HEADER TRANSFERASE 10-JUN-15 5BYD
TITLE CRYSTAL STRUCTURE OF HUMAN RIBOKINASE IN P21 SPACEGROUP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBOKINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.7.1.15;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: RBKS, RBSK;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.PARK,J.CHAKRABARTI,B.SINGH,R.S.GUPTA,M.S.JUNOP
REVDAT 3 27-SEP-23 5BYD 1 LINK
REVDAT 2 26-APR-17 5BYD 1 AUTHOR JRNL
REVDAT 1 15-JUN-16 5BYD 0
JRNL AUTH J.PARK,J.CHAKRABARTI,B.SINGH,R.S.GUPTA,M.S.JUNOP
JRNL TITL CRYSTAL STRUCTURE OF HUMAN RIBOKINASE IN P21 SPACEGROUP
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.96
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 32999
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) : 0.174
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1762
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2326
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.25
REMARK 3 BIN R VALUE (WORKING SET) : 0.2570
REMARK 3 BIN FREE R VALUE SET COUNT : 121
REMARK 3 BIN FREE R VALUE : 0.3170
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4564
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 155
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.75
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.86000
REMARK 3 B22 (A**2) : 0.65000
REMARK 3 B33 (A**2) : 0.50000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.02000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.215
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.176
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.135
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.871
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4654 ; 0.017 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4448 ; 0.006 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6345 ; 1.735 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10212 ; 1.152 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 629 ; 5.763 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 169 ;38.077 ;25.680
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 731 ;13.226 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 11 ;19.493 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 783 ; 0.098 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5367 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 982 ; 0.005 ; 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): 2516 ; 1.636 ; 2.170
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2515 ; 1.634 ; 2.170
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3145 ; 2.358 ; 3.249
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3146 ; 2.358 ; 3.249
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2138 ; 2.275 ; 2.426
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2139 ; 2.274 ; 2.426
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3200 ; 3.462 ; 3.540
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 5049 ; 5.713 ;17.914
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 5015 ; 5.705 ;17.752
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 15 325 B 15 325 17406 0.09 0.05
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 15 A 39
REMARK 3 ORIGIN FOR THE GROUP (A): 5.2605 2.3684 -25.7648
REMARK 3 T TENSOR
REMARK 3 T11: 0.0810 T22: 0.0380
REMARK 3 T33: 0.1218 T12: 0.0411
REMARK 3 T13: 0.0358 T23: 0.0209
REMARK 3 L TENSOR
REMARK 3 L11: 2.3852 L22: 5.0025
REMARK 3 L33: 3.2593 L12: 2.7502
REMARK 3 L13: 2.5926 L23: 2.1418
REMARK 3 S TENSOR
REMARK 3 S11: -0.1490 S12: -0.0434 S13: 0.0758
REMARK 3 S21: -0.0087 S22: -0.0003 S23: -0.1837
REMARK 3 S31: -0.2800 S32: -0.0799 S33: 0.1493
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 40 A 68
REMARK 3 ORIGIN FOR THE GROUP (A): 1.2188 5.9829 -26.6119
REMARK 3 T TENSOR
REMARK 3 T11: 0.0809 T22: 0.0320
REMARK 3 T33: 0.0770 T12: 0.0256
REMARK 3 T13: -0.0287 T23: 0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 5.6525 L22: 2.1027
REMARK 3 L33: 4.3004 L12: 1.6335
REMARK 3 L13: 3.3594 L23: 2.1473
REMARK 3 S TENSOR
REMARK 3 S11: -0.2319 S12: -0.2636 S13: 0.4248
REMARK 3 S21: -0.0782 S22: -0.0932 S23: 0.0517
REMARK 3 S31: -0.4468 S32: -0.1861 S33: 0.3250
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 : A 69 A 97
REMARK 3 ORIGIN FOR THE GROUP (A): -6.1106 -4.0883 -20.1730
REMARK 3 T TENSOR
REMARK 3 T11: 0.0465 T22: 0.1283
REMARK 3 T33: 0.0616 T12: 0.0369
REMARK 3 T13: 0.0493 T23: 0.0332
REMARK 3 L TENSOR
REMARK 3 L11: 4.6334 L22: 4.4329
REMARK 3 L33: 4.5753 L12: 0.8092
REMARK 3 L13: 1.5829 L23: 0.4567
REMARK 3 S TENSOR
REMARK 3 S11: -0.0446 S12: -0.3762 S13: -0.0449
REMARK 3 S21: 0.1623 S22: 0.0461 S23: 0.1934
REMARK 3 S31: -0.1102 S32: -0.4955 S33: -0.0015
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 : A 98 A 140
REMARK 3 ORIGIN FOR THE GROUP (A): 6.6467 -3.8836 -22.1257
REMARK 3 T TENSOR
REMARK 3 T11: 0.0544 T22: 0.0412
REMARK 3 T33: 0.0462 T12: 0.0327
REMARK 3 T13: 0.0013 T23: 0.0182
REMARK 3 L TENSOR
REMARK 3 L11: 4.5130 L22: 5.8168
REMARK 3 L33: 2.3287 L12: 2.8690
REMARK 3 L13: 0.3247 L23: 0.3776
REMARK 3 S TENSOR
REMARK 3 S11: -0.1353 S12: -0.0511 S13: -0.0268
REMARK 3 S21: -0.1393 S22: 0.0909 S23: -0.1829
REMARK 3 S31: -0.0822 S32: 0.0060 S33: 0.0445
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 : A 141 A 161
REMARK 3 ORIGIN FOR THE GROUP (A): -2.3058 -14.6825 -31.3231
REMARK 3 T TENSOR
REMARK 3 T11: 0.1230 T22: 0.0181
REMARK 3 T33: 0.1970 T12: -0.0363
REMARK 3 T13: -0.0167 T23: 0.0252
REMARK 3 L TENSOR
REMARK 3 L11: 0.4964 L22: 2.3087
REMARK 3 L33: 5.1004 L12: -1.0291
REMARK 3 L13: 0.3048 L23: -1.0982
REMARK 3 S TENSOR
REMARK 3 S11: 0.0055 S12: -0.0481 S13: -0.1311
REMARK 3 S21: -0.0259 S22: 0.1075 S23: 0.1306
REMARK 3 S31: 0.4318 S32: -0.2474 S33: -0.1130
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 : A 162 A 192
REMARK 3 ORIGIN FOR THE GROUP (A): 2.7841 -17.1406 -37.0481
REMARK 3 T TENSOR
REMARK 3 T11: 0.2358 T22: 0.0536
REMARK 3 T33: 0.1315 T12: 0.0272
REMARK 3 T13: -0.0429 T23: -0.0125
REMARK 3 L TENSOR
REMARK 3 L11: 6.0745 L22: 4.8975
REMARK 3 L33: 2.8482 L12: 0.8984
REMARK 3 L13: -1.0468 L23: -0.7708
REMARK 3 S TENSOR
REMARK 3 S11: 0.0227 S12: 0.1221 S13: -0.5266
REMARK 3 S21: 0.1565 S22: -0.0050 S23: -0.2287
REMARK 3 S31: 0.6823 S32: 0.2080 S33: -0.0178
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 : A 193 A 257
REMARK 3 ORIGIN FOR THE GROUP (A): 6.1577 -7.4871 -49.7911
REMARK 3 T TENSOR
REMARK 3 T11: 0.1189 T22: 0.1651
REMARK 3 T33: 0.1265 T12: 0.0076
REMARK 3 T13: 0.0299 T23: -0.0380
REMARK 3 L TENSOR
REMARK 3 L11: 4.6153 L22: 3.6183
REMARK 3 L33: 4.5626 L12: -1.1072
REMARK 3 L13: 1.0188 L23: -1.1638
REMARK 3 S TENSOR
REMARK 3 S11: 0.0918 S12: 0.5958 S13: 0.0111
REMARK 3 S21: -0.3609 S22: -0.1624 S23: -0.1503
REMARK 3 S31: 0.1901 S32: 0.3267 S33: 0.0706
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 : A 258 A 329
REMARK 3 ORIGIN FOR THE GROUP (A): -9.2085 1.7672 -42.7754
REMARK 3 T TENSOR
REMARK 3 T11: 0.0396 T22: 0.0893
REMARK 3 T33: 0.0252 T12: 0.0256
REMARK 3 T13: -0.0095 T23: 0.0232
REMARK 3 L TENSOR
REMARK 3 L11: 5.0225 L22: 3.7035
REMARK 3 L33: 4.8561 L12: 0.2249
REMARK 3 L13: 0.5867 L23: -0.3091
REMARK 3 S TENSOR
REMARK 3 S11: -0.1571 S12: 0.3627 S13: 0.1502
REMARK 3 S21: -0.1092 S22: 0.1116 S23: 0.1082
REMARK 3 S31: -0.3669 S32: -0.4478 S33: 0.0455
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 : B 15 B 77
REMARK 3 ORIGIN FOR THE GROUP (A): 12.6468 10.0223 -5.7380
REMARK 3 T TENSOR
REMARK 3 T11: 0.1196 T22: 0.0675
REMARK 3 T33: 0.1742 T12: -0.0809
REMARK 3 T13: -0.0893 T23: 0.0604
REMARK 3 L TENSOR
REMARK 3 L11: 0.6202 L22: 2.9264
REMARK 3 L33: 3.2392 L12: -0.2140
REMARK 3 L13: 0.7875 L23: 1.8113
REMARK 3 S TENSOR
REMARK 3 S11: 0.0364 S12: 0.0441 S13: 0.0837
REMARK 3 S21: -0.1569 S22: 0.0060 S23: 0.1376
REMARK 3 S31: 0.2256 S32: -0.1249 S33: -0.0424
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 : B 78 B 153
REMARK 3 ORIGIN FOR THE GROUP (A): 8.3133 17.0350 -3.4906
REMARK 3 T TENSOR
REMARK 3 T11: 0.0151 T22: 0.0373
REMARK 3 T33: 0.1519 T12: -0.0181
REMARK 3 T13: -0.0373 T23: 0.0256
REMARK 3 L TENSOR
REMARK 3 L11: 1.9539 L22: 2.8116
REMARK 3 L33: 4.0950 L12: -0.4628
REMARK 3 L13: -0.4768 L23: 1.4573
REMARK 3 S TENSOR
REMARK 3 S11: -0.0580 S12: 0.0317 S13: 0.1036
REMARK 3 S21: -0.1151 S22: 0.0778 S23: 0.2308
REMARK 3 S31: 0.0737 S32: -0.3009 S33: -0.0198
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 : B 154 B 179
REMARK 3 ORIGIN FOR THE GROUP (A): 15.1365 28.7954 2.9714
REMARK 3 T TENSOR
REMARK 3 T11: 0.0183 T22: 0.0107
REMARK 3 T33: 0.1733 T12: -0.0089
REMARK 3 T13: 0.0084 T23: -0.0215
REMARK 3 L TENSOR
REMARK 3 L11: 3.2953 L22: 4.5083
REMARK 3 L33: 8.1145 L12: -1.3575
REMARK 3 L13: 0.1302 L23: 1.7700
REMARK 3 S TENSOR
REMARK 3 S11: -0.1038 S12: 0.0310 S13: 0.3714
REMARK 3 S21: 0.0279 S22: 0.0799 S23: 0.0785
REMARK 3 S31: -0.3126 S32: 0.1225 S33: 0.0239
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 : B 180 B 186
REMARK 3 ORIGIN FOR THE GROUP (A): 23.1638 28.6730 -8.1362
REMARK 3 T TENSOR
REMARK 3 T11: 0.2654 T22: 0.3898
REMARK 3 T33: 0.2092 T12: -0.0403
REMARK 3 T13: -0.0460 T23: 0.0669
REMARK 3 L TENSOR
REMARK 3 L11: 0.5851 L22: 10.3972
REMARK 3 L33: 0.1480 L12: 0.6355
REMARK 3 L13: -0.2125 L23: -1.0511
REMARK 3 S TENSOR
REMARK 3 S11: -0.0659 S12: 0.4419 S13: 0.1598
REMARK 3 S21: -0.4770 S22: 0.0781 S23: -0.2634
REMARK 3 S31: 0.0404 S32: -0.1289 S33: -0.0123
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 : B 187 B 254
REMARK 3 ORIGIN FOR THE GROUP (A): 32.0874 25.9296 2.6529
REMARK 3 T TENSOR
REMARK 3 T11: 0.0494 T22: 0.1461
REMARK 3 T33: 0.1396 T12: -0.0687
REMARK 3 T13: -0.0114 T23: -0.0481
REMARK 3 L TENSOR
REMARK 3 L11: 7.9811 L22: 3.8093
REMARK 3 L33: 4.5428 L12: 0.8831
REMARK 3 L13: -1.5691 L23: 0.4759
REMARK 3 S TENSOR
REMARK 3 S11: -0.2913 S12: 0.4149 S13: 0.1103
REMARK 3 S21: -0.1618 S22: 0.2508 S23: -0.1658
REMARK 3 S31: -0.1043 S32: 0.3815 S33: 0.0406
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 : B 255 B 266
REMARK 3 ORIGIN FOR THE GROUP (A): 30.5651 5.3022 1.6126
REMARK 3 T TENSOR
REMARK 3 T11: 0.5229 T22: 0.4398
REMARK 3 T33: 0.6233 T12: 0.0903
REMARK 3 T13: 0.0668 T23: -0.0986
REMARK 3 L TENSOR
REMARK 3 L11: 0.2132 L22: 7.4631
REMARK 3 L33: 0.0483 L12: -1.2251
REMARK 3 L13: 0.0777 L23: -0.5341
REMARK 3 S TENSOR
REMARK 3 S11: -0.0042 S12: 0.0102 S13: -0.0233
REMARK 3 S21: -0.1549 S22: -0.0772 S23: -0.3508
REMARK 3 S31: 0.0634 S32: 0.0206 S33: 0.0814
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 : B 267 B 307
REMARK 3 ORIGIN FOR THE GROUP (A): 23.9583 12.8624 10.3559
REMARK 3 T TENSOR
REMARK 3 T11: 0.0295 T22: 0.0638
REMARK 3 T33: 0.0949 T12: 0.0304
REMARK 3 T13: -0.0093 T23: 0.0173
REMARK 3 L TENSOR
REMARK 3 L11: 4.9179 L22: 4.4011
REMARK 3 L33: 7.0965 L12: -0.3221
REMARK 3 L13: -1.5009 L23: -0.2620
REMARK 3 S TENSOR
REMARK 3 S11: -0.0249 S12: -0.1420 S13: -0.2750
REMARK 3 S21: 0.2467 S22: 0.0049 S23: -0.3508
REMARK 3 S31: 0.2618 S32: 0.6355 S33: 0.0201
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 : B 308 B 326
REMARK 3 ORIGIN FOR THE GROUP (A): 20.3700 5.7983 14.6683
REMARK 3 T TENSOR
REMARK 3 T11: 0.2139 T22: 0.0549
REMARK 3 T33: 0.1586 T12: 0.0378
REMARK 3 T13: 0.0328 T23: 0.0347
REMARK 3 L TENSOR
REMARK 3 L11: 4.2378 L22: 0.8471
REMARK 3 L33: 9.0019 L12: 0.7671
REMARK 3 L13: 4.0588 L23: -0.7200
REMARK 3 S TENSOR
REMARK 3 S11: 0.0579 S12: -0.2763 S13: -0.4237
REMARK 3 S21: 0.0633 S22: -0.0766 S23: -0.1468
REMARK 3 S31: 0.5759 S32: -0.1118 S33: 0.0187
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 5BYD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JUN-15.
REMARK 100 THE DEPOSITION ID IS D_1000210749.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-APR-10
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 : NSLS
REMARK 200 BEAMLINE : X25
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34784
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 44.960
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.08300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.51800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
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: 2FV7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM HEPES, 25% PEG 6000, PH
REMARK 280 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 44.95500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: 2390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 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 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 1
REMARK 465 ALA A 2
REMARK 465 ALA A 3
REMARK 465 SER A 4
REMARK 465 GLY A 5
REMARK 465 GLU A 6
REMARK 465 PRO A 7
REMARK 465 GLN A 8
REMARK 465 ARG A 9
REMARK 465 GLN A 10
REMARK 465 TRP A 11
REMARK 465 GLN A 12
REMARK 465 GLU A 13
REMARK 465 GLU A 14
REMARK 465 HIS A 330
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 ALA B 3
REMARK 465 SER B 4
REMARK 465 GLY B 5
REMARK 465 GLU B 6
REMARK 465 PRO B 7
REMARK 465 GLN B 8
REMARK 465 ARG B 9
REMARK 465 GLN B 10
REMARK 465 TRP B 11
REMARK 465 GLN B 12
REMARK 465 GLU B 13
REMARK 465 GLU B 14
REMARK 465 HIS B 327
REMARK 465 HIS B 328
REMARK 465 HIS B 329
REMARK 465 HIS B 330
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 34 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 37 CG CD CE NZ
REMARK 470 GLU A 86 CD OE1 OE2
REMARK 470 GLU A 134 CD OE1 OE2
REMARK 470 ARG A 137 NE CZ NH1 NH2
REMARK 470 ARG A 145 NE CZ NH1 NH2
REMARK 470 ASP A 184 CG OD1 OD2
REMARK 470 LYS A 226 CG CD CE NZ
REMARK 470 GLU A 239 CG CD OE1 OE2
REMARK 470 LYS A 260 CD CE NZ
REMARK 470 LYS A 315 CE NZ
REMARK 470 HIS A 325 CG ND1 CD2 CE1 NE2
REMARK 470 ARG B 34 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 37 CG CD CE NZ
REMARK 470 LYS B 46 NZ
REMARK 470 LYS B 102 CD CE NZ
REMARK 470 ARG B 169 CD NE CZ NH1 NH2
REMARK 470 ASP B 184 CG OD1 OD2
REMARK 470 GLU B 239 CG CD OE1 OE2
REMARK 470 GLU B 257 CG CD OE1 OE2
REMARK 470 LYS B 258 CD CE NZ
REMARK 470 LYS B 260 CG CD CE NZ
REMARK 470 VAL B 262 CG1 CG2
REMARK 470 GLU B 288 CD OE1 OE2
REMARK 470 LYS B 315 CE NZ
REMARK 470 HIS B 326 CG ND1 CD2 CE1 NE2
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 ARG B 145 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG B 145 NE - CZ - NH2 ANGL. DEV. = -3.5 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 GLU A 116 -3.46 -52.12
REMARK 500 GLN A 152 -158.97 -133.70
REMARK 500 ASP A 184 46.42 -104.20
REMARK 500 THR A 307 -114.01 55.39
REMARK 500 GLU B 116 -5.57 -53.87
REMARK 500 ASP B 184 45.19 -107.11
REMARK 500 THR B 307 -94.34 -109.95
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 401 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 263 O
REMARK 620 2 SER A 301 O 97.5
REMARK 620 3 ALA A 304 O 89.9 80.5
REMARK 620 4 SER A 310 OG 168.0 76.8 99.5
REMARK 620 5 HOH A 530 O 85.1 82.8 161.7 83.7
REMARK 620 6 HOH A 536 O 90.9 171.1 102.6 94.4 95.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B 401 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 263 O
REMARK 620 2 THR B 265 O 90.0
REMARK 620 3 SER B 301 O 92.1 125.5
REMARK 620 4 ALA B 304 O 90.3 161.8 72.7
REMARK 620 5 GLY B 306 O 127.1 66.7 140.5 99.0
REMARK 620 6 SER B 310 OG 160.0 92.7 70.3 93.3 71.7
REMARK 620 7 HOH B 506 O 80.7 47.5 79.2 150.1 109.2 86.6
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K B 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5BYC RELATED DB: PDB
REMARK 900 RELATED ID: 5BYE RELATED DB: PDB
REMARK 900 RELATED ID: 5BYF RELATED DB: PDB
DBREF 5BYD A 1 322 UNP Q9H477 RBSK_HUMAN 1 322
DBREF 5BYD B 1 322 UNP Q9H477 RBSK_HUMAN 1 322
SEQADV 5BYD LEU A 323 UNP Q9H477 EXPRESSION TAG
SEQADV 5BYD GLU A 324 UNP Q9H477 EXPRESSION TAG
SEQADV 5BYD HIS A 325 UNP Q9H477 EXPRESSION TAG
SEQADV 5BYD HIS A 326 UNP Q9H477 EXPRESSION TAG
SEQADV 5BYD HIS A 327 UNP Q9H477 EXPRESSION TAG
SEQADV 5BYD HIS A 328 UNP Q9H477 EXPRESSION TAG
SEQADV 5BYD HIS A 329 UNP Q9H477 EXPRESSION TAG
SEQADV 5BYD HIS A 330 UNP Q9H477 EXPRESSION TAG
SEQADV 5BYD LEU B 323 UNP Q9H477 EXPRESSION TAG
SEQADV 5BYD GLU B 324 UNP Q9H477 EXPRESSION TAG
SEQADV 5BYD HIS B 325 UNP Q9H477 EXPRESSION TAG
SEQADV 5BYD HIS B 326 UNP Q9H477 EXPRESSION TAG
SEQADV 5BYD HIS B 327 UNP Q9H477 EXPRESSION TAG
SEQADV 5BYD HIS B 328 UNP Q9H477 EXPRESSION TAG
SEQADV 5BYD HIS B 329 UNP Q9H477 EXPRESSION TAG
SEQADV 5BYD HIS B 330 UNP Q9H477 EXPRESSION TAG
SEQRES 1 A 330 MET ALA ALA SER GLY GLU PRO GLN ARG GLN TRP GLN GLU
SEQRES 2 A 330 GLU VAL ALA ALA VAL VAL VAL VAL GLY SER CYS MET THR
SEQRES 3 A 330 ASP LEU VAL SER LEU THR SER ARG LEU PRO LYS THR GLY
SEQRES 4 A 330 GLU THR ILE HIS GLY HIS LYS PHE PHE ILE GLY PHE GLY
SEQRES 5 A 330 GLY LYS GLY ALA ASN GLN CYS VAL GLN ALA ALA ARG LEU
SEQRES 6 A 330 GLY ALA MET THR SER MET VAL CYS LYS VAL GLY LYS ASP
SEQRES 7 A 330 SER PHE GLY ASN ASP TYR ILE GLU ASN LEU LYS GLN ASN
SEQRES 8 A 330 ASP ILE SER THR GLU PHE THR TYR GLN THR LYS ASP ALA
SEQRES 9 A 330 ALA THR GLY THR ALA SER ILE ILE VAL ASN ASN GLU GLY
SEQRES 10 A 330 GLN ASN ILE ILE VAL ILE VAL ALA GLY ALA ASN LEU LEU
SEQRES 11 A 330 LEU ASN THR GLU ASP LEU ARG ALA ALA ALA ASN VAL ILE
SEQRES 12 A 330 SER ARG ALA LYS VAL MET VAL CYS GLN LEU GLU ILE THR
SEQRES 13 A 330 PRO ALA THR SER LEU GLU ALA LEU THR MET ALA ARG ARG
SEQRES 14 A 330 SER GLY VAL LYS THR LEU PHE ASN PRO ALA PRO ALA ILE
SEQRES 15 A 330 ALA ASP LEU ASP PRO GLN PHE TYR THR LEU SER ASP VAL
SEQRES 16 A 330 PHE CYS CYS ASN GLU SER GLU ALA GLU ILE LEU THR GLY
SEQRES 17 A 330 LEU THR VAL GLY SER ALA ALA ASP ALA GLY GLU ALA ALA
SEQRES 18 A 330 LEU VAL LEU LEU LYS ARG GLY CYS GLN VAL VAL ILE ILE
SEQRES 19 A 330 THR LEU GLY ALA GLU GLY CYS VAL VAL LEU SER GLN THR
SEQRES 20 A 330 GLU PRO GLU PRO LYS HIS ILE PRO THR GLU LYS VAL LYS
SEQRES 21 A 330 ALA VAL ASP THR THR GLY ALA GLY ASP SER PHE VAL GLY
SEQRES 22 A 330 ALA LEU ALA PHE TYR LEU ALA TYR TYR PRO ASN LEU SER
SEQRES 23 A 330 LEU GLU ASP MET LEU ASN ARG SER ASN PHE ILE ALA ALA
SEQRES 24 A 330 VAL SER VAL GLN ALA ALA GLY THR GLN SER SER TYR PRO
SEQRES 25 A 330 TYR LYS LYS ASP LEU PRO LEU THR LEU PHE LEU GLU HIS
SEQRES 26 A 330 HIS HIS HIS HIS HIS
SEQRES 1 B 330 MET ALA ALA SER GLY GLU PRO GLN ARG GLN TRP GLN GLU
SEQRES 2 B 330 GLU VAL ALA ALA VAL VAL VAL VAL GLY SER CYS MET THR
SEQRES 3 B 330 ASP LEU VAL SER LEU THR SER ARG LEU PRO LYS THR GLY
SEQRES 4 B 330 GLU THR ILE HIS GLY HIS LYS PHE PHE ILE GLY PHE GLY
SEQRES 5 B 330 GLY LYS GLY ALA ASN GLN CYS VAL GLN ALA ALA ARG LEU
SEQRES 6 B 330 GLY ALA MET THR SER MET VAL CYS LYS VAL GLY LYS ASP
SEQRES 7 B 330 SER PHE GLY ASN ASP TYR ILE GLU ASN LEU LYS GLN ASN
SEQRES 8 B 330 ASP ILE SER THR GLU PHE THR TYR GLN THR LYS ASP ALA
SEQRES 9 B 330 ALA THR GLY THR ALA SER ILE ILE VAL ASN ASN GLU GLY
SEQRES 10 B 330 GLN ASN ILE ILE VAL ILE VAL ALA GLY ALA ASN LEU LEU
SEQRES 11 B 330 LEU ASN THR GLU ASP LEU ARG ALA ALA ALA ASN VAL ILE
SEQRES 12 B 330 SER ARG ALA LYS VAL MET VAL CYS GLN LEU GLU ILE THR
SEQRES 13 B 330 PRO ALA THR SER LEU GLU ALA LEU THR MET ALA ARG ARG
SEQRES 14 B 330 SER GLY VAL LYS THR LEU PHE ASN PRO ALA PRO ALA ILE
SEQRES 15 B 330 ALA ASP LEU ASP PRO GLN PHE TYR THR LEU SER ASP VAL
SEQRES 16 B 330 PHE CYS CYS ASN GLU SER GLU ALA GLU ILE LEU THR GLY
SEQRES 17 B 330 LEU THR VAL GLY SER ALA ALA ASP ALA GLY GLU ALA ALA
SEQRES 18 B 330 LEU VAL LEU LEU LYS ARG GLY CYS GLN VAL VAL ILE ILE
SEQRES 19 B 330 THR LEU GLY ALA GLU GLY CYS VAL VAL LEU SER GLN THR
SEQRES 20 B 330 GLU PRO GLU PRO LYS HIS ILE PRO THR GLU LYS VAL LYS
SEQRES 21 B 330 ALA VAL ASP THR THR GLY ALA GLY ASP SER PHE VAL GLY
SEQRES 22 B 330 ALA LEU ALA PHE TYR LEU ALA TYR TYR PRO ASN LEU SER
SEQRES 23 B 330 LEU GLU ASP MET LEU ASN ARG SER ASN PHE ILE ALA ALA
SEQRES 24 B 330 VAL SER VAL GLN ALA ALA GLY THR GLN SER SER TYR PRO
SEQRES 25 B 330 TYR LYS LYS ASP LEU PRO LEU THR LEU PHE LEU GLU HIS
SEQRES 26 B 330 HIS HIS HIS HIS HIS
HET NA A 401 1
HET K B 401 1
HETNAM NA SODIUM ION
HETNAM K POTASSIUM ION
FORMUL 3 NA NA 1+
FORMUL 4 K K 1+
FORMUL 5 HOH *155(H2 O)
HELIX 1 AA1 GLY A 53 LEU A 65 1 13
HELIX 2 AA2 ASP A 78 ASN A 91 1 14
HELIX 3 AA3 ALA A 125 LEU A 131 5 7
HELIX 4 AA4 ASN A 132 ALA A 139 1 8
HELIX 5 AA5 ALA A 139 ARG A 145 1 7
HELIX 6 AA6 THR A 156 SER A 170 1 15
HELIX 7 AA7 PRO A 187 LEU A 192 1 6
HELIX 8 AA8 GLU A 200 GLY A 208 1 9
HELIX 9 AA9 SER A 213 ARG A 227 1 15
HELIX 10 AB1 GLY A 237 GLU A 239 5 3
HELIX 11 AB2 GLY A 266 TYR A 282 1 17
HELIX 12 AB3 SER A 286 VAL A 302 1 17
HELIX 13 AB4 GLY A 306 TYR A 311 5 6
HELIX 14 AB5 TYR A 313 LEU A 317 5 5
HELIX 15 AB6 PRO A 318 LEU A 323 5 6
HELIX 16 AB7 GLY B 53 LEU B 65 1 13
HELIX 17 AB8 ASP B 78 ASN B 91 1 14
HELIX 18 AB9 ALA B 125 LEU B 131 5 7
HELIX 19 AC1 ASN B 132 ALA B 139 1 8
HELIX 20 AC2 ALA B 139 ARG B 145 1 7
HELIX 21 AC3 THR B 156 SER B 170 1 15
HELIX 22 AC4 PRO B 187 LEU B 192 1 6
HELIX 23 AC5 GLU B 200 GLY B 208 1 9
HELIX 24 AC6 SER B 213 ARG B 227 1 15
HELIX 25 AC7 GLY B 237 GLU B 239 5 3
HELIX 26 AC8 GLY B 266 TYR B 282 1 17
HELIX 27 AC9 SER B 286 VAL B 302 1 17
HELIX 28 AD1 THR B 307 TYR B 311 5 5
HELIX 29 AD2 TYR B 313 LEU B 317 5 5
HELIX 30 AD3 PRO B 318 LEU B 323 5 6
SHEET 1 AA1 9 THR A 98 THR A 101 0
SHEET 2 AA1 9 THR A 69 GLY A 76 1 N CYS A 73 O TYR A 99
SHEET 3 AA1 9 VAL A 18 VAL A 21 1 N VAL A 20 O VAL A 72
SHEET 4 AA1 9 VAL A 148 CYS A 151 1 O VAL A 148 N VAL A 19
SHEET 5 AA1 9 LYS A 173 PHE A 176 1 O LEU A 175 N MET A 149
SHEET 6 AA1 9 VAL A 195 ASN A 199 1 O VAL A 195 N PHE A 176
SHEET 7 AA1 9 VAL A 231 THR A 235 1 O THR A 235 N CYS A 198
SHEET 8 AA1 9 CYS A 241 SER A 245 -1 O LEU A 244 N VAL A 232
SHEET 9 AA1 9 LYS A 252 ILE A 254 -1 O ILE A 254 N CYS A 241
SHEET 1 AA2 5 LYS A 46 GLY A 52 0
SHEET 2 AA2 5 MET A 25 LEU A 31 -1 N LEU A 31 O LYS A 46
SHEET 3 AA2 5 GLY A 107 VAL A 113 1 O ILE A 111 N SER A 30
SHEET 4 AA2 5 ASN A 119 VAL A 124 -1 O VAL A 122 N SER A 110
SHEET 5 AA2 5 THR B 41 HIS B 43 1 O ILE B 42 N ILE A 123
SHEET 1 AA3 5 THR A 41 HIS A 43 0
SHEET 2 AA3 5 ASN B 119 VAL B 124 1 O ILE B 123 N ILE A 42
SHEET 3 AA3 5 GLY B 107 VAL B 113 -1 N THR B 108 O VAL B 124
SHEET 4 AA3 5 MET B 25 LEU B 31 1 N SER B 30 O ILE B 111
SHEET 5 AA3 5 LYS B 46 GLY B 52 -1 O LYS B 46 N LEU B 31
SHEET 1 AA4 9 THR B 98 THR B 101 0
SHEET 2 AA4 9 THR B 69 GLY B 76 1 N CYS B 73 O TYR B 99
SHEET 3 AA4 9 VAL B 18 VAL B 21 1 N VAL B 20 O VAL B 72
SHEET 4 AA4 9 VAL B 148 CYS B 151 1 O VAL B 148 N VAL B 19
SHEET 5 AA4 9 LYS B 173 PHE B 176 1 O LEU B 175 N MET B 149
SHEET 6 AA4 9 VAL B 195 ASN B 199 1 O VAL B 195 N PHE B 176
SHEET 7 AA4 9 VAL B 231 THR B 235 1 O THR B 235 N CYS B 198
SHEET 8 AA4 9 CYS B 241 SER B 245 -1 O LEU B 244 N VAL B 232
SHEET 9 AA4 9 LYS B 252 ILE B 254 -1 O ILE B 254 N CYS B 241
LINK O ASP A 263 NA NA A 401 1555 1555 2.71
LINK O SER A 301 NA NA A 401 1555 1555 2.38
LINK O ALA A 304 NA NA A 401 1555 1555 2.45
LINK OG SER A 310 NA NA A 401 1555 1555 2.62
LINK NA NA A 401 O HOH A 530 1555 1555 2.45
LINK NA NA A 401 O HOH A 536 1555 1555 2.28
LINK O ASP B 263 K K B 401 1555 1555 2.68
LINK O THR B 265 K K B 401 1555 1555 3.41
LINK O SER B 301 K K B 401 1555 1555 2.65
LINK O ALA B 304 K K B 401 1555 1555 2.55
LINK O GLY B 306 K K B 401 1555 1555 2.88
LINK OG SER B 310 K K B 401 1555 1555 2.91
LINK K K B 401 O HOH B 506 1555 1555 2.78
CISPEP 1 ALA A 179 PRO A 180 0 -9.62
CISPEP 2 ALA B 179 PRO B 180 0 -5.30
SITE 1 AC1 7 ASP A 263 THR A 265 SER A 301 ALA A 304
SITE 2 AC1 7 SER A 310 HOH A 530 HOH A 536
SITE 1 AC2 7 ASP B 263 THR B 265 SER B 301 ALA B 304
SITE 2 AC2 7 GLY B 306 SER B 310 HOH B 506
CRYST1 46.590 89.910 75.140 90.00 98.80 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.021464 0.000000 0.003323 0.00000
SCALE2 0.000000 0.011122 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013467 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
