 N THR C 6
SHEET 5 C 5 PHE C 178 ASN C 182 1 O VAL C 181 N ASN C 132
SHEET 1 D 5 VAL D 32 ARG D 36 0
SHEET 2 D 5 VAL D 87 ASP D 91 1 O LEU D 89 N ILE D 33
SHEET 3 D 5 ALA D 3 GLU D 8 1 N ILE D 5 O VAL D 88
SHEET 4 D 5 LEU D 127 ASN D 132 1 O ILE D 129 N GLU D 8
SHEET 5 D 5 PHE D 178 ASN D 182 1 O LYS D 179 N TYR D 130
SHEET 1 E 5 VAL E 32 ARG E 36 0
SHEET 2 E 5 VAL E 87 ASP E 91 1 O LEU E 89 N ILE E 33
SHEET 3 E 5 ALA E 3 GLU E 8 1 N ALA E 3 O VAL E 88
SHEET 4 E 5 LEU E 127 ASN E 132 1 O ILE E 129 N GLU E 8
SHEET 5 E 5 PHE E 178 ASN E 182 1 O LYS E 179 N TYR E 130
SHEET 1 F 5 VAL F 32 THR F 35 0
SHEET 2 F 5 VAL F 87 ASP F 91 1 O LEU F 89 N ILE F 33
SHEET 3 F 5 ALA F 3 GLU F 8 1 N ILE F 5 O VAL F 88
SHEET 4 F 5 LEU F 127 ASN F 132 1 O LEU F 131 N GLU F 8
SHEET 5 F 5 PHE F 178 ASN F 182 1 O LYS F 179 N TYR F 130
SHEET 1 G 5 VAL G 32 ARG G 36 0
SHEET 2 G 5 VAL G 87 ASP G 91 1 O VAL G 87 N ILE G 33
SHEET 3 G 5 ALA G 3 GLU G 8 1 N ALA G 3 O VAL G 88
SHEET 4 G 5 LEU G 127 ASN G 132 1 O ILE G 129 N GLU G 8
SHEET 5 G 5 PHE G 178 ASN G 182 1 O VAL G 181 N TYR G 130
SHEET 1 H 5 VAL H 32 ARG H 36 0
SHEET 2 H 5 VAL H 87 ASP H 91 1 O LEU H 89 N ILE H 33
SHEET 3 H 5 ALA H 3 GLU H 8 1 N ILE H 5 O VAL H 88
SHEET 4 H 5 LEU H 127 ASN H 132 1 O ILE H 129 N GLU H 8
SHEET 5 H 5 PHE H 178 ASN H 182 1 O LYS H 179 N TYR H 130
CISPEP 1 GLU A 37 PRO A 38 0 0.15
CISPEP 2 GLU B 37 PRO B 38 0 1.49
CISPEP 3 GLU C 37 PRO C 38 0 -0.47
CISPEP 4 GLU D 37 PRO D 38 0 -0.25
CISPEP 5 GLU E 37 PRO E 38 0 1.42
CISPEP 6 GLU F 37 PRO F 38 0 2.35
CISPEP 7 GLU G 37 PRO G 38 0 -0.41
CISPEP 8 GLU H 37 PRO H 38 0 0.24
SITE 1 AC1 8 ARG A 36 ARG A 48 PHE A 66 ARG A 70
SITE 2 AC1 8 ARG A 92 SER A 97 TYR A 100 GLN A 101
SITE 1 AC2 10 LYS B 15 THR B 16 ARG B 36 PHE B 66
SITE 2 AC2 10 ARG B 70 ASP B 91 ARG B 92 SER B 96
SITE 3 AC2 10 SER B 97 GLN B 101
SITE 1 AC3 7 LYS C 15 THR C 16 PHE C 66 ARG C 70
SITE 2 AC3 7 ARG C 92 SER C 97 GLN C 101
SITE 1 AC4 9 LYS D 15 ARG D 36 PHE D 66 ARG D 70
SITE 2 AC4 9 ASP D 91 ARG D 92 SER D 97 TYR D 100
SITE 3 AC4 9 GLN D 101
SITE 1 AC5 5 GLU F 37 PHE F 66 ARG F 70 SER F 97
SITE 2 AC5 5 GLN F 101
SITE 1 AC6 8 LYS G 15 ARG G 36 PHE G 66 ARG G 70
SITE 2 AC6 8 ARG G 92 SER G 97 TYR G 100 GLN G 101
SITE 1 AC7 8 LYS H 15 ARG H 36 PHE H 66 ARG H 70
SITE 2 AC7 8 ARG H 92 SER H 97 TYR H 100 GLN H 101
CRYST1 58.662 73.409 96.868 81.48 90.10 90.12 P 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.017047 0.000035 0.000024 0.00000
SCALE2 0.000000 0.013622 -0.002041 0.00000
SCALE3 0.000000 0.000000 0.010439 0.00000
MTRIX1 1 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 1 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 1 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 2 0.999996 -0.002746 -0.000905 -0.08248 1
MTRIX2 2 -0.002753 -0.999966 -0.007742 -102.79011 1
MTRIX3 2 -0.000884 0.007744 -0.999970 -16.78860 1
(ATOM LINES ARE NOT SHOWN.)
END
