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HEADER HYDROLASE 03-FEB-22 7R1K
TITLE PHOSPHORYLATED BACILLUS PUMILUS LIPASE A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS PUMILUS;
SOURCE 3 ORGANISM_TAXID: 1408;
SOURCE 4 GENE: L5;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: NICO21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS LIPASE, ESTERASE, INTERMEDIATE, COMPLEX, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.A.LUND
REVDAT 1 25-MAY-22 7R1K 0
JRNL AUTH B.A.LUND,L.SVALBERG,M.PURG,G.CHUKWU,M.WIDERSTEN,G.V.ISAKSEN,
JRNL AUTH 2 B.O.BRANDSDAL,J.AQVIST
JRNL TITL STRUCTURE AND MECHANISM OF A COLD-ADAPTED BACTERIAL LIPASE
JRNL REF BIOCHEMISTRY V. 61 933 2022
JRNL REFN ISSN 0006-2960
JRNL DOI 10.1021/ACS.BIOCHEM.2C00087
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20RC4_4425
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.93
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 47147
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.142
REMARK 3 R VALUE (WORKING SET) : 0.141
REMARK 3 FREE R VALUE : 0.165
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.860
REMARK 3 FREE R VALUE TEST SET COUNT : 2291
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 20.9300 - 3.7700 0.93 2691 101 0.1276 0.1362
REMARK 3 2 3.7700 - 3.0000 0.99 2776 161 0.1132 0.1261
REMARK 3 3 3.0000 - 2.6200 0.99 2839 130 0.1160 0.1104
REMARK 3 4 2.6200 - 2.3800 0.96 2738 108 0.1170 0.1703
REMARK 3 5 2.3800 - 2.2100 0.99 2829 146 0.1007 0.1173
REMARK 3 6 2.2100 - 2.0800 1.00 2848 149 0.1142 0.1594
REMARK 3 7 2.0800 - 1.9800 0.99 2814 159 0.1148 0.1564
REMARK 3 8 1.9800 - 1.8900 1.00 2803 154 0.1231 0.1722
REMARK 3 9 1.8900 - 1.8200 1.00 2894 124 0.1406 0.1720
REMARK 3 10 1.8200 - 1.7500 1.00 2831 148 0.1748 0.1979
REMARK 3 11 1.7500 - 1.7000 1.00 2814 141 0.1928 0.2395
REMARK 3 12 1.7000 - 1.6500 0.99 2783 150 0.2111 0.2514
REMARK 3 13 1.6500 - 1.6100 0.99 2844 173 0.2340 0.2659
REMARK 3 14 1.6100 - 1.5700 0.99 2809 130 0.2493 0.2417
REMARK 3 15 1.5700 - 1.5300 0.99 2797 180 0.2739 0.2993
REMARK 3 16 1.5300 - 1.5000 0.98 2746 137 0.3105 0.3154
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 0.90
REMARK 3 SHRINKAGE RADIUS : 0.40
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.177
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.449
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.89
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.56
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 : 0.008 1440
REMARK 3 ANGLE : 0.873 1949
REMARK 3 CHIRALITY : 0.060 217
REMARK 3 PLANARITY : 0.010 258
REMARK 3 DIHEDRAL : 15.437 522
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 11
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 4 THROUGH 16 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.8770 -14.1506 9.7307
REMARK 3 T TENSOR
REMARK 3 T11: 0.0982 T22: 0.1126
REMARK 3 T33: 0.0934 T12: -0.0043
REMARK 3 T13: -0.0150 T23: -0.0082
REMARK 3 L TENSOR
REMARK 3 L11: 3.7027 L22: 8.4965
REMARK 3 L33: 3.1824 L12: -3.9746
REMARK 3 L13: 0.7459 L23: -3.2737
REMARK 3 S TENSOR
REMARK 3 S11: 0.0891 S12: 0.0467 S13: -0.2233
REMARK 3 S21: -0.0113 S22: 0.0359 S23: 0.4212
REMARK 3 S31: -0.0219 S32: 0.0543 S33: -0.0797
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 17 THROUGH 30 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.8634 -18.7047 6.4145
REMARK 3 T TENSOR
REMARK 3 T11: 0.0960 T22: 0.1111
REMARK 3 T33: 0.0748 T12: -0.0175
REMARK 3 T13: -0.0090 T23: -0.0134
REMARK 3 L TENSOR
REMARK 3 L11: 5.5854 L22: 4.5608
REMARK 3 L33: 3.6035 L12: -0.9293
REMARK 3 L13: 1.3305 L23: -0.2043
REMARK 3 S TENSOR
REMARK 3 S11: -0.0611 S12: 0.1287 S13: -0.2561
REMARK 3 S21: -0.0810 S22: 0.0776 S23: 0.2279
REMARK 3 S31: 0.0182 S32: -0.1139 S33: -0.0294
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 31 THROUGH 39 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.9091 -11.2055 1.1332
REMARK 3 T TENSOR
REMARK 3 T11: 0.1899 T22: 0.2254
REMARK 3 T33: 0.1162 T12: 0.0080
REMARK 3 T13: -0.0162 T23: 0.0126
REMARK 3 L TENSOR
REMARK 3 L11: 2.1764 L22: 1.2171
REMARK 3 L33: 0.1703 L12: -1.3233
REMARK 3 L13: -0.4739 L23: 0.1233
REMARK 3 S TENSOR
REMARK 3 S11: 0.1147 S12: 0.5891 S13: 0.0696
REMARK 3 S21: -0.1560 S22: -0.0531 S23: 0.1354
REMARK 3 S31: 0.1659 S32: -0.0356 S33: -0.0646
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 40 THROUGH 48 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.7638 -20.3589 12.0806
REMARK 3 T TENSOR
REMARK 3 T11: 0.1226 T22: 0.1433
REMARK 3 T33: 0.1324 T12: 0.0254
REMARK 3 T13: 0.0150 T23: -0.0019
REMARK 3 L TENSOR
REMARK 3 L11: 4.7172 L22: 2.8417
REMARK 3 L33: 5.4409 L12: -2.3059
REMARK 3 L13: 5.0597 L23: -2.6277
REMARK 3 S TENSOR
REMARK 3 S11: -0.0025 S12: 0.0770 S13: -0.0663
REMARK 3 S21: 0.1000 S22: -0.0368 S23: -0.0037
REMARK 3 S31: 0.0079 S32: 0.1528 S33: 0.0608
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 49 THROUGH 67 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.1581 -9.7908 6.5931
REMARK 3 T TENSOR
REMARK 3 T11: 0.0950 T22: 0.1182
REMARK 3 T33: 0.1166 T12: 0.0001
REMARK 3 T13: 0.0098 T23: -0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 3.9992 L22: 4.2867
REMARK 3 L33: 6.9561 L12: -2.9509
REMARK 3 L13: 3.5064 L23: -3.3695
REMARK 3 S TENSOR
REMARK 3 S11: 0.0188 S12: 0.1888 S13: 0.0437
REMARK 3 S21: -0.1278 S22: -0.0883 S23: -0.1963
REMARK 3 S31: 0.0764 S32: 0.1971 S33: 0.0180
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 68 THROUGH 90 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.4884 -8.2364 14.5714
REMARK 3 T TENSOR
REMARK 3 T11: 0.0962 T22: 0.0995
REMARK 3 T33: 0.0846 T12: 0.0071
REMARK 3 T13: 0.0104 T23: -0.0130
REMARK 3 L TENSOR
REMARK 3 L11: 1.9319 L22: 2.3727
REMARK 3 L33: 2.8675 L12: 0.2809
REMARK 3 L13: 0.0418 L23: -0.8335
REMARK 3 S TENSOR
REMARK 3 S11: -0.0123 S12: -0.0749 S13: 0.0326
REMARK 3 S21: 0.0319 S22: 0.0454 S23: -0.1427
REMARK 3 S31: -0.1078 S32: 0.1327 S33: -0.0092
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 91 THROUGH 109 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.3049 -6.8660 16.4781
REMARK 3 T TENSOR
REMARK 3 T11: 0.1158 T22: 0.0995
REMARK 3 T33: 0.0931 T12: -0.0008
REMARK 3 T13: 0.0003 T23: -0.0194
REMARK 3 L TENSOR
REMARK 3 L11: 2.2291 L22: 1.0133
REMARK 3 L33: 1.0057 L12: 0.6288
REMARK 3 L13: -0.7173 L23: -0.3443
REMARK 3 S TENSOR
REMARK 3 S11: 0.0243 S12: -0.0852 S13: 0.1188
REMARK 3 S21: 0.0490 S22: 0.0117 S23: -0.0739
REMARK 3 S31: -0.0692 S32: 0.0456 S33: -0.0550
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 110 THROUGH 124 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.2041 1.2473 20.0830
REMARK 3 T TENSOR
REMARK 3 T11: 0.1480 T22: 0.1379
REMARK 3 T33: 0.1850 T12: -0.0189
REMARK 3 T13: -0.0028 T23: -0.0353
REMARK 3 L TENSOR
REMARK 3 L11: 4.1742 L22: 4.9971
REMARK 3 L33: 2.6948 L12: -0.3950
REMARK 3 L13: -0.6489 L23: -0.3173
REMARK 3 S TENSOR
REMARK 3 S11: -0.0420 S12: -0.0984 S13: 0.5073
REMARK 3 S21: 0.0907 S22: 0.0772 S23: 0.1388
REMARK 3 S31: -0.3878 S32: 0.0819 S33: -0.1073
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 125 THROUGH 158 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.6224 -14.8975 25.5994
REMARK 3 T TENSOR
REMARK 3 T11: 0.1353 T22: 0.1344
REMARK 3 T33: 0.0956 T12: -0.0056
REMARK 3 T13: 0.0176 T23: 0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 1.0684 L22: 2.7401
REMARK 3 L33: 1.4685 L12: -0.1832
REMARK 3 L13: 0.0674 L23: -0.2515
REMARK 3 S TENSOR
REMARK 3 S11: 0.0320 S12: -0.1356 S13: -0.0859
REMARK 3 S21: 0.1520 S22: -0.0300 S23: 0.0962
REMARK 3 S31: 0.1072 S32: -0.0572 S33: 0.0248
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 159 THROUGH 174 )
REMARK 3 ORIGIN FOR THE GROUP (A): -25.0516 -14.7832 15.4527
REMARK 3 T TENSOR
REMARK 3 T11: 0.0964 T22: 0.1355
REMARK 3 T33: 0.0956 T12: -0.0066
REMARK 3 T13: -0.0020 T23: -0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 2.2499 L22: 7.2102
REMARK 3 L33: 1.1523 L12: 1.1226
REMARK 3 L13: 0.2082 L23: 0.3557
REMARK 3 S TENSOR
REMARK 3 S11: 0.0648 S12: -0.1066 S13: 0.0641
REMARK 3 S21: 0.1776 S22: -0.1063 S23: 0.2109
REMARK 3 S31: 0.0510 S32: -0.0707 S33: 0.0122
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 175 THROUGH 184 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.8324 1.7323 21.6993
REMARK 3 T TENSOR
REMARK 3 T11: 0.1747 T22: 0.1352
REMARK 3 T33: 0.1581 T12: 0.0008
REMARK 3 T13: 0.0106 T23: -0.0371
REMARK 3 L TENSOR
REMARK 3 L11: 3.7862 L22: 3.6915
REMARK 3 L33: 8.2164 L12: 2.1840
REMARK 3 L13: 5.1010 L23: 3.2748
REMARK 3 S TENSOR
REMARK 3 S11: -0.1044 S12: 0.0208 S13: 0.2240
REMARK 3 S21: -0.0033 S22: 0.1094 S23: 0.0289
REMARK 3 S31: -0.4889 S32: 0.1286 S33: -0.1158
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 7R1K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-FEB-22.
REMARK 100 THE DEPOSITION ID IS D_1292120769.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-NOV-20
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : SEALED TUBE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : BRUKER D8 QUEST
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : BRUKER PHOTON II
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.3
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47178
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 20.930
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : 0.12300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.4200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.55
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 1.49200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.050
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.8.3
REMARK 200 STARTING MODEL: 1ISP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 34.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6.5 18-22 % PEG 4000 0.1
REMARK 280 -0.5 M LITHIUM CITRATE 1:100 DILUTED PARAOXON-ETHYL MIXED WITH
REMARK 280 ENZYME, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 28.69800
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 21.42150
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 28.69800
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 21.42150
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: 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 303 LIES ON A SPECIAL POSITION.
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 ALA A 2
REMARK 465 GLU A 3
REMARK 465 HIS A 185
REMARK 465 HIS A 186
REMARK 465 HIS A 187
REMARK 465 HIS A 188
REMARK 465 HIS A 189
REMARK 465 HIS A 190
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 78 -122.41 51.86
REMARK 500 LEU A 91 -148.48 -109.19
REMARK 500 GLU A 98 -66.74 -108.40
REMARK 500 GLN A 122 105.38 -165.07
REMARK 500
REMARK 500 REMARK: NULL
DBREF 7R1K A 2 182 UNP W8FKE7 W8FKE7_BACPU 35 215
SEQADV 7R1K MET A 1 UNP W8FKE7 INITIATING METHIONINE
SEQADV 7R1K LEU A 183 UNP W8FKE7 EXPRESSION TAG
SEQADV 7R1K GLU A 184 UNP W8FKE7 EXPRESSION TAG
SEQADV 7R1K HIS A 185 UNP W8FKE7 EXPRESSION TAG
SEQADV 7R1K HIS A 186 UNP W8FKE7 EXPRESSION TAG
SEQADV 7R1K HIS A 187 UNP W8FKE7 EXPRESSION TAG
SEQADV 7R1K HIS A 188 UNP W8FKE7 EXPRESSION TAG
SEQADV 7R1K HIS A 189 UNP W8FKE7 EXPRESSION TAG
SEQADV 7R1K HIS A 190 UNP W8FKE7 EXPRESSION TAG
SEQRES 1 A 190 MET ALA GLU HIS ASN PRO VAL VAL MET VAL HIS GLY MET
SEQRES 2 A 190 GLY GLY ALA SER TYR ASN PHE ALA SER ILE LYS SER TYR
SEQRES 3 A 190 LEU VAL THR GLN GLY TRP ASP ARG ASN GLN LEU PHE ALA
SEQRES 4 A 190 ILE ASP PHE ILE ASP LYS THR GLY ASN ASN ARG ASN ASN
SEQRES 5 A 190 GLY PRO ARG LEU SER ARG PHE VAL LYS ASP VAL LEU GLY
SEQRES 6 A 190 LYS THR GLY ALA LYS LYS VAL ASP ILE VAL ALA HIS SER
SEQRES 7 A 190 MET GLY GLY ALA ASN THR LEU TYR TYR ILE LYS ASN LEU
SEQRES 8 A 190 ASP GLY GLY ASP LYS ILE GLU ASN VAL VAL THR LEU GLY
SEQRES 9 A 190 GLY ALA ASN GLY LEU VAL SER LEU ARG ALA LEU PRO GLY
SEQRES 10 A 190 THR ASP PRO ASN GLN LYS ILE LEU TYR THR SER VAL TYR
SEQRES 11 A 190 SER SER ALA ASP MET ILE VAL VAL ASN SER LEU SER ARG
SEQRES 12 A 190 LEU ILE GLY ALA ARG ASN VAL LEU ILE HIS GLY VAL GLY
SEQRES 13 A 190 HIS ILE SER LEU LEU ALA SER SER GLN VAL LYS GLY TYR
SEQRES 14 A 190 ILE LYS GLU GLY LEU ASN GLY GLY GLY GLN ASN THR ASN
SEQRES 15 A 190 LEU GLU HIS HIS HIS HIS HIS HIS
HET OAA A 201 22
HET DEP A 202 18
HETNAM OAA OXALOACETATE ION
HETNAM DEP DIETHYL PHOSPHONATE
FORMUL 2 OAA C4 H3 O5 1-
FORMUL 3 DEP C4 H11 O3 P
FORMUL 4 HOH *99(H2 O)
HELIX 1 AA1 ALA A 16 ASN A 19 5 4
HELIX 2 AA2 PHE A 20 GLN A 30 1 11
HELIX 3 AA3 ASP A 33 ASN A 35 5 3
HELIX 4 AA4 ASN A 48 GLY A 68 1 21
HELIX 5 AA5 MET A 79 LEU A 91 1 13
HELIX 6 AA6 ALA A 106 VAL A 110 5 5
HELIX 7 AA7 VAL A 138 ARG A 143 1 6
HELIX 8 AA8 ILE A 158 ALA A 162 5 5
HELIX 9 AA9 SER A 163 ASN A 175 1 13
SHEET 1 AA1 6 LEU A 37 ALA A 39 0
SHEET 2 AA1 6 VAL A 7 VAL A 10 1 N VAL A 7 O PHE A 38
SHEET 3 AA1 6 VAL A 72 HIS A 77 1 O ASP A 73 N VAL A 8
SHEET 4 AA1 6 ILE A 97 LEU A 103 1 O LEU A 103 N ALA A 76
SHEET 5 AA1 6 LEU A 125 SER A 131 1 O LEU A 125 N VAL A 100
SHEET 6 AA1 6 ARG A 148 ILE A 152 1 O VAL A 150 N SER A 128
LINK OG SER A 78 P DEP A 202 1555 1555 1.55
CRYST1 57.396 42.843 62.660 90.00 91.28 90.00 C 1 2 1 4
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 0.017423 0.000000 0.000389 0.00000
SCALE2 0.000000 0.023341 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015963 0.00000
TER 2790 GLU A 184
MASTER 413 0 2 9 6 0 0 6 1474 1 41 15
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