HEADER IMMUNE SYSTEM 25-NOV-13 4NQC
TITLE CRYSTAL STRUCTURE OF TCR-MR1 TERNARY COMPLEX AND COVALENTLY BOUND 5-
TITLE 2 (2-OXOPROPYLIDENEAMINO)-6-D-RIBITYLAMINOURACIL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MAJOR HISTOCOMPATIBILITY COMPLEX CLASS I-RELATED GENE
COMPND 3 PROTEIN;
COMPND 4 CHAIN: A, C;
COMPND 5 SYNONYM: MHC CLASS I-RELATED GENE PROTEIN, CLASS I HISTOCOMPATIBILITY
COMPND 6 ANTIGEN-LIKE PROTEIN;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: BETA-2-MICROGLOBULIN;
COMPND 10 CHAIN: B, F;
COMPND 11 SYNONYM: BETA-2-MICROGLOBULIN FORM PI 5.3;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: TCR ALPHA CHAIN;
COMPND 15 CHAIN: D, G;
COMPND 16 ENGINEERED: YES;
COMPND 17 MOL_ID: 4;
COMPND 18 MOLECULE: TCR BETA CHAIN;
COMPND 19 CHAIN: E, H;
COMPND 20 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: MR1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 GENE: B2M, BETA 2 MICROGLOBULIN, CDABP0092, HDCMA22P;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 17 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 19 MOL_ID: 3;
SOURCE 20 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 21 ORGANISM_TAXID: 9606;
SOURCE 22 GENE: TCR-ALPHA;
SOURCE 23 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 24 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 25 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 26 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 27 MOL_ID: 4;
SOURCE 28 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 29 ORGANISM_TAXID: 9606;
SOURCE 30 GENE: TCR-BETA;
SOURCE 31 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 32 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 33 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 34 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS MR1, T-CELL RECEPTOR, IMMUNE RECEPTOR COMPLEX, IG-FOLD, PROTEIN
KEYWDS 2 BINDING, SCHIFF BASE, MEMBRANE, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR R.W.BIRKINSHAW,J.ROSSJOHN
REVDAT 3 19-NOV-14 4NQC 1 TITLE
REVDAT 2 28-MAY-14 4NQC 1 JRNL
REVDAT 1 16-APR-14 4NQC 0
JRNL AUTH A.J.CORBETT,S.B.ECKLE,R.W.BIRKINSHAW,L.LIU,O.PATEL,J.MAHONY,
JRNL AUTH 2 Z.CHEN,R.REANTRAGOON,B.MEEHAN,H.CAO,N.A.WILLIAMSON,
JRNL AUTH 3 R.A.STRUGNELL,D.VAN SINDEREN,J.Y.MAK,D.P.FAIRLIE,
JRNL AUTH 4 L.KJER-NIELSEN,J.ROSSJOHN,J.MCCLUSKEY
JRNL TITL T-CELL ACTIVATION BY TRANSITORY NEO-ANTIGENS DERIVED FROM
JRNL TITL 2 DISTINCT MICROBIAL PATHWAYS.
JRNL REF NATURE V. 509 361 2014
JRNL REFN ISSN 0028-0836
JRNL PMID 24695216
JRNL DOI 10.1038/NATURE13160
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.0
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.42
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 74553
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) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 3757
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.56
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 5461
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2145
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5180
REMARK 3 BIN R VALUE (WORKING SET) : 0.2103
REMARK 3 BIN FREE R VALUE : 0.2923
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.15
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 281
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12382
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 45
REMARK 3 SOLVENT ATOMS : 1040
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 40.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.73
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.18170
REMARK 3 B22 (A**2) : -8.23930
REMARK 3 B33 (A**2) : 5.05750
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.08960
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.273
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.335
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.931
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.892
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 12828 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 17481 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 4200 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 300 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1901 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 12828 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 2 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 1647 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 14657 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.16
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.43
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.99
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 25
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|0 - A|84 }
REMARK 3 ORIGIN FOR THE GROUP (A): 48.1944 77.2281 225.4665
REMARK 3 T TENSOR
REMARK 3 T11: -0.1040 T22: 0.0162
REMARK 3 T33: 0.0038 T12: -0.0443
REMARK 3 T13: -0.0247 T23: -0.0047
REMARK 3 L TENSOR
REMARK 3 L11: 1.4131 L22: 1.0240
REMARK 3 L33: 1.5514 L12: -0.3373
REMARK 3 L13: 0.3746 L23: -0.0557
REMARK 3 S TENSOR
REMARK 3 S11: -0.0025 S12: 0.2402 S13: 0.2211
REMARK 3 S21: 0.0101 S22: 0.0129 S23: -0.1836
REMARK 3 S31: 0.1135 S32: 0.1598 S33: -0.0104
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { A|85 - A|114 }
REMARK 3 ORIGIN FOR THE GROUP (A): 42.4580 80.9379 235.9761
REMARK 3 T TENSOR
REMARK 3 T11: -0.1036 T22: -0.0360
REMARK 3 T33: -0.0298 T12: 0.0011
REMARK 3 T13: -0.0140 T23: -0.0478
REMARK 3 L TENSOR
REMARK 3 L11: 3.1493 L22: 0.0020
REMARK 3 L33: 0.1207 L12: -1.0418
REMARK 3 L13: 0.6454 L23: 1.5730
REMARK 3 S TENSOR
REMARK 3 S11: 0.0327 S12: -0.1642 S13: 0.1328
REMARK 3 S21: 0.1475 S22: 0.0196 S23: -0.0081
REMARK 3 S31: 0.0124 S32: 0.1434 S33: -0.0523
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { A|115 - A|182 }
REMARK 3 ORIGIN FOR THE GROUP (A): 39.7597 74.1724 236.3441
REMARK 3 T TENSOR
REMARK 3 T11: -0.0487 T22: -0.0032
REMARK 3 T33: -0.0211 T12: -0.0100
REMARK 3 T13: 0.0112 T23: -0.0139
REMARK 3 L TENSOR
REMARK 3 L11: 0.6114 L22: 0.9396
REMARK 3 L33: 0.6957 L12: 0.3850
REMARK 3 L13: 0.3253 L23: 0.1129
REMARK 3 S TENSOR
REMARK 3 S11: 0.1281 S12: -0.1147 S13: 0.1741
REMARK 3 S21: 0.0465 S22: -0.0050 S23: 0.1019
REMARK 3 S31: 0.0731 S32: -0.0560 S33: -0.1232
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: { A|183 - A|244 }
REMARK 3 ORIGIN FOR THE GROUP (A): 66.7079 80.5468 253.3782
REMARK 3 T TENSOR
REMARK 3 T11: -0.0916 T22: -0.0018
REMARK 3 T33: 0.0044 T12: 0.0313
REMARK 3 T13: -0.0856 T23: -0.0614
REMARK 3 L TENSOR
REMARK 3 L11: 4.3679 L22: 3.4801
REMARK 3 L33: 4.2923 L12: 0.3580
REMARK 3 L13: 1.2075 L23: 3.0710
REMARK 3 S TENSOR
REMARK 3 S11: -0.1535 S12: -0.0550 S13: 0.4976
REMARK 3 S21: 0.1830 S22: 0.0321 S23: -0.0020
REMARK 3 S31: -0.1700 S32: 0.0012 S33: 0.1215
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: { A|251 - A|269 }
REMARK 3 ORIGIN FOR THE GROUP (A): 67.8897 75.9570 262.2372
REMARK 3 T TENSOR
REMARK 3 T11: -0.0553 T22: 0.0711
REMARK 3 T33: -0.0597 T12: 0.0458
REMARK 3 T13: -0.0811 T23: -0.1052
REMARK 3 L TENSOR
REMARK 3 L11: 1.0250 L22: 1.1119
REMARK 3 L33: 0.9933 L12: -1.7138
REMARK 3 L13: -0.7483 L23: 0.0539
REMARK 3 S TENSOR
REMARK 3 S11: -0.0595 S12: -0.0767 S13: 0.1434
REMARK 3 S21: 0.1047 S22: 0.0486 S23: -0.1183
REMARK 3 S31: 0.0013 S32: -0.0551 S33: 0.0110
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: { B|1 - B|96 }
REMARK 3 ORIGIN FOR THE GROUP (A): 67.3830 89.2066 235.1816
REMARK 3 T TENSOR
REMARK 3 T11: -0.2247 T22: 0.0006
REMARK 3 T33: 0.0259 T12: -0.1297
REMARK 3 T13: -0.0566 T23: 0.0139
REMARK 3 L TENSOR
REMARK 3 L11: 4.9112 L22: 2.2060
REMARK 3 L33: 2.2038 L12: 0.3414
REMARK 3 L13: 1.1402 L23: -0.4718
REMARK 3 S TENSOR
REMARK 3 S11: -0.0747 S12: 0.3527 S13: 0.5044
REMARK 3 S21: 0.0732 S22: -0.0499 S23: -0.5260
REMARK 3 S31: -0.3127 S32: 0.6427 S33: 0.1246
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: { C|0 - C|84 }
REMARK 3 ORIGIN FOR THE GROUP (A): -5.7959 62.8106 161.8369
REMARK 3 T TENSOR
REMARK 3 T11: -0.0495 T22: -0.0190
REMARK 3 T33: -0.0561 T12: 0.0025
REMARK 3 T13: 0.0131 T23: -0.0192
REMARK 3 L TENSOR
REMARK 3 L11: 0.8119 L22: 3.1766
REMARK 3 L33: 1.8950 L12: 0.2936
REMARK 3 L13: -0.1700 L23: 0.8240
REMARK 3 S TENSOR
REMARK 3 S11: 0.0032 S12: 0.0984 S13: 0.0198
REMARK 3 S21: -0.0613 S22: -0.0178 S23: 0.1927
REMARK 3 S31: -0.1425 S32: -0.0192 S33: 0.0146
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: { C|85 - C|171 }
REMARK 3 ORIGIN FOR THE GROUP (A): 1.8758 55.6738 171.8288
REMARK 3 T TENSOR
REMARK 3 T11: -0.0286 T22: -0.0340
REMARK 3 T33: -0.0877 T12: -0.0202
REMARK 3 T13: -0.0043 T23: -0.0142
REMARK 3 L TENSOR
REMARK 3 L11: 1.7042 L22: 2.1851
REMARK 3 L33: 1.2247 L12: 0.1979
REMARK 3 L13: -0.2979 L23: -0.0603
REMARK 3 S TENSOR
REMARK 3 S11: -0.0390 S12: -0.0970 S13: -0.0485
REMARK 3 S21: 0.0887 S22: -0.0830 S23: 0.0137
REMARK 3 S31: 0.1146 S32: 0.1178 S33: 0.1221
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: { C|172 - C|216 }
REMARK 3 ORIGIN FOR THE GROUP (A): -22.5148 73.4728 190.0198
REMARK 3 T TENSOR
REMARK 3 T11: -0.0132 T22: -0.0685
REMARK 3 T33: 0.0325 T12: 0.0330
REMARK 3 T13: 0.0424 T23: 0.0066
REMARK 3 L TENSOR
REMARK 3 L11: 2.4338 L22: 0.6036
REMARK 3 L33: 2.0381 L12: 0.7264
REMARK 3 L13: -1.6107 L23: -0.2121
REMARK 3 S TENSOR
REMARK 3 S11: 0.0451 S12: -0.2246 S13: -0.0585
REMARK 3 S21: -0.0167 S22: -0.0053 S23: 0.2037
REMARK 3 S31: 0.0045 S32: -0.0417 S33: -0.0398
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: { C|217 - C|269 }
REMARK 3 ORIGIN FOR THE GROUP (A): -21.6135 70.6755 193.9926
REMARK 3 T TENSOR
REMARK 3 T11: -0.0232 T22: -0.0336
REMARK 3 T33: -0.0061 T12: 0.0250
REMARK 3 T13: 0.0598 T23: 0.0158
REMARK 3 L TENSOR
REMARK 3 L11: 1.7442 L22: 2.7582
REMARK 3 L33: 0.0507 L12: 0.0178
REMARK 3 L13: -0.3994 L23: 0.3720
REMARK 3 S TENSOR
REMARK 3 S11: -0.0489 S12: -0.2579 S13: 0.0020
REMARK 3 S21: 0.3721 S22: -0.0325 S23: 0.2976
REMARK 3 S31: 0.1760 S32: 0.0791 S33: 0.0814
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: { D|2 - D|83 }
REMARK 3 ORIGIN FOR THE GROUP (A): 28.5589 61.6993 161.5011
REMARK 3 T TENSOR
REMARK 3 T11: -0.0901 T22: -0.0145
REMARK 3 T33: -0.0889 T12: 0.0079
REMARK 3 T13: -0.0186 T23: 0.0356
REMARK 3 L TENSOR
REMARK 3 L11: 2.4669 L22: 0.7398
REMARK 3 L33: 2.2661 L12: 0.6368
REMARK 3 L13: -0.1528 L23: -0.0862
REMARK 3 S TENSOR
REMARK 3 S11: -0.0069 S12: -0.0109 S13: 0.0557
REMARK 3 S21: -0.0359 S22: -0.0106 S23: -0.1056
REMARK 3 S31: 0.0957 S32: 0.2256 S33: 0.0175
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: { D|84 - D|135 }
REMARK 3 ORIGIN FOR THE GROUP (A): 38.0143 62.6100 150.0477
REMARK 3 T TENSOR
REMARK 3 T11: -0.1101 T22: 0.1343
REMARK 3 T33: -0.0362 T12: 0.0183
REMARK 3 T13: -0.0096 T23: 0.0241
REMARK 3 L TENSOR
REMARK 3 L11: 4.5666 L22: 0.2343
REMARK 3 L33: 1.5306 L12: -0.4378
REMARK 3 L13: -2.4568 L23: 0.1162
REMARK 3 S TENSOR
REMARK 3 S11: 0.0053 S12: 0.0102 S13: 0.0929
REMARK 3 S21: 0.0613 S22: -0.0180 S23: -0.2988
REMARK 3 S31: 0.0707 S32: 0.2916 S33: 0.0127
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: { D|136 - D|198 }
REMARK 3 ORIGIN FOR THE GROUP (A): 53.4574 63.6451 141.0767
REMARK 3 T TENSOR
REMARK 3 T11: -0.2414 T22: 0.0146
REMARK 3 T33: 0.1111 T12: 0.0667
REMARK 3 T13: 0.0092 T23: 0.0728
REMARK 3 L TENSOR
REMARK 3 L11: 6.3198 L22: 1.7034
REMARK 3 L33: 2.9037 L12: 0.5933
REMARK 3 L13: 1.8114 L23: 2.0776
REMARK 3 S TENSOR
REMARK 3 S11: -0.1785 S12: -0.0365 S13: 0.5069
REMARK 3 S21: 0.0176 S22: 0.0848 S23: -0.2394
REMARK 3 S31: 0.0859 S32: 0.2891 S33: 0.0937
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: { E|3 - E|73 }
REMARK 3 ORIGIN FOR THE GROUP (A): 12.2587 61.7922 141.3616
REMARK 3 T TENSOR
REMARK 3 T11: -0.0348 T22: 0.0217
REMARK 3 T33: -0.0769 T12: -0.0208
REMARK 3 T13: -0.0085 T23: 0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 1.7382 L22: 1.2331
REMARK 3 L33: 2.3338 L12: 0.3967
REMARK 3 L13: -1.0756 L23: -1.0006
REMARK 3 S TENSOR
REMARK 3 S11: -0.0979 S12: 0.2131 S13: 0.0421
REMARK 3 S21: -0.1593 S22: -0.0891 S23: 0.0145
REMARK 3 S31: 0.1445 S32: -0.1182 S33: 0.1871
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: { E|74 - E|109 }
REMARK 3 ORIGIN FOR THE GROUP (A): 14.8454 61.3637 144.4568
REMARK 3 T TENSOR
REMARK 3 T11: 0.0295 T22: 0.0239
REMARK 3 T33: -0.0600 T12: -0.0074
REMARK 3 T13: 0.0184 T23: -0.0061
REMARK 3 L TENSOR
REMARK 3 L11: 1.4184 L22: 0.0027
REMARK 3 L33: 2.1409 L12: 0.1930
REMARK 3 L13: -1.3736 L23: -0.8882
REMARK 3 S TENSOR
REMARK 3 S11: -0.0075 S12: 0.0837 S13: 0.0395
REMARK 3 S21: -0.0732 S22: -0.0960 S23: -0.0650
REMARK 3 S31: -0.1358 S32: 0.0327 S33: 0.1035
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: { E|110 - E|124 }
REMARK 3 ORIGIN FOR THE GROUP (A): 27.2234 67.4426 125.5592
REMARK 3 T TENSOR
REMARK 3 T11: -0.0700 T22: 0.0084
REMARK 3 T33: -0.0772 T12: -0.0174
REMARK 3 T13: 0.0502 T23: 0.0787
REMARK 3 L TENSOR
REMARK 3 L11: -0.8169 L22: 0.0000
REMARK 3 L33: 2.6574 L12: -1.9101
REMARK 3 L13: 1.1854 L23: 1.9067
REMARK 3 S TENSOR
REMARK 3 S11: -0.0345 S12: 0.1572 S13: 0.1484
REMARK 3 S21: -0.0589 S22: 0.1192 S23: 0.0596
REMARK 3 S31: 0.0300 S32: -0.0215 S33: -0.0848
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: { E|125 - E|239 }
REMARK 3 ORIGIN FOR THE GROUP (A): 41.8751 56.2338 129.9746
REMARK 3 T TENSOR
REMARK 3 T11: -0.0461 T22: -0.1416
REMARK 3 T33: -0.1829 T12: 0.1165
REMARK 3 T13: 0.0478 T23: 0.0035
REMARK 3 L TENSOR
REMARK 3 L11: 4.6964 L22: 2.8019
REMARK 3 L33: 4.6811 L12: -1.2681
REMARK 3 L13: 2.5312 L23: -0.6700
REMARK 3 S TENSOR
REMARK 3 S11: 0.2511 S12: 0.2597 S13: -0.3738
REMARK 3 S21: -0.1002 S22: 0.0012 S23: -0.1494
REMARK 3 S31: 0.5784 S32: 0.6015 S33: -0.2523
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: { F|1 - F|97 }
REMARK 3 ORIGIN FOR THE GROUP (A): -28.8897 64.9295 171.7054
REMARK 3 T TENSOR
REMARK 3 T11: -0.1071 T22: -0.0161
REMARK 3 T33: -0.0665 T12: 0.0022
REMARK 3 T13: -0.0055 T23: 0.0035
REMARK 3 L TENSOR
REMARK 3 L11: 2.4664 L22: 3.0222
REMARK 3 L33: 1.9842 L12: 0.5292
REMARK 3 L13: 0.4262 L23: 0.5026
REMARK 3 S TENSOR
REMARK 3 S11: -0.1086 S12: 0.4824 S13: 0.1505
REMARK 3 S21: -0.1419 S22: -0.0693 S23: 0.4752
REMARK 3 S31: -0.1828 S32: -0.4045 S33: 0.1778
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: { G|2 - G|91 }
REMARK 3 ORIGIN FOR THE GROUP (A): 20.1412 57.4557 224.4361
REMARK 3 T TENSOR
REMARK 3 T11: -0.0306 T22: -0.0368
REMARK 3 T33: -0.0548 T12: -0.0457
REMARK 3 T13: 0.0173 T23: 0.0537
REMARK 3 L TENSOR
REMARK 3 L11: 3.0212 L22: 1.5240
REMARK 3 L33: 1.3927 L12: 1.3615
REMARK 3 L13: 1.3672 L23: 0.9423
REMARK 3 S TENSOR
REMARK 3 S11: -0.0244 S12: -0.0052 S13: -0.0799
REMARK 3 S21: 0.0040 S22: 0.0631 S23: 0.0736
REMARK 3 S31: 0.0989 S32: 0.0043 S33: -0.0387
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: { G|92 - G|120 }
REMARK 3 ORIGIN FOR THE GROUP (A): 12.5520 52.1185 214.9809
REMARK 3 T TENSOR
REMARK 3 T11: -0.0125 T22: 0.0395
REMARK 3 T33: 0.0018 T12: -0.0536
REMARK 3 T13: 0.0102 T23: 0.0226
REMARK 3 L TENSOR
REMARK 3 L11: 1.4199 L22: 0.8390
REMARK 3 L33: 1.0097 L12: 1.3610
REMARK 3 L13: 1.9132 L23: 1.0240
REMARK 3 S TENSOR
REMARK 3 S11: -0.0287 S12: -0.1214 S13: -0.1254
REMARK 3 S21: 0.0840 S22: 0.0226 S23: -0.0549
REMARK 3 S31: 0.0147 S32: -0.0806 S33: 0.0061
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: { G|121 - G|199 }
REMARK 3 ORIGIN FOR THE GROUP (A): -1.0075 42.5364 200.7445
REMARK 3 T TENSOR
REMARK 3 T11: -0.0703 T22: -0.1605
REMARK 3 T33: -0.0215 T12: -0.0088
REMARK 3 T13: 0.0310 T23: 0.0721
REMARK 3 L TENSOR
REMARK 3 L11: 3.1375 L22: 1.5929
REMARK 3 L33: 7.0965 L12: 0.3457
REMARK 3 L13: -1.1205 L23: 0.5519
REMARK 3 S TENSOR
REMARK 3 S11: -0.0901 S12: -0.2116 S13: -0.3074
REMARK 3 S21: -0.2750 S22: -0.0607 S23: -0.0005
REMARK 3 S31: 0.4837 S32: 0.3434 S33: 0.1508
REMARK 3
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: { H|1 - H|109 }
REMARK 3 ORIGIN FOR THE GROUP (A): 31.7519 67.1740 205.7171
REMARK 3 T TENSOR
REMARK 3 T11: -0.0577 T22: 0.0412
REMARK 3 T33: -0.0637 T12: -0.0534
REMARK 3 T13: -0.0171 T23: 0.0546
REMARK 3 L TENSOR
REMARK 3 L11: 1.1609 L22: 1.3201
REMARK 3 L33: 1.9696 L12: 0.4827
REMARK 3 L13: 0.5300 L23: 1.2063
REMARK 3 S TENSOR
REMARK 3 S11: -0.0576 S12: 0.1906 S13: 0.0318
REMARK 3 S21: -0.1528 S22: 0.0133 S23: -0.0028
REMARK 3 S31: -0.1063 S32: 0.1578 S33: 0.0443
REMARK 3
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: { H|110 - H|124 }
REMARK 3 ORIGIN FOR THE GROUP (A): 24.3693 53.9282 189.5304
REMARK 3 T TENSOR
REMARK 3 T11: -0.0688 T22: 0.0915
REMARK 3 T33: -0.0756 T12: -0.0004
REMARK 3 T13: -0.0211 T23: 0.0125
REMARK 3 L TENSOR
REMARK 3 L11: 0.3618 L22: 0.0000
REMARK 3 L33: 0.6084 L12: 0.8677
REMARK 3 L13: -0.7620 L23: 0.3395
REMARK 3 S TENSOR
REMARK 3 S11: -0.0122 S12: -0.0684 S13: -0.0939
REMARK 3 S21: 0.0838 S22: -0.0381 S23: -0.1249
REMARK 3 S31: 0.1789 S32: 0.1412 S33: 0.0503
REMARK 3
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: { H|125 - H|202 }
REMARK 3 ORIGIN FOR THE GROUP (A): 2.4894 53.2587 196.5785
REMARK 3 T TENSOR
REMARK 3 T11: -0.0249 T22: -0.0608
REMARK 3 T33: -0.1150 T12: -0.0372
REMARK 3 T13: -0.0055 T23: 0.0184
REMARK 3 L TENSOR
REMARK 3 L11: 5.5478 L22: 1.5136
REMARK 3 L33: 2.4542 L12: -0.0221
REMARK 3 L13: -2.1901 L23: -0.2335
REMARK 3 S TENSOR
REMARK 3 S11: 0.0978 S12: -0.4085 S13: -0.1411
REMARK 3 S21: -0.0536 S22: -0.0523 S23: -0.0461
REMARK 3 S31: -0.0402 S32: 0.2073 S33: -0.0455
REMARK 3
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: { H|203 - H|243 }
REMARK 3 ORIGIN FOR THE GROUP (A): 7.4336 59.9907 186.2972
REMARK 3 T TENSOR
REMARK 3 T11: 0.0089 T22: -0.0178
REMARK 3 T33: 0.0243 T12: -0.0326
REMARK 3 T13: -0.0368 T23: 0.0409
REMARK 3 L TENSOR
REMARK 3 L11: 4.3065 L22: 0.0000
REMARK 3 L33: 1.4581 L12: -0.0715
REMARK 3 L13: -2.3182 L23: -0.4232
REMARK 3 S TENSOR
REMARK 3 S11: 0.0366 S12: 0.0088 S13: 0.0940
REMARK 3 S21: -0.0808 S22: 0.0126 S23: 0.0026
REMARK 3 S31: -0.0445 S32: 0.1089 S33: -0.0493
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4NQC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-NOV-13.
REMARK 100 THE RCSB ID CODE IS RCSB083523.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : SINGLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 74555
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 33.420
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 7.800
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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 (%): 57.52
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% (W/V) PEG3350, 0.2 M SODIUM
REMARK 280 CITRATE, 0.1 M BIS-TRIS PROPANE, PH 6.3, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 109.38000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.55500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 109.38000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 35.55500
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, 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 300 REMARK: HETERODIMER WITH BETA MICROGLOBULIN
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: 2340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17350 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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: 2280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18110 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, F
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: 3540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19090 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E
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: 3960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, 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 LYS A 189
REMARK 465 GLU A 190
REMARK 465 THR A 191
REMARK 465 PHE A 192
REMARK 465 PRO A 193
REMARK 465 GLY A 194
REMARK 465 VAL A 195
REMARK 465 THR A 196
REMARK 465 ALA A 197
REMARK 465 GLU A 245
REMARK 465 LEU A 246
REMARK 465 ASP A 247
REMARK 465 PRO A 248
REMARK 465 GLN A 249
REMARK 465 SER A 250
REMARK 465 PRO A 270
REMARK 465 ARG B 97
REMARK 465 ASP B 98
REMARK 465 MET B 99
REMARK 465 HIS C 17
REMARK 465 GLY C 18
REMARK 465 ASP C 247
REMARK 465 PRO C 248
REMARK 465 GLN C 249
REMARK 465 SER C 250
REMARK 465 SER C 251
REMARK 465 PRO C 270
REMARK 465 GLY D 1
REMARK 465 ASP D 123
REMARK 465 SER D 124
REMARK 465 LYS D 125
REMARK 465 SER D 126
REMARK 465 SER D 127
REMARK 465 ASP D 128
REMARK 465 LYS D 129
REMARK 465 SER D 130
REMARK 465 LYS D 177
REMARK 465 SER D 178
REMARK 465 ASP D 179
REMARK 465 PHE D 180
REMARK 465 SER D 199
REMARK 465 PRO D 200
REMARK 465 GLU D 201
REMARK 465 SER D 202
REMARK 465 SER D 203
REMARK 465 ASN E 1
REMARK 465 ALA E 2
REMARK 465 ARG E 243
REMARK 465 ALA E 244
REMARK 465 ASP E 245
REMARK 465 ASP F 98
REMARK 465 MET F 99
REMARK 465 GLY G 1
REMARK 465 PRO G 200
REMARK 465 GLU G 201
REMARK 465 SER G 202
REMARK 465 SER G 203
REMARK 465 ALA H 244
REMARK 465 ASP H 245
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 HIS A 17 CG ND1 CD2 CE1 NE2
REMARK 470 GLU A 102 CG CD OE1 OE2
REMARK 470 GLU A 219 CG CD OE1 OE2
REMARK 470 GLU A 220 CG CD OE1 OE2
REMARK 470 ILE A 221 CG1 CG2 CD1
REMARK 470 VAL A 222 CG1 CG2
REMARK 470 GLN A 223 CG CD OE1 NE2
REMARK 470 GLU A 224 CG CD OE1 OE2
REMARK 470 GLU B 16 CG CD OE1 OE2
REMARK 470 LYS B 19 CG CD CE NZ
REMARK 470 GLU B 36 CG CD OE1 OE2
REMARK 470 GLU B 44 CG CD OE1 OE2
REMARK 470 GLU B 47 CG CD OE1 OE2
REMARK 470 LYS B 48 CG CD CE NZ
REMARK 470 GLU B 74 CG CD OE1 OE2
REMARK 470 LYS B 75 CG CD CE NZ
REMARK 470 GLU B 77 CG CD OE1 OE2
REMARK 470 GLN B 89 CG CD OE1 NE2
REMARK 470 LYS B 94 CG CD CE NZ
REMARK 470 ILE C 16 CG1 CG2 CD1
REMARK 470 LYS C 216 CG CD CE NZ
REMARK 470 GLU C 219 CG CD OE1 OE2
REMARK 470 GLU C 220 CG CD OE1 OE2
REMARK 470 VAL C 222 CG1 CG2
REMARK 470 GLN C 223 CG CD OE1 NE2
REMARK 470 GLU C 224 CG CD OE1 OE2
REMARK 470 ASN C 252 CG OD1 ND2
REMARK 470 LEU C 253 CG CD1 CD2
REMARK 470 GLN D 25 CG CD OE1 NE2
REMARK 470 GLU D 56 CG CD OE1 OE2
REMARK 470 GLN D 112 CG CD OE1 NE2
REMARK 470 ASN D 113 CG OD1 ND2
REMARK 470 ARG D 122 CG CD NE CZ NH1 NH2
REMARK 470 ASP D 138 CG OD1 OD2
REMARK 470 ASN D 142 CG OD1 ND2
REMARK 470 SER D 144 OG
REMARK 470 GLN D 145 CG CD OE1 NE2
REMARK 470 LYS D 147 CG CD CE NZ
REMARK 470 ASP D 148 CG OD1 OD2
REMARK 470 SER D 149 OG
REMARK 470 ASP D 150 CG OD1 OD2
REMARK 470 ASP D 155 CG OD1 OD2
REMARK 470 ARG D 162 CG CD NE CZ NH1 NH2
REMARK 470 SER D 163 OG
REMARK 470 MET D 164 CG SD CE
REMARK 470 ASP D 165 CG OD1 OD2
REMARK 470 ASN D 176 CG OD1 ND2
REMARK 470 ASN D 184 CG OD1 ND2
REMARK 470 ASN D 187 CG OD1 ND2
REMARK 470 ASN D 188 CG OD1 ND2
REMARK 470 SER D 189 OG
REMARK 470 ILE D 190 CG1 CG2 CD1
REMARK 470 GLU D 193 CG CD OE1 OE2
REMARK 470 ASP D 194 CG OD1 OD2
REMARK 470 THR D 195 OG1 CG2
REMARK 470 LYS E 9 CG CD CE NZ
REMARK 470 LYS E 14 CG CD CE NZ
REMARK 470 ARG E 77 CG CD NE CZ NH1 NH2
REMARK 470 GLU E 116 CG CD OE1 OE2
REMARK 470 GLU E 130 CG CD OE1 OE2
REMARK 470 GLU E 133 CG CD OE1 OE2
REMARK 470 LYS E 165 CG CD CE NZ
REMARK 470 GLN E 176 CG CD OE1 NE2
REMARK 470 ARG E 206 CG CD NE CZ NH1 NH2
REMARK 470 HIS E 208 CG ND1 CD2 CE1 NE2
REMARK 470 GLU E 220 CG CD OE1 OE2
REMARK 470 ASN E 221 CG OD1 ND2
REMARK 470 GLU E 223 CG CD OE1 OE2
REMARK 470 ASP E 227 CG OD1 OD2
REMARK 470 GLU F 36 CG CD OE1 OE2
REMARK 470 GLU F 44 CG CD OE1 OE2
REMARK 470 GLU F 47 CG CD OE1 OE2
REMARK 470 LYS F 48 CG CD CE NZ
REMARK 470 LYS F 58 CG CD CE NZ
REMARK 470 GLU F 74 CG CD OE1 OE2
REMARK 470 LYS F 75 CG CD CE NZ
REMARK 470 GLU F 77 CG CD OE1 OE2
REMARK 470 ARG F 97 CG CD NE CZ NH1 NH2
REMARK 470 LYS G 76 CG CD CE NZ
REMARK 470 GLN G 112 CG CD OE1 NE2
REMARK 470 GLN G 140 CG CD OE1 NE2
REMARK 470 GLN G 145 CG CD OE1 NE2
REMARK 470 LYS G 147 CG CD CE NZ
REMARK 470 ASP G 148 CG OD1 OD2
REMARK 470 ARG G 162 CG CD NE CZ NH1 NH2
REMARK 470 ASP G 165 CG OD1 OD2
REMARK 470 LYS G 177 CG CD CE NZ
REMARK 470 ASP G 179 CG OD1 OD2
REMARK 470 ASN G 184 CG OD1 ND2
REMARK 470 ASN H 1 CG OD1 ND2
REMARK 470 LYS H 9 CG CD CE NZ
REMARK 470 LYS H 119 CG CD CE NZ
REMARK 470 GLU H 133 CG CD OE1 OE2
REMARK 470 LYS H 165 CG CD CE NZ
REMARK 470 GLN H 176 CG CD OE1 NE2
REMARK 470 LEU H 184 CG CD1 CD2
REMARK 470 ASN H 185 CG OD1 ND2
REMARK 470 GLU H 220 CG CD OE1 OE2
REMARK 470 ASN H 221 CG OD1 ND2
REMARK 470 GLU H 223 CG CD OE1 OE2
REMARK 470 ARG H 243 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 ND1 HIS C 257 O HOH C 585 2.19
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 VAL A 19 122.72 -32.59
REMARK 500 ASP A 29 -121.25 61.12
REMARK 500 ASN A 146 70.24 -108.80
REMARK 500 GLU A 159 -62.21 -109.66
REMARK 500 THR A 175 -60.42 -93.03
REMARK 500 GLU A 220 -79.30 -64.10
REMARK 500 ILE A 221 63.13 67.62
REMARK 500 TRP B 60 -2.41 81.34
REMARK 500 ASP C 29 -121.15 60.98
REMARK 500 PHE C 119 -58.16 -122.62
REMARK 500 ASN C 146 75.50 -102.48
REMARK 500 THR C 191 -102.72 -99.44
REMARK 500 PRO C 193 115.14 -38.57
REMARK 500 VAL D 50 -33.78 -133.38
REMARK 500 ALA D 84 -179.28 -170.48
REMARK 500 ILE E 46 -60.57 -91.23
REMARK 500 VAL E 60 59.57 -119.20
REMARK 500 SER E 87 -175.44 -176.45
REMARK 500 HIS E 168 -31.15 -131.40
REMARK 500 PRO F 32 -179.82 -69.85
REMARK 500 TRP F 60 -1.32 81.12
REMARK 500 VAL G 50 -33.60 -133.18
REMARK 500 ILE H 46 -61.70 -91.68
REMARK 500 SER H 87 -175.26 -175.79
REMARK 500 HIS H 168 -32.54 -132.61
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 LYS A 173 24.2 L L OUTSIDE RANGE
REMARK 500 ARG A 188 24.5 L L OUTSIDE RANGE
REMARK 500 LYS C 173 24.0 L L OUTSIDE RANGE
REMARK 500 SER E 101 24.7 L L OUTSIDE RANGE
REMARK 500 SER H 101 24.5 L L OUTSIDE RANGE
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 H 301 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH H 574 O
REMARK 620 2 TYR H 64 O 149.6
REMARK 620 3 HOH H 571 O 103.9 106.4
REMARK 620 4 TYR H 47 OH 94.9 89.1 85.2
REMARK 620 5 HOH H 575 O 76.6 101.0 91.3 169.9
REMARK 620 6 PRO H 61 O 78.5 71.6 173.1 88.1 95.6
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2LJ A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2LJ C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA H 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4LCW RELATED DB: PDB
REMARK 900 RELATED ID: 4L4V RELATED DB: PDB
REMARK 900 RELATED ID: 4GUP RELATED DB: PDB
REMARK 900 RELATED ID: 4NQD RELATED DB: PDB
REMARK 900 RELATED ID: 4NQE RELATED DB: PDB
DBREF 4NQC A 1 270 UNP Q95460 HMR1_HUMAN 23 292
DBREF 4NQC B 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 4NQC C 1 270 UNP Q95460 HMR1_HUMAN 23 292
DBREF 4NQC F 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 4NQC D 1 203 PDB 4NQC 4NQC 1 203
DBREF 4NQC G 1 201 PDB 4NQC 4NQC 1 201
DBREF 4NQC E 1 245 PDB 4NQC 4NQC 1 245
DBREF 4NQC H 1 245 PDB 4NQC 4NQC 1 245
SEQADV 4NQC MET A 0 UNP Q95460 EXPRESSION TAG
SEQADV 4NQC SER A 261 UNP Q95460 CYS 283 ENGINEERED MUTATION
SEQADV 4NQC MET C 0 UNP Q95460 EXPRESSION TAG
SEQADV 4NQC SER C 261 UNP Q95460 CYS 283 ENGINEERED MUTATION
SEQRES 1 A 271 MET ARG THR HIS SER LEU ARG TYR PHE ARG LEU GLY VAL
SEQRES 2 A 271 SER ASP PRO ILE HIS GLY VAL PRO GLU PHE ILE SER VAL
SEQRES 3 A 271 GLY TYR VAL ASP SER HIS PRO ILE THR THR TYR ASP SER
SEQRES 4 A 271 VAL THR ARG GLN LYS GLU PRO ARG ALA PRO TRP MET ALA
SEQRES 5 A 271 GLU ASN LEU ALA PRO ASP HIS TRP GLU ARG TYR THR GLN
SEQRES 6 A 271 LEU LEU ARG GLY TRP GLN GLN MET PHE LYS VAL GLU LEU
SEQRES 7 A 271 LYS ARG LEU GLN ARG HIS TYR ASN HIS SER GLY SER HIS
SEQRES 8 A 271 THR TYR GLN ARG MET ILE GLY CYS GLU LEU LEU GLU ASP
SEQRES 9 A 271 GLY SER THR THR GLY PHE LEU GLN TYR ALA TYR ASP GLY
SEQRES 10 A 271 GLN ASP PHE LEU ILE PHE ASN LYS ASP THR LEU SER TRP
SEQRES 11 A 271 LEU ALA VAL ASP ASN VAL ALA HIS THR ILE LYS GLN ALA
SEQRES 12 A 271 TRP GLU ALA ASN GLN HIS GLU LEU LEU TYR GLN LYS ASN
SEQRES 13 A 271 TRP LEU GLU GLU GLU CYS ILE ALA TRP LEU LYS ARG PHE
SEQRES 14 A 271 LEU GLU TYR GLY LYS ASP THR LEU GLN ARG THR GLU PRO
SEQRES 15 A 271 PRO LEU VAL ARG VAL ASN ARG LYS GLU THR PHE PRO GLY
SEQRES 16 A 271 VAL THR ALA LEU PHE CYS LYS ALA HIS GLY PHE TYR PRO
SEQRES 17 A 271 PRO GLU ILE TYR MET THR TRP MET LYS ASN GLY GLU GLU
SEQRES 18 A 271 ILE VAL GLN GLU ILE ASP TYR GLY ASP ILE LEU PRO SER
SEQRES 19 A 271 GLY ASP GLY THR TYR GLN ALA TRP ALA SER ILE GLU LEU
SEQRES 20 A 271 ASP PRO GLN SER SER ASN LEU TYR SER CYS HIS VAL GLU
SEQRES 21 A 271 HIS SER GLY VAL HIS MET VAL LEU GLN VAL PRO
SEQRES 1 B 99 ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG HIS
SEQRES 2 B 99 PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS TYR
SEQRES 3 B 99 VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP LEU
SEQRES 4 B 99 LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS SER
SEQRES 5 B 99 ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU LEU
SEQRES 6 B 99 TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU TYR
SEQRES 7 B 99 ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO LYS
SEQRES 8 B 99 ILE VAL LYS TRP ASP ARG ASP MET
SEQRES 1 C 271 MET ARG THR HIS SER LEU ARG TYR PHE ARG LEU GLY VAL
SEQRES 2 C 271 SER ASP PRO ILE HIS GLY VAL PRO GLU PHE ILE SER VAL
SEQRES 3 C 271 GLY TYR VAL ASP SER HIS PRO ILE THR THR TYR ASP SER
SEQRES 4 C 271 VAL THR ARG GLN LYS GLU PRO ARG ALA PRO TRP MET ALA
SEQRES 5 C 271 GLU ASN LEU ALA PRO ASP HIS TRP GLU ARG TYR THR GLN
SEQRES 6 C 271 LEU LEU ARG GLY TRP GLN GLN MET PHE LYS VAL GLU LEU
SEQRES 7 C 271 LYS ARG LEU GLN ARG HIS TYR ASN HIS SER GLY SER HIS
SEQRES 8 C 271 THR TYR GLN ARG MET ILE GLY CYS GLU LEU LEU GLU ASP
SEQRES 9 C 271 GLY SER THR THR GLY PHE LEU GLN TYR ALA TYR ASP GLY
SEQRES 10 C 271 GLN ASP PHE LEU ILE PHE ASN LYS ASP THR LEU SER TRP
SEQRES 11 C 271 LEU ALA VAL ASP ASN VAL ALA HIS THR ILE LYS GLN ALA
SEQRES 12 C 271 TRP GLU ALA ASN GLN HIS GLU LEU LEU TYR GLN LYS ASN
SEQRES 13 C 271 TRP LEU GLU GLU GLU CYS ILE ALA TRP LEU LYS ARG PHE
SEQRES 14 C 271 LEU GLU TYR GLY LYS ASP THR LEU GLN ARG THR GLU PRO
SEQRES 15 C 271 PRO LEU VAL ARG VAL ASN ARG LYS GLU THR PHE PRO GLY
SEQRES 16 C 271 VAL THR ALA LEU PHE CYS LYS ALA HIS GLY PHE TYR PRO
SEQRES 17 C 271 PRO GLU ILE TYR MET THR TRP MET LYS ASN GLY GLU GLU
SEQRES 18 C 271 ILE VAL GLN GLU ILE ASP TYR GLY ASP ILE LEU PRO SER
SEQRES 19 C 271 GLY ASP GLY THR TYR GLN ALA TRP ALA SER ILE GLU LEU
SEQRES 20 C 271 ASP PRO GLN SER SER ASN LEU TYR SER CYS HIS VAL GLU
SEQRES 21 C 271 HIS SER GLY VAL HIS MET VAL LEU GLN VAL PRO
SEQRES 1 D 203 GLY GLN ASN ILE ASP GLN PRO THR GLU MET THR ALA THR
SEQRES 2 D 203 GLU GLY ALA ILE VAL GLN ILE ASN CYS THR TYR GLN THR
SEQRES 3 D 203 SER GLY PHE ASN GLY LEU PHE TRP TYR GLN GLN HIS ALA
SEQRES 4 D 203 GLY GLU ALA PRO THR PHE LEU SER TYR ASN VAL LEU ASP
SEQRES 5 D 203 GLY LEU GLU GLU LYS GLY ARG PHE SER SER PHE LEU SER
SEQRES 6 D 203 ARG SER LYS GLY TYR SER TYR LEU LEU LEU LYS GLU LEU
SEQRES 7 D 203 GLN MET LYS ASP SER ALA SER TYR LEU CYS ALA VAL LYS
SEQRES 8 D 203 ASP SER ASN TYR GLN LEU ILE TRP GLY ALA GLY THR LYS
SEQRES 9 D 203 LEU ILE ILE LYS PRO ASP ILE GLN ASN PRO ASP PRO ALA
SEQRES 10 D 203 VAL TYR GLN LEU ARG ASP SER LYS SER SER ASP LYS SER
SEQRES 11 D 203 VAL CYS LEU PHE THR ASP PHE ASP SER GLN THR ASN VAL
SEQRES 12 D 203 SER GLN SER LYS ASP SER ASP VAL TYR ILE THR ASP LYS
SEQRES 13 D 203 CYS VAL LEU ASP MET ARG SER MET ASP PHE LYS SER ASN
SEQRES 14 D 203 SER ALA VAL ALA TRP SER ASN LYS SER ASP PHE ALA CYS
SEQRES 15 D 203 ALA ASN ALA PHE ASN ASN SER ILE ILE PRO GLU ASP THR
SEQRES 16 D 203 PHE PHE PRO SER PRO GLU SER SER
SEQRES 1 E 245 ASN ALA GLY VAL THR GLN THR PRO LYS PHE GLN VAL LEU
SEQRES 2 E 245 LYS THR GLY GLN SER MET THR LEU GLN CYS ALA GLN ASP
SEQRES 3 E 245 MET ASN HIS ASN SER MET TYR TRP TYR ARG GLN ASP PRO
SEQRES 4 E 245 GLY MET GLY LEU ARG LEU ILE TYR TYR SER ALA SER GLU
SEQRES 5 E 245 GLY THR THR ASP LYS GLY GLU VAL PRO ASN GLY TYR ASN
SEQRES 6 E 245 VAL SER ARG LEU ASN LYS ARG GLU PHE SER LEU ARG LEU
SEQRES 7 E 245 GLU SER ALA ALA PRO SER GLN THR SER VAL TYR PHE CYS
SEQRES 8 E 245 ALA SER SER VAL TRP THR GLY GLU GLY SER GLY GLU LEU
SEQRES 9 E 245 PHE PHE GLY GLU GLY SER ARG LEU THR VAL LEU GLU ASP
SEQRES 10 E 245 LEU LYS ASN VAL PHE PRO PRO GLU VAL ALA VAL PHE GLU
SEQRES 11 E 245 PRO SER GLU ALA GLU ILE SER HIS THR GLN LYS ALA THR
SEQRES 12 E 245 LEU VAL CYS LEU ALA THR GLY PHE TYR PRO ASP HIS VAL
SEQRES 13 E 245 GLU LEU SER TRP TRP VAL ASN GLY LYS GLU VAL HIS SER
SEQRES 14 E 245 GLY VAL CYS THR ASP PRO GLN PRO LEU LYS GLU GLN PRO
SEQRES 15 E 245 ALA LEU ASN ASP SER ARG TYR ALA LEU SER SER ARG LEU
SEQRES 16 E 245 ARG VAL SER ALA THR PHE TRP GLN ASN PRO ARG ASN HIS
SEQRES 17 E 245 PHE ARG CYS GLN VAL GLN PHE TYR GLY LEU SER GLU ASN
SEQRES 18 E 245 ASP GLU TRP THR GLN ASP ARG ALA LYS PRO VAL THR GLN
SEQRES 19 E 245 ILE VAL SER ALA GLU ALA TRP GLY ARG ALA ASP
SEQRES 1 F 99 ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG HIS
SEQRES 2 F 99 PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS TYR
SEQRES 3 F 99 VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP LEU
SEQRES 4 F 99 LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS SER
SEQRES 5 F 99 ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU LEU
SEQRES 6 F 99 TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU TYR
SEQRES 7 F 99 ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO LYS
SEQRES 8 F 99 ILE VAL LYS TRP ASP ARG ASP MET
SEQRES 1 G 203 GLY GLN ASN ILE ASP GLN PRO THR GLU MET THR ALA THR
SEQRES 2 G 203 GLU GLY ALA ILE VAL GLN ILE ASN CYS THR TYR GLN THR
SEQRES 3 G 203 SER GLY PHE ASN GLY LEU PHE TRP TYR GLN GLN HIS ALA
SEQRES 4 G 203 GLY GLU ALA PRO THR PHE LEU SER TYR ASN VAL LEU ASP
SEQRES 5 G 203 GLY LEU GLU GLU LYS GLY ARG PHE SER SER PHE LEU SER
SEQRES 6 G 203 ARG SER LYS GLY TYR SER TYR LEU LEU LEU LYS GLU LEU
SEQRES 7 G 203 GLN MET LYS ASP SER ALA SER TYR LEU CYS ALA VAL LYS
SEQRES 8 G 203 ASP SER ASN TYR GLN LEU ILE TRP GLY ALA GLY THR LYS
SEQRES 9 G 203 LEU ILE ILE LYS PRO ASP ILE GLN ASN PRO ASP PRO ALA
SEQRES 10 G 203 VAL TYR GLN LEU ARG ASP SER LYS SER SER ASP LYS SER
SEQRES 11 G 203 VAL CYS LEU PHE THR ASP PHE ASP SER GLN THR ASN VAL
SEQRES 12 G 203 SER GLN SER LYS ASP SER ASP VAL TYR ILE THR ASP LYS
SEQRES 13 G 203 CYS VAL LEU ASP MET ARG SER MET ASP PHE LYS SER ASN
SEQRES 14 G 203 SER ALA VAL ALA TRP SER ASN LYS SER ASP PHE ALA CYS
SEQRES 15 G 203 ALA ASN ALA PHE ASN ASN SER ILE ILE PRO GLU ASP THR
SEQRES 16 G 203 PHE PHE PRO SER PRO GLU SER SER
SEQRES 1 H 245 ASN ALA GLY VAL THR GLN THR PRO LYS PHE GLN VAL LEU
SEQRES 2 H 245 LYS THR GLY GLN SER MET THR LEU GLN CYS ALA GLN ASP
SEQRES 3 H 245 MET ASN HIS ASN SER MET TYR TRP TYR ARG GLN ASP PRO
SEQRES 4 H 245 GLY MET GLY LEU ARG LEU ILE TYR TYR SER ALA SER GLU
SEQRES 5 H 245 GLY THR THR ASP LYS GLY GLU VAL PRO ASN GLY TYR ASN
SEQRES 6 H 245 VAL SER ARG LEU ASN LYS ARG GLU PHE SER LEU ARG LEU
SEQRES 7 H 245 GLU SER ALA ALA PRO SER GLN THR SER VAL TYR PHE CYS
SEQRES 8 H 245 ALA SER SER VAL TRP THR GLY GLU GLY SER GLY GLU LEU
SEQRES 9 H 245 PHE PHE GLY GLU GLY SER ARG LEU THR VAL LEU GLU ASP
SEQRES 10 H 245 LEU LYS ASN VAL PHE PRO PRO GLU VAL ALA VAL PHE GLU
SEQRES 11 H 245 PRO SER GLU ALA GLU ILE SER HIS THR GLN LYS ALA THR
SEQRES 12 H 245 LEU VAL CYS LEU ALA THR GLY PHE TYR PRO ASP HIS VAL
SEQRES 13 H 245 GLU LEU SER TRP TRP VAL ASN GLY LYS GLU VAL HIS SER
SEQRES 14 H 245 GLY VAL CYS THR ASP PRO GLN PRO LEU LYS GLU GLN PRO
SEQRES 15 H 245 ALA LEU ASN ASP SER ARG TYR ALA LEU SER SER ARG LEU
SEQRES 16 H 245 ARG VAL SER ALA THR PHE TRP GLN ASN PRO ARG ASN HIS
SEQRES 17 H 245 PHE ARG CYS GLN VAL GLN PHE TYR GLY LEU SER GLU ASN
SEQRES 18 H 245 ASP GLU TRP THR GLN ASP ARG ALA LYS PRO VAL THR GLN
SEQRES 19 H 245 ILE VAL SER ALA GLU ALA TRP GLY ARG ALA ASP
HET 2LJ A 301 22
HET 2LJ C 301 22
HET NA H 301 1
HETNAM 2LJ 1-DEOXY-1-({2,6-DIOXO-5-[(E)-(2-OXOPROPYLIDENE)AMINO]-
HETNAM 2 2LJ 1,2,3,6-TETRAHYDROPYRIMIDIN-4-YL}AMINO)-D-RIBITOL
HETNAM NA SODIUM ION
HETSYN 2LJ 5-(2-OXOPROPYLIDENEAMINO)-6-D-RIBITYLAMINOURACIL
FORMUL 9 2LJ 2(C12 H18 N4 O7)
FORMUL 11 NA NA 1+
FORMUL 12 HOH *1040(H2 O)
HELIX 1 1 ALA A 47 GLU A 52 1 6
HELIX 2 2 ALA A 55 ASN A 85 1 31
HELIX 3 3 ASP A 133 GLU A 144 1 12
HELIX 4 4 ASN A 146 GLU A 159 1 14
HELIX 5 5 GLU A 159 GLY A 172 1 14
HELIX 6 6 GLY A 172 GLN A 177 1 6
HELIX 7 7 ILE A 221 ILE A 225 5 5
HELIX 8 8 ALA C 47 GLU C 52 1 6
HELIX 9 9 ALA C 55 ASN C 85 1 31
HELIX 10 10 ASP C 133 GLU C 144 1 12
HELIX 11 11 ASN C 146 GLU C 159 1 14
HELIX 12 12 GLU C 159 GLY C 172 1 14
HELIX 13 13 GLY C 172 GLN C 177 1 6
HELIX 14 14 GLN D 79 SER D 83 5 5
HELIX 15 15 ARG D 162 ASP D 165 5 4
HELIX 16 16 CYS D 182 PHE D 186 1 5
HELIX 17 17 ALA E 82 THR E 86 5 5
HELIX 18 18 SER E 132 GLN E 140 1 9
HELIX 19 19 ALA E 199 ASN E 204 1 6
HELIX 20 20 GLN G 79 SER G 83 5 5
HELIX 21 21 ARG G 162 ASP G 165 5 4
HELIX 22 22 ALA G 181 PHE G 186 1 6
HELIX 23 23 ALA H 82 THR H 86 5 5
HELIX 24 24 ASP H 117 VAL H 121 5 5
HELIX 25 25 SER H 132 GLN H 140 1 9
HELIX 26 26 ALA H 199 GLN H 203 1 5
SHEET 1 A 8 GLU A 44 PRO A 45 0
SHEET 2 A 8 HIS A 31 ASP A 37 -1 N THR A 35 O GLU A 44
SHEET 3 A 8 PHE A 22 VAL A 28 -1 N GLY A 26 O ILE A 33
SHEET 4 A 8 HIS A 3 VAL A 12 -1 N ARG A 6 O TYR A 27
SHEET 5 A 8 THR A 91 LEU A 100 -1 O TYR A 92 N GLY A 11
SHEET 6 A 8 THR A 106 TYR A 114 -1 O PHE A 109 N GLY A 97
SHEET 7 A 8 GLN A 117 ASN A 123 -1 O PHE A 119 N TYR A 112
SHEET 8 A 8 SER A 128 ALA A 131 -1 O LEU A 130 N ILE A 121
SHEET 1 B 4 LEU A 183 ASN A 187 0
SHEET 2 B 4 PHE A 199 PHE A 205 -1 O PHE A 199 N ASN A 187
SHEET 3 B 4 TYR A 238 SER A 243 -1 O ALA A 240 N ALA A 202
SHEET 4 B 4 ASP A 226 TYR A 227 -1 N ASP A 226 O SER A 243
SHEET 1 C 4 LEU A 183 ASN A 187 0
SHEET 2 C 4 PHE A 199 PHE A 205 -1 O PHE A 199 N ASN A 187
SHEET 3 C 4 TYR A 238 SER A 243 -1 O ALA A 240 N ALA A 202
SHEET 4 C 4 LEU A 231 PRO A 232 -1 N LEU A 231 O GLN A 239
SHEET 1 D 3 TYR A 211 LYS A 216 0
SHEET 2 D 3 TYR A 254 HIS A 260 -1 O HIS A 257 N THR A 213
SHEET 3 D 3 VAL A 263 GLN A 268 -1 O LEU A 267 N CYS A 256
SHEET 1 E 4 LYS B 6 SER B 11 0
SHEET 2 E 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10
SHEET 3 E 4 PHE B 62 PHE B 70 -1 O PHE B 70 N ASN B 21
SHEET 4 E 4 GLU B 50 HIS B 51 -1 N GLU B 50 O TYR B 67
SHEET 1 F 4 LYS B 6 SER B 11 0
SHEET 2 F 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10
SHEET 3 F 4 PHE B 62 PHE B 70 -1 O PHE B 70 N ASN B 21
SHEET 4 F 4 SER B 55 PHE B 56 -1 N SER B 55 O TYR B 63
SHEET 1 G 4 GLU B 44 ARG B 45 0
SHEET 2 G 4 GLU B 36 LYS B 41 -1 N LYS B 41 O GLU B 44
SHEET 3 G 4 TYR B 78 ASN B 83 -1 O ARG B 81 N ASP B 38
SHEET 4 G 4 LYS B 91 LYS B 94 -1 O VAL B 93 N CYS B 80
SHEET 1 H 8 GLU C 44 PRO C 45 0
SHEET 2 H 8 HIS C 31 ASP C 37 -1 N THR C 35 O GLU C 44
SHEET 3 H 8 PHE C 22 VAL C 28 -1 N GLY C 26 O ILE C 33
SHEET 4 H 8 HIS C 3 VAL C 12 -1 N ARG C 6 O TYR C 27
SHEET 5 H 8 THR C 91 LEU C 100 -1 O TYR C 92 N GLY C 11
SHEET 6 H 8 THR C 106 TYR C 114 -1 O ALA C 113 N GLN C 93
SHEET 7 H 8 GLN C 117 ASN C 123 -1 O PHE C 122 N LEU C 110
SHEET 8 H 8 SER C 128 ALA C 131 -1 O LEU C 130 N ILE C 121
SHEET 1 I 4 LEU C 183 GLU C 190 0
SHEET 2 I 4 THR C 196 PHE C 205 -1 O PHE C 199 N ASN C 187
SHEET 3 I 4 TYR C 238 GLU C 245 -1 O ALA C 242 N CYS C 200
SHEET 4 I 4 ASP C 226 TYR C 227 -1 N ASP C 226 O SER C 243
SHEET 1 J 4 LEU C 183 GLU C 190 0
SHEET 2 J 4 THR C 196 PHE C 205 -1 O PHE C 199 N ASN C 187
SHEET 3 J 4 TYR C 238 GLU C 245 -1 O ALA C 242 N CYS C 200
SHEET 4 J 4 LEU C 231 PRO C 232 -1 N LEU C 231 O GLN C 239
SHEET 1 K 4 GLU C 219 GLU C 220 0
SHEET 2 K 4 TYR C 211 LYS C 216 -1 N LYS C 216 O GLU C 219
SHEET 3 K 4 TYR C 254 HIS C 260 -1 O HIS C 257 N THR C 213
SHEET 4 K 4 VAL C 263 GLN C 268 -1 O LEU C 267 N CYS C 256
SHEET 1 L 5 ASN D 3 ASP D 5 0
SHEET 2 L 5 VAL D 18 GLN D 25 -1 O GLN D 25 N ASN D 3
SHEET 3 L 5 TYR D 70 LEU D 75 -1 O LEU D 73 N ILE D 20
SHEET 4 L 5 PHE D 60 SER D 65 -1 N SER D 61 O LEU D 74
SHEET 5 L 5 GLY D 53 LYS D 57 -1 N LYS D 57 O PHE D 60
SHEET 1 M 5 GLU D 9 THR D 13 0
SHEET 2 M 5 THR D 103 LYS D 108 1 O LYS D 108 N ALA D 12
SHEET 3 M 5 ALA D 84 LYS D 91 -1 N ALA D 84 O LEU D 105
SHEET 4 M 5 LEU D 32 GLN D 37 -1 N PHE D 33 O ALA D 89
SHEET 5 M 5 THR D 44 ASN D 49 -1 O ASN D 49 N LEU D 32
SHEET 1 N 4 GLU D 9 THR D 13 0
SHEET 2 N 4 THR D 103 LYS D 108 1 O LYS D 108 N ALA D 12
SHEET 3 N 4 ALA D 84 LYS D 91 -1 N ALA D 84 O LEU D 105
SHEET 4 N 4 LEU D 97 TRP D 99 -1 O ILE D 98 N VAL D 90
SHEET 1 O 4 ALA D 117 GLN D 120 0
SHEET 2 O 4 CYS D 132 THR D 135 -1 O THR D 135 N ALA D 117
SHEET 3 O 4 PHE D 166 SER D 175 -1 O ALA D 173 N CYS D 132
SHEET 4 O 4 VAL D 151 ILE D 153 -1 N TYR D 152 O TRP D 174
SHEET 1 P 4 ALA D 117 GLN D 120 0
SHEET 2 P 4 CYS D 132 THR D 135 -1 O THR D 135 N ALA D 117
SHEET 3 P 4 PHE D 166 SER D 175 -1 O ALA D 173 N CYS D 132
SHEET 4 P 4 CYS D 157 MET D 161 -1 N MET D 161 O PHE D 166
SHEET 1 Q 4 VAL E 4 THR E 7 0
SHEET 2 Q 4 MET E 19 GLN E 25 -1 O ALA E 24 N THR E 5
SHEET 3 Q 4 PHE E 74 LEU E 78 -1 O LEU E 78 N MET E 19
SHEET 4 Q 4 TYR E 64 ARG E 68 -1 N ASN E 65 O ARG E 77
SHEET 1 R 6 PHE E 10 LYS E 14 0
SHEET 2 R 6 SER E 110 LEU E 115 1 O LEU E 115 N LEU E 13
SHEET 3 R 6 SER E 87 SER E 94 -1 N SER E 87 O LEU E 112
SHEET 4 R 6 SER E 31 GLN E 37 -1 N GLN E 37 O VAL E 88
SHEET 5 R 6 ARG E 44 SER E 51 -1 O ILE E 46 N TRP E 34
SHEET 6 R 6 THR E 54 LYS E 57 -1 O ASP E 56 N TYR E 48
SHEET 1 S 4 PHE E 10 LYS E 14 0
SHEET 2 S 4 SER E 110 LEU E 115 1 O LEU E 115 N LEU E 13
SHEET 3 S 4 SER E 87 SER E 94 -1 N SER E 87 O LEU E 112
SHEET 4 S 4 PHE E 105 PHE E 106 -1 O PHE E 105 N SER E 93
SHEET 1 T 4 GLU E 125 PHE E 129 0
SHEET 2 T 4 LYS E 141 PHE E 151 -1 O VAL E 145 N PHE E 129
SHEET 3 T 4 TYR E 189 SER E 198 -1 O VAL E 197 N ALA E 142
SHEET 4 T 4 VAL E 171 THR E 173 -1 N CYS E 172 O ARG E 194
SHEET 1 U 4 GLU E 125 PHE E 129 0
SHEET 2 U 4 LYS E 141 PHE E 151 -1 O VAL E 145 N PHE E 129
SHEET 3 U 4 TYR E 189 SER E 198 -1 O VAL E 197 N ALA E 142
SHEET 4 U 4 LEU E 178 LYS E 179 -1 N LEU E 178 O ALA E 190
SHEET 1 V 4 LYS E 165 VAL E 167 0
SHEET 2 V 4 VAL E 156 VAL E 162 -1 N VAL E 162 O LYS E 165
SHEET 3 V 4 HIS E 208 PHE E 215 -1 O GLN E 212 N SER E 159
SHEET 4 V 4 GLN E 234 TRP E 241 -1 O GLN E 234 N PHE E 215
SHEET 1 W 4 LYS F 6 SER F 11 0
SHEET 2 W 4 ASN F 21 PHE F 30 -1 O ASN F 24 N TYR F 10
SHEET 3 W 4 PHE F 62 PHE F 70 -1 O PHE F 70 N ASN F 21
SHEET 4 W 4 GLU F 50 HIS F 51 -1 N GLU F 50 O TYR F 67
SHEET 1 X 4 LYS F 6 SER F 11 0
SHEET 2 X 4 ASN F 21 PHE F 30 -1 O ASN F 24 N TYR F 10
SHEET 3 X 4 PHE F 62 PHE F 70 -1 O PHE F 70 N ASN F 21
SHEET 4 X 4 SER F 55 PHE F 56 -1 N SER F 55 O TYR F 63
SHEET 1 Y 4 GLU F 44 ARG F 45 0
SHEET 2 Y 4 ILE F 35 LYS F 41 -1 N LYS F 41 O GLU F 44
SHEET 3 Y 4 TYR F 78 HIS F 84 -1 O ARG F 81 N ASP F 38
SHEET 4 Y 4 LYS F 91 LYS F 94 -1 O VAL F 93 N CYS F 80
SHEET 1 Z 5 ASN G 3 ASP G 5 0
SHEET 2 Z 5 VAL G 18 GLN G 25 -1 O THR G 23 N ASP G 5
SHEET 3 Z 5 TYR G 70 LEU G 75 -1 O LEU G 73 N ILE G 20
SHEET 4 Z 5 PHE G 60 SER G 65 -1 N SER G 61 O LEU G 74
SHEET 5 Z 5 GLY G 53 LYS G 57 -1 N LYS G 57 O PHE G 60
SHEET 1 AA 5 GLU G 9 THR G 13 0
SHEET 2 AA 5 THR G 103 LYS G 108 1 O ILE G 106 N MET G 10
SHEET 3 AA 5 ALA G 84 LYS G 91 -1 N ALA G 84 O LEU G 105
SHEET 4 AA 5 LEU G 32 GLN G 37 -1 N PHE G 33 O ALA G 89
SHEET 5 AA 5 THR G 44 ASN G 49 -1 O ASN G 49 N LEU G 32
SHEET 1 AB 4 GLU G 9 THR G 13 0
SHEET 2 AB 4 THR G 103 LYS G 108 1 O ILE G 106 N MET G 10
SHEET 3 AB 4 ALA G 84 LYS G 91 -1 N ALA G 84 O LEU G 105
SHEET 4 AB 4 LEU G 97 TRP G 99 -1 O ILE G 98 N VAL G 90
SHEET 1 AC 4 ALA G 117 GLN G 120 0
SHEET 2 AC 4 SER G 130 THR G 135 -1 O LEU G 133 N TYR G 119
SHEET 3 AC 4 PHE G 166 SER G 175 -1 O ALA G 173 N CYS G 132
SHEET 4 AC 4 VAL G 151 ILE G 153 -1 N TYR G 152 O TRP G 174
SHEET 1 AD 4 ALA G 117 GLN G 120 0
SHEET 2 AD 4 SER G 130 THR G 135 -1 O LEU G 133 N TYR G 119
SHEET 3 AD 4 PHE G 166 SER G 175 -1 O ALA G 173 N CYS G 132
SHEET 4 AD 4 CYS G 157 MET G 161 -1 N MET G 161 O PHE G 166
SHEET 1 AE 4 VAL H 4 THR H 7 0
SHEET 2 AE 4 MET H 19 GLN H 25 -1 O ALA H 24 N THR H 5
SHEET 3 AE 4 PHE H 74 LEU H 78 -1 O LEU H 76 N LEU H 21
SHEET 4 AE 4 ASN H 65 ARG H 68 -1 N ASN H 65 O ARG H 77
SHEET 1 AF 6 PHE H 10 LYS H 14 0
SHEET 2 AF 6 SER H 110 LEU H 115 1 O LEU H 115 N LEU H 13
SHEET 3 AF 6 SER H 87 SER H 94 -1 N TYR H 89 O SER H 110
SHEET 4 AF 6 SER H 31 GLN H 37 -1 N GLN H 37 O VAL H 88
SHEET 5 AF 6 ARG H 44 SER H 49 -1 O ILE H 46 N TRP H 34
SHEET 6 AF 6 ASP H 56 LYS H 57 -1 O ASP H 56 N TYR H 48
SHEET 1 AG 4 PHE H 10 LYS H 14 0
SHEET 2 AG 4 SER H 110 LEU H 115 1 O LEU H 115 N LEU H 13
SHEET 3 AG 4 SER H 87 SER H 94 -1 N TYR H 89 O SER H 110
SHEET 4 AG 4 PHE H 105 PHE H 106 -1 O PHE H 105 N SER H 93
SHEET 1 AH 4 GLU H 125 PHE H 129 0
SHEET 2 AH 4 LYS H 141 PHE H 151 -1 O VAL H 145 N PHE H 129
SHEET 3 AH 4 TYR H 189 SER H 198 -1 O TYR H 189 N PHE H 151
SHEET 4 AH 4 VAL H 171 THR H 173 -1 N CYS H 172 O ARG H 194
SHEET 1 AI 4 GLU H 125 PHE H 129 0
SHEET 2 AI 4 LYS H 141 PHE H 151 -1 O VAL H 145 N PHE H 129
SHEET 3 AI 4 TYR H 189 SER H 198 -1 O TYR H 189 N PHE H 151
SHEET 4 AI 4 LEU H 178 LYS H 179 -1 N LEU H 178 O ALA H 190
SHEET 1 AJ 4 LYS H 165 VAL H 167 0
SHEET 2 AJ 4 VAL H 156 VAL H 162 -1 N VAL H 162 O LYS H 165
SHEET 3 AJ 4 HIS H 208 PHE H 215 -1 O GLN H 212 N SER H 159
SHEET 4 AJ 4 GLN H 234 TRP H 241 -1 O ALA H 240 N PHE H 209
SSBOND 1 CYS A 98 CYS A 161 1555 1555 2.05
SSBOND 2 CYS A 200 CYS A 256 1555 1555 2.01
SSBOND 3 CYS B 25 CYS B 80 1555 1555 2.03
SSBOND 4 CYS C 98 CYS C 161 1555 1555 2.06
SSBOND 5 CYS C 200 CYS C 256 1555 1555 2.02
SSBOND 6 CYS D 22 CYS D 88 1555 1555 2.02
SSBOND 7 CYS D 132 CYS D 182 1555 1555 2.05
SSBOND 8 CYS D 157 CYS E 172 1555 1555 2.03
SSBOND 9 CYS E 23 CYS E 91 1555 1555 2.02
SSBOND 10 CYS E 146 CYS E 211 1555 1555 2.02
SSBOND 11 CYS F 25 CYS F 80 1555 1555 2.03
SSBOND 12 CYS G 22 CYS G 88 1555 1555 2.01
SSBOND 13 CYS G 132 CYS G 182 1555 1555 2.05
SSBOND 14 CYS G 157 CYS H 172 1555 1555 2.05
SSBOND 15 CYS H 23 CYS H 91 1555 1555 2.01
SSBOND 16 CYS H 146 CYS H 211 1555 1555 2.02
LINK NA NA H 301 O HOH H 574 1555 1555 2.23
LINK O TYR H 64 NA NA H 301 1555 1555 2.24
LINK NA NA H 301 O HOH H 571 1555 1555 2.40
LINK OH TYR H 47 NA NA H 301 1555 1555 2.47
LINK NA NA H 301 O HOH H 575 1555 1555 2.52
LINK O PRO H 61 NA NA H 301 1555 1555 2.94
LINK NZ LYS A 43 C7 2LJ A 301 1555 1555 1.30
LINK NZ LYS C 43 C7 2LJ C 301 1555 1555 1.30
CISPEP 1 TYR A 206 PRO A 207 0 1.99
CISPEP 2 HIS B 31 PRO B 32 0 -0.78
CISPEP 3 TYR C 206 PRO C 207 0 0.93
CISPEP 4 SER D 149 ASP D 150 0 8.31
CISPEP 5 THR E 7 PRO E 8 0 -2.38
CISPEP 6 TYR E 152 PRO E 153 0 -4.60
CISPEP 7 HIS F 31 PRO F 32 0 -0.09
CISPEP 8 THR H 7 PRO H 8 0 -3.97
CISPEP 9 TYR H 152 PRO H 153 0 -4.61
SITE 1 AC1 18 TYR A 7 ARG A 9 SER A 24 LYS A 43
SITE 2 AC1 18 HIS A 58 TYR A 62 LEU A 66 TRP A 69
SITE 3 AC1 18 ARG A 94 ILE A 96 TYR A 152 GLN A 153
SITE 4 AC1 18 TRP A 156 HOH A 408 HOH A 412 HOH A 512
SITE 5 AC1 18 TYR G 95 HOH H 544
SITE 1 AC2 17 TYR C 7 ARG C 9 SER C 24 LYS C 43
SITE 2 AC2 17 TYR C 62 LEU C 66 TRP C 69 ARG C 94
SITE 3 AC2 17 ILE C 96 TYR C 152 GLN C 153 TRP C 156
SITE 4 AC2 17 HOH C 401 HOH C 408 HOH C 411 HOH C 416
SITE 5 AC2 17 TYR D 95
SITE 1 AC3 6 TYR H 47 PRO H 61 TYR H 64 HOH H 571
SITE 2 AC3 6 HOH H 574 HOH H 575
CRYST1 218.760 71.110 144.280 90.00 104.87 90.00 C 1 2 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 0.004571 0.000000 0.001214 0.00000
SCALE2 0.000000 0.014063 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007171 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
