HEADER OXIDOREDUCTASE 22-MAR-11 3R7C
TITLE THE STRUCTURE OF A HEXAHESTIDINE-TAGGED FORM OF AUGMENTER OF LIVER
TITLE 2 REGENERATION REVEALS A NOVEL CD(2)CL(4)O(6) CLUSTER THAT AIDS IN
TITLE 3 CRYSTAL PACKING
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FAD-LINKED SULFHYDRYL OXIDASE ALR;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: RESIDUES 74-198;
COMPND 5 SYNONYM: AUGMENTER OF LIVER REGENERATION;
COMPND 6 EC: 1.8.3.2;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: ALR, GFER, GFER (ALR);
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PHRALR
KEYWDS NOVEL CD(2)CL(4)O(6) CLUSTER, FOUR-HELICAL UP-AND-DOWN BUNDLE, ALL-
KEYWDS 2 HELICAL FAD BINDING MOTIF, FAD-LINKED SULFHYDRYL OXIDASE, LIVER
KEYWDS 3 REGENERATION, FAD BINDING, MITOCHONDRIAL INTERMEMBRANE SPACE,
KEYWDS 4 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Q.J.FLORENCE,C.-K.WU,J.T.SWINDELL II,B.C.WANG,J.P.ROSE
REVDAT 2 08-NOV-17 3R7C 1 AUTHOR REMARK
REVDAT 1 28-MAR-12 3R7C 0
JRNL AUTH Q.J.FLORENCE,C.-K.WU,J.E.HABEL,J.T.SWINDELL II,B.C.WANG,
JRNL AUTH 2 J.P.ROSE
JRNL TITL THE STRUCTURE OF A HEXAHESTIDINE-TAGGED FORM OF AUGMENTER OF
JRNL TITL 2 LIVER REGENERATION REVEALS A NOVEL CD(2)CL(4)O(6) CLUSTER
JRNL TITL 3 THAT AIDS IN CRYSTAL PACKING
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.-K.WU,T.A.DAILEY,H.A.DAILEY,A.FRANCOVILLA,T.E.STARZL,
REMARK 1 AUTH 2 B.C.WANG,J.P.ROSE
REMARK 1 TITL EXPRESSION, PURIFICATION, CRYSTALLIZATION AND PRELIMINARY
REMARK 1 TITL 2 ANALYSIS OF THE AUGMENTER OF LIVER REGENERATION
REMARK 1 REF PROTEIN AND PEPTIDE LETTERS V. 7 25 2000
REMARK 1 REFN ISSN 0929-8665
REMARK 1 REFERENCE 2
REMARK 1 AUTH C.K.WU,T.A.DAILEY,H.A.DAILEY,B.C.WANG,J.P.ROSE
REMARK 1 TITL THE CRYSTAL STRUCTURE OF AUGMENTER OF LIVER REGENERATION: A
REMARK 1 TITL 2 MAMMALIAN FAD -DEPENDENT SULFHYDRYL OXIDASE.
REMARK 1 REF PROTEIN SCI. V. 12 1109 2003
REMARK 1 REFN ISSN 0961-8368
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7_650)
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.64
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 41958
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.162
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980
REMARK 3 FREE R VALUE TEST SET COUNT : 2091
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 19.6381 - 5.8700 1.00 2710 148 0.1806 0.2036
REMARK 3 2 5.8700 - 4.6799 1.00 2695 146 0.1547 0.1855
REMARK 3 3 4.6799 - 4.0945 1.00 2688 136 0.1209 0.1518
REMARK 3 4 4.0945 - 3.7229 1.00 2694 147 0.1429 0.1822
REMARK 3 5 3.7229 - 3.4576 1.00 2730 132 0.1617 0.2117
REMARK 3 6 3.4576 - 3.2547 1.00 2656 135 0.1630 0.1869
REMARK 3 7 3.2547 - 3.0924 0.99 2708 139 0.1563 0.2235
REMARK 3 8 3.0924 - 2.9582 0.98 2673 149 0.1674 0.2112
REMARK 3 9 2.9582 - 2.8447 0.98 2623 135 0.1729 0.2595
REMARK 3 10 2.8447 - 2.7468 0.97 2602 137 0.1729 0.2423
REMARK 3 11 2.7468 - 2.6611 0.98 2624 136 0.1685 0.2444
REMARK 3 12 2.6611 - 2.5852 0.97 2653 140 0.1813 0.2330
REMARK 3 13 2.5852 - 2.5173 0.96 2600 143 0.1876 0.2856
REMARK 3 14 2.5173 - 2.4560 0.96 2644 133 0.1967 0.2897
REMARK 3 15 2.4560 - 2.4003 0.95 2567 135 0.1910 0.2561
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.95
REMARK 3 K_SOL : 0.34
REMARK 3 B_SOL : 25.99
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.350
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
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) : -2.25270
REMARK 3 B22 (A**2) : -2.25270
REMARK 3 B33 (A**2) : 4.50550
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 : 0.007 3990
REMARK 3 ANGLE : 1.146 5420
REMARK 3 CHIRALITY : 0.076 515
REMARK 3 PLANARITY : 0.005 691
REMARK 3 DIHEDRAL : 17.579 1484
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 19
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 14:59)
REMARK 3 ORIGIN FOR THE GROUP (A): 43.7887 28.8388 41.4438
REMARK 3 T TENSOR
REMARK 3 T11: 0.0984 T22: 0.0796
REMARK 3 T33: 0.0728 T12: 0.0013
REMARK 3 T13: 0.0057 T23: -0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 0.3581 L22: 0.1557
REMARK 3 L33: 0.1276 L12: -0.0942
REMARK 3 L13: 0.0443 L23: 0.0183
REMARK 3 S TENSOR
REMARK 3 S11: 0.1103 S12: -0.0165 S13: -0.0715
REMARK 3 S21: -0.0613 S22: -0.0834 S23: -0.0099
REMARK 3 S31: 0.1007 S32: -0.0073 S33: -0.0021
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 60:82)
REMARK 3 ORIGIN FOR THE GROUP (A): 44.3124 38.5352 47.3434
REMARK 3 T TENSOR
REMARK 3 T11: 0.0794 T22: 0.1859
REMARK 3 T33: 0.1046 T12: -0.0421
REMARK 3 T13: -0.0133 T23: 0.0043
REMARK 3 L TENSOR
REMARK 3 L11: 0.3372 L22: 0.2643
REMARK 3 L33: 0.1152 L12: 0.0669
REMARK 3 L13: 0.1368 L23: 0.1197
REMARK 3 S TENSOR
REMARK 3 S11: 0.0035 S12: -0.0111 S13: 0.0683
REMARK 3 S21: 0.0321 S22: -0.1131 S23: 0.0685
REMARK 3 S31: -0.0044 S32: 0.0964 S33: 0.0507
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 83:124)
REMARK 3 ORIGIN FOR THE GROUP (A): 48.1183 37.3209 31.3697
REMARK 3 T TENSOR
REMARK 3 T11: 0.1002 T22: 0.1369
REMARK 3 T33: -0.0087 T12: -0.0437
REMARK 3 T13: 0.0569 T23: 0.1051
REMARK 3 L TENSOR
REMARK 3 L11: 0.1061 L22: 0.0115
REMARK 3 L33: 0.0127 L12: 0.0323
REMARK 3 L13: 0.0150 L23: -0.0000
REMARK 3 S TENSOR
REMARK 3 S11: -0.0573 S12: 0.1437 S13: 0.0534
REMARK 3 S21: -0.0608 S22: 0.0477 S23: 0.0077
REMARK 3 S31: -0.0693 S32: 0.0587 S33: -0.0278
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 14:35)
REMARK 3 ORIGIN FOR THE GROUP (A): 22.5283 45.0770 66.7171
REMARK 3 T TENSOR
REMARK 3 T11: 0.1394 T22: 0.1428
REMARK 3 T33: 0.1169 T12: 0.0048
REMARK 3 T13: -0.0150 T23: -0.0161
REMARK 3 L TENSOR
REMARK 3 L11: 0.1765 L22: 0.8215
REMARK 3 L33: 0.2024 L12: 0.0273
REMARK 3 L13: 0.0181 L23: -0.2910
REMARK 3 S TENSOR
REMARK 3 S11: -0.0054 S12: -0.0144 S13: -0.0003
REMARK 3 S21: 0.1208 S22: -0.0444 S23: 0.1076
REMARK 3 S31: -0.0295 S32: 0.0259 S33: 0.0171
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 36:59)
REMARK 3 ORIGIN FOR THE GROUP (A): 33.9020 48.8279 52.2108
REMARK 3 T TENSOR
REMARK 3 T11: 0.0767 T22: 0.0815
REMARK 3 T33: 0.1533 T12: -0.0203
REMARK 3 T13: -0.0062 T23: -0.0145
REMARK 3 L TENSOR
REMARK 3 L11: 0.2162 L22: 0.3264
REMARK 3 L33: 0.1536 L12: 0.0662
REMARK 3 L13: -0.0377 L23: -0.1059
REMARK 3 S TENSOR
REMARK 3 S11: -0.0715 S12: 0.1021 S13: 0.1144
REMARK 3 S21: 0.0374 S22: 0.1202 S23: -0.0535
REMARK 3 S31: -0.0555 S32: 0.0262 S33: 0.0113
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 60:68)
REMARK 3 ORIGIN FOR THE GROUP (A): 26.3838 33.5065 63.2314
REMARK 3 T TENSOR
REMARK 3 T11: 0.1659 T22: 0.1256
REMARK 3 T33: 0.1640 T12: 0.0294
REMARK 3 T13: -0.0409 T23: 0.0597
REMARK 3 L TENSOR
REMARK 3 L11: 0.0567 L22: 0.0752
REMARK 3 L33: 0.1716 L12: 0.0377
REMARK 3 L13: -0.0758 L23: 0.0097
REMARK 3 S TENSOR
REMARK 3 S11: -0.0670 S12: -0.0318 S13: -0.0358
REMARK 3 S21: 0.0578 S22: 0.0463 S23: -0.0053
REMARK 3 S31: 0.0291 S32: -0.0175 S33: -0.0424
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 69:82)
REMARK 3 ORIGIN FOR THE GROUP (A): 30.1464 38.1703 49.9996
REMARK 3 T TENSOR
REMARK 3 T11: 0.1225 T22: 0.1585
REMARK 3 T33: 0.1189 T12: -0.0236
REMARK 3 T13: -0.0078 T23: -0.0438
REMARK 3 L TENSOR
REMARK 3 L11: 0.0179 L22: 0.1272
REMARK 3 L33: 0.0260 L12: 0.0471
REMARK 3 L13: -0.0016 L23: 0.0072
REMARK 3 S TENSOR
REMARK 3 S11: -0.0134 S12: 0.0012 S13: 0.0396
REMARK 3 S21: -0.0321 S22: 0.0400 S23: -0.0326
REMARK 3 S31: 0.0014 S32: -0.0446 S33: 0.0028
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 83:101)
REMARK 3 ORIGIN FOR THE GROUP (A): 20.4656 41.6269 52.5848
REMARK 3 T TENSOR
REMARK 3 T11: 0.0327 T22: 0.0893
REMARK 3 T33: 0.1338 T12: -0.0188
REMARK 3 T13: -0.0584 T23: -0.0679
REMARK 3 L TENSOR
REMARK 3 L11: 0.1466 L22: 0.0363
REMARK 3 L33: 0.0747 L12: 0.0721
REMARK 3 L13: 0.0801 L23: 0.0409
REMARK 3 S TENSOR
REMARK 3 S11: -0.0672 S12: 0.0960 S13: 0.0205
REMARK 3 S21: -0.0328 S22: -0.0098 S23: 0.0330
REMARK 3 S31: -0.0394 S32: 0.0090 S33: -0.0861
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 102:124)
REMARK 3 ORIGIN FOR THE GROUP (A): 12.2734 51.2835 54.7869
REMARK 3 T TENSOR
REMARK 3 T11: 0.0931 T22: 0.1760
REMARK 3 T33: 0.2355 T12: 0.0438
REMARK 3 T13: -0.0268 T23: 0.0138
REMARK 3 L TENSOR
REMARK 3 L11: 0.1705 L22: 0.0642
REMARK 3 L33: 0.1812 L12: 0.0229
REMARK 3 L13: -0.0361 L23: 0.0458
REMARK 3 S TENSOR
REMARK 3 S11: -0.0665 S12: -0.0012 S13: -0.1023
REMARK 3 S21: -0.0379 S22: 0.0253 S23: 0.1045
REMARK 3 S31: -0.0632 S32: -0.1050 S33: -0.0154
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 14:35)
REMARK 3 ORIGIN FOR THE GROUP (A): 51.0609 21.0778 37.7690
REMARK 3 T TENSOR
REMARK 3 T11: 0.0929 T22: 0.0661
REMARK 3 T33: 0.1157 T12: 0.0262
REMARK 3 T13: 0.0358 T23: 0.0139
REMARK 3 L TENSOR
REMARK 3 L11: 0.0356 L22: 0.0229
REMARK 3 L33: 0.0652 L12: 0.0278
REMARK 3 L13: -0.0242 L23: -0.0235
REMARK 3 S TENSOR
REMARK 3 S11: -0.0196 S12: 0.0166 S13: -0.0707
REMARK 3 S21: -0.0301 S22: 0.0434 S23: -0.0542
REMARK 3 S31: 0.0353 S32: 0.0315 S33: 0.0171
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 36:59)
REMARK 3 ORIGIN FOR THE GROUP (A): 41.0728 22.8650 53.4470
REMARK 3 T TENSOR
REMARK 3 T11: 0.1551 T22: 0.0958
REMARK 3 T33: 0.1280 T12: -0.0400
REMARK 3 T13: 0.0036 T23: 0.0083
REMARK 3 L TENSOR
REMARK 3 L11: 0.0366 L22: 0.1880
REMARK 3 L33: 0.1680 L12: -0.0552
REMARK 3 L13: 0.0593 L23: -0.0278
REMARK 3 S TENSOR
REMARK 3 S11: -0.0665 S12: 0.0093 S13: 0.0013
REMARK 3 S21: 0.1416 S22: -0.0245 S23: 0.0922
REMARK 3 S31: -0.0260 S32: 0.0544 S33: 0.0096
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 60:75)
REMARK 3 ORIGIN FOR THE GROUP (A): 38.4359 13.2671 39.5912
REMARK 3 T TENSOR
REMARK 3 T11: 0.1843 T22: 0.1839
REMARK 3 T33: 0.2677 T12: -0.0264
REMARK 3 T13: 0.0744 T23: -0.0411
REMARK 3 L TENSOR
REMARK 3 L11: 0.3884 L22: 0.0387
REMARK 3 L33: 1.1113 L12: 0.0900
REMARK 3 L13: -0.5287 L23: -0.0609
REMARK 3 S TENSOR
REMARK 3 S11: -0.1321 S12: 0.0045 S13: -0.0964
REMARK 3 S21: -0.0167 S22: -0.1081 S23: -0.0716
REMARK 3 S31: 0.2314 S32: -0.0744 S33: 0.1553
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 76:107)
REMARK 3 ORIGIN FOR THE GROUP (A): 47.9975 10.4790 48.2591
REMARK 3 T TENSOR
REMARK 3 T11: 0.1979 T22: 0.0887
REMARK 3 T33: 0.2009 T12: 0.0276
REMARK 3 T13: 0.0386 T23: 0.0170
REMARK 3 L TENSOR
REMARK 3 L11: 0.0988 L22: 0.0025
REMARK 3 L33: 0.0906 L12: 0.0147
REMARK 3 L13: -0.0318 L23: 0.0081
REMARK 3 S TENSOR
REMARK 3 S11: -0.0376 S12: -0.0328 S13: -0.1334
REMARK 3 S21: 0.0142 S22: -0.0169 S23: -0.0272
REMARK 3 S31: 0.0791 S32: -0.0106 S33: 0.0222
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 108:115)
REMARK 3 ORIGIN FOR THE GROUP (A): 58.4250 13.3495 50.7709
REMARK 3 T TENSOR
REMARK 3 T11: 0.1245 T22: 0.2708
REMARK 3 T33: 0.2564 T12: 0.0415
REMARK 3 T13: -0.0588 T23: 0.0452
REMARK 3 L TENSOR
REMARK 3 L11: 0.7127 L22: 0.1886
REMARK 3 L33: 0.0821 L12: -0.2079
REMARK 3 L13: 0.0618 L23: 0.0534
REMARK 3 S TENSOR
REMARK 3 S11: 0.0074 S12: 0.0258 S13: 0.1308
REMARK 3 S21: 0.0453 S22: -0.0091 S23: -0.1421
REMARK 3 S31: 0.0065 S32: 0.0313 S33: 0.0047
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 116:124)
REMARK 3 ORIGIN FOR THE GROUP (A): 66.0245 16.7098 52.3698
REMARK 3 T TENSOR
REMARK 3 T11: 0.3028 T22: 0.5466
REMARK 3 T33: 0.5802 T12: 0.1091
REMARK 3 T13: -0.1689 T23: 0.1094
REMARK 3 L TENSOR
REMARK 3 L11: 0.1212 L22: 0.4231
REMARK 3 L33: 0.0513 L12: 0.1652
REMARK 3 L13: -0.0039 L23: 0.0537
REMARK 3 S TENSOR
REMARK 3 S11: 0.0443 S12: 0.1702 S13: -0.1195
REMARK 3 S21: -0.0296 S22: -0.1930 S23: -0.2929
REMARK 3 S31: 0.0249 S32: 0.1254 S33: 0.1019
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 14:59)
REMARK 3 ORIGIN FOR THE GROUP (A): 33.3346 47.9326 65.8725
REMARK 3 T TENSOR
REMARK 3 T11: 0.1376 T22: 0.1193
REMARK 3 T33: 0.1016 T12: 0.0119
REMARK 3 T13: -0.0911 T23: -0.0673
REMARK 3 L TENSOR
REMARK 3 L11: 0.0943 L22: 0.1705
REMARK 3 L33: 0.1259 L12: -0.0136
REMARK 3 L13: -0.0556 L23: -0.0964
REMARK 3 S TENSOR
REMARK 3 S11: 0.0149 S12: -0.0062 S13: 0.0031
REMARK 3 S21: 0.0559 S22: 0.1442 S23: -0.0220
REMARK 3 S31: -0.0310 S32: 0.1108 S33: 0.2087
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 60:72)
REMARK 3 ORIGIN FOR THE GROUP (A): 33.1226 61.8031 63.5339
REMARK 3 T TENSOR
REMARK 3 T11: 0.2220 T22: 0.1190
REMARK 3 T33: 0.3094 T12: -0.0707
REMARK 3 T13: 0.0877 T23: -0.0277
REMARK 3 L TENSOR
REMARK 3 L11: 0.9470 L22: 0.2283
REMARK 3 L33: 0.7819 L12: 0.2227
REMARK 3 L13: 0.1441 L23: -0.3324
REMARK 3 S TENSOR
REMARK 3 S11: 0.0613 S12: -0.0470 S13: 0.2951
REMARK 3 S21: 0.0300 S22: 0.0548 S23: -0.1304
REMARK 3 S31: -0.1999 S32: 0.0676 S33: -0.0595
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 73:82)
REMARK 3 ORIGIN FOR THE GROUP (A): 45.1922 50.7010 68.8355
REMARK 3 T TENSOR
REMARK 3 T11: 0.3965 T22: 0.3660
REMARK 3 T33: 0.3422 T12: -0.0407
REMARK 3 T13: -0.0832 T23: -0.0788
REMARK 3 L TENSOR
REMARK 3 L11: 2.7937 L22: 0.5684
REMARK 3 L33: 1.8865 L12: 0.8308
REMARK 3 L13: 0.0948 L23: 0.5641
REMARK 3 S TENSOR
REMARK 3 S11: 0.0651 S12: -0.0715 S13: 0.2456
REMARK 3 S21: -0.0044 S22: 0.0692 S23: 0.0743
REMARK 3 S31: 0.0615 S32: 0.0826 S33: -0.0890
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 83:124)
REMARK 3 ORIGIN FOR THE GROUP (A): 33.3634 50.0495 79.5684
REMARK 3 T TENSOR
REMARK 3 T11: 0.2523 T22: 0.0766
REMARK 3 T33: 0.1337 T12: 0.0090
REMARK 3 T13: -0.1758 T23: -0.0939
REMARK 3 L TENSOR
REMARK 3 L11: 0.0129 L22: 0.0519
REMARK 3 L33: 0.0324 L12: 0.0106
REMARK 3 L13: 0.0039 L23: 0.0343
REMARK 3 S TENSOR
REMARK 3 S11: -0.0191 S12: -0.0618 S13: 0.0182
REMARK 3 S21: 0.0769 S22: 0.0161 S23: 0.0042
REMARK 3 S31: 0.0514 S32: 0.0017 S33: -0.0174
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 3R7C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAR-11.
REMARK 100 THE DEPOSITION ID IS D_1000064580.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUN-98
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RUH2R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : YALE MIRRORS
REMARK 200 OPTICS : YALE MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 300 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42700
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 30.88
REMARK 200 R MERGE (I) : 0.08900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.45200
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: CD-SAD
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: A TOTAL OF 720 ONE-DEGREE OSCILLATION IMAGES WERE RECORDED
REMARK 200 FROM A SINGLE CRYSTAL GIVING A BIJVOET REDUNDANCY OF 15.44
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEGMME 2000, 0.1M NAOAC, 50 MM
REMARK 280 CDCL(2), SEE REFERENCE 1, PH 4.6, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K (SEE REFERENCE 1).
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 3555 -Y,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X,Z+3/4
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y,Z
REMARK 290 7555 -Y+1/2,X,Z+3/4
REMARK 290 8555 Y,-X+1/2,Z+1/4
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 49.84400
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 49.84400
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.80500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 49.84400
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 28.40250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 49.84400
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 85.20750
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 49.84400
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 49.84400
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 56.80500
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 49.84400
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 85.20750
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 49.84400
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 28.40250
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -86.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -96.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -211.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -13
REMARK 465 GLY A -12
REMARK 465 GLY A -11
REMARK 465 SER A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 GLY A -3
REMARK 465 MET A -2
REMARK 465 ALA A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 ARG A 2
REMARK 465 THR A 3
REMARK 465 GLN A 4
REMARK 465 GLN A 5
REMARK 465 LYS A 6
REMARK 465 ARG A 7
REMARK 465 ASP A 8
REMARK 465 ILE A 9
REMARK 465 LYS A 10
REMARK 465 PHE A 11
REMARK 465 ARG A 12
REMARK 465 GLU A 13
REMARK 465 ASP A 125
REMARK 465 MET B -13
REMARK 465 GLY B -12
REMARK 465 GLY B -11
REMARK 465 SER B -10
REMARK 465 HIS B -9
REMARK 465 HIS B -8
REMARK 465 HIS B -7
REMARK 465 HIS B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 GLY B -3
REMARK 465 MET B -2
REMARK 465 ALA B -1
REMARK 465 SER B 0
REMARK 465 MET B 1
REMARK 465 ARG B 2
REMARK 465 THR B 3
REMARK 465 GLN B 4
REMARK 465 GLN B 5
REMARK 465 LYS B 6
REMARK 465 ARG B 7
REMARK 465 ASP B 8
REMARK 465 ILE B 9
REMARK 465 LYS B 10
REMARK 465 PHE B 11
REMARK 465 ARG B 12
REMARK 465 GLU B 13
REMARK 465 ASP B 125
REMARK 465 MET C -13
REMARK 465 GLY C -12
REMARK 465 GLY C -11
REMARK 465 SER C -10
REMARK 465 HIS C -9
REMARK 465 HIS C -8
REMARK 465 HIS C -7
REMARK 465 HIS C -6
REMARK 465 HIS C -5
REMARK 465 HIS C -4
REMARK 465 GLY C -3
REMARK 465 MET C -2
REMARK 465 ALA C -1
REMARK 465 SER C 0
REMARK 465 MET C 1
REMARK 465 ARG C 2
REMARK 465 THR C 3
REMARK 465 GLN C 4
REMARK 465 GLN C 5
REMARK 465 LYS C 6
REMARK 465 ARG C 7
REMARK 465 ASP C 8
REMARK 465 ILE C 9
REMARK 465 LYS C 10
REMARK 465 PHE C 11
REMARK 465 ARG C 12
REMARK 465 GLU C 13
REMARK 465 ASP C 125
REMARK 465 MET D -13
REMARK 465 GLY D -12
REMARK 465 GLY D -11
REMARK 465 SER D -10
REMARK 465 HIS D -9
REMARK 465 HIS D -8
REMARK 465 HIS D -7
REMARK 465 HIS D -6
REMARK 465 HIS D -5
REMARK 465 HIS D -4
REMARK 465 GLY D -3
REMARK 465 MET D -2
REMARK 465 ALA D -1
REMARK 465 SER D 0
REMARK 465 MET D 1
REMARK 465 ARG D 2
REMARK 465 THR D 3
REMARK 465 GLN D 4
REMARK 465 GLN D 5
REMARK 465 LYS D 6
REMARK 465 ARG D 7
REMARK 465 ASP D 8
REMARK 465 ILE D 9
REMARK 465 LYS D 10
REMARK 465 PHE D 11
REMARK 465 ARG D 12
REMARK 465 GLU D 13
REMARK 465 ASP D 125
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 GLU A 63 CB CG CD OE1 OE2
REMARK 470 GLU A 64 CB CG CD OE1 OE2
REMARK 470 GLU B 63 CB CG CD OE1 OE2
REMARK 470 GLU B 64 CB CG CD OE1 OE2
REMARK 470 ARG B 110 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 63 CB CG CD OE1 OE2
REMARK 470 GLU C 64 CB CG CD OE1 OE2
REMARK 470 GLU D 63 CB CG CD OE1 OE2
REMARK 470 GLU D 64 CB CG CD OE1 OE2
REMARK 470 GLU D 67 CB CG CD OE1 OE2
REMARK 470 LYS D 71 CB CG CD CE NZ
REMARK 470 ARG D 72 CB CG CD NE CZ NH1 NH2
REMARK 470 ASP D 74 CB CG OD1 OD2
REMARK 470 ARG D 75 CB CG CD NE CZ NH1 NH2
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 CYS A 62 65.61 -156.02
REMARK 500 SER A 76 79.32 -104.70
REMARK 500 ARG B 116 -66.13 -121.64
REMARK 500 ARG C 116 -64.71 -130.74
REMARK 500 CYS D 62 95.68 -166.77
REMARK 500 GLU D 64 7.19 88.31
REMARK 500 ARG D 75 -52.12 167.06
REMARK 500 ARG D 116 -57.52 -144.23
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 SO4 D 127
REMARK 610 SO4 D 129
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 CD A 500 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CL A 502 CL
REMARK 620 2 CL A 503 CL 88.8
REMARK 620 3 CL A 504 CL 99.4 97.3
REMARK 620 4 HOH A 506 O 86.5 158.8 103.8
REMARK 620 5 ASP A 74 OD1 103.8 90.5 155.6 70.7
REMARK 620 6 ASP A 74 OD2 156.1 88.2 104.5 87.8 52.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A 501 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CL A 502 CL
REMARK 620 2 CL A 503 CL 87.5
REMARK 620 3 CL A 505 CL 97.3 104.6
REMARK 620 4 HOH A 507 O 168.4 89.1 94.3
REMARK 620 5 ASP B 74 OD1 87.7 104.7 150.5 82.4
REMARK 620 6 ASP B 74 OD2 93.5 157.4 97.6 85.4 52.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD B 130 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 113 OE1
REMARK 620 2 HOH B 138 O 95.3
REMARK 620 3 HOH B 139 O 118.5 107.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD C 127 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C 129 O
REMARK 620 2 ASP C 107 OD1 111.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD B 131 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 141 O
REMARK 620 2 GLN B 47 OE1 89.0
REMARK 620 3 GLU B 44 OE2 116.3 87.5
REMARK 620 4 HOH A 133 O 106.7 88.3 136.6
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 126
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 130
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 131
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 126
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 130
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 131
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 132
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 133
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD C 126
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD C 127
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 128
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD D 126
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 127
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 128
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 129
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 505
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1OQC RELATED DB: PDB
REMARK 900 THE NATIVE ALR CRYSTAL STRUCTURE
DBREF 3R7C A 1 125 UNP Q63042 ALR_RAT 74 198
DBREF 3R7C B 1 125 UNP Q63042 ALR_RAT 74 198
DBREF 3R7C C 1 125 UNP Q63042 ALR_RAT 74 198
DBREF 3R7C D 1 125 UNP Q63042 ALR_RAT 74 198
SEQADV 3R7C MET A -13 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C GLY A -12 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C GLY A -11 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C SER A -10 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C HIS A -9 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C HIS A -8 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C HIS A -7 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C HIS A -6 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C HIS A -5 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C HIS A -4 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C GLY A -3 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C MET A -2 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C ALA A -1 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C SER A 0 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C MET B -13 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C GLY B -12 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C GLY B -11 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C SER B -10 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C HIS B -9 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C HIS B -8 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C HIS B -7 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C HIS B -6 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C HIS B -5 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C HIS B -4 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C GLY B -3 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C MET B -2 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C ALA B -1 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C SER B 0 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C MET C -13 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C GLY C -12 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C GLY C -11 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C SER C -10 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C HIS C -9 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C HIS C -8 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C HIS C -7 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C HIS C -6 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C HIS C -5 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C HIS C -4 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C GLY C -3 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C MET C -2 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C ALA C -1 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C SER C 0 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C MET D -13 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C GLY D -12 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C GLY D -11 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C SER D -10 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C HIS D -9 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C HIS D -8 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C HIS D -7 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C HIS D -6 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C HIS D -5 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C HIS D -4 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C GLY D -3 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C MET D -2 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C ALA D -1 UNP Q63042 EXPRESSION TAG
SEQADV 3R7C SER D 0 UNP Q63042 EXPRESSION TAG
SEQRES 1 A 139 MET GLY GLY SER HIS HIS HIS HIS HIS HIS GLY MET ALA
SEQRES 2 A 139 SER MET ARG THR GLN GLN LYS ARG ASP ILE LYS PHE ARG
SEQRES 3 A 139 GLU ASP CYS PRO GLN ASP ARG GLU GLU LEU GLY ARG ASN
SEQRES 4 A 139 THR TRP ALA PHE LEU HIS THR LEU ALA ALA TYR TYR PRO
SEQRES 5 A 139 ASP MET PRO THR PRO GLU GLN GLN GLN ASP MET ALA GLN
SEQRES 6 A 139 PHE ILE HIS ILE PHE SER LYS PHE TYR PRO CYS GLU GLU
SEQRES 7 A 139 CYS ALA GLU ASP ILE ARG LYS ARG ILE ASP ARG SER GLN
SEQRES 8 A 139 PRO ASP THR SER THR ARG VAL SER PHE SER GLN TRP LEU
SEQRES 9 A 139 CYS ARG LEU HIS ASN GLU VAL ASN ARG LYS LEU GLY LYS
SEQRES 10 A 139 PRO ASP PHE ASP CYS SER ARG VAL ASP GLU ARG TRP ARG
SEQRES 11 A 139 ASP GLY TRP LYS ASP GLY SER CYS ASP
SEQRES 1 B 139 MET GLY GLY SER HIS HIS HIS HIS HIS HIS GLY MET ALA
SEQRES 2 B 139 SER MET ARG THR GLN GLN LYS ARG ASP ILE LYS PHE ARG
SEQRES 3 B 139 GLU ASP CYS PRO GLN ASP ARG GLU GLU LEU GLY ARG ASN
SEQRES 4 B 139 THR TRP ALA PHE LEU HIS THR LEU ALA ALA TYR TYR PRO
SEQRES 5 B 139 ASP MET PRO THR PRO GLU GLN GLN GLN ASP MET ALA GLN
SEQRES 6 B 139 PHE ILE HIS ILE PHE SER LYS PHE TYR PRO CYS GLU GLU
SEQRES 7 B 139 CYS ALA GLU ASP ILE ARG LYS ARG ILE ASP ARG SER GLN
SEQRES 8 B 139 PRO ASP THR SER THR ARG VAL SER PHE SER GLN TRP LEU
SEQRES 9 B 139 CYS ARG LEU HIS ASN GLU VAL ASN ARG LYS LEU GLY LYS
SEQRES 10 B 139 PRO ASP PHE ASP CYS SER ARG VAL ASP GLU ARG TRP ARG
SEQRES 11 B 139 ASP GLY TRP LYS ASP GLY SER CYS ASP
SEQRES 1 C 139 MET GLY GLY SER HIS HIS HIS HIS HIS HIS GLY MET ALA
SEQRES 2 C 139 SER MET ARG THR GLN GLN LYS ARG ASP ILE LYS PHE ARG
SEQRES 3 C 139 GLU ASP CYS PRO GLN ASP ARG GLU GLU LEU GLY ARG ASN
SEQRES 4 C 139 THR TRP ALA PHE LEU HIS THR LEU ALA ALA TYR TYR PRO
SEQRES 5 C 139 ASP MET PRO THR PRO GLU GLN GLN GLN ASP MET ALA GLN
SEQRES 6 C 139 PHE ILE HIS ILE PHE SER LYS PHE TYR PRO CYS GLU GLU
SEQRES 7 C 139 CYS ALA GLU ASP ILE ARG LYS ARG ILE ASP ARG SER GLN
SEQRES 8 C 139 PRO ASP THR SER THR ARG VAL SER PHE SER GLN TRP LEU
SEQRES 9 C 139 CYS ARG LEU HIS ASN GLU VAL ASN ARG LYS LEU GLY LYS
SEQRES 10 C 139 PRO ASP PHE ASP CYS SER ARG VAL ASP GLU ARG TRP ARG
SEQRES 11 C 139 ASP GLY TRP LYS ASP GLY SER CYS ASP
SEQRES 1 D 139 MET GLY GLY SER HIS HIS HIS HIS HIS HIS GLY MET ALA
SEQRES 2 D 139 SER MET ARG THR GLN GLN LYS ARG ASP ILE LYS PHE ARG
SEQRES 3 D 139 GLU ASP CYS PRO GLN ASP ARG GLU GLU LEU GLY ARG ASN
SEQRES 4 D 139 THR TRP ALA PHE LEU HIS THR LEU ALA ALA TYR TYR PRO
SEQRES 5 D 139 ASP MET PRO THR PRO GLU GLN GLN GLN ASP MET ALA GLN
SEQRES 6 D 139 PHE ILE HIS ILE PHE SER LYS PHE TYR PRO CYS GLU GLU
SEQRES 7 D 139 CYS ALA GLU ASP ILE ARG LYS ARG ILE ASP ARG SER GLN
SEQRES 8 D 139 PRO ASP THR SER THR ARG VAL SER PHE SER GLN TRP LEU
SEQRES 9 D 139 CYS ARG LEU HIS ASN GLU VAL ASN ARG LYS LEU GLY LYS
SEQRES 10 D 139 PRO ASP PHE ASP CYS SER ARG VAL ASP GLU ARG TRP ARG
SEQRES 11 D 139 ASP GLY TRP LYS ASP GLY SER CYS ASP
HET FAD A 126 53
HET CL A 130 1
HET CL A 131 1
HET CD A 500 1
HET CD A 501 1
HET CL A 502 1
HET CL A 503 1
HET CL A 504 1
HET CL A 505 1
HET FAD B 126 53
HET CD B 130 1
HET CD B 131 1
HET CL B 132 1
HET CL B 133 1
HET FAD C 126 53
HET CD C 127 1
HET CL C 128 1
HET FAD D 126 53
HET SO4 D 127 1
HET CL D 128 1
HET SO4 D 129 1
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM CL CHLORIDE ION
HETNAM CD CADMIUM ION
HETNAM SO4 SULFATE ION
FORMUL 5 FAD 4(C27 H33 N9 O15 P2)
FORMUL 6 CL 10(CL 1-)
FORMUL 8 CD 5(CD 2+)
FORMUL 23 SO4 2(O4 S 2-)
FORMUL 26 HOH *237(H2 O)
HELIX 1 1 ASP A 18 TYR A 36 1 19
HELIX 2 2 THR A 42 TYR A 60 1 19
HELIX 3 3 ASP A 68 SER A 76 1 9
HELIX 4 4 THR A 82 GLY A 102 1 21
HELIX 5 5 ASP A 107 SER A 109 5 3
HELIX 6 6 ARG A 110 ARG A 116 1 7
HELIX 7 7 ASP B 18 TYR B 36 1 19
HELIX 8 8 THR B 42 TYR B 60 1 19
HELIX 9 9 ASP B 68 SER B 76 1 9
HELIX 10 10 THR B 82 LEU B 101 1 20
HELIX 11 11 ASP B 107 SER B 109 5 3
HELIX 12 12 ARG B 110 ARG B 116 1 7
HELIX 13 13 ASP C 18 TYR C 36 1 19
HELIX 14 14 THR C 42 TYR C 60 1 19
HELIX 15 15 CYS C 62 SER C 76 1 15
HELIX 16 16 THR C 82 GLY C 102 1 21
HELIX 17 17 ASP C 107 SER C 109 5 3
HELIX 18 18 ARG C 110 ARG C 116 1 7
HELIX 19 19 ASP D 18 TYR D 36 1 19
HELIX 20 20 THR D 42 TYR D 60 1 19
HELIX 21 21 ASP D 68 ILE D 73 1 6
HELIX 22 22 THR D 82 LEU D 101 1 20
HELIX 23 23 ASP D 107 SER D 109 5 3
HELIX 24 24 ARG D 110 ARG D 116 1 7
SSBOND 1 CYS A 15 CYS C 124 1555 1555 2.03
SSBOND 2 CYS A 62 CYS A 65 1555 1555 2.03
SSBOND 3 CYS A 91 CYS A 108 1555 1555 2.04
SSBOND 4 CYS A 124 CYS C 15 1555 1555 2.03
SSBOND 5 CYS B 15 CYS D 124 1555 1555 2.03
SSBOND 6 CYS B 62 CYS B 65 1555 1555 2.02
SSBOND 7 CYS B 91 CYS B 108 1555 1555 2.03
SSBOND 8 CYS B 124 CYS D 15 1555 1555 2.02
SSBOND 9 CYS C 62 CYS C 65 1555 1555 2.04
SSBOND 10 CYS C 91 CYS C 108 1555 1555 2.04
SSBOND 11 CYS D 62 CYS D 65 1555 1555 2.02
SSBOND 12 CYS D 91 CYS D 108 1555 1555 2.04
LINK CD CD A 500 CL CL A 502 1555 1555 2.58
LINK CD CD A 500 CL CL A 503 1555 1555 2.70
LINK CD CD A 500 CL CL A 504 1555 1555 2.49
LINK CD CD A 500 O HOH A 506 1555 1555 2.29
LINK OD1 ASP A 74 CD CD A 500 1555 1555 2.56
LINK OD2 ASP A 74 CD CD A 500 1555 1555 2.37
LINK CD CD A 501 CL CL A 502 1555 1555 2.74
LINK CD CD A 501 CL CL A 503 1555 1555 2.59
LINK CD CD A 501 CL CL A 505 1555 1555 2.40
LINK CD CD A 501 O HOH A 507 1555 1555 2.51
LINK OD1 ASP B 74 CD CD A 501 1555 1555 2.48
LINK OD2 ASP B 74 CD CD A 501 1555 1555 2.49
LINK OE1 GLU B 113 CD CD B 130 1555 1555 2.42
LINK CD CD C 127 O HOH C 129 1555 1555 2.52
LINK CD CD B 130 O HOH B 138 1555 1555 2.53
LINK CD CD B 130 O HOH B 139 1555 1555 2.55
LINK CD CD B 131 O HOH B 141 1555 1555 2.55
LINK OE1 GLN B 47 CD CD B 131 1555 1555 2.60
LINK OD1 ASP C 107 CD CD C 127 1555 1555 2.62
LINK OE2 GLU B 44 CD CD B 131 1555 1555 2.69
LINK CD CD B 131 O HOH A 133 1555 1555 2.69
CISPEP 1 GLU B 63 GLU B 64 0 -0.81
SITE 1 AC1 30 ARG A 19 GLU A 20 GLY A 23 ARG A 24
SITE 2 AC1 30 TRP A 27 HIS A 31 TYR A 60 CYS A 62
SITE 3 AC1 30 CYS A 65 ALA A 66 GLU A 67 CYS A 91
SITE 4 AC1 30 HIS A 94 ASN A 95 VAL A 97 ASN A 98
SITE 5 AC1 30 LEU A 101 LYS A 103 PHE A 106 ARG A 114
SITE 6 AC1 30 TRP A 115 HOH A 141 HOH A 143 HOH A 156
SITE 7 AC1 30 HOH A 162 HOH A 165 HOH A 171 HOH A 189
SITE 8 AC1 30 ASP C 14 HOH C 144
SITE 1 AC2 5 GLU A 44 GLN A 47 HOH A 168 HOH A 223
SITE 2 AC2 5 HOH B 222
SITE 1 AC3 5 GLU A 44 ASP A 48 ARG B 75 LYS C 58
SITE 2 AC3 5 HOH C 150
SITE 1 AC4 30 ARG B 19 GLU B 20 GLY B 23 ARG B 24
SITE 2 AC4 30 TRP B 27 HIS B 31 TYR B 60 CYS B 62
SITE 3 AC4 30 CYS B 65 ALA B 66 GLU B 67 CYS B 91
SITE 4 AC4 30 HIS B 94 ASN B 95 VAL B 97 ASN B 98
SITE 5 AC4 30 LEU B 101 LYS B 103 PHE B 106 ARG B 114
SITE 6 AC4 30 TRP B 115 HOH B 135 HOH B 144 HOH B 151
SITE 7 AC4 30 HOH B 163 HOH B 172 HOH B 173 HOH B 179
SITE 8 AC4 30 HOH B 181 HOH B 190
SITE 1 AC5 4 GLU B 113 HOH B 138 HOH B 139 HOH D 137
SITE 1 AC6 5 HOH A 133 HOH A 199 GLU B 44 GLN B 47
SITE 2 AC6 5 HOH B 141
SITE 1 AC7 4 CYS B 15 GLN B 17 HOH B 174 HOH B 185
SITE 1 AC8 1 ARG B 92
SITE 1 AC9 21 GLU C 20 GLY C 23 ARG C 24 TRP C 27
SITE 2 AC9 21 HIS C 31 TYR C 60 CYS C 65 ILE C 69
SITE 3 AC9 21 CYS C 91 HIS C 94 ASN C 95 VAL C 97
SITE 4 AC9 21 ASN C 98 LYS C 100 LEU C 101 LYS C 103
SITE 5 AC9 21 PHE C 106 VAL C 111 ARG C 114 TRP C 115
SITE 6 AC9 21 HOH C 145
SITE 1 BC1 4 ASP C 107 SER C 109 HOH C 129 HOH C 131
SITE 1 BC2 2 GLN C 17 ASN C 25
SITE 1 BC3 24 ARG D 19 GLU D 20 GLY D 23 ARG D 24
SITE 2 BC3 24 TRP D 27 HIS D 31 TYR D 60 CYS D 65
SITE 3 BC3 24 ALA D 66 GLU D 67 ILE D 69 CYS D 91
SITE 4 BC3 24 HIS D 94 ASN D 95 VAL D 97 ASN D 98
SITE 5 BC3 24 LEU D 101 LYS D 103 PHE D 106 ARG D 114
SITE 6 BC3 24 TRP D 115 HOH D 130 HOH D 138 HOH D 187
SITE 1 BC4 3 ASP B 105 ASP D 112 HOH D 173
SITE 1 BC5 2 GLU D 21 HOH D 148
SITE 1 BC6 2 GLN D 17 ASN D 25
SITE 1 BC7 5 ASP A 74 CL A 502 CL A 503 CL A 504
SITE 2 BC7 5 HOH A 506
SITE 1 BC8 5 CL A 502 CL A 503 CL A 505 HOH A 507
SITE 2 BC8 5 ASP B 74
SITE 1 BC9 6 HIS A 54 LYS A 58 CD A 500 CD A 501
SITE 2 BC9 6 CL A 503 ASP B 74
SITE 1 CC1 6 ASP A 74 CD A 500 CD A 501 CL A 502
SITE 2 CC1 6 HIS B 54 LYS B 58
SITE 1 CC2 4 LYS A 58 ARG A 70 CD A 500 LYS B 58
SITE 1 CC3 4 LYS A 58 CD A 501 ARG B 70 ASP B 74
CRYST1 99.688 99.688 113.610 90.00 90.00 90.00 I 41 32
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 0.010031 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010031 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008802 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
