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HEADER HYDROLASE 17-FEB-23 8CLN
TITLE ZEARALENONE LACTONASE FROM STREPTOMYCES COELICOFLAVUS, SEMET
TITLE 2 DERIVATIVE FOR SAD PHASING
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYDROLASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES COELICOFLAVUS;
SOURCE 3 ORGANISM_TAXID: 285562;
SOURCE 4 GENE: SMCF_1294;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ZEARALENONE, MYCOTOXIN, LACTONASE, CARBOXYLESTERASE, ESTERASE,
KEYWDS 2 HYDROLASE, BIODEGRADATION, SEMET, SELENOMETHIONINE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.PUEHRINGER,I.GRISHKOVSKAYA,G.MLYNEK,J.KOSTAN
REVDAT 1 21-FEB-24 8CLN 0
JRNL AUTH S.FRUHAUF,D.PUEHRINGER,M.THAMHESL,P.FAJTL,E.KUNZ-VEKIRO,
JRNL AUTH 2 A.HOEBARTNER-GUSSL,J.PANHOELZL,K.PREM,V.KLINGENBRUNNER,
JRNL AUTH 3 G.SCHATZMAYR,G.ADAM,J.DAMBORSKY,K.DJINOVIC-CARUGO,Z.PROKOP,
JRNL AUTH 4 W.D.MOLL
JRNL TITL BACTERIAL LACTONASES ZENA WITH NONCANONICAL STRUCTURAL
JRNL TITL 2 FEATURES HYDROLYSE THE MYCOTOXIN ZEARALENONE
JRNL REF ACS CATALYSIS 2024
JRNL REFN ESSN 2155-5435
JRNL DOI 10.1021/ACSCATAL.4C00271
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1-4489
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.91
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 47730
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.170
REMARK 3 FREE R VALUE TEST SET COUNT : 3707
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 46.9100 - 7.4000 1.00 3268 148 0.1612 0.1884
REMARK 3 2 7.3900 - 5.8800 1.00 3270 135 0.1956 0.2157
REMARK 3 3 5.8700 - 5.1300 1.00 3308 144 0.1717 0.2057
REMARK 3 4 5.1300 - 4.6600 1.00 3245 144 0.1562 0.1967
REMARK 3 5 4.6600 - 4.3300 1.00 3313 132 0.1455 0.2247
REMARK 3 6 4.3300 - 4.0800 1.00 3292 146 0.1484 0.1824
REMARK 3 7 4.0700 - 3.8700 1.00 3299 148 0.1595 0.2353
REMARK 3 8 3.8700 - 3.7000 1.00 3269 138 0.1766 0.2182
REMARK 3 9 3.7000 - 3.5600 1.00 3240 150 0.1808 0.2398
REMARK 3 10 3.5600 - 3.4400 1.00 3232 132 0.1830 0.2223
REMARK 3 11 3.4400 - 3.3300 1.00 3348 148 0.1911 0.2327
REMARK 3 12 3.3300 - 3.2300 1.00 3292 139 0.2004 0.3049
REMARK 3 13 3.2300 - 3.1500 1.00 3257 138 0.1937 0.2415
REMARK 3 14 3.1500 - 3.0700 1.00 3312 138 0.2083 0.2695
REMARK 3 15 3.0700 - 3.0000 1.00 3256 144 0.2298 0.2741
REMARK 3 16 3.0000 - 2.9400 1.00 3289 148 0.2137 0.2524
REMARK 3 17 2.9400 - 2.8800 1.00 3246 148 0.2075 0.2754
REMARK 3 18 2.8800 - 2.8300 1.00 3345 146 0.2096 0.2891
REMARK 3 19 2.8300 - 2.7800 1.00 3162 138 0.2099 0.2484
REMARK 3 20 2.7800 - 2.7300 1.00 3356 143 0.2183 0.3188
REMARK 3 21 2.7300 - 2.6800 1.00 3230 138 0.2199 0.2418
REMARK 3 22 2.6800 - 2.6400 1.00 3355 150 0.2274 0.3088
REMARK 3 23 2.6400 - 2.6000 1.00 3163 134 0.2300 0.3359
REMARK 3 24 2.6000 - 2.5700 1.00 3356 150 0.2317 0.2789
REMARK 3 25 2.5700 - 2.5300 1.00 3268 146 0.2469 0.2718
REMARK 3 26 2.5300 - 2.5000 1.00 3263 142 0.2505 0.2723
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.920
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.75
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 : 0.004 9663
REMARK 3 ANGLE : 0.719 13179
REMARK 3 CHIRALITY : 0.043 1384
REMARK 3 PLANARITY : 0.013 1744
REMARK 3 DIHEDRAL : 5.616 1329
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN 'A' AND RESID 3 THROUGH 307)
REMARK 3 ORIGIN FOR THE GROUP (A): 35.0037 6.0528 58.9055
REMARK 3 T TENSOR
REMARK 3 T11: 0.2739 T22: 0.2560
REMARK 3 T33: 0.2788 T12: 0.0653
REMARK 3 T13: -0.0103 T23: -0.0150
REMARK 3 L TENSOR
REMARK 3 L11: 0.8401 L22: 0.9560
REMARK 3 L33: 1.9647 L12: -0.0667
REMARK 3 L13: -0.2122 L23: 0.1594
REMARK 3 S TENSOR
REMARK 3 S11: 0.0364 S12: 0.0192 S13: 0.0183
REMARK 3 S21: 0.1971 S22: 0.0083 S23: -0.0644
REMARK 3 S31: -0.0812 S32: 0.1274 S33: -0.0380
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN 'B' AND RESID 5 THROUGH 308)
REMARK 3 ORIGIN FOR THE GROUP (A): 23.4185 -21.5756 42.4529
REMARK 3 T TENSOR
REMARK 3 T11: 0.3916 T22: 0.3039
REMARK 3 T33: 0.3267 T12: -0.0592
REMARK 3 T13: -0.0100 T23: -0.0614
REMARK 3 L TENSOR
REMARK 3 L11: 1.2444 L22: 1.3509
REMARK 3 L33: 1.6071 L12: 0.0698
REMARK 3 L13: 0.0112 L23: -0.2850
REMARK 3 S TENSOR
REMARK 3 S11: -0.0093 S12: 0.2272 S13: -0.1902
REMARK 3 S21: -0.0811 S22: 0.0660 S23: 0.1266
REMARK 3 S31: 0.4810 S32: -0.3230 S33: -0.0465
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN 'C' AND RESID 9 THROUGH 307)
REMARK 3 ORIGIN FOR THE GROUP (A): 28.0145 16.9645 17.9418
REMARK 3 T TENSOR
REMARK 3 T11: 0.3634 T22: 0.5125
REMARK 3 T33: 0.2546 T12: -0.0064
REMARK 3 T13: 0.0029 T23: 0.0556
REMARK 3 L TENSOR
REMARK 3 L11: 0.8104 L22: 1.7157
REMARK 3 L33: 1.5794 L12: 0.0844
REMARK 3 L13: -0.2200 L23: -0.3093
REMARK 3 S TENSOR
REMARK 3 S11: -0.0236 S12: 0.2530 S13: 0.1268
REMARK 3 S21: -0.2286 S22: 0.1767 S23: 0.1571
REMARK 3 S31: -0.2327 S32: -0.2339 S33: -0.1499
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN 'D' AND RESID 10 THROUGH 308)
REMARK 3 ORIGIN FOR THE GROUP (A): 54.9442 -4.1818 18.9880
REMARK 3 T TENSOR
REMARK 3 T11: 0.3435 T22: 0.6265
REMARK 3 T33: 0.3684 T12: -0.0162
REMARK 3 T13: 0.0718 T23: -0.1476
REMARK 3 L TENSOR
REMARK 3 L11: 0.8642 L22: 1.3226
REMARK 3 L33: 2.0631 L12: 0.1413
REMARK 3 L13: -0.4597 L23: -0.1332
REMARK 3 S TENSOR
REMARK 3 S11: -0.0500 S12: 0.1804 S13: -0.0576
REMARK 3 S21: -0.2871 S22: 0.1744 S23: -0.3705
REMARK 3 S31: 0.0748 S32: 0.4120 S33: -0.0824
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 8CLN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-FEB-23.
REMARK 100 THE DEPOSITION ID IS D_1292128031.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-DEC-15
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 : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.977
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47746
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 46.910
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 19.20
REMARK 200 R MERGE (I) : 0.12020
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 20.7500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 18.90
REMARK 200 R MERGE FOR SHELL (I) : 0.72280
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.860
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: CRANK2
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.02M CACL2, 0.1M NAACETATE 4.6, 30%
REMARK 280 MPD, PH 4.6, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 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+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 134.87300
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 269.74600
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 269.74600
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 134.87300
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 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 1
REMARK 465 VAL A 2
REMARK 465 ALA A 308
REMARK 465 PRO A 309
REMARK 465 HIS A 310
REMARK 465 HIS A 311
REMARK 465 HIS A 312
REMARK 465 HIS A 313
REMARK 465 HIS A 314
REMARK 465 HIS A 315
REMARK 465 MET B 1
REMARK 465 VAL B 2
REMARK 465 THR B 3
REMARK 465 SER B 4
REMARK 465 PRO B 309
REMARK 465 HIS B 310
REMARK 465 HIS B 311
REMARK 465 HIS B 312
REMARK 465 HIS B 313
REMARK 465 HIS B 314
REMARK 465 HIS B 315
REMARK 465 MET C 1
REMARK 465 VAL C 2
REMARK 465 THR C 3
REMARK 465 SER C 4
REMARK 465 PRO C 5
REMARK 465 ALA C 6
REMARK 465 LEU C 7
REMARK 465 ARG C 8
REMARK 465 ALA C 308
REMARK 465 PRO C 309
REMARK 465 HIS C 310
REMARK 465 HIS C 311
REMARK 465 HIS C 312
REMARK 465 HIS C 313
REMARK 465 HIS C 314
REMARK 465 HIS C 315
REMARK 465 MET D 1
REMARK 465 VAL D 2
REMARK 465 THR D 3
REMARK 465 SER D 4
REMARK 465 PRO D 5
REMARK 465 ALA D 6
REMARK 465 LEU D 7
REMARK 465 ARG D 8
REMARK 465 ASP D 9
REMARK 465 PRO D 309
REMARK 465 HIS D 310
REMARK 465 HIS D 311
REMARK 465 HIS D 312
REMARK 465 HIS D 313
REMARK 465 HIS D 314
REMARK 465 HIS D 315
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 TRP A 52 0.25 -69.61
REMARK 500 SER A 112 -116.64 54.88
REMARK 500 PHE A 141 -22.97 70.83
REMARK 500 MET A 243 135.44 -38.77
REMARK 500 MET A 287 74.19 -101.46
REMARK 500 THR B 48 -3.03 76.90
REMARK 500 VAL B 101 -57.48 -121.20
REMARK 500 SER B 112 -116.22 57.99
REMARK 500 PHE B 141 -19.75 72.91
REMARK 500 VAL B 174 -63.78 -95.66
REMARK 500 MET B 287 75.68 -100.77
REMARK 500 THR C 48 -1.19 69.54
REMARK 500 SER C 112 -121.47 60.02
REMARK 500 PHE C 141 -24.65 71.51
REMARK 500 MET C 243 131.84 -36.01
REMARK 500 MET C 287 76.03 -102.31
REMARK 500 TRP D 52 5.52 -67.95
REMARK 500 SER D 112 -117.74 62.75
REMARK 500 PHE D 141 -20.75 71.81
REMARK 500 VAL D 174 -62.41 -95.72
REMARK 500 VAL D 281 77.64 -114.48
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 ARG A 228 0.09 SIDE CHAIN
REMARK 500 ARG B 182 0.08 SIDE CHAIN
REMARK 500 ARG D 266 0.09 SIDE CHAIN
REMARK 500 ARG D 302 0.11 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 8CLN A 1 309 UNP H1Q8U7 H1Q8U7_9ACTN 1 309
DBREF 8CLN B 1 309 UNP H1Q8U7 H1Q8U7_9ACTN 1 309
DBREF 8CLN C 1 309 UNP H1Q8U7 H1Q8U7_9ACTN 1 309
DBREF 8CLN D 1 309 UNP H1Q8U7 H1Q8U7_9ACTN 1 309
SEQADV 8CLN HIS A 310 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLN HIS A 311 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLN HIS A 312 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLN HIS A 313 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLN HIS A 314 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLN HIS A 315 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLN HIS B 310 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLN HIS B 311 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLN HIS B 312 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLN HIS B 313 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLN HIS B 314 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLN HIS B 315 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLN HIS C 310 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLN HIS C 311 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLN HIS C 312 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLN HIS C 313 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLN HIS C 314 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLN HIS C 315 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLN HIS D 310 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLN HIS D 311 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLN HIS D 312 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLN HIS D 313 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLN HIS D 314 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLN HIS D 315 UNP H1Q8U7 EXPRESSION TAG
SEQRES 1 A 315 MET VAL THR SER PRO ALA LEU ARG ASP VAL HIS VAL PRO
SEQRES 2 A 315 HIS ALA TYR PRO GLU GLN GLN VAL ASP LEU GLY GLU ILE
SEQRES 3 A 315 THR MET ASN TYR ALA GLU ALA GLY ASP PRO ASP ARG PRO
SEQRES 4 A 315 ALA VAL LEU LEU ILE PRO GLU GLN THR GLY SER TRP TRP
SEQRES 5 A 315 SER TYR GLU GLU ALA MET GLY LEU LEU SER GLU HIS PHE
SEQRES 6 A 315 HIS VAL TYR ALA VAL ASP LEU ARG GLY GLN GLY ARG SER
SEQRES 7 A 315 SER TRP THR PRO LYS ARG TYR SER LEU ASP ASN PHE GLY
SEQRES 8 A 315 ASN ASP LEU VAL ARG PHE ILE ALA LEU VAL VAL LYS ARG
SEQRES 9 A 315 PRO VAL VAL VAL ALA GLY ASN SER SER GLY GLY VAL LEU
SEQRES 10 A 315 ALA ALA TRP LEU SER ALA TYR SER MET PRO GLY GLN LEU
SEQRES 11 A 315 ARG GLY VAL LEU CYS GLU ASP PRO PRO PHE PHE ALA SER
SEQRES 12 A 315 GLU LEU VAL PRO ALA HIS GLY HIS SER VAL ARG GLN GLY
SEQRES 13 A 315 ALA GLY PRO VAL PHE GLU LEU PHE ARG THR TYR LEU GLY
SEQRES 14 A 315 ASP GLN TRP SER VAL GLY ASP TRP GLU GLY PHE CYS ARG
SEQRES 15 A 315 ALA ALA GLY ALA SER ALA SER PRO MET ALA ARG SER PHE
SEQRES 16 A 315 VAL ALA ASP GLY ILE PRO GLN HIS LEU GLN GLU TYR ASP
SEQRES 17 A 315 PRO GLU TRP ALA ARG VAL PHE TYR GLU GLY THR VAL GLY
SEQRES 18 A 315 LEU SER CYS PRO HIS GLU ARG MET LEU GLY GLN VAL LYS
SEQRES 19 A 315 THR PRO VAL LEU LEU THR HIS HIS MET ARG GLY ILE ASP
SEQRES 20 A 315 PRO GLU THR GLY ASN LEU LEU GLY ALA LEU SER ASP GLU
SEQRES 21 A 315 GLN ALA LEU ARG ALA ARG ARG LEU MET ASP SER ALA GLY
SEQRES 22 A 315 VAL THR VAL ASP TYR GLU SER VAL PRO ASP ALA SER HIS
SEQRES 23 A 315 MET MET HIS GLN SER ALA PRO ALA ARG TYR VAL GLU ILE
SEQRES 24 A 315 PHE THR ARG TRP ALA ALA ALA LEU ALA PRO HIS HIS HIS
SEQRES 25 A 315 HIS HIS HIS
SEQRES 1 B 315 MET VAL THR SER PRO ALA LEU ARG ASP VAL HIS VAL PRO
SEQRES 2 B 315 HIS ALA TYR PRO GLU GLN GLN VAL ASP LEU GLY GLU ILE
SEQRES 3 B 315 THR MET ASN TYR ALA GLU ALA GLY ASP PRO ASP ARG PRO
SEQRES 4 B 315 ALA VAL LEU LEU ILE PRO GLU GLN THR GLY SER TRP TRP
SEQRES 5 B 315 SER TYR GLU GLU ALA MET GLY LEU LEU SER GLU HIS PHE
SEQRES 6 B 315 HIS VAL TYR ALA VAL ASP LEU ARG GLY GLN GLY ARG SER
SEQRES 7 B 315 SER TRP THR PRO LYS ARG TYR SER LEU ASP ASN PHE GLY
SEQRES 8 B 315 ASN ASP LEU VAL ARG PHE ILE ALA LEU VAL VAL LYS ARG
SEQRES 9 B 315 PRO VAL VAL VAL ALA GLY ASN SER SER GLY GLY VAL LEU
SEQRES 10 B 315 ALA ALA TRP LEU SER ALA TYR SER MET PRO GLY GLN LEU
SEQRES 11 B 315 ARG GLY VAL LEU CYS GLU ASP PRO PRO PHE PHE ALA SER
SEQRES 12 B 315 GLU LEU VAL PRO ALA HIS GLY HIS SER VAL ARG GLN GLY
SEQRES 13 B 315 ALA GLY PRO VAL PHE GLU LEU PHE ARG THR TYR LEU GLY
SEQRES 14 B 315 ASP GLN TRP SER VAL GLY ASP TRP GLU GLY PHE CYS ARG
SEQRES 15 B 315 ALA ALA GLY ALA SER ALA SER PRO MET ALA ARG SER PHE
SEQRES 16 B 315 VAL ALA ASP GLY ILE PRO GLN HIS LEU GLN GLU TYR ASP
SEQRES 17 B 315 PRO GLU TRP ALA ARG VAL PHE TYR GLU GLY THR VAL GLY
SEQRES 18 B 315 LEU SER CYS PRO HIS GLU ARG MET LEU GLY GLN VAL LYS
SEQRES 19 B 315 THR PRO VAL LEU LEU THR HIS HIS MET ARG GLY ILE ASP
SEQRES 20 B 315 PRO GLU THR GLY ASN LEU LEU GLY ALA LEU SER ASP GLU
SEQRES 21 B 315 GLN ALA LEU ARG ALA ARG ARG LEU MET ASP SER ALA GLY
SEQRES 22 B 315 VAL THR VAL ASP TYR GLU SER VAL PRO ASP ALA SER HIS
SEQRES 23 B 315 MET MET HIS GLN SER ALA PRO ALA ARG TYR VAL GLU ILE
SEQRES 24 B 315 PHE THR ARG TRP ALA ALA ALA LEU ALA PRO HIS HIS HIS
SEQRES 25 B 315 HIS HIS HIS
SEQRES 1 C 315 MET VAL THR SER PRO ALA LEU ARG ASP VAL HIS VAL PRO
SEQRES 2 C 315 HIS ALA TYR PRO GLU GLN GLN VAL ASP LEU GLY GLU ILE
SEQRES 3 C 315 THR MET ASN TYR ALA GLU ALA GLY ASP PRO ASP ARG PRO
SEQRES 4 C 315 ALA VAL LEU LEU ILE PRO GLU GLN THR GLY SER TRP TRP
SEQRES 5 C 315 SER TYR GLU GLU ALA MET GLY LEU LEU SER GLU HIS PHE
SEQRES 6 C 315 HIS VAL TYR ALA VAL ASP LEU ARG GLY GLN GLY ARG SER
SEQRES 7 C 315 SER TRP THR PRO LYS ARG TYR SER LEU ASP ASN PHE GLY
SEQRES 8 C 315 ASN ASP LEU VAL ARG PHE ILE ALA LEU VAL VAL LYS ARG
SEQRES 9 C 315 PRO VAL VAL VAL ALA GLY ASN SER SER GLY GLY VAL LEU
SEQRES 10 C 315 ALA ALA TRP LEU SER ALA TYR SER MET PRO GLY GLN LEU
SEQRES 11 C 315 ARG GLY VAL LEU CYS GLU ASP PRO PRO PHE PHE ALA SER
SEQRES 12 C 315 GLU LEU VAL PRO ALA HIS GLY HIS SER VAL ARG GLN GLY
SEQRES 13 C 315 ALA GLY PRO VAL PHE GLU LEU PHE ARG THR TYR LEU GLY
SEQRES 14 C 315 ASP GLN TRP SER VAL GLY ASP TRP GLU GLY PHE CYS ARG
SEQRES 15 C 315 ALA ALA GLY ALA SER ALA SER PRO MET ALA ARG SER PHE
SEQRES 16 C 315 VAL ALA ASP GLY ILE PRO GLN HIS LEU GLN GLU TYR ASP
SEQRES 17 C 315 PRO GLU TRP ALA ARG VAL PHE TYR GLU GLY THR VAL GLY
SEQRES 18 C 315 LEU SER CYS PRO HIS GLU ARG MET LEU GLY GLN VAL LYS
SEQRES 19 C 315 THR PRO VAL LEU LEU THR HIS HIS MET ARG GLY ILE ASP
SEQRES 20 C 315 PRO GLU THR GLY ASN LEU LEU GLY ALA LEU SER ASP GLU
SEQRES 21 C 315 GLN ALA LEU ARG ALA ARG ARG LEU MET ASP SER ALA GLY
SEQRES 22 C 315 VAL THR VAL ASP TYR GLU SER VAL PRO ASP ALA SER HIS
SEQRES 23 C 315 MET MET HIS GLN SER ALA PRO ALA ARG TYR VAL GLU ILE
SEQRES 24 C 315 PHE THR ARG TRP ALA ALA ALA LEU ALA PRO HIS HIS HIS
SEQRES 25 C 315 HIS HIS HIS
SEQRES 1 D 315 MET VAL THR SER PRO ALA LEU ARG ASP VAL HIS VAL PRO
SEQRES 2 D 315 HIS ALA TYR PRO GLU GLN GLN VAL ASP LEU GLY GLU ILE
SEQRES 3 D 315 THR MET ASN TYR ALA GLU ALA GLY ASP PRO ASP ARG PRO
SEQRES 4 D 315 ALA VAL LEU LEU ILE PRO GLU GLN THR GLY SER TRP TRP
SEQRES 5 D 315 SER TYR GLU GLU ALA MET GLY LEU LEU SER GLU HIS PHE
SEQRES 6 D 315 HIS VAL TYR ALA VAL ASP LEU ARG GLY GLN GLY ARG SER
SEQRES 7 D 315 SER TRP THR PRO LYS ARG TYR SER LEU ASP ASN PHE GLY
SEQRES 8 D 315 ASN ASP LEU VAL ARG PHE ILE ALA LEU VAL VAL LYS ARG
SEQRES 9 D 315 PRO VAL VAL VAL ALA GLY ASN SER SER GLY GLY VAL LEU
SEQRES 10 D 315 ALA ALA TRP LEU SER ALA TYR SER MET PRO GLY GLN LEU
SEQRES 11 D 315 ARG GLY VAL LEU CYS GLU ASP PRO PRO PHE PHE ALA SER
SEQRES 12 D 315 GLU LEU VAL PRO ALA HIS GLY HIS SER VAL ARG GLN GLY
SEQRES 13 D 315 ALA GLY PRO VAL PHE GLU LEU PHE ARG THR TYR LEU GLY
SEQRES 14 D 315 ASP GLN TRP SER VAL GLY ASP TRP GLU GLY PHE CYS ARG
SEQRES 15 D 315 ALA ALA GLY ALA SER ALA SER PRO MET ALA ARG SER PHE
SEQRES 16 D 315 VAL ALA ASP GLY ILE PRO GLN HIS LEU GLN GLU TYR ASP
SEQRES 17 D 315 PRO GLU TRP ALA ARG VAL PHE TYR GLU GLY THR VAL GLY
SEQRES 18 D 315 LEU SER CYS PRO HIS GLU ARG MET LEU GLY GLN VAL LYS
SEQRES 19 D 315 THR PRO VAL LEU LEU THR HIS HIS MET ARG GLY ILE ASP
SEQRES 20 D 315 PRO GLU THR GLY ASN LEU LEU GLY ALA LEU SER ASP GLU
SEQRES 21 D 315 GLN ALA LEU ARG ALA ARG ARG LEU MET ASP SER ALA GLY
SEQRES 22 D 315 VAL THR VAL ASP TYR GLU SER VAL PRO ASP ALA SER HIS
SEQRES 23 D 315 MET MET HIS GLN SER ALA PRO ALA ARG TYR VAL GLU ILE
SEQRES 24 D 315 PHE THR ARG TRP ALA ALA ALA LEU ALA PRO HIS HIS HIS
SEQRES 25 D 315 HIS HIS HIS
FORMUL 5 HOH *38(H2 O)
HELIX 1 AA1 SER A 50 SER A 53 5 4
HELIX 2 AA2 TYR A 54 GLU A 63 1 10
HELIX 3 AA3 SER A 86 VAL A 101 1 16
HELIX 4 AA4 SER A 112 SER A 125 1 14
HELIX 5 AA5 SER A 152 GLY A 156 5 5
HELIX 6 AA6 ALA A 157 LEU A 168 1 12
HELIX 7 AA7 GLY A 169 SER A 173 5 5
HELIX 8 AA8 ASP A 176 ALA A 186 1 11
HELIX 9 AA9 SER A 189 PHE A 195 1 7
HELIX 10 AB1 PRO A 201 GLU A 206 1 6
HELIX 11 AB2 PRO A 209 GLU A 217 1 9
HELIX 12 AB3 PRO A 225 GLN A 232 1 8
HELIX 13 AB4 SER A 258 ALA A 272 1 15
HELIX 14 AB5 MET A 287 ALA A 292 1 6
HELIX 15 AB6 ALA A 292 LEU A 307 1 16
HELIX 16 AB7 SER B 50 SER B 53 5 4
HELIX 17 AB8 TYR B 54 SER B 62 1 9
HELIX 18 AB9 SER B 86 VAL B 101 1 16
HELIX 19 AC1 SER B 112 SER B 125 1 14
HELIX 20 AC2 SER B 152 GLY B 156 5 5
HELIX 21 AC3 ALA B 157 LEU B 168 1 12
HELIX 22 AC4 GLY B 169 SER B 173 5 5
HELIX 23 AC5 ASP B 176 ALA B 186 1 11
HELIX 24 AC6 SER B 189 PHE B 195 1 7
HELIX 25 AC7 PRO B 201 GLU B 206 1 6
HELIX 26 AC8 PRO B 209 GLU B 217 1 9
HELIX 27 AC9 PRO B 225 GLN B 232 1 8
HELIX 28 AD1 SER B 258 ALA B 272 1 15
HELIX 29 AD2 MET B 287 ALA B 292 1 6
HELIX 30 AD3 ALA B 292 ALA B 306 1 15
HELIX 31 AD4 SER C 50 SER C 53 5 4
HELIX 32 AD5 TYR C 54 SER C 62 1 9
HELIX 33 AD6 SER C 86 VAL C 101 1 16
HELIX 34 AD7 SER C 112 SER C 125 1 14
HELIX 35 AD8 SER C 152 GLY C 156 5 5
HELIX 36 AD9 ALA C 157 LEU C 168 1 12
HELIX 37 AE1 GLY C 169 SER C 173 5 5
HELIX 38 AE2 ASP C 176 ALA C 186 1 11
HELIX 39 AE3 SER C 189 PHE C 195 1 7
HELIX 40 AE4 PRO C 201 GLU C 206 1 6
HELIX 41 AE5 PRO C 209 GLU C 217 1 9
HELIX 42 AE6 PRO C 225 GLN C 232 1 8
HELIX 43 AE7 SER C 258 ALA C 272 1 15
HELIX 44 AE8 MET C 287 ALA C 292 1 6
HELIX 45 AE9 ALA C 292 ALA C 305 1 14
HELIX 46 AF1 SER D 50 SER D 53 5 4
HELIX 47 AF2 TYR D 54 GLU D 63 1 10
HELIX 48 AF3 SER D 86 VAL D 101 1 16
HELIX 49 AF4 SER D 112 SER D 125 1 14
HELIX 50 AF5 SER D 152 GLY D 156 5 5
HELIX 51 AF6 ALA D 157 LEU D 168 1 12
HELIX 52 AF7 GLY D 169 SER D 173 5 5
HELIX 53 AF8 ASP D 176 ALA D 186 1 11
HELIX 54 AF9 SER D 189 PHE D 195 1 7
HELIX 55 AG1 PRO D 201 GLU D 206 1 6
HELIX 56 AG2 PRO D 209 GLU D 217 1 9
HELIX 57 AG3 PRO D 225 GLN D 232 1 8
HELIX 58 AG4 SER D 258 ALA D 272 1 15
HELIX 59 AG5 MET D 287 ALA D 292 1 6
HELIX 60 AG6 ALA D 292 ALA D 306 1 15
SHEET 1 AA1 8 GLU A 18 ASP A 22 0
SHEET 2 AA1 8 THR A 27 ALA A 33 -1 O MET A 28 N VAL A 21
SHEET 3 AA1 8 HIS A 66 VAL A 70 -1 O VAL A 67 N ALA A 33
SHEET 4 AA1 8 ALA A 40 ILE A 44 1 N VAL A 41 O TYR A 68
SHEET 5 AA1 8 VAL A 106 ASN A 111 1 O ALA A 109 N LEU A 42
SHEET 6 AA1 8 LEU A 130 GLU A 136 1 O GLU A 136 N GLY A 110
SHEET 7 AA1 8 VAL A 237 HIS A 241 1 O LEU A 238 N CYS A 135
SHEET 8 AA1 8 VAL A 276 SER A 280 1 O ASP A 277 N LEU A 239
SHEET 1 AA2 2 GLY A 245 ILE A 246 0
SHEET 2 AA2 2 LEU A 253 LEU A 254 -1 O LEU A 254 N GLY A 245
SHEET 1 AA3 8 GLN B 19 ASP B 22 0
SHEET 2 AA3 8 THR B 27 ALA B 33 -1 O TYR B 30 N GLN B 19
SHEET 3 AA3 8 HIS B 66 VAL B 70 -1 O VAL B 67 N ALA B 33
SHEET 4 AA3 8 ALA B 40 ILE B 44 1 N LEU B 43 O TYR B 68
SHEET 5 AA3 8 VAL B 106 ASN B 111 1 O ALA B 109 N LEU B 42
SHEET 6 AA3 8 LEU B 130 GLU B 136 1 O LEU B 134 N VAL B 108
SHEET 7 AA3 8 VAL B 237 HIS B 241 1 O LEU B 238 N CYS B 135
SHEET 8 AA3 8 VAL B 276 SER B 280 1 O GLU B 279 N LEU B 239
SHEET 1 AA4 2 ARG B 244 ILE B 246 0
SHEET 2 AA4 2 LEU B 253 GLY B 255 -1 O LEU B 254 N GLY B 245
SHEET 1 AA5 8 GLU C 18 ASP C 22 0
SHEET 2 AA5 8 THR C 27 ALA C 33 -1 O TYR C 30 N GLN C 19
SHEET 3 AA5 8 HIS C 66 VAL C 70 -1 O VAL C 67 N ALA C 33
SHEET 4 AA5 8 ALA C 40 ILE C 44 1 N LEU C 43 O TYR C 68
SHEET 5 AA5 8 VAL C 106 ASN C 111 1 O ALA C 109 N ILE C 44
SHEET 6 AA5 8 LEU C 130 GLU C 136 1 O GLU C 136 N GLY C 110
SHEET 7 AA5 8 VAL C 237 HIS C 241 1 O LEU C 238 N CYS C 135
SHEET 8 AA5 8 VAL C 276 SER C 280 1 O ASP C 277 N LEU C 239
SHEET 1 AA6 2 ARG C 244 ILE C 246 0
SHEET 2 AA6 2 LEU C 253 GLY C 255 -1 O LEU C 254 N GLY C 245
SHEET 1 AA7 8 GLU D 18 ASP D 22 0
SHEET 2 AA7 8 THR D 27 ALA D 33 -1 O MET D 28 N VAL D 21
SHEET 3 AA7 8 HIS D 66 VAL D 70 -1 O ALA D 69 N ALA D 31
SHEET 4 AA7 8 ALA D 40 ILE D 44 1 N VAL D 41 O HIS D 66
SHEET 5 AA7 8 VAL D 106 ASN D 111 1 O ALA D 109 N LEU D 42
SHEET 6 AA7 8 LEU D 130 GLU D 136 1 O GLU D 136 N GLY D 110
SHEET 7 AA7 8 VAL D 237 HIS D 241 1 O LEU D 238 N CYS D 135
SHEET 8 AA7 8 VAL D 276 SER D 280 1 O GLU D 279 N LEU D 239
SHEET 1 AA8 2 GLY D 245 ILE D 246 0
SHEET 2 AA8 2 LEU D 253 LEU D 254 -1 O LEU D 254 N GLY D 245
CRYST1 75.386 75.386 404.619 90.00 90.00 120.00 P 31 2 1 24
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 0.013265 0.007659 0.000000 0.00000
SCALE2 0.000000 0.015317 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002471 0.00000
TER 4639 LEU A 307
TER 9255 ALA B 308
TER 13794 LEU C 307
TER 18344 ALA D 308
MASTER 402 0 0 60 40 0 0 6 9411 4 0 100
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