HEADER TRANSFERASE/RNA 16-MAY-13 4KR9
TITLE CRYSTAL STRUCTURE OF A 4-THIOURIDINE SYNTHETASE - RNA COMPLEX AT 3.5
TITLE 2 ANGSTROM RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE TRNA SULFURTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: SULFUR CARRIER PROTEIN THIS SULFURTRANSFERASE, THIAMINE
COMPND 5 BIOSYNTHESIS PROTEIN THII, TRNA 4-THIOURIDINE SYNTHASE;
COMPND 6 EC: 2.8.1.4;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: RNA (39-MER);
COMPND 11 CHAIN: M, X;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;
SOURCE 3 ORGANISM_TAXID: 243274;
SOURCE 4 STRAIN: ATCC 43589;
SOURCE 5 GENE: AAD36761, THII, TM_1694;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-28A;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES
KEYWDS TRNA MODIFICATION, THIOURIDINE, SULFURTRANSFERASE, ADENYLATION, THUMP
KEYWDS 2 DOMAIN, PP-LOOP MOTIF, 4-THIOURIDINE SYNTHESIS, TRANSFERASE-RNA
KEYWDS 3 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR P.NEUMANN,R.FICNER,K.LAKOMEK
REVDAT 4 28-FEB-24 4KR9 1 REMARK
REVDAT 3 15-APR-20 4KR9 1 REMARK SEQADV
REVDAT 2 16-JUL-14 4KR9 1 JRNL
REVDAT 1 23-APR-14 4KR9 0
JRNL AUTH P.NEUMANN,K.LAKOMEK,P.T.NAUMANN,W.M.ERWIN,C.T.LAUHON,
JRNL AUTH 2 R.FICNER
JRNL TITL CRYSTAL STRUCTURE OF A 4-THIOURIDINE SYNTHETASE-RNA COMPLEX
JRNL TITL 2 REVEALS SPECIFICITY OF TRNA U8 MODIFICATION.
JRNL REF NUCLEIC ACIDS RES. V. 42 6673 2014
JRNL REFN ISSN 0305-1048
JRNL PMID 24705700
JRNL DOI 10.1093/NAR/GKU249
REMARK 2
REMARK 2 RESOLUTION. 3.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.6.1_357
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.75
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 19940
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.232
REMARK 3 R VALUE (WORKING SET) : 0.230
REMARK 3 FREE R VALUE : 0.269
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 996
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 29.7461 - 6.6736 0.94 2711 147 0.2004 0.2381
REMARK 3 2 6.6736 - 5.3069 1.00 2744 143 0.2153 0.2547
REMARK 3 3 5.3069 - 4.6389 1.00 2732 142 0.1989 0.2684
REMARK 3 4 4.6389 - 4.2161 1.00 2697 142 0.2145 0.2201
REMARK 3 5 4.2161 - 3.9146 1.00 2684 143 0.2593 0.2943
REMARK 3 6 3.9146 - 3.6842 1.00 2690 139 0.2761 0.3096
REMARK 3 7 3.6842 - 3.5000 1.00 2686 140 0.3012 0.3381
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3 K_SOL : 0.37
REMARK 3 B_SOL : 127.0
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.480
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.080
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 102.5
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 159.2
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 7.49520
REMARK 3 B22 (A**2) : -9.13950
REMARK 3 B33 (A**2) : 1.64440
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.009 8439
REMARK 3 ANGLE : 0.979 11406
REMARK 3 CHIRALITY : 0.100 1342
REMARK 3 PLANARITY : 0.005 1162
REMARK 3 DIHEDRAL : 21.141 3360
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ( CHAIN A AND RESID 77:162 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.4793 43.6711 7.7948
REMARK 3 T TENSOR
REMARK 3 T11: 1.3106 T22: 1.3848
REMARK 3 T33: 1.5632 T12: -0.1571
REMARK 3 T13: 0.0567 T23: -0.1579
REMARK 3 L TENSOR
REMARK 3 L11: 2.2060 L22: 3.4546
REMARK 3 L33: 1.9007 L12: 0.6561
REMARK 3 L13: 1.9552 L23: -0.0363
REMARK 3 S TENSOR
REMARK 3 S11: -0.2888 S12: -0.1076 S13: 0.8338
REMARK 3 S21: -0.0500 S22: 0.4328 S23: 0.5137
REMARK 3 S31: -0.1366 S32: 0.0772 S33: 0.0002
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: ( CHAIN A AND RESID 3:76 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.7859 21.5564 9.0589
REMARK 3 T TENSOR
REMARK 3 T11: 1.2080 T22: 1.5976
REMARK 3 T33: 1.1573 T12: 0.0519
REMARK 3 T13: 0.0489 T23: -0.0551
REMARK 3 L TENSOR
REMARK 3 L11: 1.3958 L22: 3.2013
REMARK 3 L33: 2.3530 L12: -0.4605
REMARK 3 L13: -0.4465 L23: -0.2640
REMARK 3 S TENSOR
REMARK 3 S11: -0.2943 S12: -0.1254 S13: 0.4228
REMARK 3 S21: 0.3249 S22: 0.2646 S23: 0.0753
REMARK 3 S31: 0.0826 S32: -0.0852 S33: 0.0004
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: ( CHAIN A AND RESID 163:388 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.2618 -3.9650 -13.0678
REMARK 3 T TENSOR
REMARK 3 T11: 1.1647 T22: 1.1610
REMARK 3 T33: 1.2769 T12: 0.1117
REMARK 3 T13: 0.0936 T23: -0.0134
REMARK 3 L TENSOR
REMARK 3 L11: 1.3242 L22: 2.2272
REMARK 3 L33: 0.8468 L12: 0.0571
REMARK 3 L13: -0.9938 L23: 0.4452
REMARK 3 S TENSOR
REMARK 3 S11: -0.2210 S12: -0.0755 S13: -0.3375
REMARK 3 S21: 0.0747 S22: 0.1601 S23: -0.1212
REMARK 3 S31: 0.2338 S32: 0.4402 S33: -0.0001
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: ( CHAIN B AND RESID 77:162 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.7328 34.2587 -43.7100
REMARK 3 T TENSOR
REMARK 3 T11: 1.7933 T22: 1.3754
REMARK 3 T33: 1.5543 T12: -0.3688
REMARK 3 T13: 0.3605 T23: 0.0406
REMARK 3 L TENSOR
REMARK 3 L11: 3.7218 L22: 1.6578
REMARK 3 L33: 0.0997 L12: 0.1705
REMARK 3 L13: -0.5118 L23: 0.3749
REMARK 3 S TENSOR
REMARK 3 S11: -0.0033 S12: 0.1835 S13: 0.2877
REMARK 3 S21: -0.3677 S22: 0.5604 S23: 0.1162
REMARK 3 S31: -0.2171 S32: -0.0500 S33: -0.0003
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: ( CHAIN B AND RESID 3:76 )
REMARK 3 ORIGIN FOR THE GROUP (A): -22.5955 17.7615 -41.8984
REMARK 3 T TENSOR
REMARK 3 T11: 1.4934 T22: 1.5442
REMARK 3 T33: 1.1522 T12: -0.1686
REMARK 3 T13: 0.0789 T23: 0.0210
REMARK 3 L TENSOR
REMARK 3 L11: 3.7971 L22: 0.4690
REMARK 3 L33: 2.9031 L12: 1.0537
REMARK 3 L13: 0.8394 L23: -0.4769
REMARK 3 S TENSOR
REMARK 3 S11: -0.1784 S12: 0.7391 S13: 0.0193
REMARK 3 S21: -0.4831 S22: 0.2999 S23: -0.2174
REMARK 3 S31: 0.2812 S32: -0.1756 S33: -0.0002
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: ( CHAIN B AND RESID 163:388 )
REMARK 3 ORIGIN FOR THE GROUP (A): -42.2734 5.3166 -16.8630
REMARK 3 T TENSOR
REMARK 3 T11: 1.0685 T22: 1.1973
REMARK 3 T33: 1.2465 T12: -0.0224
REMARK 3 T13: 0.0833 T23: 0.0328
REMARK 3 L TENSOR
REMARK 3 L11: 2.3676 L22: 2.0736
REMARK 3 L33: 2.7591 L12: 0.7192
REMARK 3 L13: -1.3938 L23: -0.1301
REMARK 3 S TENSOR
REMARK 3 S11: -0.1773 S12: 0.1210 S13: -0.0962
REMARK 3 S21: -0.1412 S22: 0.1873 S23: 0.2743
REMARK 3 S31: -0.1586 S32: -0.5110 S33: 0.0000
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: ( CHAIN M AND RESID 1:39 )
REMARK 3 ORIGIN FOR THE GROUP (A): -42.6731 27.6431 7.5285
REMARK 3 T TENSOR
REMARK 3 T11: 2.1135 T22: 1.8281
REMARK 3 T33: 2.1691 T12: -0.1573
REMARK 3 T13: 0.0623 T23: 0.1312
REMARK 3 L TENSOR
REMARK 3 L11: 2.3806 L22: 2.6451
REMARK 3 L33: 0.2830 L12: 1.8840
REMARK 3 L13: -0.7465 L23: -0.1650
REMARK 3 S TENSOR
REMARK 3 S11: -0.0815 S12: -0.4407 S13: 0.6918
REMARK 3 S21: -0.3140 S22: 0.2285 S23: 0.9187
REMARK 3 S31: 0.4542 S32: 0.2599 S33: 0.0004
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: ( CHAIN X AND RESID 1:39 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.4481 8.1212 -38.8393
REMARK 3 T TENSOR
REMARK 3 T11: 2.0159 T22: 1.9211
REMARK 3 T33: 1.7945 T12: -0.1583
REMARK 3 T13: 0.1078 T23: -0.3527
REMARK 3 L TENSOR
REMARK 3 L11: 0.5075 L22: 3.1708
REMARK 3 L33: 1.2827 L12: 0.1475
REMARK 3 L13: 0.1494 L23: -1.5649
REMARK 3 S TENSOR
REMARK 3 S11: 0.1188 S12: 0.2792 S13: -0.2820
REMARK 3 S21: 0.0878 S22: -0.0988 S23: -1.7678
REMARK 3 S31: 0.2373 S32: -0.0401 S33: -0.0001
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 5
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: ((CHAIN A AND (RESID 3:11 OR RESID 23:26
REMARK 3 OR RESID 27:45 OR RESID 46:61 OR RESID 63:
REMARK 3 78 ) AND (NAME CA OR NAME N OR NAME C OR
REMARK 3 NAME O )) OR (CHAIN A AND (RESID 3:11 OR
REMARK 3 RESID 24 OR RESID 27:28 OR RESID 31:40 OR
REMARK 3 RESID 44:55 OR RESID 56:59 OR RESID 61:67
REMARK 3 OR RESID 70 OR RESID 72:78 ) AND NOT
REMARK 3 (NAME CA OR NAME N OR NAME C OR NAME O)))
REMARK 3 SELECTION : ((CHAIN B AND (RESID 3:11 OR RESID 23:26
REMARK 3 OR RESID 27:45 OR RESID 46:61 OR RESID 63:
REMARK 3 78 ) AND (NAME CA OR NAME N OR NAME C OR
REMARK 3 NAME O )) OR (CHAIN B AND (RESID 3:11 OR
REMARK 3 RESID 24 OR RESID 27:28 OR RESID 31:40 OR
REMARK 3 RESID 44:55 OR RESID 56:59 OR RESID 61:67
REMARK 3 OR RESID 70 OR RESID 72:78 ) AND NOT
REMARK 3 (NAME CA OR NAME N OR NAME C OR NAME O)))
REMARK 3 ATOM PAIRS NUMBER : 488
REMARK 3 RMSD : 0.007
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: ((CHAIN A AND (RESID 79:113 OR RESID 114:
REMARK 3 137 OR RESID 138:150 OR RESID 153:159 )
REMARK 3 AND (NAME CA OR NAME N OR NAME C OR NAME
REMARK 3 O) ) OR (CHAIN A AND (RESID 79:80 OR
REMARK 3 RESID 82:84 OR RESID 86:91 OR RESID 93:96
REMARK 3 OR RESID 98:100 OR RESID 102:109 OR RESID
REMARK 3 110:140 OR RESID 143:150 OR RESID 153:159)
REMARK 3 AND NOT (NAME CA OR NAME N OR NAME C OR
REMARK 3 NAME O) ) )
REMARK 3 SELECTION : ((CHAIN B AND (RESID 79:113 OR RESID 114:
REMARK 3 137 OR RESID 138:150 OR RESID 153:159 )
REMARK 3 AND (NAME CA OR NAME N OR NAME C OR NAME
REMARK 3 O) ) OR (CHAIN B AND (RESID 79:80 OR
REMARK 3 RESID 82:84 OR RESID 86:91 OR RESID 93:96
REMARK 3 OR RESID 98:100 OR RESID 102:109 OR RESID
REMARK 3 110:140 OR RESID 143:150 OR RESID 153:159)
REMARK 3 AND NOT (NAME CA OR NAME N OR NAME C OR
REMARK 3 NAME O) ) )
REMARK 3 ATOM PAIRS NUMBER : 609
REMARK 3 RMSD : 0.003
REMARK 3 NCS GROUP : 3
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: ((CHAIN A AND (RESID 165:181 OR RESID
REMARK 3 182:208 OR RESID 217:246 OR RESID 247:288
REMARK 3 OR RESID 296:323 OR RESID 324:335 OR
REMARK 3 RESID 348:370 OR RESID 371:387) AND (NAME
REMARK 3 CA OR NAME N OR NAME C OR NAME O)) OR
REMARK 3 (CHAIN A AND (RESID 165:180 OR RESID 182:
REMARK 3 208 OR RESID 217 OR RESID 220:244 OR
REMARK 3 RESID 246: 263 OR RESID 265:288 OR RESID
REMARK 3 296:319 OR RESID 321:324 OR RESID 326:332
REMARK 3 OR RESID 348:364 OR RESID 366:370 OR
REMARK 3 RESID 371:383 OR RESID 384:387 ) AND NOT
REMARK 3 (NAME CA OR NAME N OR NAME C OR NAME O)) )
REMARK 3 SELECTION : ((CHAIN B AND (RESID 165:181 OR RESID
REMARK 3 182:208 OR RESID 217:246 OR RESID 247:288
REMARK 3 OR RESID 296:323 OR RESID 324:335 OR
REMARK 3 RESID 348:370 OR RESID 371:387) AND (NAME
REMARK 3 CA OR NAME N OR NAME C OR NAME O)) OR
REMARK 3 (CHAIN B AND (RESID 165:180 OR RESID 182:
REMARK 3 208 OR RESID 217 OR RESID 220:244 OR
REMARK 3 RESID 246: 263 OR RESID 265:288 OR RESID
REMARK 3 296:319 OR RESID 321:324 OR RESID 326:332
REMARK 3 OR RESID 348:364 OR RESID 366:370 OR
REMARK 3 RESID 371:383 OR RESID 384:387 ) AND NOT
REMARK 3 (NAME CA OR NAME N OR NAME C OR NAME O)) )
REMARK 3 ATOM PAIRS NUMBER : 1482
REMARK 3 RMSD : 0.004
REMARK 3 NCS GROUP : 4
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN M AND (RESSEQ 1:8 OR RESSEQ 28:35 )
REMARK 3 SELECTION : CHAIN X AND (RESSEQ 1:8 OR RESSEQ 28:35 )
REMARK 3 ATOM PAIRS NUMBER : 340
REMARK 3 RMSD : 0.083
REMARK 3 NCS GROUP : 5
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN M AND (RESID 17:19 OR RESID 24:27 )
REMARK 3 SELECTION : CHAIN X AND (RESID 17:19 OR RESID 24:27 )
REMARK 3 ATOM PAIRS NUMBER : 150
REMARK 3 RMSD : 0.711
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT WAS BASED ON SIMULATED
REMARK 3 ANNEALING IN TORSION ANGLE SPACE AND GROUPED B-FACTORS.
REMARK 4
REMARK 4 4KR9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAY-13.
REMARK 100 THE DEPOSITION ID IS D_1000079694.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-JUN-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.978000
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.16
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20061
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.474
REMARK 200 RESOLUTION RANGE LOW (A) : 52.165
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.61100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 MICRO-LITER OF THII-RNA COMPLEX
REMARK 280 SOLUTION AT 10 MG/ML IN A BUFFER CONSISTING OF 150 MM AMMONIUM
REMARK 280 SULFATE, 20MM TRIS/HCL PH 7.5 WAS MIXED WITH 3 MICRO-LITER OF
REMARK 280 FRESHLY PREPARED RESERVOIR SOLUTION (2.0 M SODIUM FORMATE, 100
REMARK 280 MM SODIUM CITRATE 2 MMDTT), VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 292K, PH 4.6
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 51.64200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 66.07550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.77550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 66.07550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 51.64200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 56.77550
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, M, X
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 GLU A 2
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 GLY A 233 N - CA - C ANGL. DEV. = 24.0 DEGREES
REMARK 500 GLY B 233 N - CA - C ANGL. DEV. = 23.8 DEGREES
REMARK 500 ARG B 253 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 U M 11 OP1 - P - OP2 ANGL. DEV. = -10.2 DEGREES
REMARK 500 G M 12 OP1 - P - OP2 ANGL. DEV. = -9.8 DEGREES
REMARK 500 G M 12 C1' - O4' - C4' ANGL. DEV. = -7.5 DEGREES
REMARK 500 G M 12 C3' - C2' - C1' ANGL. DEV. = -5.1 DEGREES
REMARK 500 G M 12 N9 - C1' - C2' ANGL. DEV. = 17.2 DEGREES
REMARK 500 U M 13 OP1 - P - OP2 ANGL. DEV. = -9.5 DEGREES
REMARK 500 C X 14 C6 - N1 - C1' ANGL. DEV. = -7.8 DEGREES
REMARK 500 C X 14 C2 - N1 - C1' ANGL. DEV. = 8.6 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 52 -162.49 -71.70
REMARK 500 TYR A 111 73.02 -104.53
REMARK 500 GLU A 113 9.74 -61.76
REMARK 500 ASN A 142 68.09 -150.15
REMARK 500 ASP A 161 171.35 170.58
REMARK 500 PRO A 210 32.41 -96.70
REMARK 500 PRO A 255 168.19 -47.97
REMARK 500 SER A 316 1.11 -54.13
REMARK 500 TYR A 340 56.60 -90.48
REMARK 500 SER A 343 172.11 -31.89
REMARK 500 PHE A 346 -71.01 -45.03
REMARK 500 SER B 12 -53.32 -150.34
REMARK 500 GLU B 13 -15.35 -44.44
REMARK 500 LYS B 17 95.61 -56.55
REMARK 500 ASN B 20 87.35 -56.96
REMARK 500 ASP B 52 -162.44 -71.74
REMARK 500 TYR B 111 73.00 -104.42
REMARK 500 GLU B 113 9.80 -61.79
REMARK 500 ASN B 142 68.02 -150.33
REMARK 500 ASP B 161 -170.68 177.33
REMARK 500 SER B 213 141.39 -31.26
REMARK 500 PRO B 255 168.14 -48.00
REMARK 500 GLN B 295 35.50 -143.75
REMARK 500 SER B 316 1.05 -54.11
REMARK 500 LYS B 338 175.12 54.16
REMARK 500 TYR B 340 -6.26 174.36
REMARK 500 SER B 343 83.50 -174.34
REMARK 500 CYS B 344 25.39 100.62
REMARK 500 PHE B 346 -28.10 44.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY A 232 GLY A 233 -124.08
REMARK 500 GLY B 232 GLY B 233 -124.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 G M 12 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4KR6 RELATED DB: PDB
REMARK 900 RELATED ID: 4KR7 RELATED DB: PDB
DBREF 4KR9 A 1 388 UNP Q9X220 THII_THEMA 1 388
DBREF 4KR9 B 1 388 UNP Q9X220 THII_THEMA 1 388
DBREF 4KR9 M 1 39 PDB 4KR9 4KR9 1 39
DBREF 4KR9 X 1 39 PDB 4KR9 4KR9 1 39
SEQADV 4KR9 GLU A 2 UNP Q9X220 LYS 2 ENGINEERED MUTATION
SEQADV 4KR9 GLU B 2 UNP Q9X220 LYS 2 ENGINEERED MUTATION
SEQRES 1 A 388 MET GLU GLU LEU ARG VAL TYR ILE VAL ARG TYR SER GLU
SEQRES 2 A 388 ILE GLY LEU LYS GLY LYS ASN ARG LYS ASP PHE GLU GLU
SEQRES 3 A 388 ALA LEU ARG ARG ASN ILE GLU ARG VAL THR GLY MET LYS
SEQRES 4 A 388 VAL LYS ARG GLN TRP GLY ARG PHE LEU ILE PRO ILE ASP
SEQRES 5 A 388 GLU ASN VAL THR LEU ASP ASP LYS LEU LYS LYS ILE PHE
SEQRES 6 A 388 GLY ILE GLN ASN PHE SER LYS GLY PHE LEU VAL SER HIS
SEQRES 7 A 388 ASP PHE GLU GLU VAL LYS LYS TYR SER LEU ILE ALA VAL
SEQRES 8 A 388 LYS GLU LYS LEU GLU LYS GLY ASN TYR ARG THR PHE LYS
SEQRES 9 A 388 VAL GLN ALA LYS LYS ALA TYR LYS GLU TYR LYS LYS GLY
SEQRES 10 A 388 VAL TYR GLU ILE ASN SER GLU LEU GLY ALA LEU ILE LEU
SEQRES 11 A 388 LYS ASN PHE LYS GLU LEU SER VAL ASP VAL ARG ASN PRO
SEQRES 12 A 388 ASP PHE VAL LEU GLY VAL GLU VAL ARG PRO GLU GLY VAL
SEQRES 13 A 388 LEU ILE PHE THR ASP ARG VAL GLU CYS TYR GLY GLY LEU
SEQRES 14 A 388 PRO VAL GLY THR GLY GLY LYS ALA VAL LEU LEU LEU SER
SEQRES 15 A 388 GLY GLY ILE ASP SER PRO VAL ALA GLY TRP TYR ALA LEU
SEQRES 16 A 388 LYS ARG GLY VAL LEU ILE GLU SER VAL THR PHE VAL SER
SEQRES 17 A 388 PRO PRO PHE THR SER GLU GLY ALA VAL GLU LYS VAL ARG
SEQRES 18 A 388 ASP ILE LEU ARG VAL LEU ARG GLU PHE SER GLY GLY HIS
SEQRES 19 A 388 PRO LEU ARG LEU HIS ILE VAL ASN LEU THR LYS LEU GLN
SEQRES 20 A 388 LEU GLU VAL LYS LYS ARG VAL PRO ASP LYS TYR SER LEU
SEQRES 21 A 388 ILE MET TYR ARG ARG SER MET PHE ARG ILE ALA GLU LYS
SEQRES 22 A 388 ILE ALA GLU GLU THR GLY ALA VAL ALA PHE TYR THR GLY
SEQRES 23 A 388 GLU ASN ILE GLY GLN VAL ALA SER GLN THR LEU GLU ASN
SEQRES 24 A 388 LEU TRP SER ILE GLU SER VAL THR THR ARG PRO VAL ILE
SEQRES 25 A 388 ARG PRO LEU SER GLY PHE ASP LYS THR GLU ILE VAL GLU
SEQRES 26 A 388 LYS ALA LYS GLU ILE GLY THR TYR GLU ILE SER ILE LYS
SEQRES 27 A 388 PRO TYR GLN ASP SER CYS VAL PHE PHE ALA PRO LYS ASN
SEQRES 28 A 388 PRO ALA THR ARG SER HIS PRO SER ILE LEU GLU LYS LEU
SEQRES 29 A 388 GLU GLN GLN VAL PRO ASP LEU PRO VAL LEU GLU GLU GLU
SEQRES 30 A 388 ALA PHE THR SER ARG LYS VAL GLU VAL ILE GLU
SEQRES 1 B 388 MET GLU GLU LEU ARG VAL TYR ILE VAL ARG TYR SER GLU
SEQRES 2 B 388 ILE GLY LEU LYS GLY LYS ASN ARG LYS ASP PHE GLU GLU
SEQRES 3 B 388 ALA LEU ARG ARG ASN ILE GLU ARG VAL THR GLY MET LYS
SEQRES 4 B 388 VAL LYS ARG GLN TRP GLY ARG PHE LEU ILE PRO ILE ASP
SEQRES 5 B 388 GLU ASN VAL THR LEU ASP ASP LYS LEU LYS LYS ILE PHE
SEQRES 6 B 388 GLY ILE GLN ASN PHE SER LYS GLY PHE LEU VAL SER HIS
SEQRES 7 B 388 ASP PHE GLU GLU VAL LYS LYS TYR SER LEU ILE ALA VAL
SEQRES 8 B 388 LYS GLU LYS LEU GLU LYS GLY ASN TYR ARG THR PHE LYS
SEQRES 9 B 388 VAL GLN ALA LYS LYS ALA TYR LYS GLU TYR LYS LYS GLY
SEQRES 10 B 388 VAL TYR GLU ILE ASN SER GLU LEU GLY ALA LEU ILE LEU
SEQRES 11 B 388 LYS ASN PHE LYS GLU LEU SER VAL ASP VAL ARG ASN PRO
SEQRES 12 B 388 ASP PHE VAL LEU GLY VAL GLU VAL ARG PRO GLU GLY VAL
SEQRES 13 B 388 LEU ILE PHE THR ASP ARG VAL GLU CYS TYR GLY GLY LEU
SEQRES 14 B 388 PRO VAL GLY THR GLY GLY LYS ALA VAL LEU LEU LEU SER
SEQRES 15 B 388 GLY GLY ILE ASP SER PRO VAL ALA GLY TRP TYR ALA LEU
SEQRES 16 B 388 LYS ARG GLY VAL LEU ILE GLU SER VAL THR PHE VAL SER
SEQRES 17 B 388 PRO PRO PHE THR SER GLU GLY ALA VAL GLU LYS VAL ARG
SEQRES 18 B 388 ASP ILE LEU ARG VAL LEU ARG GLU PHE SER GLY GLY HIS
SEQRES 19 B 388 PRO LEU ARG LEU HIS ILE VAL ASN LEU THR LYS LEU GLN
SEQRES 20 B 388 LEU GLU VAL LYS LYS ARG VAL PRO ASP LYS TYR SER LEU
SEQRES 21 B 388 ILE MET TYR ARG ARG SER MET PHE ARG ILE ALA GLU LYS
SEQRES 22 B 388 ILE ALA GLU GLU THR GLY ALA VAL ALA PHE TYR THR GLY
SEQRES 23 B 388 GLU ASN ILE GLY GLN VAL ALA SER GLN THR LEU GLU ASN
SEQRES 24 B 388 LEU TRP SER ILE GLU SER VAL THR THR ARG PRO VAL ILE
SEQRES 25 B 388 ARG PRO LEU SER GLY PHE ASP LYS THR GLU ILE VAL GLU
SEQRES 26 B 388 LYS ALA LYS GLU ILE GLY THR TYR GLU ILE SER ILE LYS
SEQRES 27 B 388 PRO TYR GLN ASP SER CYS VAL PHE PHE ALA PRO LYS ASN
SEQRES 28 B 388 PRO ALA THR ARG SER HIS PRO SER ILE LEU GLU LYS LEU
SEQRES 29 B 388 GLU GLN GLN VAL PRO ASP LEU PRO VAL LEU GLU GLU GLU
SEQRES 30 B 388 ALA PHE THR SER ARG LYS VAL GLU VAL ILE GLU
SEQRES 1 M 39 G C C C G G A U A G U G U
SEQRES 2 M 39 C C U U G G G A A A C C A
SEQRES 3 M 39 A G U C C G G G C A C C A
SEQRES 1 X 39 G C C C G G A U A G U G U
SEQRES 2 X 39 C C U U G G G A A A C C A
SEQRES 3 X 39 A G U C C G G G C A C C A
HELIX 1 1 GLY A 18 GLY A 37 1 20
HELIX 2 2 LEU A 57 LYS A 63 1 7
HELIX 3 3 ASP A 79 GLY A 98 1 20
HELIX 4 4 GLY A 117 PHE A 133 1 17
HELIX 5 5 ILE A 185 ARG A 197 1 13
HELIX 6 6 GLY A 215 GLU A 229 1 15
HELIX 7 7 LEU A 243 VAL A 254 1 12
HELIX 8 8 TYR A 258 GLY A 279 1 22
HELIX 9 9 THR A 296 SER A 305 1 10
HELIX 10 10 ASP A 319 ILE A 330 1 12
HELIX 11 11 THR A 332 LYS A 338 1 7
HELIX 12 12 SER A 359 GLU A 365 1 7
HELIX 13 13 ASP A 370 SER A 381 1 12
HELIX 14 14 ASN B 20 GLY B 37 1 18
HELIX 15 15 LEU B 57 LYS B 63 1 7
HELIX 16 16 ASP B 79 GLY B 98 1 20
HELIX 17 17 GLY B 117 PHE B 133 1 17
HELIX 18 18 ILE B 185 ARG B 197 1 13
HELIX 19 19 SER B 213 GLU B 229 1 17
HELIX 20 20 LEU B 243 VAL B 254 1 12
HELIX 21 21 TYR B 258 GLY B 279 1 22
HELIX 22 22 VAL B 292 GLN B 295 5 4
HELIX 23 23 THR B 296 SER B 305 1 10
HELIX 24 24 ASP B 319 ILE B 330 1 12
HELIX 25 25 THR B 332 ILE B 337 1 6
HELIX 26 26 SER B 359 GLU B 365 1 7
HELIX 27 27 ASP B 370 SER B 381 1 12
SHEET 1 A 8 LYS A 41 GLN A 43 0
SHEET 2 A 8 ARG A 46 ILE A 51 -1 O LEU A 48 N LYS A 41
SHEET 3 A 8 LEU A 4 ARG A 10 -1 N ARG A 5 O ILE A 51
SHEET 4 A 8 ASN A 69 VAL A 76 -1 O ASN A 69 N ARG A 10
SHEET 5 A 8 GLY A 155 GLU A 164 -1 O VAL A 156 N VAL A 76
SHEET 6 A 8 PHE A 145 ARG A 152 -1 N GLY A 148 O PHE A 159
SHEET 7 A 8 THR A 102 LYS A 109 1 N LYS A 108 O VAL A 151
SHEET 8 A 8 SER A 137 VAL A 138 1 O SER A 137 N PHE A 103
SHEET 1 B 6 VAL A 311 ILE A 312 0
SHEET 2 B 6 ALA A 282 THR A 285 1 N PHE A 283 O ILE A 312
SHEET 3 B 6 LYS A 176 LEU A 180 1 N VAL A 178 O TYR A 284
SHEET 4 B 6 LEU A 200 VAL A 207 1 O LEU A 200 N ALA A 177
SHEET 5 B 6 LEU A 236 ASN A 242 1 O HIS A 239 N SER A 203
SHEET 6 B 6 LYS A 383 ILE A 387 -1 O LYS A 383 N ILE A 240
SHEET 1 C 8 LYS B 41 GLN B 43 0
SHEET 2 C 8 ARG B 46 ILE B 51 -1 O LEU B 48 N LYS B 41
SHEET 3 C 8 LEU B 4 ARG B 10 -1 N ARG B 5 O ILE B 51
SHEET 4 C 8 ASN B 69 VAL B 76 -1 O ASN B 69 N ARG B 10
SHEET 5 C 8 GLY B 155 PHE B 159 -1 O ILE B 158 N PHE B 74
SHEET 6 C 8 PHE B 145 ARG B 152 -1 N GLY B 148 O PHE B 159
SHEET 7 C 8 THR B 102 LYS B 109 1 N LYS B 108 O VAL B 151
SHEET 8 C 8 SER B 137 VAL B 138 1 O SER B 137 N PHE B 103
SHEET 1 D 5 LYS B 41 GLN B 43 0
SHEET 2 D 5 ARG B 46 ILE B 51 -1 O LEU B 48 N LYS B 41
SHEET 3 D 5 LEU B 4 ARG B 10 -1 N ARG B 5 O ILE B 51
SHEET 4 D 5 ASN B 69 VAL B 76 -1 O ASN B 69 N ARG B 10
SHEET 5 D 5 VAL B 163 GLU B 164 -1 O VAL B 163 N PHE B 70
SHEET 1 E 6 VAL B 311 ILE B 312 0
SHEET 2 E 6 ALA B 282 TYR B 284 1 N PHE B 283 O ILE B 312
SHEET 3 E 6 LYS B 176 LEU B 180 1 N VAL B 178 O TYR B 284
SHEET 4 E 6 LEU B 200 VAL B 207 1 O LEU B 200 N ALA B 177
SHEET 5 E 6 LEU B 236 ASN B 242 1 O HIS B 239 N SER B 203
SHEET 6 E 6 LYS B 383 ILE B 387 -1 O LYS B 383 N ILE B 240
CISPEP 1 PRO A 209 PRO A 210 0 0.37
CISPEP 2 PRO B 209 PRO B 210 0 -0.19
CRYST1 103.284 113.551 132.151 90.00 90.00 90.00 P 21 21 21 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 0.009682 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008807 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007567 0.00000
MTRIX1 1 -0.769961 0.633016 -0.080310 -53.56700 1
MTRIX2 1 0.637679 0.758829 -0.132450 17.24200 1
MTRIX3 1 -0.022901 -0.153193 -0.987931 -30.44540 1
MTRIX1 2 -0.775609 0.627721 -0.066317 -52.66580 1
MTRIX2 2 0.630901 0.767627 -0.112745 17.97020 1
MTRIX3 2 -0.019866 -0.129286 -0.991408 -31.29890 1
MTRIX1 3 -0.753898 0.654688 -0.054970 -52.72080 1
MTRIX2 3 0.654561 0.741284 -0.148488 17.23700 1
MTRIX3 3 -0.056465 -0.147926 -0.987385 -31.39170 1
MTRIX1 4 -0.752615 0.292585 0.589885 -23.95510 1
MTRIX2 4 0.202431 0.955281 -0.215547 12.89110 1
MTRIX3 4 -0.626572 -0.042813 -0.778187 -22.11070 1
MTRIX1 5 -0.775859 0.102933 0.622453 -20.70480 1
MTRIX2 5 0.129382 0.991591 -0.002708 20.73830 1
MTRIX3 5 -0.617498 0.078433 -0.782652 -22.55910 1
(ATOM LINES ARE NOT SHOWN.)
END
