HEADER LIGASE 06-MAY-14 4PHC
TITLE CRYSTAL STRUCTURE OF A HUMAN CYTOSOLIC HISTIDYL-TRNA SYNTHETASE,
TITLE 2 HISTIDINE-BOUND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTIDINE--TRNA LIGASE, CYTOPLASMIC;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: HISTIDYL-TRNA SYNTHETASE,HISRS;
COMPND 5 EC: 6.1.1.21;
COMPND 6 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: HARS, HRS;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: AVA0421
KEYWDS AMINOACYL-TRNA SYNTHETASE, AARS, HISRS, HUMAN, CYTOPLASMIC, LIGASE,
KEYWDS 2 PROTEIN-SUBSTRATE COMPLEX, ROSSMANN-FOLD, TRANSLATION, NUCLEOTIDE
KEYWDS 3 BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR C.Y.KOH,A.B.WETZEL,W.J.DE VAN DER SCHUEREN,W.G.J.HOL
REVDAT 7 27-DEC-23 4PHC 1 REMARK
REVDAT 6 11-DEC-19 4PHC 1 REMARK
REVDAT 5 22-NOV-17 4PHC 1 REMARK
REVDAT 4 06-SEP-17 4PHC 1 SOURCE JRNL REMARK
REVDAT 3 03-JUN-15 4PHC 1 JRNL
REVDAT 2 24-SEP-14 4PHC 1 JRNL
REVDAT 1 27-AUG-14 4PHC 0
JRNL AUTH C.Y.KOH,A.B.WETZEL,W.J.DE VAN DER SCHUEREN,W.G.HOL
JRNL TITL COMPARISON OF HISTIDINE RECOGNITION IN HUMAN AND
JRNL TITL 2 TRYPANOSOMATID HISTIDYL-TRNA SYNTHETASES.
JRNL REF BIOCHIMIE V. 106 111 2014
JRNL REFN ISSN 0300-9084
JRNL PMID 25151410
JRNL DOI 10.1016/J.BIOCHI.2014.08.005
REMARK 2
REMARK 2 RESOLUTION. 2.84 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC REFMAC_5.8.0049
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) : 2.84
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.41
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.7
REMARK 3 NUMBER OF REFLECTIONS : 49209
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) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2504
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) : 2.84
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.92
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3184
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.28
REMARK 3 BIN R VALUE (WORKING SET) : 0.3250
REMARK 3 BIN FREE R VALUE SET COUNT : 177
REMARK 3 BIN FREE R VALUE : 0.3490
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 13957
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 68
REMARK 3 SOLVENT ATOMS : 55
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 62.18
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.82000
REMARK 3 B22 (A**2) : -0.04000
REMARK 3 B33 (A**2) : 0.86000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
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): 0.385
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.290
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 33.193
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.911
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 14226 ; 0.007 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 14065 ; 0.004 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 19145 ; 1.157 ; 1.993
REMARK 3 BOND ANGLES OTHERS (DEGREES): 32359 ; 0.957 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1756 ; 5.419 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 644 ;39.289 ;24.037
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2685 ;14.481 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 114 ;18.512 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2174 ; 0.062 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 15810 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 3072 ; 0.003 ; 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): 7069 ; 1.469 ; 3.705
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 7068 ; 1.469 ; 3.705
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8810 ; 2.517 ; 5.552
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 6
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 53 504 B 53 504 26925 0.080 0.050
REMARK 3 2 A 53 504 C 53 504 26822 0.090 0.050
REMARK 3 3 A 53 504 D 53 504 26805 0.080 0.050
REMARK 3 4 B 53 504 C 53 504 27669 0.070 0.050
REMARK 3 5 B 53 504 D 53 504 27363 0.070 0.050
REMARK 3 6 C 53 504 D 53 504 27027 0.080 0.050
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
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 53 A 198
REMARK 3 ORIGIN FOR THE GROUP (A): -11.8640 17.4000 -21.2160
REMARK 3 T TENSOR
REMARK 3 T11: 0.1218 T22: 0.0275
REMARK 3 T33: 0.0790 T12: -0.0356
REMARK 3 T13: -0.0139 T23: -0.0107
REMARK 3 L TENSOR
REMARK 3 L11: 2.3854 L22: 1.5938
REMARK 3 L33: 3.4621 L12: -0.7120
REMARK 3 L13: -1.2179 L23: 0.9045
REMARK 3 S TENSOR
REMARK 3 S11: -0.0919 S12: 0.1083 S13: -0.3702
REMARK 3 S21: 0.0588 S22: 0.0093 S23: -0.0347
REMARK 3 S31: 0.4641 S32: -0.0266 S33: 0.0826
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 199 A 404
REMARK 3 ORIGIN FOR THE GROUP (A): -29.5770 10.5390 -13.6160
REMARK 3 T TENSOR
REMARK 3 T11: 0.4730 T22: 0.1860
REMARK 3 T33: 0.1556 T12: -0.1265
REMARK 3 T13: 0.0072 T23: -0.0242
REMARK 3 L TENSOR
REMARK 3 L11: 2.6739 L22: 2.6330
REMARK 3 L33: 0.9220 L12: 1.0736
REMARK 3 L13: -0.4425 L23: -0.0244
REMARK 3 S TENSOR
REMARK 3 S11: -0.0110 S12: 0.0244 S13: -0.4040
REMARK 3 S21: 0.0483 S22: -0.0466 S23: 0.0866
REMARK 3 S31: 0.6219 S32: -0.2240 S33: 0.0576
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 405 A 504
REMARK 3 ORIGIN FOR THE GROUP (A): -8.4100 46.2870 -54.0330
REMARK 3 T TENSOR
REMARK 3 T11: 0.1095 T22: 0.1427
REMARK 3 T33: 0.1023 T12: 0.0513
REMARK 3 T13: -0.0152 T23: 0.0108
REMARK 3 L TENSOR
REMARK 3 L11: 3.9894 L22: 4.9943
REMARK 3 L33: 4.7188 L12: 0.3971
REMARK 3 L13: 0.7544 L23: -0.4779
REMARK 3 S TENSOR
REMARK 3 S11: -0.0168 S12: 0.0932 S13: 0.4655
REMARK 3 S21: -0.3212 S22: -0.1312 S23: -0.1195
REMARK 3 S31: -0.5699 S32: -0.2295 S33: 0.1480
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 53 B 205
REMARK 3 ORIGIN FOR THE GROUP (A): 2.2030 23.8400 -33.6560
REMARK 3 T TENSOR
REMARK 3 T11: 0.0452 T22: 0.0939
REMARK 3 T33: 0.1406 T12: 0.0063
REMARK 3 T13: -0.0395 T23: -0.0518
REMARK 3 L TENSOR
REMARK 3 L11: 1.1952 L22: 2.2541
REMARK 3 L33: 3.8195 L12: -0.0025
REMARK 3 L13: -0.8467 L23: -1.2453
REMARK 3 S TENSOR
REMARK 3 S11: -0.0323 S12: -0.1504 S13: -0.0580
REMARK 3 S21: 0.1069 S22: 0.0234 S23: -0.4481
REMARK 3 S31: 0.2469 S32: 0.2929 S33: 0.0089
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 : B 206 B 395
REMARK 3 ORIGIN FOR THE GROUP (A): 19.7210 29.8960 -43.3740
REMARK 3 T TENSOR
REMARK 3 T11: 0.0717 T22: 0.3052
REMARK 3 T33: 0.2917 T12: 0.0025
REMARK 3 T13: -0.0117 T23: -0.1244
REMARK 3 L TENSOR
REMARK 3 L11: 2.9367 L22: 2.7102
REMARK 3 L33: 1.5247 L12: -0.6004
REMARK 3 L13: -0.2378 L23: 0.2023
REMARK 3 S TENSOR
REMARK 3 S11: 0.0439 S12: 0.0317 S13: 0.1186
REMARK 3 S21: 0.1294 S22: 0.1537 S23: -0.8053
REMARK 3 S31: 0.0636 S32: 0.6522 S33: -0.1976
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 : B 396 B 505
REMARK 3 ORIGIN FOR THE GROUP (A): -23.4760 42.9130 -6.9550
REMARK 3 T TENSOR
REMARK 3 T11: 0.2221 T22: 0.0099
REMARK 3 T33: 0.0552 T12: 0.0047
REMARK 3 T13: -0.0164 T23: -0.0151
REMARK 3 L TENSOR
REMARK 3 L11: 4.3701 L22: 4.7113
REMARK 3 L33: 3.8130 L12: 0.4640
REMARK 3 L13: -0.4433 L23: 0.8019
REMARK 3 S TENSOR
REMARK 3 S11: 0.1514 S12: -0.0567 S13: 0.3418
REMARK 3 S21: 0.1152 S22: 0.0039 S23: 0.1117
REMARK 3 S31: -0.4936 S32: 0.0237 S33: -0.1553
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 : C 53 C 187
REMARK 3 ORIGIN FOR THE GROUP (A): -43.4970 -26.0260 -32.3740
REMARK 3 T TENSOR
REMARK 3 T11: 0.1222 T22: 0.0757
REMARK 3 T33: 0.2523 T12: 0.0147
REMARK 3 T13: -0.0282 T23: -0.0669
REMARK 3 L TENSOR
REMARK 3 L11: 1.5704 L22: 1.0893
REMARK 3 L33: 3.6695 L12: 0.1069
REMARK 3 L13: -0.9441 L23: -0.7900
REMARK 3 S TENSOR
REMARK 3 S11: -0.0627 S12: 0.2049 S13: -0.4147
REMARK 3 S21: -0.1467 S22: -0.1241 S23: -0.2354
REMARK 3 S31: 0.3510 S32: 0.1292 S33: 0.1868
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 : C 188 C 404
REMARK 3 ORIGIN FOR THE GROUP (A): -53.8200 -41.2050 -22.8030
REMARK 3 T TENSOR
REMARK 3 T11: 0.2394 T22: 0.1290
REMARK 3 T33: 0.3660 T12: -0.0413
REMARK 3 T13: 0.0140 T23: -0.1364
REMARK 3 L TENSOR
REMARK 3 L11: 3.5232 L22: 2.7865
REMARK 3 L33: 1.4735 L12: -0.4132
REMARK 3 L13: 0.8177 L23: -0.5132
REMARK 3 S TENSOR
REMARK 3 S11: 0.1668 S12: 0.3085 S13: -0.7816
REMARK 3 S21: -0.0058 S22: -0.1660 S23: 0.1518
REMARK 3 S31: 0.4855 S32: 0.0296 S33: -0.0008
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 : C 405 C 505
REMARK 3 ORIGIN FOR THE GROUP (A): -63.1840 2.9030 -58.6810
REMARK 3 T TENSOR
REMARK 3 T11: 0.1520 T22: 0.1944
REMARK 3 T33: 0.1111 T12: 0.0329
REMARK 3 T13: -0.0321 T23: -0.0660
REMARK 3 L TENSOR
REMARK 3 L11: 5.0531 L22: 4.5869
REMARK 3 L33: 2.7961 L12: -0.1975
REMARK 3 L13: 0.6725 L23: 0.0288
REMARK 3 S TENSOR
REMARK 3 S11: -0.0497 S12: 0.0956 S13: 0.4636
REMARK 3 S21: -0.3846 S22: 0.0100 S23: 0.1508
REMARK 3 S31: -0.2767 S32: -0.4542 S33: 0.0397
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 : D 53 D 173
REMARK 3 ORIGIN FOR THE GROUP (A): -37.3470 -15.0130 -41.9840
REMARK 3 T TENSOR
REMARK 3 T11: 0.0616 T22: 0.1668
REMARK 3 T33: 0.1991 T12: -0.0328
REMARK 3 T13: 0.0412 T23: -0.0325
REMARK 3 L TENSOR
REMARK 3 L11: 1.7735 L22: 2.7851
REMARK 3 L33: 3.6167 L12: -0.4306
REMARK 3 L13: 0.2694 L23: -0.5941
REMARK 3 S TENSOR
REMARK 3 S11: 0.0091 S12: -0.0431 S13: -0.1339
REMARK 3 S21: -0.0117 S22: -0.1443 S23: -0.5260
REMARK 3 S31: 0.0733 S32: 0.5474 S33: 0.1352
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 : D 174 D 396
REMARK 3 ORIGIN FOR THE GROUP (A): -31.6390 2.8510 -53.5990
REMARK 3 T TENSOR
REMARK 3 T11: 0.2191 T22: 0.2687
REMARK 3 T33: 0.1947 T12: -0.0719
REMARK 3 T13: 0.0502 T23: -0.0663
REMARK 3 L TENSOR
REMARK 3 L11: 2.8108 L22: 1.3062
REMARK 3 L33: 0.5556 L12: 0.6683
REMARK 3 L13: -0.1249 L23: -0.3013
REMARK 3 S TENSOR
REMARK 3 S11: -0.0651 S12: 0.1509 S13: 0.1093
REMARK 3 S21: -0.0465 S22: 0.0849 S23: -0.3189
REMARK 3 S31: -0.2058 S32: 0.3021 S33: -0.0198
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 : D 397 D 504
REMARK 3 ORIGIN FOR THE GROUP (A): -65.6920 -12.7040 -11.5710
REMARK 3 T TENSOR
REMARK 3 T11: 0.2275 T22: 0.1219
REMARK 3 T33: 0.1517 T12: 0.0939
REMARK 3 T13: -0.0605 T23: -0.1066
REMARK 3 L TENSOR
REMARK 3 L11: 5.0834 L22: 3.6727
REMARK 3 L33: 4.2189 L12: -0.1556
REMARK 3 L13: -0.0653 L23: 1.3625
REMARK 3 S TENSOR
REMARK 3 S11: -0.0793 S12: -0.1524 S13: -0.0016
REMARK 3 S21: 0.1540 S22: -0.0273 S23: 0.2938
REMARK 3 S31: -0.3187 S32: -0.3550 S33: 0.1066
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 U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 4PHC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-MAY-14.
REMARK 100 THE DEPOSITION ID IS D_1000201392.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-FEB-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL12-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : LIQUID NITROGEN-COOLED DOUBLE
REMARK 200 CRYSTAL, SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS 0.1.27
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 2.5.2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49252
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.840
REMARK 200 RESOLUTION RANGE LOW (A) : 39.410
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.3
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.14800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.84
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.94
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.98300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS PH 7 TO 9, 0.2 M MGCL2 AND
REMARK 280 20 TO 32.5% PEG 3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 44.54350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 130.54150
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.49650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 130.54150
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 44.54350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.49650
REMARK 290 SMTRY3 4 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: 8360 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 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: 8450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 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 MET A 1
REMARK 465 ALA A 2
REMARK 465 GLU A 3
REMARK 465 ARG A 4
REMARK 465 ALA A 5
REMARK 465 ALA A 6
REMARK 465 LEU A 7
REMARK 465 GLU A 8
REMARK 465 GLU A 9
REMARK 465 LEU A 10
REMARK 465 VAL A 11
REMARK 465 LYS A 12
REMARK 465 LEU A 13
REMARK 465 GLN A 14
REMARK 465 GLY A 15
REMARK 465 GLU A 16
REMARK 465 ARG A 17
REMARK 465 VAL A 18
REMARK 465 ARG A 19
REMARK 465 GLY A 20
REMARK 465 LEU A 21
REMARK 465 LYS A 22
REMARK 465 GLN A 23
REMARK 465 GLN A 24
REMARK 465 LYS A 25
REMARK 465 ALA A 26
REMARK 465 SER A 27
REMARK 465 ALA A 28
REMARK 465 GLU A 29
REMARK 465 LEU A 30
REMARK 465 ILE A 31
REMARK 465 GLU A 32
REMARK 465 GLU A 33
REMARK 465 GLU A 34
REMARK 465 VAL A 35
REMARK 465 ALA A 36
REMARK 465 LYS A 37
REMARK 465 LEU A 38
REMARK 465 LEU A 39
REMARK 465 LYS A 40
REMARK 465 LEU A 41
REMARK 465 LYS A 42
REMARK 465 ALA A 43
REMARK 465 GLN A 44
REMARK 465 LEU A 45
REMARK 465 GLY A 46
REMARK 465 PRO A 47
REMARK 465 ASP A 48
REMARK 465 GLU A 49
REMARK 465 SER A 50
REMARK 465 LYS A 51
REMARK 465 GLN A 52
REMARK 465 PRO A 344
REMARK 465 ALA A 345
REMARK 465 GLN A 346
REMARK 465 ALA A 347
REMARK 465 GLY A 348
REMARK 465 GLU A 349
REMARK 465 GLU A 401
REMARK 465 GLU A 402
REMARK 465 PRO A 505
REMARK 465 LEU A 506
REMARK 465 CYS A 507
REMARK 465 ILE A 508
REMARK 465 CYS A 509
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 GLU B 3
REMARK 465 ARG B 4
REMARK 465 ALA B 5
REMARK 465 ALA B 6
REMARK 465 LEU B 7
REMARK 465 GLU B 8
REMARK 465 GLU B 9
REMARK 465 LEU B 10
REMARK 465 VAL B 11
REMARK 465 LYS B 12
REMARK 465 LEU B 13
REMARK 465 GLN B 14
REMARK 465 GLY B 15
REMARK 465 GLU B 16
REMARK 465 ARG B 17
REMARK 465 VAL B 18
REMARK 465 ARG B 19
REMARK 465 GLY B 20
REMARK 465 LEU B 21
REMARK 465 LYS B 22
REMARK 465 GLN B 23
REMARK 465 GLN B 24
REMARK 465 LYS B 25
REMARK 465 ALA B 26
REMARK 465 SER B 27
REMARK 465 ALA B 28
REMARK 465 GLU B 29
REMARK 465 LEU B 30
REMARK 465 ILE B 31
REMARK 465 GLU B 32
REMARK 465 GLU B 33
REMARK 465 GLU B 34
REMARK 465 VAL B 35
REMARK 465 ALA B 36
REMARK 465 LYS B 37
REMARK 465 LEU B 38
REMARK 465 LEU B 39
REMARK 465 LYS B 40
REMARK 465 LEU B 41
REMARK 465 LYS B 42
REMARK 465 ALA B 43
REMARK 465 GLN B 44
REMARK 465 LEU B 45
REMARK 465 GLY B 46
REMARK 465 PRO B 47
REMARK 465 ASP B 48
REMARK 465 GLU B 49
REMARK 465 SER B 50
REMARK 465 LYS B 51
REMARK 465 GLN B 52
REMARK 465 ALA B 347
REMARK 465 GLY B 348
REMARK 465 GLU B 349
REMARK 465 GLU B 350
REMARK 465 PRO B 351
REMARK 465 LEU B 352
REMARK 465 GLY B 353
REMARK 465 VAL B 354
REMARK 465 GLY B 355
REMARK 465 GLU B 401
REMARK 465 GLU B 402
REMARK 465 PRO B 505
REMARK 465 LEU B 506
REMARK 465 CYS B 507
REMARK 465 ILE B 508
REMARK 465 CYS B 509
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 GLU C 3
REMARK 465 ARG C 4
REMARK 465 ALA C 5
REMARK 465 ALA C 6
REMARK 465 LEU C 7
REMARK 465 GLU C 8
REMARK 465 GLU C 9
REMARK 465 LEU C 10
REMARK 465 VAL C 11
REMARK 465 LYS C 12
REMARK 465 LEU C 13
REMARK 465 GLN C 14
REMARK 465 GLY C 15
REMARK 465 GLU C 16
REMARK 465 ARG C 17
REMARK 465 VAL C 18
REMARK 465 ARG C 19
REMARK 465 GLY C 20
REMARK 465 LEU C 21
REMARK 465 LYS C 22
REMARK 465 GLN C 23
REMARK 465 GLN C 24
REMARK 465 LYS C 25
REMARK 465 ALA C 26
REMARK 465 SER C 27
REMARK 465 ALA C 28
REMARK 465 GLU C 29
REMARK 465 LEU C 30
REMARK 465 ILE C 31
REMARK 465 GLU C 32
REMARK 465 GLU C 33
REMARK 465 GLU C 34
REMARK 465 VAL C 35
REMARK 465 ALA C 36
REMARK 465 LYS C 37
REMARK 465 LEU C 38
REMARK 465 LEU C 39
REMARK 465 LYS C 40
REMARK 465 LEU C 41
REMARK 465 LYS C 42
REMARK 465 ALA C 43
REMARK 465 GLN C 44
REMARK 465 LEU C 45
REMARK 465 GLY C 46
REMARK 465 PRO C 47
REMARK 465 ASP C 48
REMARK 465 GLU C 49
REMARK 465 SER C 50
REMARK 465 LYS C 51
REMARK 465 GLN C 52
REMARK 465 ALA C 345
REMARK 465 GLN C 346
REMARK 465 ALA C 347
REMARK 465 GLY C 348
REMARK 465 GLU C 349
REMARK 465 GLU C 350
REMARK 465 PRO C 351
REMARK 465 LEU C 352
REMARK 465 GLY C 353
REMARK 465 VAL C 354
REMARK 465 GLU C 401
REMARK 465 GLU C 402
REMARK 465 PRO C 505
REMARK 465 LEU C 506
REMARK 465 CYS C 507
REMARK 465 ILE C 508
REMARK 465 CYS C 509
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 GLU D 3
REMARK 465 ARG D 4
REMARK 465 ALA D 5
REMARK 465 ALA D 6
REMARK 465 LEU D 7
REMARK 465 GLU D 8
REMARK 465 GLU D 9
REMARK 465 LEU D 10
REMARK 465 VAL D 11
REMARK 465 LYS D 12
REMARK 465 LEU D 13
REMARK 465 GLN D 14
REMARK 465 GLY D 15
REMARK 465 GLU D 16
REMARK 465 ARG D 17
REMARK 465 VAL D 18
REMARK 465 ARG D 19
REMARK 465 GLY D 20
REMARK 465 LEU D 21
REMARK 465 LYS D 22
REMARK 465 GLN D 23
REMARK 465 GLN D 24
REMARK 465 LYS D 25
REMARK 465 ALA D 26
REMARK 465 SER D 27
REMARK 465 ALA D 28
REMARK 465 GLU D 29
REMARK 465 LEU D 30
REMARK 465 ILE D 31
REMARK 465 GLU D 32
REMARK 465 GLU D 33
REMARK 465 GLU D 34
REMARK 465 VAL D 35
REMARK 465 ALA D 36
REMARK 465 LYS D 37
REMARK 465 LEU D 38
REMARK 465 LEU D 39
REMARK 465 LYS D 40
REMARK 465 LEU D 41
REMARK 465 LYS D 42
REMARK 465 ALA D 43
REMARK 465 GLN D 44
REMARK 465 LEU D 45
REMARK 465 GLY D 46
REMARK 465 PRO D 47
REMARK 465 ASP D 48
REMARK 465 GLU D 49
REMARK 465 SER D 50
REMARK 465 LYS D 51
REMARK 465 GLN D 52
REMARK 465 GLN D 346
REMARK 465 ALA D 347
REMARK 465 GLY D 348
REMARK 465 GLU D 349
REMARK 465 GLU D 350
REMARK 465 PRO D 351
REMARK 465 LEU D 352
REMARK 465 GLY D 353
REMARK 465 VAL D 354
REMARK 465 GLY D 355
REMARK 465 PRO D 505
REMARK 465 LEU D 506
REMARK 465 CYS D 507
REMARK 465 ILE D 508
REMARK 465 CYS D 509
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 LYS A 53 CG CD CE NZ
REMARK 470 LYS A 60 CG CD CE NZ
REMARK 470 GLU A 109 CG CD OE1 OE2
REMARK 470 LYS A 112 CG CD CE NZ
REMARK 470 ARG A 214 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 232 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 256 CG CD OE1 OE2
REMARK 470 LYS A 257 CG CD CE NZ
REMARK 470 GLU A 350 CG CD OE1 OE2
REMARK 470 LYS A 403 CG CD CE NZ
REMARK 470 LYS B 53 CG CD CE NZ
REMARK 470 ARG B 63 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 165 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 403 CG CD CE NZ
REMARK 470 GLN B 504 CG CD OE1 NE2
REMARK 470 ARG C 63 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 112 CG CD CE NZ
REMARK 470 ARG C 165 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 403 CG CD CE NZ
REMARK 470 LYS C 447 CG CD CE NZ
REMARK 470 LYS D 53 CG CD CE NZ
REMARK 470 GLN D 285 CG CD OE1 NE2
REMARK 470 LYS D 288 CG CD CE NZ
REMARK 470 LYS D 403 CG CD CE NZ
REMARK 470 LYS D 444 CG CD CE NZ
REMARK 470 GLN D 504 CG CD OE1 NE2
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 MET A 185 -2.42 71.06
REMARK 500 LEU A 352 -75.90 -79.27
REMARK 500 MET B 185 -2.37 70.22
REMARK 500 MET C 185 -1.80 69.74
REMARK 500 LYS D 57 141.82 -171.37
REMARK 500 MET D 185 -1.92 70.44
REMARK 500 LEU D 341 -76.98 -69.13
REMARK 500 GLU D 401 34.30 39.81
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 HIS A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HIS B 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HIS C 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HIS D 1001
DBREF 4PHC A 1 509 UNP P12081 SYHC_HUMAN 1 509
DBREF 4PHC B 1 509 UNP P12081 SYHC_HUMAN 1 509
DBREF 4PHC C 1 509 UNP P12081 SYHC_HUMAN 1 509
DBREF 4PHC D 1 509 UNP P12081 SYHC_HUMAN 1 509
SEQRES 1 A 509 MET ALA GLU ARG ALA ALA LEU GLU GLU LEU VAL LYS LEU
SEQRES 2 A 509 GLN GLY GLU ARG VAL ARG GLY LEU LYS GLN GLN LYS ALA
SEQRES 3 A 509 SER ALA GLU LEU ILE GLU GLU GLU VAL ALA LYS LEU LEU
SEQRES 4 A 509 LYS LEU LYS ALA GLN LEU GLY PRO ASP GLU SER LYS GLN
SEQRES 5 A 509 LYS PHE VAL LEU LYS THR PRO LYS GLY THR ARG ASP TYR
SEQRES 6 A 509 SER PRO ARG GLN MET ALA VAL ARG GLU LYS VAL PHE ASP
SEQRES 7 A 509 VAL ILE ILE ARG CYS PHE LYS ARG HIS GLY ALA GLU VAL
SEQRES 8 A 509 ILE ASP THR PRO VAL PHE GLU LEU LYS GLU THR LEU MET
SEQRES 9 A 509 GLY LYS TYR GLY GLU ASP SER LYS LEU ILE TYR ASP LEU
SEQRES 10 A 509 LYS ASP GLN GLY GLY GLU LEU LEU SER LEU ARG TYR ASP
SEQRES 11 A 509 LEU THR VAL PRO PHE ALA ARG TYR LEU ALA MET ASN LYS
SEQRES 12 A 509 LEU THR ASN ILE LYS ARG TYR HIS ILE ALA LYS VAL TYR
SEQRES 13 A 509 ARG ARG ASP ASN PRO ALA MET THR ARG GLY ARG TYR ARG
SEQRES 14 A 509 GLU PHE TYR GLN CYS ASP PHE ASP ILE ALA GLY ASN PHE
SEQRES 15 A 509 ASP PRO MET ILE PRO ASP ALA GLU CYS LEU LYS ILE MET
SEQRES 16 A 509 CYS GLU ILE LEU SER SER LEU GLN ILE GLY ASP PHE LEU
SEQRES 17 A 509 VAL LYS VAL ASN ASP ARG ARG ILE LEU ASP GLY MET PHE
SEQRES 18 A 509 ALA ILE CYS GLY VAL SER ASP SER LYS PHE ARG THR ILE
SEQRES 19 A 509 CYS SER SER VAL ASP LYS LEU ASP LYS VAL SER TRP GLU
SEQRES 20 A 509 GLU VAL LYS ASN GLU MET VAL GLY GLU LYS GLY LEU ALA
SEQRES 21 A 509 PRO GLU VAL ALA ASP ARG ILE GLY ASP TYR VAL GLN GLN
SEQRES 22 A 509 HIS GLY GLY VAL SER LEU VAL GLU GLN LEU LEU GLN ASP
SEQRES 23 A 509 PRO LYS LEU SER GLN ASN LYS GLN ALA LEU GLU GLY LEU
SEQRES 24 A 509 GLY ASP LEU LYS LEU LEU PHE GLU TYR LEU THR LEU PHE
SEQRES 25 A 509 GLY ILE ASP ASP LYS ILE SER PHE ASP LEU SER LEU ALA
SEQRES 26 A 509 ARG GLY LEU ASP TYR TYR THR GLY VAL ILE TYR GLU ALA
SEQRES 27 A 509 VAL LEU LEU GLN THR PRO ALA GLN ALA GLY GLU GLU PRO
SEQRES 28 A 509 LEU GLY VAL GLY SER VAL ALA ALA GLY GLY ARG TYR ASP
SEQRES 29 A 509 GLY LEU VAL GLY MET PHE ASP PRO LYS GLY ARG LYS VAL
SEQRES 30 A 509 PRO CYS VAL GLY LEU SER ILE GLY VAL GLU ARG ILE PHE
SEQRES 31 A 509 SER ILE VAL GLU GLN ARG LEU GLU ALA LEU GLU GLU LYS
SEQRES 32 A 509 ILE ARG THR THR GLU THR GLN VAL LEU VAL ALA SER ALA
SEQRES 33 A 509 GLN LYS LYS LEU LEU GLU GLU ARG LEU LYS LEU VAL SER
SEQRES 34 A 509 GLU LEU TRP ASP ALA GLY ILE LYS ALA GLU LEU LEU TYR
SEQRES 35 A 509 LYS LYS ASN PRO LYS LEU LEU ASN GLN LEU GLN TYR CYS
SEQRES 36 A 509 GLU GLU ALA GLY ILE PRO LEU VAL ALA ILE ILE GLY GLU
SEQRES 37 A 509 GLN GLU LEU LYS ASP GLY VAL ILE LYS LEU ARG SER VAL
SEQRES 38 A 509 THR SER ARG GLU GLU VAL ASP VAL ARG ARG GLU ASP LEU
SEQRES 39 A 509 VAL GLU GLU ILE LYS ARG ARG THR GLY GLN PRO LEU CYS
SEQRES 40 A 509 ILE CYS
SEQRES 1 B 509 MET ALA GLU ARG ALA ALA LEU GLU GLU LEU VAL LYS LEU
SEQRES 2 B 509 GLN GLY GLU ARG VAL ARG GLY LEU LYS GLN GLN LYS ALA
SEQRES 3 B 509 SER ALA GLU LEU ILE GLU GLU GLU VAL ALA LYS LEU LEU
SEQRES 4 B 509 LYS LEU LYS ALA GLN LEU GLY PRO ASP GLU SER LYS GLN
SEQRES 5 B 509 LYS PHE VAL LEU LYS THR PRO LYS GLY THR ARG ASP TYR
SEQRES 6 B 509 SER PRO ARG GLN MET ALA VAL ARG GLU LYS VAL PHE ASP
SEQRES 7 B 509 VAL ILE ILE ARG CYS PHE LYS ARG HIS GLY ALA GLU VAL
SEQRES 8 B 509 ILE ASP THR PRO VAL PHE GLU LEU LYS GLU THR LEU MET
SEQRES 9 B 509 GLY LYS TYR GLY GLU ASP SER LYS LEU ILE TYR ASP LEU
SEQRES 10 B 509 LYS ASP GLN GLY GLY GLU LEU LEU SER LEU ARG TYR ASP
SEQRES 11 B 509 LEU THR VAL PRO PHE ALA ARG TYR LEU ALA MET ASN LYS
SEQRES 12 B 509 LEU THR ASN ILE LYS ARG TYR HIS ILE ALA LYS VAL TYR
SEQRES 13 B 509 ARG ARG ASP ASN PRO ALA MET THR ARG GLY ARG TYR ARG
SEQRES 14 B 509 GLU PHE TYR GLN CYS ASP PHE ASP ILE ALA GLY ASN PHE
SEQRES 15 B 509 ASP PRO MET ILE PRO ASP ALA GLU CYS LEU LYS ILE MET
SEQRES 16 B 509 CYS GLU ILE LEU SER SER LEU GLN ILE GLY ASP PHE LEU
SEQRES 17 B 509 VAL LYS VAL ASN ASP ARG ARG ILE LEU ASP GLY MET PHE
SEQRES 18 B 509 ALA ILE CYS GLY VAL SER ASP SER LYS PHE ARG THR ILE
SEQRES 19 B 509 CYS SER SER VAL ASP LYS LEU ASP LYS VAL SER TRP GLU
SEQRES 20 B 509 GLU VAL LYS ASN GLU MET VAL GLY GLU LYS GLY LEU ALA
SEQRES 21 B 509 PRO GLU VAL ALA ASP ARG ILE GLY ASP TYR VAL GLN GLN
SEQRES 22 B 509 HIS GLY GLY VAL SER LEU VAL GLU GLN LEU LEU GLN ASP
SEQRES 23 B 509 PRO LYS LEU SER GLN ASN LYS GLN ALA LEU GLU GLY LEU
SEQRES 24 B 509 GLY ASP LEU LYS LEU LEU PHE GLU TYR LEU THR LEU PHE
SEQRES 25 B 509 GLY ILE ASP ASP LYS ILE SER PHE ASP LEU SER LEU ALA
SEQRES 26 B 509 ARG GLY LEU ASP TYR TYR THR GLY VAL ILE TYR GLU ALA
SEQRES 27 B 509 VAL LEU LEU GLN THR PRO ALA GLN ALA GLY GLU GLU PRO
SEQRES 28 B 509 LEU GLY VAL GLY SER VAL ALA ALA GLY GLY ARG TYR ASP
SEQRES 29 B 509 GLY LEU VAL GLY MET PHE ASP PRO LYS GLY ARG LYS VAL
SEQRES 30 B 509 PRO CYS VAL GLY LEU SER ILE GLY VAL GLU ARG ILE PHE
SEQRES 31 B 509 SER ILE VAL GLU GLN ARG LEU GLU ALA LEU GLU GLU LYS
SEQRES 32 B 509 ILE ARG THR THR GLU THR GLN VAL LEU VAL ALA SER ALA
SEQRES 33 B 509 GLN LYS LYS LEU LEU GLU GLU ARG LEU LYS LEU VAL SER
SEQRES 34 B 509 GLU LEU TRP ASP ALA GLY ILE LYS ALA GLU LEU LEU TYR
SEQRES 35 B 509 LYS LYS ASN PRO LYS LEU LEU ASN GLN LEU GLN TYR CYS
SEQRES 36 B 509 GLU GLU ALA GLY ILE PRO LEU VAL ALA ILE ILE GLY GLU
SEQRES 37 B 509 GLN GLU LEU LYS ASP GLY VAL ILE LYS LEU ARG SER VAL
SEQRES 38 B 509 THR SER ARG GLU GLU VAL ASP VAL ARG ARG GLU ASP LEU
SEQRES 39 B 509 VAL GLU GLU ILE LYS ARG ARG THR GLY GLN PRO LEU CYS
SEQRES 40 B 509 ILE CYS
SEQRES 1 C 509 MET ALA GLU ARG ALA ALA LEU GLU GLU LEU VAL LYS LEU
SEQRES 2 C 509 GLN GLY GLU ARG VAL ARG GLY LEU LYS GLN GLN LYS ALA
SEQRES 3 C 509 SER ALA GLU LEU ILE GLU GLU GLU VAL ALA LYS LEU LEU
SEQRES 4 C 509 LYS LEU LYS ALA GLN LEU GLY PRO ASP GLU SER LYS GLN
SEQRES 5 C 509 LYS PHE VAL LEU LYS THR PRO LYS GLY THR ARG ASP TYR
SEQRES 6 C 509 SER PRO ARG GLN MET ALA VAL ARG GLU LYS VAL PHE ASP
SEQRES 7 C 509 VAL ILE ILE ARG CYS PHE LYS ARG HIS GLY ALA GLU VAL
SEQRES 8 C 509 ILE ASP THR PRO VAL PHE GLU LEU LYS GLU THR LEU MET
SEQRES 9 C 509 GLY LYS TYR GLY GLU ASP SER LYS LEU ILE TYR ASP LEU
SEQRES 10 C 509 LYS ASP GLN GLY GLY GLU LEU LEU SER LEU ARG TYR ASP
SEQRES 11 C 509 LEU THR VAL PRO PHE ALA ARG TYR LEU ALA MET ASN LYS
SEQRES 12 C 509 LEU THR ASN ILE LYS ARG TYR HIS ILE ALA LYS VAL TYR
SEQRES 13 C 509 ARG ARG ASP ASN PRO ALA MET THR ARG GLY ARG TYR ARG
SEQRES 14 C 509 GLU PHE TYR GLN CYS ASP PHE ASP ILE ALA GLY ASN PHE
SEQRES 15 C 509 ASP PRO MET ILE PRO ASP ALA GLU CYS LEU LYS ILE MET
SEQRES 16 C 509 CYS GLU ILE LEU SER SER LEU GLN ILE GLY ASP PHE LEU
SEQRES 17 C 509 VAL LYS VAL ASN ASP ARG ARG ILE LEU ASP GLY MET PHE
SEQRES 18 C 509 ALA ILE CYS GLY VAL SER ASP SER LYS PHE ARG THR ILE
SEQRES 19 C 509 CYS SER SER VAL ASP LYS LEU ASP LYS VAL SER TRP GLU
SEQRES 20 C 509 GLU VAL LYS ASN GLU MET VAL GLY GLU LYS GLY LEU ALA
SEQRES 21 C 509 PRO GLU VAL ALA ASP ARG ILE GLY ASP TYR VAL GLN GLN
SEQRES 22 C 509 HIS GLY GLY VAL SER LEU VAL GLU GLN LEU LEU GLN ASP
SEQRES 23 C 509 PRO LYS LEU SER GLN ASN LYS GLN ALA LEU GLU GLY LEU
SEQRES 24 C 509 GLY ASP LEU LYS LEU LEU PHE GLU TYR LEU THR LEU PHE
SEQRES 25 C 509 GLY ILE ASP ASP LYS ILE SER PHE ASP LEU SER LEU ALA
SEQRES 26 C 509 ARG GLY LEU ASP TYR TYR THR GLY VAL ILE TYR GLU ALA
SEQRES 27 C 509 VAL LEU LEU GLN THR PRO ALA GLN ALA GLY GLU GLU PRO
SEQRES 28 C 509 LEU GLY VAL GLY SER VAL ALA ALA GLY GLY ARG TYR ASP
SEQRES 29 C 509 GLY LEU VAL GLY MET PHE ASP PRO LYS GLY ARG LYS VAL
SEQRES 30 C 509 PRO CYS VAL GLY LEU SER ILE GLY VAL GLU ARG ILE PHE
SEQRES 31 C 509 SER ILE VAL GLU GLN ARG LEU GLU ALA LEU GLU GLU LYS
SEQRES 32 C 509 ILE ARG THR THR GLU THR GLN VAL LEU VAL ALA SER ALA
SEQRES 33 C 509 GLN LYS LYS LEU LEU GLU GLU ARG LEU LYS LEU VAL SER
SEQRES 34 C 509 GLU LEU TRP ASP ALA GLY ILE LYS ALA GLU LEU LEU TYR
SEQRES 35 C 509 LYS LYS ASN PRO LYS LEU LEU ASN GLN LEU GLN TYR CYS
SEQRES 36 C 509 GLU GLU ALA GLY ILE PRO LEU VAL ALA ILE ILE GLY GLU
SEQRES 37 C 509 GLN GLU LEU LYS ASP GLY VAL ILE LYS LEU ARG SER VAL
SEQRES 38 C 509 THR SER ARG GLU GLU VAL ASP VAL ARG ARG GLU ASP LEU
SEQRES 39 C 509 VAL GLU GLU ILE LYS ARG ARG THR GLY GLN PRO LEU CYS
SEQRES 40 C 509 ILE CYS
SEQRES 1 D 509 MET ALA GLU ARG ALA ALA LEU GLU GLU LEU VAL LYS LEU
SEQRES 2 D 509 GLN GLY GLU ARG VAL ARG GLY LEU LYS GLN GLN LYS ALA
SEQRES 3 D 509 SER ALA GLU LEU ILE GLU GLU GLU VAL ALA LYS LEU LEU
SEQRES 4 D 509 LYS LEU LYS ALA GLN LEU GLY PRO ASP GLU SER LYS GLN
SEQRES 5 D 509 LYS PHE VAL LEU LYS THR PRO LYS GLY THR ARG ASP TYR
SEQRES 6 D 509 SER PRO ARG GLN MET ALA VAL ARG GLU LYS VAL PHE ASP
SEQRES 7 D 509 VAL ILE ILE ARG CYS PHE LYS ARG HIS GLY ALA GLU VAL
SEQRES 8 D 509 ILE ASP THR PRO VAL PHE GLU LEU LYS GLU THR LEU MET
SEQRES 9 D 509 GLY LYS TYR GLY GLU ASP SER LYS LEU ILE TYR ASP LEU
SEQRES 10 D 509 LYS ASP GLN GLY GLY GLU LEU LEU SER LEU ARG TYR ASP
SEQRES 11 D 509 LEU THR VAL PRO PHE ALA ARG TYR LEU ALA MET ASN LYS
SEQRES 12 D 509 LEU THR ASN ILE LYS ARG TYR HIS ILE ALA LYS VAL TYR
SEQRES 13 D 509 ARG ARG ASP ASN PRO ALA MET THR ARG GLY ARG TYR ARG
SEQRES 14 D 509 GLU PHE TYR GLN CYS ASP PHE ASP ILE ALA GLY ASN PHE
SEQRES 15 D 509 ASP PRO MET ILE PRO ASP ALA GLU CYS LEU LYS ILE MET
SEQRES 16 D 509 CYS GLU ILE LEU SER SER LEU GLN ILE GLY ASP PHE LEU
SEQRES 17 D 509 VAL LYS VAL ASN ASP ARG ARG ILE LEU ASP GLY MET PHE
SEQRES 18 D 509 ALA ILE CYS GLY VAL SER ASP SER LYS PHE ARG THR ILE
SEQRES 19 D 509 CYS SER SER VAL ASP LYS LEU ASP LYS VAL SER TRP GLU
SEQRES 20 D 509 GLU VAL LYS ASN GLU MET VAL GLY GLU LYS GLY LEU ALA
SEQRES 21 D 509 PRO GLU VAL ALA ASP ARG ILE GLY ASP TYR VAL GLN GLN
SEQRES 22 D 509 HIS GLY GLY VAL SER LEU VAL GLU GLN LEU LEU GLN ASP
SEQRES 23 D 509 PRO LYS LEU SER GLN ASN LYS GLN ALA LEU GLU GLY LEU
SEQRES 24 D 509 GLY ASP LEU LYS LEU LEU PHE GLU TYR LEU THR LEU PHE
SEQRES 25 D 509 GLY ILE ASP ASP LYS ILE SER PHE ASP LEU SER LEU ALA
SEQRES 26 D 509 ARG GLY LEU ASP TYR TYR THR GLY VAL ILE TYR GLU ALA
SEQRES 27 D 509 VAL LEU LEU GLN THR PRO ALA GLN ALA GLY GLU GLU PRO
SEQRES 28 D 509 LEU GLY VAL GLY SER VAL ALA ALA GLY GLY ARG TYR ASP
SEQRES 29 D 509 GLY LEU VAL GLY MET PHE ASP PRO LYS GLY ARG LYS VAL
SEQRES 30 D 509 PRO CYS VAL GLY LEU SER ILE GLY VAL GLU ARG ILE PHE
SEQRES 31 D 509 SER ILE VAL GLU GLN ARG LEU GLU ALA LEU GLU GLU LYS
SEQRES 32 D 509 ILE ARG THR THR GLU THR GLN VAL LEU VAL ALA SER ALA
SEQRES 33 D 509 GLN LYS LYS LEU LEU GLU GLU ARG LEU LYS LEU VAL SER
SEQRES 34 D 509 GLU LEU TRP ASP ALA GLY ILE LYS ALA GLU LEU LEU TYR
SEQRES 35 D 509 LYS LYS ASN PRO LYS LEU LEU ASN GLN LEU GLN TYR CYS
SEQRES 36 D 509 GLU GLU ALA GLY ILE PRO LEU VAL ALA ILE ILE GLY GLU
SEQRES 37 D 509 GLN GLU LEU LYS ASP GLY VAL ILE LYS LEU ARG SER VAL
SEQRES 38 D 509 THR SER ARG GLU GLU VAL ASP VAL ARG ARG GLU ASP LEU
SEQRES 39 D 509 VAL GLU GLU ILE LYS ARG ARG THR GLY GLN PRO LEU CYS
SEQRES 40 D 509 ILE CYS
HET HIS A1001 11
HET GOL A1002 6
HET HIS B1001 11
HET GOL B1002 6
HET HIS C1001 11
HET GOL C1002 6
HET GOL C1003 6
HET HIS D1001 11
HETNAM HIS HISTIDINE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 HIS 4(C6 H10 N3 O2 1+)
FORMUL 6 GOL 4(C3 H8 O3)
FORMUL 13 HOH *55(H2 O)
HELIX 1 AA1 SER A 66 HIS A 87 1 22
HELIX 2 AA2 LYS A 100 MET A 104 1 5
HELIX 3 AA3 GLY A 108 ILE A 114 5 7
HELIX 4 AA4 LEU A 131 ASN A 142 1 12
HELIX 5 AA5 MET A 185 GLN A 203 1 19
HELIX 6 AA6 ARG A 214 GLY A 225 1 12
HELIX 7 AA7 SER A 227 SER A 229 5 3
HELIX 8 AA8 LYS A 230 ASP A 239 1 10
HELIX 9 AA9 LYS A 240 LYS A 243 5 4
HELIX 10 AB1 SER A 245 GLU A 256 1 12
HELIX 11 AB2 ALA A 260 GLN A 272 1 13
HELIX 12 AB3 GLY A 276 GLN A 285 1 10
HELIX 13 AB4 LYS A 288 GLN A 291 5 4
HELIX 14 AB5 ASN A 292 PHE A 312 1 21
HELIX 15 AB6 ILE A 314 ASP A 316 5 3
HELIX 16 AB7 GLY A 365 ASP A 371 1 7
HELIX 17 AB8 VAL A 386 LEU A 400 1 15
HELIX 18 AB9 LEU A 420 ALA A 434 1 15
HELIX 19 AC1 LYS A 447 GLY A 459 1 13
HELIX 20 AC2 GLY A 467 GLY A 474 1 8
HELIX 21 AC3 ASP A 493 THR A 502 1 10
HELIX 22 AC4 SER B 66 HIS B 87 1 22
HELIX 23 AC5 LYS B 100 MET B 104 1 5
HELIX 24 AC6 GLY B 108 ILE B 114 5 7
HELIX 25 AC7 LEU B 131 LYS B 143 1 13
HELIX 26 AC8 MET B 185 GLN B 203 1 19
HELIX 27 AC9 ARG B 214 GLY B 225 1 12
HELIX 28 AD1 SER B 227 SER B 229 5 3
HELIX 29 AD2 LYS B 230 ASP B 239 1 10
HELIX 30 AD3 LYS B 240 LYS B 243 5 4
HELIX 31 AD4 SER B 245 GLU B 256 1 12
HELIX 32 AD5 ALA B 260 GLN B 272 1 13
HELIX 33 AD6 GLY B 276 GLN B 285 1 10
HELIX 34 AD7 LYS B 288 GLN B 291 5 4
HELIX 35 AD8 ASN B 292 PHE B 312 1 21
HELIX 36 AD9 ILE B 314 ASP B 316 5 3
HELIX 37 AE1 GLY B 365 ASP B 371 1 7
HELIX 38 AE2 VAL B 386 LEU B 400 1 15
HELIX 39 AE3 LEU B 420 ALA B 434 1 15
HELIX 40 AE4 LYS B 447 GLY B 459 1 13
HELIX 41 AE5 GLY B 467 GLY B 474 1 8
HELIX 42 AE6 ASP B 493 THR B 502 1 10
HELIX 43 AE7 SER C 66 HIS C 87 1 22
HELIX 44 AE8 LYS C 100 MET C 104 1 5
HELIX 45 AE9 GLY C 108 ILE C 114 5 7
HELIX 46 AF1 LEU C 131 LYS C 143 1 13
HELIX 47 AF2 MET C 185 GLN C 203 1 19
HELIX 48 AF3 ARG C 214 GLY C 225 1 12
HELIX 49 AF4 SER C 227 SER C 229 5 3
HELIX 50 AF5 LYS C 230 ASP C 239 1 10
HELIX 51 AF6 LYS C 240 LYS C 243 5 4
HELIX 52 AF7 SER C 245 GLU C 256 1 12
HELIX 53 AF8 ALA C 260 GLN C 272 1 13
HELIX 54 AF9 GLY C 276 GLN C 285 1 10
HELIX 55 AG1 LYS C 288 GLN C 291 5 4
HELIX 56 AG2 ASN C 292 PHE C 312 1 21
HELIX 57 AG3 ILE C 314 ASP C 316 5 3
HELIX 58 AG4 GLY C 365 ASP C 371 1 7
HELIX 59 AG5 VAL C 386 LEU C 400 1 15
HELIX 60 AG6 LEU C 420 ALA C 434 1 15
HELIX 61 AG7 LYS C 447 GLY C 459 1 13
HELIX 62 AG8 GLY C 467 GLY C 474 1 8
HELIX 63 AG9 ASP C 493 THR C 502 1 10
HELIX 64 AH1 SER D 66 HIS D 87 1 22
HELIX 65 AH2 LYS D 100 MET D 104 1 5
HELIX 66 AH3 GLY D 108 ILE D 114 5 7
HELIX 67 AH4 LEU D 131 LYS D 143 1 13
HELIX 68 AH5 MET D 185 GLN D 203 1 19
HELIX 69 AH6 ARG D 214 GLY D 225 1 12
HELIX 70 AH7 SER D 227 SER D 229 5 3
HELIX 71 AH8 LYS D 230 ASP D 239 1 10
HELIX 72 AH9 LYS D 240 LYS D 243 5 4
HELIX 73 AI1 SER D 245 GLU D 256 1 12
HELIX 74 AI2 ALA D 260 GLN D 272 1 13
HELIX 75 AI3 GLY D 276 GLN D 285 1 10
HELIX 76 AI4 LYS D 288 GLN D 291 5 4
HELIX 77 AI5 ASN D 292 PHE D 312 1 21
HELIX 78 AI6 ILE D 314 ASP D 316 5 3
HELIX 79 AI7 GLY D 365 ASP D 371 1 7
HELIX 80 AI8 VAL D 386 LEU D 400 1 15
HELIX 81 AI9 LEU D 420 ALA D 434 1 15
HELIX 82 AJ1 LYS D 447 GLY D 459 1 13
HELIX 83 AJ2 GLY D 467 GLY D 474 1 8
HELIX 84 AJ3 ASP D 493 THR D 502 1 10
SHEET 1 AA1 9 GLU A 90 VAL A 91 0
SHEET 2 AA1 9 ILE A 147 TYR A 156 1 O LYS A 148 N GLU A 90
SHEET 3 AA1 9 GLU A 170 ALA A 179 -1 O ALA A 179 N ILE A 147
SHEET 4 AA1 9 CYS A 379 GLY A 385 -1 O VAL A 380 N ILE A 178
SHEET 5 AA1 9 GLY A 355 ARG A 362 -1 N ALA A 359 O SER A 383
SHEET 6 AA1 9 VAL A 334 LEU A 340 -1 N ALA A 338 O ALA A 358
SHEET 7 AA1 9 PHE A 207 ASP A 213 -1 N LEU A 208 O VAL A 339
SHEET 8 AA1 9 ILE A 318 ASP A 321 1 O SER A 319 N VAL A 211
SHEET 9 AA1 9 HIS A 274 GLY A 275 -1 N GLY A 275 O PHE A 320
SHEET 1 AA2 2 PHE A 97 LEU A 99 0
SHEET 2 AA2 2 LEU A 125 LEU A 127 -1 O SER A 126 N GLU A 98
SHEET 1 AA3 5 ALA A 438 GLU A 439 0
SHEET 2 AA3 5 VAL A 411 SER A 415 1 N VAL A 413 O GLU A 439
SHEET 3 AA3 5 LEU A 462 ILE A 466 1 O ALA A 464 N ALA A 414
SHEET 4 AA3 5 VAL A 475 SER A 480 -1 O LYS A 477 N ILE A 465
SHEET 5 AA3 5 GLU A 486 ARG A 490 -1 O VAL A 487 N LEU A 478
SHEET 1 AA4 9 GLU B 90 VAL B 91 0
SHEET 2 AA4 9 ILE B 147 TYR B 156 1 O TYR B 150 N GLU B 90
SHEET 3 AA4 9 GLU B 170 ALA B 179 -1 O ASP B 175 N HIS B 151
SHEET 4 AA4 9 CYS B 379 GLY B 385 -1 O VAL B 380 N ILE B 178
SHEET 5 AA4 9 ALA B 358 ARG B 362 -1 N ALA B 359 O SER B 383
SHEET 6 AA4 9 VAL B 334 LEU B 340 -1 N ALA B 338 O ALA B 358
SHEET 7 AA4 9 PHE B 207 ASP B 213 -1 N LEU B 208 O VAL B 339
SHEET 8 AA4 9 ILE B 318 ASP B 321 1 O SER B 319 N VAL B 211
SHEET 9 AA4 9 HIS B 274 GLY B 275 -1 N GLY B 275 O PHE B 320
SHEET 1 AA5 2 PHE B 97 LEU B 99 0
SHEET 2 AA5 2 LEU B 125 LEU B 127 -1 O SER B 126 N GLU B 98
SHEET 1 AA6 5 ALA B 438 GLU B 439 0
SHEET 2 AA6 5 VAL B 411 SER B 415 1 N VAL B 413 O GLU B 439
SHEET 3 AA6 5 LEU B 462 ILE B 466 1 O ALA B 464 N ALA B 414
SHEET 4 AA6 5 VAL B 475 SER B 480 -1 O LYS B 477 N ILE B 465
SHEET 5 AA6 5 GLU B 486 ARG B 490 -1 O VAL B 487 N LEU B 478
SHEET 1 AA7 9 GLU C 90 VAL C 91 0
SHEET 2 AA7 9 ILE C 147 TYR C 156 1 O TYR C 150 N GLU C 90
SHEET 3 AA7 9 GLU C 170 ALA C 179 -1 O ALA C 179 N ILE C 147
SHEET 4 AA7 9 CYS C 379 GLY C 385 -1 O VAL C 380 N ILE C 178
SHEET 5 AA7 9 ALA C 358 ARG C 362 -1 N ALA C 359 O SER C 383
SHEET 6 AA7 9 VAL C 334 LEU C 340 -1 N ALA C 338 O ALA C 358
SHEET 7 AA7 9 PHE C 207 ASP C 213 -1 N LEU C 208 O VAL C 339
SHEET 8 AA7 9 ILE C 318 ASP C 321 1 O SER C 319 N VAL C 211
SHEET 9 AA7 9 HIS C 274 GLY C 275 -1 N GLY C 275 O PHE C 320
SHEET 1 AA8 2 PHE C 97 LEU C 99 0
SHEET 2 AA8 2 LEU C 125 LEU C 127 -1 O SER C 126 N GLU C 98
SHEET 1 AA9 5 ALA C 438 GLU C 439 0
SHEET 2 AA9 5 VAL C 411 SER C 415 1 N VAL C 413 O GLU C 439
SHEET 3 AA9 5 LEU C 462 ILE C 466 1 O ALA C 464 N ALA C 414
SHEET 4 AA9 5 VAL C 475 SER C 480 -1 O LYS C 477 N ILE C 465
SHEET 5 AA9 5 GLU C 486 ARG C 490 -1 O VAL C 487 N LEU C 478
SHEET 1 AB1 9 GLU D 90 VAL D 91 0
SHEET 2 AB1 9 ILE D 147 TYR D 156 1 O TYR D 150 N GLU D 90
SHEET 3 AB1 9 GLU D 170 ALA D 179 -1 O ASP D 175 N HIS D 151
SHEET 4 AB1 9 CYS D 379 GLY D 385 -1 O VAL D 380 N ILE D 178
SHEET 5 AB1 9 ALA D 358 ARG D 362 -1 N ALA D 359 O SER D 383
SHEET 6 AB1 9 VAL D 334 LEU D 340 -1 N ALA D 338 O ALA D 358
SHEET 7 AB1 9 PHE D 207 ASP D 213 -1 N LEU D 208 O VAL D 339
SHEET 8 AB1 9 ILE D 318 ASP D 321 1 O SER D 319 N VAL D 209
SHEET 9 AB1 9 HIS D 274 GLY D 275 -1 N GLY D 275 O PHE D 320
SHEET 1 AB2 2 PHE D 97 LEU D 99 0
SHEET 2 AB2 2 LEU D 125 LEU D 127 -1 O SER D 126 N GLU D 98
SHEET 1 AB3 5 ALA D 438 GLU D 439 0
SHEET 2 AB3 5 VAL D 411 SER D 415 1 N VAL D 413 O GLU D 439
SHEET 3 AB3 5 LEU D 462 ILE D 466 1 O ALA D 464 N ALA D 414
SHEET 4 AB3 5 VAL D 475 SER D 480 -1 O LYS D 477 N ILE D 465
SHEET 5 AB3 5 GLU D 486 ARG D 490 -1 O VAL D 487 N LEU D 478
SITE 1 AC1 16 ASP A 130 THR A 132 ARG A 157 GLN A 173
SITE 2 AC1 16 ASP A 175 ASP A 177 ARG A 326 LEU A 328
SITE 3 AC1 16 TYR A 330 TYR A 331 GLY A 360 TYR A 363
SITE 4 AC1 16 GLY A 381 LEU A 382 SER A 383 HOH A1113
SITE 1 AC2 2 ASN A 146 TYR B 454
SITE 1 AC3 14 ASP B 130 THR B 132 ARG B 157 GLN B 173
SITE 2 AC3 14 ASP B 175 ASP B 177 ARG B 326 TYR B 330
SITE 3 AC3 14 TYR B 331 GLY B 360 TYR B 363 GLY B 381
SITE 4 AC3 14 LEU B 382 HOH B1116
SITE 1 AC4 2 TYR A 454 ASN B 146
SITE 1 AC5 13 ASP C 130 THR C 132 ARG C 157 GLN C 173
SITE 2 AC5 13 ASP C 175 ASP C 177 ARG C 326 LEU C 328
SITE 3 AC5 13 TYR C 330 TYR C 331 TYR C 363 GLY C 381
SITE 4 AC5 13 LEU C 382
SITE 1 AC6 2 ASN C 146 TYR D 454
SITE 1 AC7 3 TYR C 454 GLU D 90 ASN D 146
SITE 1 AC8 14 ASP D 130 THR D 132 ARG D 157 GLN D 173
SITE 2 AC8 14 ASP D 175 ASP D 177 ARG D 326 TYR D 330
SITE 3 AC8 14 TYR D 331 GLY D 360 GLY D 381 LEU D 382
SITE 4 AC8 14 SER D 383 HOH D1109
CRYST1 89.087 92.993 261.083 90.00 90.00 90.00 P 21 21 21 16
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 0.011225 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010753 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003830 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
