HEADER IMMUNE SYSTEM 12-MAY-14 4PJX
TITLE STRUCTURE OF HUMAN MR1-AC-6-FP IN COMPLEX WITH HUMAN MAIT C-A11 TCR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MAJOR HISTOCOMPATIBILITY COMPLEX CLASS I-RELATED GENE
COMPND 3 PROTEIN;
COMPND 4 CHAIN: A, C;
COMPND 5 FRAGMENT: UNP RESIDUES 23-292;
COMPND 6 SYNONYM: MHC CLASS I-RELATED GENE PROTEIN,CLASS I HISTOCOMPATIBILITY
COMPND 7 ANTIGEN-LIKE PROTEIN;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: BETA-2-MICROGLOBULIN;
COMPND 12 CHAIN: B, D;
COMPND 13 ENGINEERED: YES;
COMPND 14 MOL_ID: 3;
COMPND 15 MOLECULE: TCR-ALPHA;
COMPND 16 CHAIN: E, G;
COMPND 17 ENGINEERED: YES;
COMPND 18 MOL_ID: 4;
COMPND 19 MOLECULE: TCR-BETA;
COMPND 20 CHAIN: F, H;
COMPND 21 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 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: B2M, CDABP0092, HDCMA22P;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 MOL_ID: 3;
SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 17 ORGANISM_COMMON: HUMAN;
SOURCE 18 ORGANISM_TAXID: 9606;
SOURCE 19 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 20 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 21 MOL_ID: 4;
SOURCE 22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 23 ORGANISM_COMMON: HUMAN;
SOURCE 24 ORGANISM_TAXID: 9606;
SOURCE 25 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 26 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS MR1, TCR, IMMUNE COMPLEX, AC-6-FP, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR R.W.BIRKINSHAW,J.ROSSJOHN
REVDAT 4 27-DEC-23 4PJX 1 HEADER SOURCE JRNL REMARK
REVDAT 3 01-OCT-14 4PJX 1 JRNL
REVDAT 2 06-AUG-14 4PJX 1 JRNL
REVDAT 1 02-JUL-14 4PJX 0
JRNL AUTH S.B.ECKLE,R.W.BIRKINSHAW,L.KOSTENKO,A.J.CORBETT,
JRNL AUTH 2 H.E.MCWILLIAM,R.REANTRAGOON,Z.CHEN,N.A.GHERARDIN,T.BEDDOE,
JRNL AUTH 3 L.LIU,O.PATEL,B.MEEHAN,D.P.FAIRLIE,J.A.VILLADANGOS,
JRNL AUTH 4 D.I.GODFREY,L.KJER-NIELSEN,J.MCCLUSKEY,J.ROSSJOHN
JRNL TITL A MOLECULAR BASIS UNDERPINNING THE T CELL RECEPTOR
JRNL TITL 2 HETEROGENEITY OF MUCOSAL-ASSOCIATED INVARIANT T CELLS.
JRNL REF J.EXP.MED. V. 211 1585 2014
JRNL REFN ESSN 1540-9538
JRNL PMID 25049336
JRNL DOI 10.1084/JEM.20140484
REMARK 2
REMARK 2 RESOLUTION. 2.25 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) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.94
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 96819
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) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4840
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) : 2.25
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.31
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.85
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 7064
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2067
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6695
REMARK 3 BIN R VALUE (WORKING SET) : 0.2040
REMARK 3 BIN FREE R VALUE : 0.2532
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.22
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 369
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 : 12229
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 107
REMARK 3 SOLVENT ATOMS : 910
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 44.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.74
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.66990
REMARK 3 B22 (A**2) : -6.17270
REMARK 3 B33 (A**2) : 7.84250
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 6.95380
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.277
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.215
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.169
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.210
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.169
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 : 0.942
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.927
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 12725 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 17342 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 5612 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 289 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1903 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 12725 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 1633 ; 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 : 14818 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.07
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.83
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 2.68
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 23
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: {A|0 - 55}
REMARK 3 ORIGIN FOR THE GROUP (A): -5.2154 26.8748 163.0574
REMARK 3 T TENSOR
REMARK 3 T11: -0.0584 T22: 0.0065
REMARK 3 T33: -0.0408 T12: -0.0413
REMARK 3 T13: 0.0205 T23: -0.0196
REMARK 3 L TENSOR
REMARK 3 L11: 0.8939 L22: 2.6397
REMARK 3 L33: 2.0018 L12: 0.3531
REMARK 3 L13: 0.7105 L23: 1.2184
REMARK 3 S TENSOR
REMARK 3 S11: -0.0290 S12: 0.2347 S13: 0.1148
REMARK 3 S21: -0.1641 S22: -0.1572 S23: 0.2210
REMARK 3 S31: -0.3056 S32: -0.1208 S33: 0.1862
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: {A|56 - 171}
REMARK 3 ORIGIN FOR THE GROUP (A): 3.4699 15.7030 166.4319
REMARK 3 T TENSOR
REMARK 3 T11: -0.0638 T22: 0.0461
REMARK 3 T33: -0.0658 T12: -0.0497
REMARK 3 T13: 0.0194 T23: -0.0406
REMARK 3 L TENSOR
REMARK 3 L11: 0.7537 L22: 1.9977
REMARK 3 L33: 0.9187 L12: 0.0560
REMARK 3 L13: 0.0438 L23: -0.1182
REMARK 3 S TENSOR
REMARK 3 S11: 0.0142 S12: 0.1277 S13: 0.0032
REMARK 3 S21: 0.1095 S22: -0.0840 S23: -0.0993
REMARK 3 S31: -0.0047 S32: 0.0887 S33: 0.0698
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: {A|172 - 195}
REMARK 3 ORIGIN FOR THE GROUP (A): -20.4997 34.9496 187.5809
REMARK 3 T TENSOR
REMARK 3 T11: 0.0357 T22: -0.0711
REMARK 3 T33: 0.0146 T12: 0.0456
REMARK 3 T13: -0.0396 T23: -0.0121
REMARK 3 L TENSOR
REMARK 3 L11: 3.2634 L22: 1.5488
REMARK 3 L33: 1.4991 L12: 1.0722
REMARK 3 L13: -1.0763 L23: -0.0460
REMARK 3 S TENSOR
REMARK 3 S11: 0.0512 S12: -0.2094 S13: -0.0287
REMARK 3 S21: 0.1258 S22: -0.1036 S23: 0.2012
REMARK 3 S31: -0.1270 S32: -0.1069 S33: 0.0524
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: {A|196 - 269}
REMARK 3 ORIGIN FOR THE GROUP (A): -18.0502 30.6597 191.6460
REMARK 3 T TENSOR
REMARK 3 T11: -0.0267 T22: -0.0417
REMARK 3 T33: -0.0627 T12: 0.0060
REMARK 3 T13: -0.0231 T23: 0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 1.2290 L22: 2.6085
REMARK 3 L33: 0.7808 L12: 0.3855
REMARK 3 L13: -0.0733 L23: 0.2539
REMARK 3 S TENSOR
REMARK 3 S11: 0.0525 S12: -0.2214 S13: -0.2058
REMARK 3 S21: 0.2539 S22: -0.0892 S23: 0.0564
REMARK 3 S31: 0.1493 S32: -0.0814 S33: 0.0366
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: {B|0 - 30}
REMARK 3 ORIGIN FOR THE GROUP (A): -24.5226 26.6386 174.3992
REMARK 3 T TENSOR
REMARK 3 T11: -0.0982 T22: -0.0423
REMARK 3 T33: -0.0590 T12: -0.0132
REMARK 3 T13: -0.0497 T23: -0.0504
REMARK 3 L TENSOR
REMARK 3 L11: 3.0228 L22: 0.0000
REMARK 3 L33: 1.8890 L12: 0.9512
REMARK 3 L13: -0.4724 L23: 0.0253
REMARK 3 S TENSOR
REMARK 3 S11: -0.0492 S12: 0.1499 S13: 0.2173
REMARK 3 S21: 0.0706 S22: -0.0907 S23: 0.0541
REMARK 3 S31: -0.1463 S32: -0.2020 S33: 0.1399
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: {B|31 - 51}
REMARK 3 ORIGIN FOR THE GROUP (A): -27.7624 24.5513 164.1607
REMARK 3 T TENSOR
REMARK 3 T11: 0.0455 T22: 0.1242
REMARK 3 T33: -0.0360 T12: 0.0216
REMARK 3 T13: -0.0878 T23: -0.0330
REMARK 3 L TENSOR
REMARK 3 L11: 0.6934 L22: 5.5969
REMARK 3 L33: -0.1585 L12: -1.0133
REMARK 3 L13: -1.2040 L23: 1.7106
REMARK 3 S TENSOR
REMARK 3 S11: -0.1379 S12: 0.3625 S13: 0.2106
REMARK 3 S21: -0.5802 S22: -0.0668 S23: 0.1476
REMARK 3 S31: -0.2744 S32: -0.1409 S33: 0.2048
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: {B|52 - 77}
REMARK 3 ORIGIN FOR THE GROUP (A): -22.1231 27.1218 170.0002
REMARK 3 T TENSOR
REMARK 3 T11: -0.0622 T22: -0.0653
REMARK 3 T33: -0.0637 T12: -0.0041
REMARK 3 T13: -0.0357 T23: -0.0282
REMARK 3 L TENSOR
REMARK 3 L11: 5.7505 L22: 2.7280
REMARK 3 L33: 2.0999 L12: -1.7408
REMARK 3 L13: -0.6568 L23: 0.5207
REMARK 3 S TENSOR
REMARK 3 S11: -0.1184 S12: 0.3594 S13: 0.3676
REMARK 3 S21: -0.2196 S22: 0.0618 S23: 0.2298
REMARK 3 S31: -0.3986 S32: -0.2763 S33: 0.0566
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: {B|78 - 98}
REMARK 3 ORIGIN FOR THE GROUP (A): -31.2396 20.6096 171.2321
REMARK 3 T TENSOR
REMARK 3 T11: -0.1182 T22: 0.0891
REMARK 3 T33: 0.0385 T12: -0.0083
REMARK 3 T13: -0.0540 T23: -0.1087
REMARK 3 L TENSOR
REMARK 3 L11: 1.1359 L22: 4.2276
REMARK 3 L33: 0.0154 L12: -1.7547
REMARK 3 L13: -0.1793 L23: 0.5362
REMARK 3 S TENSOR
REMARK 3 S11: -0.0883 S12: 0.1108 S13: -0.0846
REMARK 3 S21: -0.3131 S22: -0.0200 S23: 0.4245
REMARK 3 S31: -0.0755 S32: -0.2948 S33: 0.1083
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: {E|2 - 116}
REMARK 3 ORIGIN FOR THE GROUP (A): 32.1538 21.4111 158.2712
REMARK 3 T TENSOR
REMARK 3 T11: -0.1694 T22: 0.0450
REMARK 3 T33: -0.1051 T12: -0.0405
REMARK 3 T13: -0.0256 T23: 0.0674
REMARK 3 L TENSOR
REMARK 3 L11: 1.9058 L22: 0.9387
REMARK 3 L33: 2.4690 L12: 0.6213
REMARK 3 L13: -0.7848 L23: -0.5721
REMARK 3 S TENSOR
REMARK 3 S11: -0.0459 S12: 0.0831 S13: 0.0532
REMARK 3 S21: -0.0350 S22: -0.1138 S23: -0.1324
REMARK 3 S31: 0.1529 S32: 0.3002 S33: 0.1596
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: {E|117 - 198}
REMARK 3 ORIGIN FOR THE GROUP (A): 57.0533 23.8689 136.9738
REMARK 3 T TENSOR
REMARK 3 T11: -0.3072 T22: 0.2250
REMARK 3 T33: -0.0701 T12: 0.0933
REMARK 3 T13: 0.1268 T23: 0.1820
REMARK 3 L TENSOR
REMARK 3 L11: 8.8999 L22: 2.7698
REMARK 3 L33: 5.5303 L12: 0.6204
REMARK 3 L13: 1.1240 L23: -0.2107
REMARK 3 S TENSOR
REMARK 3 S11: -0.1876 S12: -0.3804 S13: 0.5450
REMARK 3 S21: -0.2067 S22: 0.1314 S23: -0.3098
REMARK 3 S31: -0.2259 S32: 0.7553 S33: 0.0561
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: {F|3 - 108}
REMARK 3 ORIGIN FOR THE GROUP (A): 16.0063 20.5151 140.8545
REMARK 3 T TENSOR
REMARK 3 T11: -0.0829 T22: 0.0594
REMARK 3 T33: -0.1299 T12: -0.0862
REMARK 3 T13: 0.0028 T23: 0.0156
REMARK 3 L TENSOR
REMARK 3 L11: 2.3667 L22: 1.4488
REMARK 3 L33: 3.6389 L12: -0.0414
REMARK 3 L13: -1.1024 L23: -1.1110
REMARK 3 S TENSOR
REMARK 3 S11: -0.0382 S12: 0.3113 S13: 0.0429
REMARK 3 S21: -0.1499 S22: -0.0778 S23: 0.0054
REMARK 3 S31: 0.2028 S32: -0.2278 S33: 0.1160
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: {F|109 - 123}
REMARK 3 ORIGIN FOR THE GROUP (A): 29.6217 25.8972 124.3213
REMARK 3 T TENSOR
REMARK 3 T11: -0.0740 T22: -0.0297
REMARK 3 T33: -0.1619 T12: 0.0180
REMARK 3 T13: 0.0812 T23: 0.0777
REMARK 3 L TENSOR
REMARK 3 L11: -0.0740 L22: 0.0000
REMARK 3 L33: 3.6305 L12: 1.6328
REMARK 3 L13: -0.2926 L23: -0.9021
REMARK 3 S TENSOR
REMARK 3 S11: -0.0376 S12: -0.0030 S13: 0.3518
REMARK 3 S21: -0.2709 S22: 0.0409 S23: 0.0368
REMARK 3 S31: -0.1166 S32: -0.0983 S33: -0.0034
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: {F|124 - 214}
REMARK 3 ORIGIN FOR THE GROUP (A): 47.4233 15.0157 131.2301
REMARK 3 T TENSOR
REMARK 3 T11: -0.1069 T22: -0.0467
REMARK 3 T33: -0.0256 T12: 0.1645
REMARK 3 T13: 0.1202 T23: 0.1582
REMARK 3 L TENSOR
REMARK 3 L11: 5.3063 L22: 1.6988
REMARK 3 L33: 3.5039 L12: -0.8325
REMARK 3 L13: 1.3450 L23: -0.8136
REMARK 3 S TENSOR
REMARK 3 S11: -0.0359 S12: -0.3117 S13: -1.0095
REMARK 3 S21: -0.0452 S22: 0.0780 S23: -0.3060
REMARK 3 S31: 0.6577 S32: 0.6606 S33: -0.0421
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: {F|215 - 241}
REMARK 3 ORIGIN FOR THE GROUP (A): 34.7195 16.0084 119.0060
REMARK 3 T TENSOR
REMARK 3 T11: 0.0677 T22: -0.1426
REMARK 3 T33: -0.1485 T12: 0.0491
REMARK 3 T13: 0.1106 T23: -0.0445
REMARK 3 L TENSOR
REMARK 3 L11: 4.5845 L22: 4.3684
REMARK 3 L33: 5.2633 L12: 0.6553
REMARK 3 L13: 0.0569 L23: 1.3938
REMARK 3 S TENSOR
REMARK 3 S11: -0.1619 S12: 0.5297 S13: -0.4369
REMARK 3 S21: -0.6052 S22: 0.2392 S23: -0.0585
REMARK 3 S31: 0.4631 S32: -0.2868 S33: -0.0773
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: {C|0 - 83}
REMARK 3 ORIGIN FOR THE GROUP (A): -46.5375 1.8060 191.8826
REMARK 3 T TENSOR
REMARK 3 T11: -0.0203 T22: 0.0592
REMARK 3 T33: -0.0606 T12: 0.0592
REMARK 3 T13: 0.0021 T23: 0.0004
REMARK 3 L TENSOR
REMARK 3 L11: 1.2703 L22: 1.1073
REMARK 3 L33: 1.6867 L12: 0.2253
REMARK 3 L13: 0.3593 L23: -0.0493
REMARK 3 S TENSOR
REMARK 3 S11: 0.0369 S12: -0.2531 S13: 0.1046
REMARK 3 S21: 0.2984 S22: 0.0646 S23: 0.1698
REMARK 3 S31: 0.1671 S32: -0.1367 S33: -0.1016
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: {C|84 - 171}
REMARK 3 ORIGIN FOR THE GROUP (A): -36.0058 2.9186 181.8942
REMARK 3 T TENSOR
REMARK 3 T11: -0.0599 T22: -0.0072
REMARK 3 T33: -0.0878 T12: 0.0492
REMARK 3 T13: -0.0352 T23: -0.0107
REMARK 3 L TENSOR
REMARK 3 L11: 1.3130 L22: 3.3336
REMARK 3 L33: 0.7953 L12: 0.7010
REMARK 3 L13: 0.0008 L23: 0.0915
REMARK 3 S TENSOR
REMARK 3 S11: 0.0365 S12: 0.0305 S13: 0.0436
REMARK 3 S21: -0.0695 S22: 0.0489 S23: -0.1737
REMARK 3 S31: 0.0848 S32: 0.0818 S33: -0.0853
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: {C|172 - 269}
REMARK 3 ORIGIN FOR THE GROUP (A): -64.2404 1.7328 163.7055
REMARK 3 T TENSOR
REMARK 3 T11: -0.2184 T22: 0.0342
REMARK 3 T33: 0.0078 T12: -0.1243
REMARK 3 T13: -0.0777 T23: 0.1774
REMARK 3 L TENSOR
REMARK 3 L11: 3.0349 L22: 1.9827
REMARK 3 L33: 4.9952 L12: -0.2470
REMARK 3 L13: 2.0383 L23: -0.3091
REMARK 3 S TENSOR
REMARK 3 S11: -0.2551 S12: 0.2143 S13: 0.4703
REMARK 3 S21: -0.0726 S22: 0.0990 S23: 0.1379
REMARK 3 S31: -0.4422 S32: 0.1141 S33: 0.1561
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: {D|1 - 96}
REMARK 3 ORIGIN FOR THE GROUP (A): -65.5729 13.8104 181.5970
REMARK 3 T TENSOR
REMARK 3 T11: -0.3063 T22: -0.0548
REMARK 3 T33: 0.1095 T12: 0.1217
REMARK 3 T13: 0.0349 T23: 0.0511
REMARK 3 L TENSOR
REMARK 3 L11: 5.9274 L22: 3.0941
REMARK 3 L33: 2.3410 L12: 0.6110
REMARK 3 L13: 0.6779 L23: 0.1805
REMARK 3 S TENSOR
REMARK 3 S11: -0.1907 S12: -0.4507 S13: 0.8996
REMARK 3 S21: 0.1847 S22: 0.1630 S23: 0.9848
REMARK 3 S31: -0.3038 S32: -0.5725 S33: 0.0277
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: {G|2 - 116}
REMARK 3 ORIGIN FOR THE GROUP (A): -17.0617 -18.0462 194.1525
REMARK 3 T TENSOR
REMARK 3 T11: 0.0037 T22: -0.0558
REMARK 3 T33: -0.0387 T12: 0.0535
REMARK 3 T13: -0.0684 T23: -0.0560
REMARK 3 L TENSOR
REMARK 3 L11: 2.4407 L22: 0.8080
REMARK 3 L33: 1.2257 L12: -1.1380
REMARK 3 L13: 1.2432 L23: -0.5935
REMARK 3 S TENSOR
REMARK 3 S11: 0.0052 S12: -0.1209 S13: 0.0016
REMARK 3 S21: 0.0270 S22: 0.0040 S23: -0.0189
REMARK 3 S31: -0.0264 S32: -0.0989 S33: -0.0092
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: {G|117 - 199}
REMARK 3 ORIGIN FOR THE GROUP (A): 3.4665 -31.8508 216.1868
REMARK 3 T TENSOR
REMARK 3 T11: 0.1756 T22: -0.1172
REMARK 3 T33: -0.0646 T12: 0.0239
REMARK 3 T13: -0.0556 T23: -0.0099
REMARK 3 L TENSOR
REMARK 3 L11: 2.1537 L22: 1.6369
REMARK 3 L33: 3.8410 L12: 0.3221
REMARK 3 L13: -0.6536 L23: 1.3717
REMARK 3 S TENSOR
REMARK 3 S11: -0.0933 S12: 0.0989 S13: -0.2113
REMARK 3 S21: 0.4511 S22: 0.0284 S23: -0.1117
REMARK 3 S31: 0.4026 S32: -0.0359 S33: 0.0648
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: {H|3 - 123}
REMARK 3 ORIGIN FOR THE GROUP (A): -28.8112 -9.7786 213.3945
REMARK 3 T TENSOR
REMARK 3 T11: 0.0931 T22: -0.0169
REMARK 3 T33: -0.1466 T12: 0.0602
REMARK 3 T13: -0.0607 T23: -0.0253
REMARK 3 L TENSOR
REMARK 3 L11: 0.7841 L22: 0.5896
REMARK 3 L33: 2.1627 L12: -0.5952
REMARK 3 L13: 0.8417 L23: -1.4565
REMARK 3 S TENSOR
REMARK 3 S11: -0.0228 S12: -0.2375 S13: -0.0470
REMARK 3 S21: 0.2147 S22: 0.0308 S23: -0.0015
REMARK 3 S31: -0.2124 S32: -0.3281 S33: -0.0080
REMARK 3
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: {H|124 - 214}
REMARK 3 ORIGIN FOR THE GROUP (A): 0.5276 -20.1539 221.1087
REMARK 3 T TENSOR
REMARK 3 T11: 0.0234 T22: -0.1554
REMARK 3 T33: -0.1481 T12: 0.0261
REMARK 3 T13: -0.0458 T23: -0.0167
REMARK 3 L TENSOR
REMARK 3 L11: 3.6052 L22: 1.2589
REMARK 3 L33: 2.4437 L12: -0.3352
REMARK 3 L13: -1.4541 L23: 0.3069
REMARK 3 S TENSOR
REMARK 3 S11: 0.0964 S12: 0.1463 S13: 0.1171
REMARK 3 S21: 0.1231 S22: 0.0366 S23: -0.0231
REMARK 3 S31: -0.0278 S32: -0.1302 S33: -0.1330
REMARK 3
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: {H|215 - 243}
REMARK 3 ORIGIN FOR THE GROUP (A): -11.7191 -15.9443 233.4624
REMARK 3 T TENSOR
REMARK 3 T11: 0.0456 T22: -0.0047
REMARK 3 T33: -0.1103 T12: 0.0134
REMARK 3 T13: -0.0483 T23: -0.0417
REMARK 3 L TENSOR
REMARK 3 L11: 7.6380 L22: 1.2395
REMARK 3 L33: 2.5159 L12: 0.7738
REMARK 3 L13: -3.0685 L23: 0.3452
REMARK 3 S TENSOR
REMARK 3 S11: -0.0153 S12: -0.0380 S13: 0.0469
REMARK 3 S21: 0.1166 S22: 0.0033 S23: -0.0452
REMARK 3 S31: -0.0612 S32: -0.2875 S33: 0.0120
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4PJX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-MAY-14.
REMARK 100 THE DEPOSITION ID IS D_1000201529.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-MAR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
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) : 0.95
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 96851
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 47.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.9000
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: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, BIS-TRIS PROPANE, SODIUM
REMARK 280 ACETATE, VAPOR DIFFUSION, HANGING 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 106.96050
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.79050
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 106.96050
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 34.79050
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, 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 HIS A 17
REMARK 465 GLY A 18
REMARK 465 ASP A 247
REMARK 465 PRO A 248
REMARK 465 GLN A 249
REMARK 465 SER A 250
REMARK 465 SER A 251
REMARK 465 ASN A 252
REMARK 465 PRO A 270
REMARK 465 MET B 99
REMARK 465 LYS C 189
REMARK 465 GLU C 190
REMARK 465 THR C 191
REMARK 465 PHE C 192
REMARK 465 PRO C 193
REMARK 465 GLY C 194
REMARK 465 VAL C 195
REMARK 465 THR C 196
REMARK 465 GLY C 218
REMARK 465 GLU C 219
REMARK 465 GLU C 220
REMARK 465 ILE C 221
REMARK 465 VAL C 222
REMARK 465 GLN C 223
REMARK 465 GLU C 224
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 MET D 0
REMARK 465 ARG D 97
REMARK 465 ASP D 98
REMARK 465 MET D 99
REMARK 465 HIS E -1
REMARK 465 MET E 0
REMARK 465 GLY E 1
REMARK 465 SER E 124
REMARK 465 LYS E 125
REMARK 465 SER E 126
REMARK 465 SER E 127
REMARK 465 ASP E 128
REMARK 465 LYS E 129
REMARK 465 ARG E 162
REMARK 465 SER E 163
REMARK 465 MET E 164
REMARK 465 ASP E 165
REMARK 465 SER E 199
REMARK 465 PRO E 200
REMARK 465 GLU E 201
REMARK 465 SER E 202
REMARK 465 SER E 203
REMARK 465 HIS F -1
REMARK 465 MET F 0
REMARK 465 ASN F 1
REMARK 465 ALA F 2
REMARK 465 ARG F 205
REMARK 465 ASN F 206
REMARK 465 ARG F 242
REMARK 465 ALA F 243
REMARK 465 ASP F 244
REMARK 465 HIS G -1
REMARK 465 MET G 0
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 HIS H -1
REMARK 465 MET H 0
REMARK 465 ASN H 1
REMARK 465 ALA H 2
REMARK 465 ASP H 244
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 ASP A 14 CG OD1 OD2
REMARK 470 ILE A 16 CG1 CG2 CD1
REMARK 470 LYS A 173 CD CE NZ
REMARK 470 GLU A 190 OE1 OE2
REMARK 470 LYS A 216 CE NZ
REMARK 470 GLU A 219 CG CD OE1 OE2
REMARK 470 GLU A 220 CG CD OE1 OE2
REMARK 470 GLU A 224 CG CD OE1 OE2
REMARK 470 LEU A 246 CG CD1 CD2
REMARK 470 LEU A 253 CG CD1 CD2
REMARK 470 LYS B 19 CG CD CE NZ
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 50 CG CD OE1 OE2
REMARK 470 LYS B 58 CG CD CE NZ
REMARK 470 GLU B 74 CG CD OE1 OE2
REMARK 470 LYS B 75 CG CD CE NZ
REMARK 470 ILE C 16 CG1 CG2 CD1
REMARK 470 HIS C 17 CG ND1 CD2 CE1 NE2
REMARK 470 VAL C 19 CG1 CG2
REMARK 470 GLU C 52 CG CD OE1 OE2
REMARK 470 LYS C 78 CG CD CE NZ
REMARK 470 LYS C 173 CG CD CE NZ
REMARK 470 ARG C 188 CG CD NE CZ NH1 NH2
REMARK 470 TYR C 211 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS C 216 CG CD CE NZ
REMARK 470 GLU C 245 CG CD OE1 OE2
REMARK 470 LEU C 246 CG CD1 CD2
REMARK 470 ASN C 252 CG OD1 ND2
REMARK 470 LEU C 253 CG CD1 CD2
REMARK 470 GLU D 16 CG CD OE1 OE2
REMARK 470 LYS D 19 CG CD CE NZ
REMARK 470 GLU D 36 CG CD OE1 OE2
REMARK 470 LYS D 41 CG CD CE NZ
REMARK 470 GLU D 44 CG CD OE1 OE2
REMARK 470 ARG D 45 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 47 CG CD OE1 OE2
REMARK 470 LYS D 48 CG CD CE NZ
REMARK 470 VAL D 49 CG1 CG2
REMARK 470 LYS D 58 CG CD CE NZ
REMARK 470 GLU D 74 CG CD OE1 OE2
REMARK 470 LYS D 75 CG CD CE NZ
REMARK 470 GLU D 77 CG CD OE1 OE2
REMARK 470 SER D 88 OG
REMARK 470 GLN D 89 CG CD OE1 NE2
REMARK 470 LYS D 91 CE NZ
REMARK 470 ILE D 92 CG1 CG2 CD1
REMARK 470 LYS D 94 CG CD CE NZ
REMARK 470 ASP D 96 CG OD1 OD2
REMARK 470 ILE E 4 CD1
REMARK 470 GLU E 9 CD OE1 OE2
REMARK 470 GLN E 25 CD OE1 NE2
REMARK 470 GLN E 112 CG CD OE1 NE2
REMARK 470 ASN E 113 CG OD1 ND2
REMARK 470 ARG E 122 CG CD NE CZ NH1 NH2
REMARK 470 ASP E 123 CG OD1 OD2
REMARK 470 SER E 130 OG
REMARK 470 ASP E 138 CG OD1 OD2
REMARK 470 GLN E 140 CG CD OE1 NE2
REMARK 470 SER E 144 OG
REMARK 470 GLN E 145 CG CD OE1 NE2
REMARK 470 SER E 146 OG
REMARK 470 LYS E 147 CG CD CE NZ
REMARK 470 ASP E 148 CG OD1 OD2
REMARK 470 SER E 149 OG
REMARK 470 VAL E 151 CG1 CG2
REMARK 470 ASP E 160 CG OD1 OD2
REMARK 470 LYS E 167 CD CE NZ
REMARK 470 LYS E 177 CG CD CE NZ
REMARK 470 SER E 178 OG
REMARK 470 ASP E 179 CG OD1 OD2
REMARK 470 ASN E 184 CG OD1 ND2
REMARK 470 ASN E 188 CG OD1 ND2
REMARK 470 ILE E 190 CG1 CG2 CD1
REMARK 470 ILE E 191 CG1 CG2 CD1
REMARK 470 GLU E 193 CG CD OE1 OE2
REMARK 470 ASP E 194 CG OD1 OD2
REMARK 470 LYS F 9 CG CD CE NZ
REMARK 470 LYS F 14 NZ
REMARK 470 GLU F 79 CG CD OE1 OE2
REMARK 470 GLU F 107 CG CD OE1 OE2
REMARK 470 LYS F 118 CE NZ
REMARK 470 GLU F 129 CG CD OE1 OE2
REMARK 470 GLU F 132 CG CD OE1 OE2
REMARK 470 ILE F 135 CG1 CG2 CD1
REMARK 470 SER F 136 OG
REMARK 470 GLN F 139 CG CD OE1 NE2
REMARK 470 LYS F 140 CG CD CE NZ
REMARK 470 LYS F 164 CG CD CE NZ
REMARK 470 VAL F 166 CG1 CG2
REMARK 470 SER F 168 OG
REMARK 470 GLN F 175 CG CD OE1 NE2
REMARK 470 SER F 197 OG
REMARK 470 THR F 199 OG1 CG2
REMARK 470 ASN F 203 CG OD1 ND2
REMARK 470 HIS F 207 CG ND1 CD2 CE1 NE2
REMARK 470 PHE F 208 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER F 218 OG
REMARK 470 GLU F 219 CG CD OE1 OE2
REMARK 470 ASN F 220 CG OD1 ND2
REMARK 470 GLU F 222 CG CD OE1 OE2
REMARK 470 THR F 224 OG1 CG2
REMARK 470 ASP F 226 CG OD1 OD2
REMARK 470 GLU G 55 CG CD OE1 OE2
REMARK 470 LYS G 57 CD CE NZ
REMARK 470 LYS G 68 CD CE NZ
REMARK 470 LYS G 76 NZ
REMARK 470 GLN G 96 CG CD OE1 NE2
REMARK 470 GLN G 112 CG CD OE1 NE2
REMARK 470 ASP G 138 CG OD1 OD2
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 SER G 149 OG
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 G 188 CG OD1 ND2
REMARK 470 ASP G 194 CG OD1 OD2
REMARK 470 SER G 199 OG
REMARK 470 LYS H 9 CG CD CE NZ
REMARK 470 GLN H 22 CD OE1 NE2
REMARK 470 LYS H 57 CG CD CE NZ
REMARK 470 ARG H 77 CG CD NE CZ NH1 NH2
REMARK 470 GLU H 79 CG CD OE1 OE2
REMARK 470 GLU H 107 CG CD OE1 OE2
REMARK 470 GLU H 115 CG CD OE1 OE2
REMARK 470 LYS H 118 CD CE NZ
REMARK 470 GLU H 132 CG CD OE1 OE2
REMARK 470 LYS H 164 CG CD CE NZ
REMARK 470 GLN H 175 CG CD OE1 NE2
REMARK 470 GLN H 180 OE1 NE2
REMARK 470 LEU H 183 CD1 CD2
REMARK 470 ASN H 184 CG OD1 ND2
REMARK 470 ASP H 185 CG OD1 OD2
REMARK 470 GLU H 222 CG CD OE1 OE2
REMARK 470 ARG H 242 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 A 257 O HOH A 597 2.08
REMARK 500 CD2 HIS C 257 O HOH C 539 2.08
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 ASP A 29 -124.57 61.85
REMARK 500 PHE A 119 -57.36 -126.11
REMARK 500 THR A 191 -98.14 -102.23
REMARK 500 GLU A 219 -97.15 -83.32
REMARK 500 GLU A 224 70.26 50.11
REMARK 500 SER A 261 60.22 38.15
REMARK 500 TRP B 60 -1.71 76.95
REMARK 500 VAL C 19 127.81 -24.83
REMARK 500 ASP C 29 -123.61 60.99
REMARK 500 PHE C 119 -56.78 -125.22
REMARK 500 TRP D 60 -2.62 77.56
REMARK 500 SER F 87 -179.05 -171.97
REMARK 500 ASP G 115 57.67 -145.44
REMARK 500 HIS H 167 -32.78 -131.55
REMARK 500 GLN H 180 75.28 -118.29
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH E 351 DISTANCE = 6.25 ANGSTROMS
REMARK 525 HOH F 440 DISTANCE = 6.58 ANGSTROMS
REMARK 525 HOH F 464 DISTANCE = 6.81 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 30W A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue B3P A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 30W C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue B3P C 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL F 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4L4T RELATED DB: PDB
REMARK 900 RELATED ID: 4NQC RELATED DB: PDB
REMARK 900 RELATED ID: 4PJ5 RELATED DB: PDB
REMARK 900 RELATED ID: 4PJ7 RELATED DB: PDB
REMARK 900 RELATED ID: 4PJ8 RELATED DB: PDB
REMARK 900 RELATED ID: 4PJ9 RELATED DB: PDB
REMARK 900 RELATED ID: 4PJA RELATED DB: PDB
REMARK 900 RELATED ID: 4PJB RELATED DB: PDB
REMARK 900 RELATED ID: 4PJC RELATED DB: PDB
REMARK 900 RELATED ID: 4PJD RELATED DB: PDB
REMARK 900 RELATED ID: 4PJE RELATED DB: PDB
REMARK 900 RELATED ID: 4PJF RELATED DB: PDB
REMARK 900 RELATED ID: 4PJG RELATED DB: PDB
REMARK 900 RELATED ID: 4PJH RELATED DB: PDB
REMARK 900 RELATED ID: 4PJI RELATED DB: PDB
DBREF 4PJX A 1 270 UNP Q95460 HMR1_HUMAN 23 292
DBREF 4PJX B 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 4PJX C 1 270 UNP Q95460 HMR1_HUMAN 23 292
DBREF 4PJX D 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 4PJX E -1 203 PDB 4PJX 4PJX -1 203
DBREF 4PJX F -1 244 PDB 4PJX 4PJX -1 244
DBREF 4PJX G -1 203 PDB 4PJX 4PJX -1 203
DBREF 4PJX H -1 244 PDB 4PJX 4PJX -1 244
SEQADV 4PJX MET A 0 UNP Q95460 INITIATING METHIONINE
SEQADV 4PJX SER A 261 UNP Q95460 CYS 283 ENGINEERED MUTATION
SEQADV 4PJX MET B 0 UNP P61769 INITIATING METHIONINE
SEQADV 4PJX MET C 0 UNP Q95460 INITIATING METHIONINE
SEQADV 4PJX SER C 261 UNP Q95460 CYS 283 ENGINEERED MUTATION
SEQADV 4PJX MET D 0 UNP P61769 INITIATING METHIONINE
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 100 MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG
SEQRES 2 B 100 HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS
SEQRES 3 B 100 TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP
SEQRES 4 B 100 LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS
SEQRES 5 B 100 SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU
SEQRES 6 B 100 LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU
SEQRES 7 B 100 TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO
SEQRES 8 B 100 LYS 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 100 MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG
SEQRES 2 D 100 HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS
SEQRES 3 D 100 TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP
SEQRES 4 D 100 LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS
SEQRES 5 D 100 SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU
SEQRES 6 D 100 LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU
SEQRES 7 D 100 TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO
SEQRES 8 D 100 LYS ILE VAL LYS TRP ASP ARG ASP MET
SEQRES 1 E 205 HIS MET GLY GLN ASN ILE ASP GLN PRO THR GLU MET THR
SEQRES 2 E 205 ALA THR GLU GLY ALA ILE VAL GLN ILE ASN CYS THR TYR
SEQRES 3 E 205 GLN THR SER GLY PHE ASN GLY LEU PHE TRP TYR GLN GLN
SEQRES 4 E 205 HIS ALA GLY GLU ALA PRO THR PHE LEU SER TYR ASN VAL
SEQRES 5 E 205 LEU ASP GLY LEU GLU GLU LYS GLY ARG PHE SER SER PHE
SEQRES 6 E 205 LEU SER ARG SER LYS GLY TYR SER TYR LEU LEU LEU LYS
SEQRES 7 E 205 GLU LEU GLN MET LYS ASP SER ALA SER TYR LEU CYS ALA
SEQRES 8 E 205 VAL ARG ASP SER ASN TYR GLN LEU ILE TRP GLY ALA GLY
SEQRES 9 E 205 THR LYS LEU ILE ILE LYS PRO ASP ILE GLN ASN PRO ASP
SEQRES 10 E 205 PRO ALA VAL TYR GLN LEU ARG ASP SER LYS SER SER ASP
SEQRES 11 E 205 LYS SER VAL CYS LEU PHE THR ASP PHE ASP SER GLN THR
SEQRES 12 E 205 ASN VAL SER GLN SER LYS ASP SER ASP VAL TYR ILE THR
SEQRES 13 E 205 ASP LYS CYS VAL LEU ASP MET ARG SER MET ASP PHE LYS
SEQRES 14 E 205 SER ASN SER ALA VAL ALA TRP SER ASN LYS SER ASP PHE
SEQRES 15 E 205 ALA CYS ALA ASN ALA PHE ASN ASN SER ILE ILE PRO GLU
SEQRES 16 E 205 ASP THR PHE PHE PRO SER PRO GLU SER SER
SEQRES 1 F 246 HIS MET ASN ALA GLY VAL THR GLN THR PRO LYS PHE GLN
SEQRES 2 F 246 VAL LEU LYS THR GLY GLN SER MET THR LEU GLN CYS ALA
SEQRES 3 F 246 GLN ASP MET ASN HIS ASN SER MET TYR TRP TYR ARG GLN
SEQRES 4 F 246 ASP PRO GLY MET GLY LEU ARG LEU ILE TYR TYR SER ALA
SEQRES 5 F 246 SER GLU GLY THR THR ASP LYS GLY GLU VAL PRO ASN GLY
SEQRES 6 F 246 TYR ASN VAL SER ARG LEU ASN LYS ARG GLU PHE SER LEU
SEQRES 7 F 246 ARG LEU GLU SER ALA ALA PRO SER GLN THR SER VAL TYR
SEQRES 8 F 246 PHE CYS ALA SER SER ALA ALA VAL GLU GLY GLY ASN THR
SEQRES 9 F 246 ILE TYR PHE GLY GLU GLY SER ARG LEU THR VAL LEU GLU
SEQRES 10 F 246 ASP LEU LYS ASN VAL PHE PRO PRO GLU VAL ALA VAL PHE
SEQRES 11 F 246 GLU PRO SER GLU ALA GLU ILE SER HIS THR GLN LYS ALA
SEQRES 12 F 246 THR LEU VAL CYS LEU ALA THR GLY PHE TYR PRO ASP HIS
SEQRES 13 F 246 VAL GLU LEU SER TRP TRP VAL ASN GLY LYS GLU VAL HIS
SEQRES 14 F 246 SER GLY VAL CYS THR ASP PRO GLN PRO LEU LYS GLU GLN
SEQRES 15 F 246 PRO ALA LEU ASN ASP SER ARG TYR ALA LEU SER SER ARG
SEQRES 16 F 246 LEU ARG VAL SER ALA THR PHE TRP GLN ASN PRO ARG ASN
SEQRES 17 F 246 HIS PHE ARG CYS GLN VAL GLN PHE TYR GLY LEU SER GLU
SEQRES 18 F 246 ASN ASP GLU TRP THR GLN ASP ARG ALA LYS PRO VAL THR
SEQRES 19 F 246 GLN ILE VAL SER ALA GLU ALA TRP GLY ARG ALA ASP
SEQRES 1 G 205 HIS MET GLY GLN ASN ILE ASP GLN PRO THR GLU MET THR
SEQRES 2 G 205 ALA THR GLU GLY ALA ILE VAL GLN ILE ASN CYS THR TYR
SEQRES 3 G 205 GLN THR SER GLY PHE ASN GLY LEU PHE TRP TYR GLN GLN
SEQRES 4 G 205 HIS ALA GLY GLU ALA PRO THR PHE LEU SER TYR ASN VAL
SEQRES 5 G 205 LEU ASP GLY LEU GLU GLU LYS GLY ARG PHE SER SER PHE
SEQRES 6 G 205 LEU SER ARG SER LYS GLY TYR SER TYR LEU LEU LEU LYS
SEQRES 7 G 205 GLU LEU GLN MET LYS ASP SER ALA SER TYR LEU CYS ALA
SEQRES 8 G 205 VAL ARG ASP SER ASN TYR GLN LEU ILE TRP GLY ALA GLY
SEQRES 9 G 205 THR LYS LEU ILE ILE LYS PRO ASP ILE GLN ASN PRO ASP
SEQRES 10 G 205 PRO ALA VAL TYR GLN LEU ARG ASP SER LYS SER SER ASP
SEQRES 11 G 205 LYS SER VAL CYS LEU PHE THR ASP PHE ASP SER GLN THR
SEQRES 12 G 205 ASN VAL SER GLN SER LYS ASP SER ASP VAL TYR ILE THR
SEQRES 13 G 205 ASP LYS CYS VAL LEU ASP MET ARG SER MET ASP PHE LYS
SEQRES 14 G 205 SER ASN SER ALA VAL ALA TRP SER ASN LYS SER ASP PHE
SEQRES 15 G 205 ALA CYS ALA ASN ALA PHE ASN ASN SER ILE ILE PRO GLU
SEQRES 16 G 205 ASP THR PHE PHE PRO SER PRO GLU SER SER
SEQRES 1 H 246 HIS MET ASN ALA GLY VAL THR GLN THR PRO LYS PHE GLN
SEQRES 2 H 246 VAL LEU LYS THR GLY GLN SER MET THR LEU GLN CYS ALA
SEQRES 3 H 246 GLN ASP MET ASN HIS ASN SER MET TYR TRP TYR ARG GLN
SEQRES 4 H 246 ASP PRO GLY MET GLY LEU ARG LEU ILE TYR TYR SER ALA
SEQRES 5 H 246 SER GLU GLY THR THR ASP LYS GLY GLU VAL PRO ASN GLY
SEQRES 6 H 246 TYR ASN VAL SER ARG LEU ASN LYS ARG GLU PHE SER LEU
SEQRES 7 H 246 ARG LEU GLU SER ALA ALA PRO SER GLN THR SER VAL TYR
SEQRES 8 H 246 PHE CYS ALA SER SER ALA ALA VAL GLU GLY GLY ASN THR
SEQRES 9 H 246 ILE TYR PHE GLY GLU GLY SER ARG LEU THR VAL LEU GLU
SEQRES 10 H 246 ASP LEU LYS ASN VAL PHE PRO PRO GLU VAL ALA VAL PHE
SEQRES 11 H 246 GLU PRO SER GLU ALA GLU ILE SER HIS THR GLN LYS ALA
SEQRES 12 H 246 THR LEU VAL CYS LEU ALA THR GLY PHE TYR PRO ASP HIS
SEQRES 13 H 246 VAL GLU LEU SER TRP TRP VAL ASN GLY LYS GLU VAL HIS
SEQRES 14 H 246 SER GLY VAL CYS THR ASP PRO GLN PRO LEU LYS GLU GLN
SEQRES 15 H 246 PRO ALA LEU ASN ASP SER ARG TYR ALA LEU SER SER ARG
SEQRES 16 H 246 LEU ARG VAL SER ALA THR PHE TRP GLN ASN PRO ARG ASN
SEQRES 17 H 246 HIS PHE ARG CYS GLN VAL GLN PHE TYR GLY LEU SER GLU
SEQRES 18 H 246 ASN ASP GLU TRP THR GLN ASP ARG ALA LYS PRO VAL THR
SEQRES 19 H 246 GLN ILE VAL SER ALA GLU ALA TRP GLY ARG ALA ASP
HET 30W A 301 16
HET CL A 302 1
HET GOL A 303 6
HET B3P A 304 19
HET GOL B 101 6
HET GOL B 102 12
HET 30W C 301 16
HET GOL C 302 6
HET GOL C 303 6
HET B3P C 304 19
HET GOL F 301 6
HETNAM 30W N-(6-FORMYL-4-OXO-3,4-DIHYDROPTERIDIN-2-YL)ACETAMIDE
HETNAM CL CHLORIDE ION
HETNAM GOL GLYCEROL
HETNAM B3P 2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-
HETNAM 2 B3P PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETSYN 30W ACETYL 6-FORMYLPTERIN
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 9 30W 2(C9 H7 N5 O3)
FORMUL 10 CL CL 1-
FORMUL 11 GOL 6(C3 H8 O3)
FORMUL 12 B3P 2(C11 H26 N2 O6)
FORMUL 20 HOH *910(H2 O)
HELIX 1 AA1 ALA A 47 GLU A 52 1 6
HELIX 2 AA2 ALA A 55 ASN A 85 1 31
HELIX 3 AA3 ASP A 133 ALA A 145 1 13
HELIX 4 AA4 ASN A 146 GLU A 159 1 14
HELIX 5 AA5 GLU A 159 GLY A 172 1 14
HELIX 6 AA6 GLY A 172 GLN A 177 1 6
HELIX 7 AA7 ALA C 47 GLU C 52 1 6
HELIX 8 AA8 ALA C 55 ASN C 85 1 31
HELIX 9 AA9 ASP C 133 ALA C 145 1 13
HELIX 10 AB1 ASN C 146 GLU C 159 1 14
HELIX 11 AB2 GLU C 159 GLY C 172 1 14
HELIX 12 AB3 GLY C 172 GLN C 177 1 6
HELIX 13 AB4 GLN E 79 SER E 83 5 5
HELIX 14 AB5 ALA F 82 THR F 86 5 5
HELIX 15 AB6 SER F 131 GLN F 139 1 9
HELIX 16 AB7 ALA F 198 GLN F 202 1 5
HELIX 17 AB8 GLN G 79 SER G 83 5 5
HELIX 18 AB9 ARG G 162 ASP G 165 5 4
HELIX 19 AC1 ALA G 181 PHE G 186 1 6
HELIX 20 AC2 ALA H 82 THR H 86 5 5
HELIX 21 AC3 ASP H 116 VAL H 120 5 5
HELIX 22 AC4 SER H 131 GLN H 139 1 9
HELIX 23 AC5 ALA H 198 GLN H 202 1 5
SHEET 1 AA1 8 GLU A 44 PRO A 45 0
SHEET 2 AA1 8 HIS A 31 ASP A 37 -1 N THR A 35 O GLU A 44
SHEET 3 AA1 8 PHE A 22 VAL A 28 -1 N GLY A 26 O ILE A 33
SHEET 4 AA1 8 HIS A 3 VAL A 12 -1 N ARG A 6 O TYR A 27
SHEET 5 AA1 8 THR A 91 LEU A 100 -1 O TYR A 92 N GLY A 11
SHEET 6 AA1 8 THR A 106 TYR A 114 -1 O PHE A 109 N GLY A 97
SHEET 7 AA1 8 GLN A 117 ASN A 123 -1 O PHE A 122 N LEU A 110
SHEET 8 AA1 8 SER A 128 ALA A 131 -1 O SER A 128 N ASN A 123
SHEET 1 AA2 4 LEU A 183 GLU A 190 0
SHEET 2 AA2 4 THR A 196 PHE A 205 -1 O HIS A 203 N LEU A 183
SHEET 3 AA2 4 TYR A 238 LEU A 246 -1 O LEU A 246 N THR A 196
SHEET 4 AA2 4 ASP A 226 TYR A 227 -1 N ASP A 226 O SER A 243
SHEET 1 AA3 4 LEU A 183 GLU A 190 0
SHEET 2 AA3 4 THR A 196 PHE A 205 -1 O HIS A 203 N LEU A 183
SHEET 3 AA3 4 TYR A 238 LEU A 246 -1 O LEU A 246 N THR A 196
SHEET 4 AA3 4 LEU A 231 PRO A 232 -1 N LEU A 231 O GLN A 239
SHEET 1 AA4 3 TYR A 211 LYS A 216 0
SHEET 2 AA4 3 TYR A 254 HIS A 260 -1 O HIS A 257 N THR A 213
SHEET 3 AA4 3 VAL A 263 GLN A 268 -1 O LEU A 267 N CYS A 256
SHEET 1 AA5 4 LYS B 6 SER B 11 0
SHEET 2 AA5 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10
SHEET 3 AA5 4 PHE B 62 PHE B 70 -1 O PHE B 70 N ASN B 21
SHEET 4 AA5 4 GLU B 50 HIS B 51 -1 N GLU B 50 O TYR B 67
SHEET 1 AA6 4 LYS B 6 SER B 11 0
SHEET 2 AA6 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10
SHEET 3 AA6 4 PHE B 62 PHE B 70 -1 O PHE B 70 N ASN B 21
SHEET 4 AA6 4 SER B 55 PHE B 56 -1 N SER B 55 O TYR B 63
SHEET 1 AA7 4 GLU B 44 ARG B 45 0
SHEET 2 AA7 4 GLU B 36 LYS B 41 -1 N LYS B 41 O GLU B 44
SHEET 3 AA7 4 TYR B 78 ASN B 83 -1 O ARG B 81 N ASP B 38
SHEET 4 AA7 4 LYS B 91 LYS B 94 -1 O LYS B 91 N VAL B 82
SHEET 1 AA8 8 GLU C 44 PRO C 45 0
SHEET 2 AA8 8 HIS C 31 ASP C 37 -1 N THR C 35 O GLU C 44
SHEET 3 AA8 8 PHE C 22 VAL C 28 -1 N SER C 24 O TYR C 36
SHEET 4 AA8 8 HIS C 3 VAL C 12 -1 N ARG C 6 O TYR C 27
SHEET 5 AA8 8 THR C 91 LEU C 100 -1 O TYR C 92 N GLY C 11
SHEET 6 AA8 8 THR C 106 TYR C 114 -1 O GLN C 111 N MET C 95
SHEET 7 AA8 8 GLN C 117 ASN C 123 -1 O PHE C 122 N LEU C 110
SHEET 8 AA8 8 SER C 128 ALA C 131 -1 O SER C 128 N ASN C 123
SHEET 1 AA9 4 LEU C 183 ASN C 187 0
SHEET 2 AA9 4 LEU C 198 PHE C 205 -1 O PHE C 199 N ASN C 187
SHEET 3 AA9 4 TYR C 238 ILE C 244 -1 O ALA C 240 N ALA C 202
SHEET 4 AA9 4 ASP C 226 TYR C 227 -1 N ASP C 226 O SER C 243
SHEET 1 AB1 4 LEU C 183 ASN C 187 0
SHEET 2 AB1 4 LEU C 198 PHE C 205 -1 O PHE C 199 N ASN C 187
SHEET 3 AB1 4 TYR C 238 ILE C 244 -1 O ALA C 240 N ALA C 202
SHEET 4 AB1 4 LEU C 231 PRO C 232 -1 N LEU C 231 O GLN C 239
SHEET 1 AB2 3 TYR C 211 LYS C 216 0
SHEET 2 AB2 3 TYR C 254 HIS C 260 -1 O HIS C 257 N THR C 213
SHEET 3 AB2 3 VAL C 263 GLN C 268 -1 O MET C 265 N VAL C 258
SHEET 1 AB3 4 LYS D 6 SER D 11 0
SHEET 2 AB3 4 ASN D 21 PHE D 30 -1 O ASN D 24 N TYR D 10
SHEET 3 AB3 4 PHE D 62 PHE D 70 -1 O PHE D 70 N ASN D 21
SHEET 4 AB3 4 GLU D 50 HIS D 51 -1 N GLU D 50 O TYR D 67
SHEET 1 AB4 4 LYS D 6 SER D 11 0
SHEET 2 AB4 4 ASN D 21 PHE D 30 -1 O ASN D 24 N TYR D 10
SHEET 3 AB4 4 PHE D 62 PHE D 70 -1 O PHE D 70 N ASN D 21
SHEET 4 AB4 4 SER D 55 PHE D 56 -1 N SER D 55 O TYR D 63
SHEET 1 AB5 4 GLU D 44 ARG D 45 0
SHEET 2 AB5 4 GLU D 36 LYS D 41 -1 N LYS D 41 O GLU D 44
SHEET 3 AB5 4 TYR D 78 ASN D 83 -1 O ARG D 81 N ASP D 38
SHEET 4 AB5 4 LYS D 91 LYS D 94 -1 O VAL D 93 N CYS D 80
SHEET 1 AB6 5 ASN E 3 ASP E 5 0
SHEET 2 AB6 5 VAL E 18 GLN E 25 -1 O THR E 23 N ASP E 5
SHEET 3 AB6 5 TYR E 70 LEU E 75 -1 O LEU E 73 N ILE E 20
SHEET 4 AB6 5 PHE E 60 SER E 65 -1 N SER E 61 O LEU E 74
SHEET 5 AB6 5 GLY E 53 LYS E 57 -1 N LYS E 57 O PHE E 60
SHEET 1 AB7 5 GLU E 9 THR E 13 0
SHEET 2 AB7 5 THR E 103 LYS E 108 1 O ILE E 106 N MET E 10
SHEET 3 AB7 5 ALA E 84 ARG E 91 -1 N ALA E 84 O LEU E 105
SHEET 4 AB7 5 LEU E 32 GLN E 37 -1 N GLN E 37 O SER E 85
SHEET 5 AB7 5 THR E 44 ASN E 49 -1 O ASN E 49 N LEU E 32
SHEET 1 AB8 4 GLU E 9 THR E 13 0
SHEET 2 AB8 4 THR E 103 LYS E 108 1 O ILE E 106 N MET E 10
SHEET 3 AB8 4 ALA E 84 ARG E 91 -1 N ALA E 84 O LEU E 105
SHEET 4 AB8 4 LEU E 97 TRP E 99 -1 O ILE E 98 N VAL E 90
SHEET 1 AB9 4 ALA E 117 LEU E 121 0
SHEET 2 AB9 4 VAL E 131 THR E 135 -1 O LEU E 133 N TYR E 119
SHEET 3 AB9 4 SER E 168 SER E 175 -1 O ALA E 173 N CYS E 132
SHEET 4 AB9 4 VAL E 151 ILE E 153 -1 N TYR E 152 O TRP E 174
SHEET 1 AC1 4 ALA E 117 LEU E 121 0
SHEET 2 AC1 4 VAL E 131 THR E 135 -1 O LEU E 133 N TYR E 119
SHEET 3 AC1 4 SER E 168 SER E 175 -1 O ALA E 173 N CYS E 132
SHEET 4 AC1 4 CYS E 157 LEU E 159 -1 N LEU E 159 O SER E 168
SHEET 1 AC2 4 VAL F 4 THR F 7 0
SHEET 2 AC2 4 MET F 19 GLN F 25 -1 O ALA F 24 N THR F 5
SHEET 3 AC2 4 PHE F 74 LEU F 78 -1 O LEU F 76 N LEU F 21
SHEET 4 AC2 4 TYR F 64 ARG F 68 -1 N ASN F 65 O ARG F 77
SHEET 1 AC3 6 PHE F 10 LYS F 14 0
SHEET 2 AC3 6 SER F 109 LEU F 114 1 O THR F 112 N LEU F 13
SHEET 3 AC3 6 SER F 87 SER F 94 -1 N TYR F 89 O SER F 109
SHEET 4 AC3 6 SER F 31 GLN F 37 -1 N TYR F 35 O PHE F 90
SHEET 5 AC3 6 ARG F 44 SER F 51 -1 O ILE F 46 N TRP F 34
SHEET 6 AC3 6 THR F 54 LYS F 57 -1 O ASP F 56 N TYR F 48
SHEET 1 AC4 4 PHE F 10 LYS F 14 0
SHEET 2 AC4 4 SER F 109 LEU F 114 1 O THR F 112 N LEU F 13
SHEET 3 AC4 4 SER F 87 SER F 94 -1 N TYR F 89 O SER F 109
SHEET 4 AC4 4 TYR F 104 PHE F 105 -1 O TYR F 104 N SER F 93
SHEET 1 AC5 4 GLU F 124 PHE F 128 0
SHEET 2 AC5 4 LYS F 140 PHE F 150 -1 O VAL F 144 N PHE F 128
SHEET 3 AC5 4 TYR F 188 SER F 197 -1 O LEU F 190 N ALA F 147
SHEET 4 AC5 4 VAL F 170 THR F 172 -1 N CYS F 171 O ARG F 193
SHEET 1 AC6 4 GLU F 124 PHE F 128 0
SHEET 2 AC6 4 LYS F 140 PHE F 150 -1 O VAL F 144 N PHE F 128
SHEET 3 AC6 4 TYR F 188 SER F 197 -1 O LEU F 190 N ALA F 147
SHEET 4 AC6 4 LEU F 177 LYS F 178 -1 N LEU F 177 O ALA F 189
SHEET 1 AC7 4 LYS F 164 VAL F 166 0
SHEET 2 AC7 4 VAL F 155 VAL F 161 -1 N VAL F 161 O LYS F 164
SHEET 3 AC7 4 PHE F 208 PHE F 214 -1 O GLN F 211 N SER F 158
SHEET 4 AC7 4 GLN F 233 ALA F 239 -1 O GLN F 233 N PHE F 214
SHEET 1 AC8 5 ASN G 3 ASP G 5 0
SHEET 2 AC8 5 VAL G 18 GLN G 25 -1 O THR G 23 N ASP G 5
SHEET 3 AC8 5 TYR G 70 LEU G 75 -1 O LEU G 73 N ILE G 20
SHEET 4 AC8 5 PHE G 60 SER G 65 -1 N SER G 61 O LEU G 74
SHEET 5 AC8 5 GLY G 53 LYS G 57 -1 N LYS G 57 O PHE G 60
SHEET 1 AC9 5 GLU G 9 THR G 13 0
SHEET 2 AC9 5 THR G 103 LYS G 108 1 O ILE G 106 N MET G 10
SHEET 3 AC9 5 ALA G 84 ARG G 91 -1 N ALA G 84 O LEU G 105
SHEET 4 AC9 5 LEU G 32 GLN G 37 -1 N GLN G 37 O SER G 85
SHEET 5 AC9 5 THR G 44 ASN G 49 -1 O ASN G 49 N LEU G 32
SHEET 1 AD1 4 GLU G 9 THR G 13 0
SHEET 2 AD1 4 THR G 103 LYS G 108 1 O ILE G 106 N MET G 10
SHEET 3 AD1 4 ALA G 84 ARG G 91 -1 N ALA G 84 O LEU G 105
SHEET 4 AD1 4 LEU G 97 TRP G 99 -1 O ILE G 98 N VAL G 90
SHEET 1 AD2 4 ALA G 117 GLN G 120 0
SHEET 2 AD2 4 SER G 130 THR G 135 -1 O LEU G 133 N TYR G 119
SHEET 3 AD2 4 PHE G 166 SER G 175 -1 O ALA G 173 N CYS G 132
SHEET 4 AD2 4 VAL G 151 ILE G 153 -1 N TYR G 152 O TRP G 174
SHEET 1 AD3 4 ALA G 117 GLN G 120 0
SHEET 2 AD3 4 SER G 130 THR G 135 -1 O LEU G 133 N TYR G 119
SHEET 3 AD3 4 PHE G 166 SER G 175 -1 O ALA G 173 N CYS G 132
SHEET 4 AD3 4 CYS G 157 MET G 161 -1 N MET G 161 O PHE G 166
SHEET 1 AD4 4 VAL H 4 THR H 7 0
SHEET 2 AD4 4 MET H 19 GLN H 25 -1 O ALA H 24 N THR H 5
SHEET 3 AD4 4 PHE H 74 LEU H 78 -1 O LEU H 76 N LEU H 21
SHEET 4 AD4 4 TYR H 64 ARG H 68 -1 N ASN H 65 O ARG H 77
SHEET 1 AD5 6 PHE H 10 LYS H 14 0
SHEET 2 AD5 6 SER H 109 LEU H 114 1 O THR H 112 N LEU H 13
SHEET 3 AD5 6 SER H 87 SER H 94 -1 N TYR H 89 O SER H 109
SHEET 4 AD5 6 SER H 31 GLN H 37 -1 N TYR H 35 O PHE H 90
SHEET 5 AD5 6 ARG H 44 SER H 51 -1 O ILE H 46 N TRP H 34
SHEET 6 AD5 6 THR H 54 LYS H 57 -1 O ASP H 56 N TYR H 48
SHEET 1 AD6 4 PHE H 10 LYS H 14 0
SHEET 2 AD6 4 SER H 109 LEU H 114 1 O THR H 112 N LEU H 13
SHEET 3 AD6 4 SER H 87 SER H 94 -1 N TYR H 89 O SER H 109
SHEET 4 AD6 4 TYR H 104 PHE H 105 -1 O TYR H 104 N SER H 93
SHEET 1 AD7 4 GLU H 124 PHE H 128 0
SHEET 2 AD7 4 LYS H 140 PHE H 150 -1 O VAL H 144 N PHE H 128
SHEET 3 AD7 4 TYR H 188 SER H 197 -1 O SER H 192 N CYS H 145
SHEET 4 AD7 4 VAL H 170 THR H 172 -1 N CYS H 171 O ARG H 193
SHEET 1 AD8 4 GLU H 124 PHE H 128 0
SHEET 2 AD8 4 LYS H 140 PHE H 150 -1 O VAL H 144 N PHE H 128
SHEET 3 AD8 4 TYR H 188 SER H 197 -1 O SER H 192 N CYS H 145
SHEET 4 AD8 4 LEU H 177 LYS H 178 -1 N LEU H 177 O ALA H 189
SHEET 1 AD9 4 LYS H 164 VAL H 166 0
SHEET 2 AD9 4 VAL H 155 VAL H 161 -1 N VAL H 161 O LYS H 164
SHEET 3 AD9 4 HIS H 207 PHE H 214 -1 O GLN H 211 N SER H 158
SHEET 4 AD9 4 GLN H 233 TRP H 240 -1 O GLN H 233 N PHE H 214
SSBOND 1 CYS A 98 CYS A 161 1555 1555 2.05
SSBOND 2 CYS A 200 CYS A 256 1555 1555 2.02
SSBOND 3 CYS B 25 CYS B 80 1555 1555 2.04
SSBOND 4 CYS C 98 CYS C 161 1555 1555 2.06
SSBOND 5 CYS C 200 CYS C 256 1555 1555 2.01
SSBOND 6 CYS D 25 CYS D 80 1555 1555 2.03
SSBOND 7 CYS E 22 CYS E 88 1555 1555 2.05
SSBOND 8 CYS E 132 CYS E 182 1555 1555 2.06
SSBOND 9 CYS E 157 CYS F 171 1555 1555 2.06
SSBOND 10 CYS F 23 CYS F 91 1555 1555 2.02
SSBOND 11 CYS F 145 CYS F 210 1555 1555 2.03
SSBOND 12 CYS G 22 CYS G 88 1555 1555 2.05
SSBOND 13 CYS G 132 CYS G 182 1555 1555 2.05
SSBOND 14 CYS G 157 CYS H 171 1555 1555 2.05
SSBOND 15 CYS H 23 CYS H 91 1555 1555 2.02
SSBOND 16 CYS H 145 CYS H 210 1555 1555 2.02
LINK NZ LYS A 43 C9 30W A 301 1555 1555 1.26
LINK NZ LYS C 43 C9 30W C 301 1555 1555 1.27
CISPEP 1 TYR A 206 PRO A 207 0 0.53
CISPEP 2 HIS B 31 PRO B 32 0 5.27
CISPEP 3 TYR C 206 PRO C 207 0 -0.01
CISPEP 4 HIS D 31 PRO D 32 0 3.81
CISPEP 5 THR F 7 PRO F 8 0 -6.80
CISPEP 6 TYR F 151 PRO F 152 0 -4.85
CISPEP 7 THR H 7 PRO H 8 0 -6.31
CISPEP 8 TYR H 151 PRO H 152 0 -4.54
SITE 1 AC1 14 TYR A 7 ARG A 9 LYS A 43 TYR A 62
SITE 2 AC1 14 TRP A 69 ARG A 94 ILE A 96 TYR A 152
SITE 3 AC1 14 TRP A 156 HOH A 448 HOH A 554 HOH A 579
SITE 4 AC1 14 TYR E 95 GLU F 98
SITE 1 AC2 5 THR A 91 GLN A 93 ALA A 113 ASP A 115
SITE 2 AC2 5 GLY A 116
SITE 1 AC3 6 ILE A 210 TYR A 211 MET A 212 TYR A 227
SITE 2 AC3 6 GLY A 228 TRP A 241
SITE 1 AC4 16 GLU A 76 ARG A 94 TYR A 112 ALA A 142
SITE 2 AC4 16 TRP A 143 ASN A 146 GLU A 149 GLN A 153
SITE 3 AC4 16 HOH A 447 HOH A 474 HOH A 490 HOH A 496
SITE 4 AC4 16 HOH A 524 HOH A 537 HOH A 546 HOH A 575
SITE 1 AC5 9 PRO B 5 LYS B 6 ILE B 7 LYS B 91
SITE 2 AC5 9 VAL B 93 HOH B 273 ALA C 131 ASP C 133
SITE 3 AC5 9 ASN C 134
SITE 1 AC6 13 LEU A 231 TRP A 241 GLN B 8 VAL B 9
SITE 2 AC6 13 VAL B 93 LYS B 94 TRP B 95 ASP B 96
SITE 3 AC6 13 HOH B 213 HOH B 242 HOH B 252 ASP C 133
SITE 4 AC6 13 ASN C 134
SITE 1 AC7 16 TYR C 7 ARG C 9 LYS C 43 TYR C 62
SITE 2 AC7 16 LEU C 66 TRP C 69 ARG C 94 ILE C 96
SITE 3 AC7 16 TYR C 152 TRP C 156 HOH C 415 HOH C 522
SITE 4 AC7 16 HOH C 530 TYR G 95 HOH G 351 GLU H 98
SITE 1 AC8 6 TYR C 84 TYR C 114 GLN C 117 ASP C 118
SITE 2 AC8 6 PHE C 119 ASP C 133
SITE 1 AC9 7 ILE C 210 TYR C 211 MET C 212 TYR C 227
SITE 2 AC9 7 GLY C 228 ILE C 230 TRP C 241
SITE 1 AD1 11 GLU C 76 ARG C 94 TYR C 112 ALA C 142
SITE 2 AD1 11 TRP C 143 GLU C 149 GLN C 153 HOH C 455
SITE 3 AD1 11 HOH C 505 HOH C 512 HOH C 521
SITE 1 AD2 5 GLY E 40 LYS F 9 PHE F 10 GLU F 107
SITE 2 AD2 5 ARG F 110
CRYST1 213.921 69.581 142.502 90.00 103.74 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 0.004675 0.000000 0.001143 0.00000
SCALE2 0.000000 0.014372 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007224 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
