HEADER METAL BINDING PROTEIN 12-JAN-16 5HIS
TITLE CRYSTAL STRUCTURE OF PQS RESPONSE PROTEIN PQSE IN COMPLEX WITH 3-
TITLE 2 METHYLTHIOPHENE-2-CARBOXYLIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PQSE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA PAO1;
SOURCE 3 ORGANISM_TAXID: 208964;
SOURCE 4 GENE: PA1000;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS QUORUM SENSING, PQS, PQSE, INHIBITOR, PSEUDOMONAS, METAL BINDING
KEYWDS 2 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR F.WITZGALL,W.BLANKENFELDT
REVDAT 3 10-JAN-24 5HIS 1 LINK
REVDAT 2 29-JUN-16 5HIS 1 JRNL
REVDAT 1 27-APR-16 5HIS 0
JRNL AUTH M.ZENDER,F.WITZGALL,S.L.DREES,E.WEIDEL,C.K.MAURER,S.FETZNER,
JRNL AUTH 2 W.BLANKENFELDT,M.EMPTING,R.W.HARTMANN
JRNL TITL DISSECTING THE MULTIPLE ROLES OF PQSE IN PSEUDOMONAS
JRNL TITL 2 AERUGINOSA VIRULENCE BY DISCOVERY OF SMALL TOOL COMPOUNDS.
JRNL REF ACS CHEM.BIOL. V. 11 1755 2016
JRNL REFN ESSN 1554-8937
JRNL PMID 27082157
JRNL DOI 10.1021/ACSCHEMBIO.6B00156
REMARK 2
REMARK 2 RESOLUTION. 1.77 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.10.1_2155
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) : 1.77
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.76
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 31750
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.162
REMARK 3 FREE R VALUE : 0.200
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.810
REMARK 3 FREE R VALUE TEST SET COUNT : 1526
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 48.7775 - 3.9359 1.00 2940 149 0.1567 0.1959
REMARK 3 2 3.9359 - 3.1242 1.00 2813 127 0.1508 0.1595
REMARK 3 3 3.1242 - 2.7293 1.00 2745 149 0.1652 0.2267
REMARK 3 4 2.7293 - 2.4798 1.00 2736 147 0.1599 0.1975
REMARK 3 5 2.4798 - 2.3021 1.00 2722 137 0.1551 0.2066
REMARK 3 6 2.3021 - 2.1663 1.00 2758 120 0.1550 0.1836
REMARK 3 7 2.1663 - 2.0578 1.00 2698 142 0.1600 0.1966
REMARK 3 8 2.0578 - 1.9683 1.00 2708 129 0.1674 0.2211
REMARK 3 9 1.9683 - 1.8925 1.00 2720 123 0.1815 0.2085
REMARK 3 10 1.8925 - 1.8272 1.00 2697 152 0.2205 0.2740
REMARK 3 11 1.8272 - 1.7701 1.00 2687 151 0.2668 0.3390
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.270
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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 : 0.018 2467
REMARK 3 ANGLE : 1.097 3347
REMARK 3 CHIRALITY : 0.061 365
REMARK 3 PLANARITY : 0.007 437
REMARK 3 DIHEDRAL : 10.817 1470
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (( CHAIN 'A' AND (RESID 18 THROUGH 93 )) OR ( CHAIN
REMARK 3 'A' AND RESID 999 ) OR ( CHAIN 'S' AND RESID 1 ) OR
REMARK 3 ( CHAIN 'S' AND RESID 5 ) OR ( CHAIN 'S' AND RESID 8
REMARK 3 ) OR ( CHAIN 'S' AND RESID 13 ) OR ( CHAIN 'S' AND
REMARK 3 RESID 15 ) OR ( CHAIN 'S' AND RESID 17 ) OR ( CHAIN '
REMARK 3 S' AND RESID 21 ) OR ( CHAIN 'S' AND RESID 24 ) OR
REMARK 3 ( CHAIN 'S' AND RESID 30 ) OR ( CHAIN 'S' AND RESID
REMARK 3 31 ) OR ( CHAIN 'S' AND RESID 39 ) OR ( CHAIN 'S'
REMARK 3 AND RESID 45 ) OR ( CHAIN 'S' AND RESID 46 ) OR (
REMARK 3 CHAIN ' S' AND RESID 58 ) OR ( CHAIN 'S' AND RESID
REMARK 3 60 ) OR ( CHAIN 'S' AND RESID 62 ) OR ( CHAIN 'S'
REMARK 3 AND RESID 63 ) OR ( CHAIN 'S' AND RESID 71 ) OR (
REMARK 3 CHAIN 'S' AND RESID 72 ) OR ( CHAIN 'S' AND RESID 79
REMARK 3 ) OR ( CHAIN ' S' AND RESID 85 ) OR ( CHAIN 'S' AND
REMARK 3 RESID 92 ) OR ( CHAIN 'S' AND RESID 93 ) OR ( CHAIN '
REMARK 3 S' AND RESID 102 ) OR ( CHAIN 'S' AND RESID 105 ) OR
REMARK 3 ( CHAIN 'S' AND RESID 109 ) OR ( CHAIN 'S' AND RESID
REMARK 3 110 ) OR ( CHAIN 'S' AND RESID 118 ) OR ( CHAIN 'S'
REMARK 3 AND RESID 126 ) OR ( CHAIN 'S' AND RESID 132 ) OR (
REMARK 3 CHAIN 'S' AND RESID 140 ) OR ( CHAIN 'S' AND RESID
REMARK 3 141 ) OR ( CHAIN 'S' AND RESID 142 ) OR ( CHAIN 'S'
REMARK 3 AND RESID 143 ) OR ( CHAIN 'S' AND RESID 144 ) OR (
REMARK 3 CHAIN 'S' AND RESID 160 ) OR ( CHAIN 'S' AND RESID
REMARK 3 161 ) OR ( CHAIN 'S' AND RESID 162 ) OR ( CHAIN 'S'
REMARK 3 AND RESID 165 ) OR ( CHAIN 'S' AND RESID 166 ) OR (
REMARK 3 CHAIN 'S' AND RESID 179 ) OR ( CHAIN 'S' AND RESID
REMARK 3 187 ) OR ( CHAIN 'S' AND RESID 189 ))
REMARK 3 ORIGIN FOR THE GROUP (A): -32.5726 -9.8156 -13.1443
REMARK 3 T TENSOR
REMARK 3 T11: 0.2844 T22: 0.2552
REMARK 3 T33: 0.2100 T12: 0.0313
REMARK 3 T13: 0.0540 T23: 0.0270
REMARK 3 L TENSOR
REMARK 3 L11: 2.0346 L22: 2.4183
REMARK 3 L33: 1.7927 L12: -0.9635
REMARK 3 L13: -0.1450 L23: -0.1214
REMARK 3 S TENSOR
REMARK 3 S11: -0.0812 S12: -0.1890 S13: -0.1754
REMARK 3 S21: 0.4100 S22: 0.0983 S23: 0.3528
REMARK 3 S31: -0.0565 S32: -0.3199 S33: -0.0259
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (( CHAIN 'A' AND (RESID 94 THROUGH 116 )) OR ( CHAIN
REMARK 3 'S' AND RESID 25 ) OR ( CHAIN 'S' AND RESID 54 ) OR
REMARK 3 ( CHAIN 'S' AND RESID 145 ) OR ( CHAIN 'S' AND RESID
REMARK 3 146 ) OR ( CHAIN 'S' AND RESID 147 ) OR ( CHAIN 'S'
REMARK 3 AND RESID 163 ) OR ( CHAIN 'S' AND RESID 164 ) OR (
REMARK 3 CHAIN 'S' AND RESID 177 ) OR ( CHAIN 'S' AND RESID
REMARK 3 182 ))
REMARK 3 ORIGIN FOR THE GROUP (A): -25.3050 -1.7707 0.4338
REMARK 3 T TENSOR
REMARK 3 T11: 0.6478 T22: 0.4978
REMARK 3 T33: 0.2070 T12: 0.1049
REMARK 3 T13: 0.0005 T23: -0.0700
REMARK 3 L TENSOR
REMARK 3 L11: 1.3130 L22: 0.4910
REMARK 3 L33: 1.4858 L12: 0.3644
REMARK 3 L13: 0.8267 L23: -0.3840
REMARK 3 S TENSOR
REMARK 3 S11: -0.1253 S12: -0.6687 S13: 0.2458
REMARK 3 S21: 0.6445 S22: -0.0778 S23: 0.0575
REMARK 3 S31: -0.2481 S32: -0.1755 S33: -0.0089
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (( CHAIN 'A' AND (RESID 117 THROUGH 136 )) OR (
REMARK 3 CHAIN 'S' AND RESID 106 ) OR ( CHAIN 'S' AND RESID
REMARK 3 114 ) OR ( CHAIN 'S' AND RESID 148 ) OR ( CHAIN 'S'
REMARK 3 AND RESID 167 ) OR ( CHAIN 'S' AND RESID 168 ) OR (
REMARK 3 CHAIN 'S' AND RESID 169 ) OR ( CHAIN 'S' AND RESID
REMARK 3 180 ) OR ( CHAIN 'S' AND RESID 181 ))
REMARK 3 ORIGIN FOR THE GROUP (A): -34.4889 -3.9593 -3.7810
REMARK 3 T TENSOR
REMARK 3 T11: 0.6107 T22: 0.5365
REMARK 3 T33: 0.3213 T12: 0.1427
REMARK 3 T13: 0.1298 T23: 0.0456
REMARK 3 L TENSOR
REMARK 3 L11: 2.4733 L22: 0.6133
REMARK 3 L33: 1.4027 L12: 0.3170
REMARK 3 L13: 0.2810 L23: 0.9219
REMARK 3 S TENSOR
REMARK 3 S11: -0.0680 S12: -0.6789 S13: 0.2094
REMARK 3 S21: -0.1281 S22: 0.0639 S23: 0.2601
REMARK 3 S31: -0.0310 S32: -0.4556 S33: 0.0922
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (( CHAIN 'A' AND (RESID 137 THROUGH 155 )) OR (
REMARK 3 CHAIN 'S' AND RESID 12 ) OR ( CHAIN 'S' AND RESID 57
REMARK 3 ) OR ( CHAIN 'S' AND RESID 67 ) OR ( CHAIN 'S' AND
REMARK 3 RESID 74 ) OR ( CHAIN 'S' AND RESID 76 ) OR ( CHAIN '
REMARK 3 S' AND RESID 83 ) OR ( CHAIN 'S' AND RESID 91 ) OR (
REMARK 3 CHAIN 'S' AND RESID 121 ) OR ( CHAIN 'S' AND RESID
REMARK 3 133 ) OR ( CHAIN 'S' AND RESID 149 ) OR ( CHAIN 'S'
REMARK 3 AND RESID 150 ) OR ( CHAIN 'S' AND RESID 170 ) OR (
REMARK 3 CHAIN 'S' AND RESID 194 ))
REMARK 3 ORIGIN FOR THE GROUP (A): -20.2632 -23.2805 -11.9334
REMARK 3 T TENSOR
REMARK 3 T11: 0.4381 T22: 0.2227
REMARK 3 T33: 0.3749 T12: 0.0571
REMARK 3 T13: -0.0076 T23: 0.0561
REMARK 3 L TENSOR
REMARK 3 L11: 3.3631 L22: 1.2657
REMARK 3 L33: 2.0601 L12: 0.3279
REMARK 3 L13: 0.3716 L23: 0.0999
REMARK 3 S TENSOR
REMARK 3 S11: -0.1299 S12: -0.1955 S13: -0.7407
REMARK 3 S21: 0.4493 S22: 0.0344 S23: -0.1567
REMARK 3 S31: 0.4925 S32: 0.1713 S33: 0.1241
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (( CHAIN 'A' AND (RESID 156 THROUGH 210 )) OR (
REMARK 3 CHAIN 'A' AND RESID 998 ) OR ( CHAIN 'S' AND RESID 3
REMARK 3 ) OR ( CHAIN 'S' AND RESID 4 ) OR ( CHAIN 'S' AND
REMARK 3 RESID 10 ) OR ( CHAIN 'S' AND RESID 11 ) OR ( CHAIN '
REMARK 3 S' AND RESID 18 ) OR ( CHAIN 'S' AND RESID 19 ) OR (
REMARK 3 CHAIN 'S' AND RESID 22 ) OR ( CHAIN 'S' AND RESID 26
REMARK 3 ) OR ( CHAIN 'S' AND RESID 27 ) OR ( CHAIN 'S' AND
REMARK 3 RESID 35 ) OR ( CHAIN 'S' AND RESID 36 ) OR ( CHAIN '
REMARK 3 S' AND RESID 37 ) OR ( CHAIN 'S' AND RESID 40 ) OR
REMARK 3 ( CHAIN 'S' AND RESID 43 ) OR ( CHAIN 'S' AND RESID
REMARK 3 52 ) OR ( CHAIN 'S' AND RESID 53 ) OR ( CHAIN 'S'
REMARK 3 AND RESID 59 ) OR ( CHAIN 'S' AND RESID 68 ) OR (
REMARK 3 CHAIN ' S' AND RESID 69 ) OR ( CHAIN 'S' AND RESID
REMARK 3 70 ) OR ( CHAIN 'S' AND RESID 78 ) OR ( CHAIN 'S'
REMARK 3 AND RESID 81 ) OR ( CHAIN 'S' AND RESID 82 ) OR (
REMARK 3 CHAIN 'S' AND RESID 86 ) OR ( CHAIN 'S' AND RESID 88
REMARK 3 ) OR ( CHAIN ' S' AND RESID 89 ) OR ( CHAIN 'S' AND
REMARK 3 RESID 104 ) OR ( CHAIN 'S' AND RESID 108 ) OR (
REMARK 3 CHAIN 'S' AND RESID 111 ) OR ( CHAIN 'S' AND RESID
REMARK 3 119 ) OR ( CHAIN 'S' AND RESID 122 ) OR ( CHAIN 'S'
REMARK 3 AND RESID 125 ) OR ( CHAIN 'S' AND RESID 128 ) OR (
REMARK 3 CHAIN 'S' AND RESID 139 ) OR ( CHAIN 'S' AND RESID
REMARK 3 151 ) OR ( CHAIN 'S' AND RESID 152 ) OR ( CHAIN 'S'
REMARK 3 AND RESID 171 ) OR ( CHAIN 'S' AND RESID 178 ) OR (
REMARK 3 CHAIN 'S' AND RESID 183 ) OR ( CHAIN 'S' AND RESID
REMARK 3 184 ) OR ( CHAIN 'S' AND RESID 195 ) OR ( CHAIN 'S'
REMARK 3 AND RESID 196 ) OR ( CHAIN 'S' AND RESID 201 ) OR (
REMARK 3 CHAIN 'S' AND RESID 203 ) OR ( CHAIN 'S' AND RESID
REMARK 3 208 ) OR ( CHAIN 'B' AND RESID 1 ))
REMARK 3 ORIGIN FOR THE GROUP (A): -12.2172 -8.8561 -15.1148
REMARK 3 T TENSOR
REMARK 3 T11: 0.2780 T22: 0.1935
REMARK 3 T33: 0.1995 T12: 0.0404
REMARK 3 T13: -0.0888 T23: -0.0097
REMARK 3 L TENSOR
REMARK 3 L11: 1.9811 L22: 1.3320
REMARK 3 L33: 1.5566 L12: 0.2915
REMARK 3 L13: -0.3554 L23: -0.1393
REMARK 3 S TENSOR
REMARK 3 S11: -0.1073 S12: -0.1049 S13: -0.0368
REMARK 3 S21: 0.3722 S22: 0.0643 S23: -0.1828
REMARK 3 S31: -0.0372 S32: 0.1337 S33: 0.0457
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (( CHAIN 'A' AND (RESID 211 THROUGH 278 )) OR (
REMARK 3 CHAIN 'S' AND RESID 2 ) OR ( CHAIN 'S' AND RESID 6 )
REMARK 3 OR ( CHAIN 'S' AND RESID 7 ) OR ( CHAIN 'S' AND
REMARK 3 RESID 9 ) OR ( CHAIN 'S' AND RESID 14 ) OR ( CHAIN '
REMARK 3 S' AND RESID 16 ) OR ( CHAIN 'S' AND RESID 20 ) OR (
REMARK 3 CHAIN ' S' AND RESID 23 ) OR ( CHAIN 'S' AND RESID
REMARK 3 28 ) OR ( CHAIN 'S' AND RESID 29 ) OR ( CHAIN 'S'
REMARK 3 AND RESID 32 ) OR ( CHAIN 'S' AND RESID 34 ) OR (
REMARK 3 CHAIN 'S' AND RESID 38 ) OR ( CHAIN 'S' AND RESID 41
REMARK 3 ) OR ( CHAIN ' S' AND RESID 42 ) OR ( CHAIN 'S' AND
REMARK 3 RESID 44 ) OR ( CHAIN 'S' AND RESID 47 ) OR ( CHAIN '
REMARK 3 S' AND RESID 48 ) OR ( CHAIN 'S' AND RESID 49 ) OR (
REMARK 3 CHAIN 'S' AND RESID 50 ) OR ( CHAIN 'S' AND RESID 51
REMARK 3 ) OR ( CHAIN ' S' AND RESID 55 ) OR ( CHAIN 'S' AND
REMARK 3 RESID 56 ) OR ( CHAIN 'S' AND RESID 64 ) OR ( CHAIN '
REMARK 3 S' AND RESID 65 ) OR ( CHAIN 'S' AND RESID 66 ) OR (
REMARK 3 CHAIN 'S' AND RESID 73 ) OR ( CHAIN 'S' AND RESID 77
REMARK 3 ) OR ( CHAIN ' S' AND RESID 84 ) OR ( CHAIN 'S' AND
REMARK 3 RESID 90 ) OR ( CHAIN 'S' AND RESID 95 ) OR ( CHAIN '
REMARK 3 S' AND RESID 96 ) OR ( CHAIN 'S' AND RESID 97 ) OR (
REMARK 3 CHAIN 'S' AND RESID 98 ) OR ( CHAIN 'S' AND RESID 99
REMARK 3 ) OR ( CHAIN ' S' AND RESID 101 ) OR ( CHAIN 'S' AND
REMARK 3 RESID 107 ) OR ( CHAIN 'S' AND RESID 113 ) OR (
REMARK 3 CHAIN 'S' AND RESID 115 ) OR ( CHAIN 'S' AND RESID
REMARK 3 120 ) OR ( CHAIN 'S' AND RESID 123 ) OR ( CHAIN 'S'
REMARK 3 AND RESID 124 ) OR ( CHAIN 'S' AND RESID 127 ) OR (
REMARK 3 CHAIN 'S' AND RESID 129 ) OR ( CHAIN 'S' AND RESID
REMARK 3 130 ) OR ( CHAIN 'S' AND RESID 135 ) OR ( CHAIN 'S'
REMARK 3 AND RESID 138 ) OR ( CHAIN 'S' AND RESID 153 ) OR (
REMARK 3 CHAIN 'S' AND RESID 154 ) OR ( CHAIN 'S' AND RESID
REMARK 3 155 ) OR ( CHAIN 'S' AND RESID 172 ) OR ( CHAIN 'S'
REMARK 3 AND RESID 173 ) OR ( CHAIN 'S' AND RESID 174 ) OR (
REMARK 3 CHAIN 'S' AND RESID 175 ) OR ( CHAIN 'S' AND RESID
REMARK 3 185 ) OR ( CHAIN 'S' AND RESID 197 ) OR ( CHAIN 'S'
REMARK 3 AND RESID 198 ) OR ( CHAIN 'S' AND RESID 199 ) OR (
REMARK 3 CHAIN 'S' AND RESID 202 ) OR ( CHAIN 'S' AND RESID
REMARK 3 211 ) OR ( CHAIN 'S' AND RESID 212 ) OR ( CHAIN 'S'
REMARK 3 AND RESID 213 ))
REMARK 3 ORIGIN FOR THE GROUP (A): -8.3880 1.1905 -18.6503
REMARK 3 T TENSOR
REMARK 3 T11: 0.3652 T22: 0.2289
REMARK 3 T33: 0.2698 T12: 0.0248
REMARK 3 T13: -0.1154 T23: -0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 1.8379 L22: 1.3340
REMARK 3 L33: 1.3799 L12: 1.2564
REMARK 3 L13: -0.0962 L23: 0.4282
REMARK 3 S TENSOR
REMARK 3 S11: -0.1197 S12: 0.0356 S13: 0.2375
REMARK 3 S21: 0.0795 S22: 0.0669 S23: -0.0043
REMARK 3 S31: -0.3131 S32: 0.1369 S33: 0.0543
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (( CHAIN 'A' AND (RESID 279 THROUGH 298 )) OR (
REMARK 3 CHAIN 'S' AND RESID 156 ) OR ( CHAIN 'S' AND RESID
REMARK 3 176 ) OR ( CHAIN 'S' AND RESID 192 ) OR ( CHAIN 'S'
REMARK 3 AND RESID 210 ))
REMARK 3 ORIGIN FOR THE GROUP (A): -8.5257 6.6857 -6.9034
REMARK 3 T TENSOR
REMARK 3 T11: 0.5785 T22: 0.3459
REMARK 3 T33: 0.2868 T12: -0.0237
REMARK 3 T13: -0.0984 T23: -0.1025
REMARK 3 L TENSOR
REMARK 3 L11: 2.9177 L22: 3.0713
REMARK 3 L33: 3.5630 L12: 0.9895
REMARK 3 L13: -0.5378 L23: 0.1271
REMARK 3 S TENSOR
REMARK 3 S11: 0.2550 S12: -0.7574 S13: 0.1389
REMARK 3 S21: 0.4750 S22: -0.2236 S23: 0.3208
REMARK 3 S31: -0.1445 S32: 0.1181 S33: 0.0620
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5HIS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-JAN-16.
REMARK 100 THE DEPOSITION ID IS D_1000217061.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-FEB-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5-8.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31806
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.770
REMARK 200 RESOLUTION RANGE LOW (A) : 48.759
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 9.700
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.77
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.10
REMARK 200 R MERGE FOR SHELL (I) : 1.14000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 2Q0I
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES, 200 MM MGCL2, 31%
REMARK 280 PEG400, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 97.51800
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 48.75900
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 48.75900
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 97.51800
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 GLY A -1
REMARK 465 LEU A 298
REMARK 465 PRO A 299
REMARK 465 LEU A 300
REMARK 465 ASP A 301
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 MET A 1 SD CE
REMARK 470 GLU A 31 CD OE1 OE2
REMARK 470 GLU A 94 CG CD OE1 OE2
REMARK 470 GLN A 98 CD OE1 NE2
REMARK 470 GLU A 103 CD OE1 OE2
REMARK 470 GLU A 120 CG CD OE1 OE2
REMARK 470 ARG A 122 CB CG CD NE CZ NH1 NH2
REMARK 470 GLU A 125 CG CD OE1 OE2
REMARK 470 GLU A 199 CD OE1 OE2
REMARK 470 GLU A 206 CD OE1 OE2
REMARK 470 ARG A 287 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 HE22 GLN A 209 O HOH A 511 1.59
REMARK 500 OD2 ASP A 12 O HOH A 501 1.79
REMARK 500 OD1 ASP A 19 O HOH A 502 1.79
REMARK 500 O HOH A 653 O HOH A 712 1.84
REMARK 500 O HOH A 555 O HOH A 666 1.98
REMARK 500 O GLY A 279 O HOH A 503 1.99
REMARK 500 O HOH A 653 O HOH A 713 1.99
REMARK 500 OE1 GLU A 155 O HOH A 504 2.05
REMARK 500 O HOH A 646 O HOH A 714 2.08
REMARK 500 OD1 ASP A 232 O HOH A 505 2.12
REMARK 500 O HOH A 507 O HOH A 657 2.14
REMARK 500 O HOH A 712 O HOH A 713 2.15
REMARK 500 O HOH A 663 O HOH A 689 2.18
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 SER A 5 39.85 -142.73
REMARK 500 GLU A 38 147.74 79.01
REMARK 500 ASP A 196 -52.79 -123.29
REMARK 500 THR A 213 130.23 -39.33
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 A 719 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH A 720 DISTANCE = 7.57 ANGSTROMS
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 FE A 401 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 69 NE2
REMARK 620 2 HIS A 71 ND1 86.4
REMARK 620 3 HIS A 159 NE2 98.3 83.6
REMARK 620 4 ASP A 178 OD2 95.9 176.6 93.6
REMARK 620 5 HOH A 520 O 119.5 101.7 141.9 79.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE A 402 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 73 OD2
REMARK 620 2 HIS A 74 NE2 83.6
REMARK 620 3 ASP A 178 OD2 157.2 88.4
REMARK 620 4 HIS A 221 NE2 83.6 89.0 117.7
REMARK 620 5 60P A 403 O08 93.1 171.5 97.5 82.8
REMARK 620 6 HOH A 520 O 81.1 97.7 78.9 162.4 89.5
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 FE A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FE A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 60P A 403
DBREF 5HIS A 1 301 UNP P20581 Y1000_PSEAE 1 301
SEQADV 5HIS GLY A -1 UNP P20581 EXPRESSION TAG
SEQADV 5HIS HIS A 0 UNP P20581 EXPRESSION TAG
SEQRES 1 A 303 GLY HIS MET LEU ARG LEU SER ALA PRO GLY GLN LEU ASP
SEQRES 2 A 303 ASP ASP LEU CYS LEU LEU GLY ASP VAL GLN VAL PRO VAL
SEQRES 3 A 303 PHE LEU LEU ARG LEU GLY GLU ALA SER TRP ALA LEU VAL
SEQRES 4 A 303 GLU GLY GLY ILE SER ARG ASP ALA GLU LEU VAL TRP ALA
SEQRES 5 A 303 ASP LEU CYS ARG TRP VAL ALA ASP PRO SER GLN VAL HIS
SEQRES 6 A 303 TYR TRP LEU ILE THR HIS LYS HIS TYR ASP HIS CYS GLY
SEQRES 7 A 303 LEU LEU PRO TYR LEU CYS PRO ARG LEU PRO ASN VAL GLN
SEQRES 8 A 303 VAL LEU ALA SER GLU ARG THR CYS GLN ALA TRP LYS SER
SEQRES 9 A 303 GLU SER ALA VAL ARG VAL VAL GLU ARG LEU ASN ARG GLN
SEQRES 10 A 303 LEU LEU ARG ALA GLU GLN ARG LEU PRO GLU ALA CYS ALA
SEQRES 11 A 303 TRP ASP ALA LEU PRO VAL ARG ALA VAL ALA ASP GLY GLU
SEQRES 12 A 303 TRP LEU GLU LEU GLY PRO ARG HIS ARG LEU GLN VAL ILE
SEQRES 13 A 303 GLU ALA HIS GLY HIS SER ASP ASP HIS VAL VAL PHE TYR
SEQRES 14 A 303 ASP VAL ARG ARG ARG ARG LEU PHE CYS GLY ASP ALA LEU
SEQRES 15 A 303 GLY GLU PHE ASP GLU ALA GLU GLY VAL TRP ARG PRO LEU
SEQRES 16 A 303 VAL PHE ASP ASP MET GLU ALA TYR LEU GLU SER LEU GLU
SEQRES 17 A 303 ARG LEU GLN ARG LEU PRO THR LEU LEU GLN LEU ILE PRO
SEQRES 18 A 303 GLY HIS GLY GLY LEU LEU ARG GLY ARG LEU ALA ALA ASP
SEQRES 19 A 303 GLY ALA GLU SER ALA TYR THR GLU CYS LEU ARG LEU CYS
SEQRES 20 A 303 ARG ARG LEU LEU TRP ARG GLN SER MET GLY GLU SER LEU
SEQRES 21 A 303 ASP GLU LEU SER GLU GLU LEU HIS ARG ALA TRP GLY GLY
SEQRES 22 A 303 GLN SER VAL ASP PHE LEU PRO GLY GLU LEU HIS LEU GLY
SEQRES 23 A 303 SER MET ARG ARG MET LEU GLU ILE LEU SER ARG GLN ALA
SEQRES 24 A 303 LEU PRO LEU ASP
HET FE A 401 1
HET FE A 402 1
HET 60P A 403 14
HETNAM FE FE (III) ION
HETNAM 60P 3-METHYLTHIOPHENE-2-CARBOXYLIC ACID
FORMUL 2 FE 2(FE 3+)
FORMUL 4 60P C6 H6 O2 S
FORMUL 5 HOH *220(H2 O)
HELIX 1 AA1 ILE A 41 ARG A 43 5 3
HELIX 2 AA2 ASP A 44 VAL A 56 1 13
HELIX 3 AA3 ASP A 58 SER A 60 5 3
HELIX 4 AA4 HIS A 71 GLY A 76 1 6
HELIX 5 AA5 LEU A 77 CYS A 82 1 6
HELIX 6 AA6 PRO A 83 LEU A 85 5 3
HELIX 7 AA7 GLU A 94 TRP A 100 1 7
HELIX 8 AA8 SER A 102 GLN A 115 1 14
HELIX 9 AA9 ALA A 128 LEU A 132 5 5
HELIX 10 AB1 ASP A 197 ARG A 210 1 14
HELIX 11 AB2 GLY A 227 ASP A 232 1 6
HELIX 12 AB3 ASP A 232 MET A 254 1 23
HELIX 13 AB4 SER A 257 GLY A 270 1 14
HELIX 14 AB5 GLU A 280 GLN A 296 1 17
SHEET 1 AA1 7 ARG A 3 LEU A 4 0
SHEET 2 AA1 7 LEU A 224 ARG A 226 -1 O LEU A 224 N LEU A 4
SHEET 3 AA1 7 GLN A 216 PRO A 219 -1 N LEU A 217 O LEU A 225
SHEET 4 AA1 7 ARG A 173 GLY A 177 1 N LEU A 174 O ILE A 218
SHEET 5 AA1 7 VAL A 164 ASP A 168 -1 N ASP A 168 O ARG A 173
SHEET 6 AA1 7 HIS A 149 GLU A 155 -1 N GLN A 152 O TYR A 167
SHEET 7 AA1 7 TRP A 142 GLY A 146 -1 N LEU A 143 O LEU A 151
SHEET 1 AA2 7 GLY A 8 ASP A 11 0
SHEET 2 AA2 7 LEU A 14 LEU A 17 -1 O LEU A 14 N LEU A 10
SHEET 3 AA2 7 VAL A 24 GLY A 30 -1 O VAL A 24 N LEU A 17
SHEET 4 AA2 7 SER A 33 VAL A 37 -1 O ALA A 35 N LEU A 27
SHEET 5 AA2 7 VAL A 62 LEU A 66 1 O LEU A 66 N LEU A 36
SHEET 6 AA2 7 GLN A 89 SER A 93 1 O LEU A 91 N TRP A 65
SHEET 7 AA2 7 VAL A 134 VAL A 137 1 O ARG A 135 N VAL A 90
SHEET 1 AA3 2 GLU A 182 PHE A 183 0
SHEET 2 AA3 2 TRP A 190 ARG A 191 -1 O ARG A 191 N GLU A 182
LINK NE2 HIS A 69 FE FE A 401 1555 1555 2.18
LINK ND1 HIS A 71 FE FE A 401 1555 1555 2.55
LINK OD2 ASP A 73 FE FE A 402 1555 1555 2.27
LINK NE2 HIS A 74 FE FE A 402 1555 1555 2.15
LINK NE2 HIS A 159 FE FE A 401 1555 1555 2.15
LINK OD2 ASP A 178 FE FE A 401 1555 1555 2.18
LINK OD2 ASP A 178 FE FE A 402 1555 1555 2.07
LINK NE2 HIS A 221 FE FE A 402 1555 1555 2.38
LINK FE FE A 401 O HOH A 520 1555 1555 1.87
LINK FE FE A 402 O08 60P A 403 1555 1555 1.96
LINK FE FE A 402 O HOH A 520 1555 1555 2.02
SITE 1 AC1 7 HIS A 69 HIS A 71 HIS A 159 ASP A 178
SITE 2 AC1 7 FE A 402 60P A 403 HOH A 520
SITE 1 AC2 7 ASP A 73 HIS A 74 ASP A 178 HIS A 221
SITE 2 AC2 7 FE A 401 60P A 403 HOH A 520
SITE 1 AC3 9 ASP A 73 HIS A 159 ASP A 178 PHE A 195
SITE 2 AC3 9 HIS A 221 HIS A 282 FE A 401 FE A 402
SITE 3 AC3 9 HOH A 520
CRYST1 61.144 61.144 146.277 90.00 90.00 120.00 P 32 2 1 6
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 0.016355 0.009442 0.000000 0.00000
SCALE2 0.000000 0.018885 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006836 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
