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HEADER HYDROLASE 25-SEP-23 8QMZ
TITLE SOLUBLE EPOXIDE HYDROLASE IN COMPLEX WITH RK4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BIFUNCTIONAL EPOXIDE HYDROLASE 2;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 3.3.2.10,3.1.3.76;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: EPHX2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS COMPLEX, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.KUMAR,F.ZHU,J.M.H.EHRLER,F.LI,C.EMPEL,Y.XU,I.ATODIRESEI,
AUTHOR 2 R.M.KOENIGS,E.PROSCHAK,S.KNAPP,STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 1 14-FEB-24 8QMZ 0
JRNL AUTH F.LI,W.F.ZHU,C.EMPEL,O.DATSENKO,A.KUMAR,Y.XU,J.H.M.EHRLER,
JRNL AUTH 2 I.ATODIRESEI,S.KNAPP,P.K.MYKHAILIUK,E.PROSCHAK,R.M.KOENIGS
JRNL TITL PHOTOSENSITIZATION ENABLES PAUSON-KHAND-TYPE REACTIONS WITH
JRNL TITL 2 NITRENES.
JRNL REF SCIENCE V. 383 498 2024
JRNL REFN ESSN 1095-9203
JRNL PMID 38301027
JRNL DOI 10.1126/SCIENCE.ADM8095
REMARK 2
REMARK 2 RESOLUTION. 1.47 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0419
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.47
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.47
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 221479
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 11504
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.47
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.51
REMARK 3 REFLECTION IN BIN (WORKING SET) : 15363
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.11
REMARK 3 BIN R VALUE (WORKING SET) : 0.3050
REMARK 3 BIN FREE R VALUE SET COUNT : 780
REMARK 3 BIN FREE R VALUE : 0.3310
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10206
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 184
REMARK 3 SOLVENT ATOMS : 841
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.38
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.14000
REMARK 3 B22 (A**2) : 0.69000
REMARK 3 B33 (A**2) : 0.45000
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.072
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.073
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.055
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.509
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.970
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.962
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 11079 ; 0.011 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): 10116 ; 0.001 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 15098 ; 1.787 ; 1.657
REMARK 3 BOND ANGLES OTHERS (DEGREES): 23415 ; 0.630 ; 1.576
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1363 ; 6.709 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 62 ; 6.632 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1800 ;15.687 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1561 ; 0.111 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 13190 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2594 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 5329 ; 2.044 ; 2.092
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 5329 ; 2.043 ; 2.092
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6730 ; 2.874 ; 3.759
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 6731 ; 2.874 ; 3.760
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5750 ; 3.210 ; 2.413
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 5751 ; 3.209 ; 2.413
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 8368 ; 4.800 ; 4.305
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 12691 ; 5.938 ;22.180
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 12692 ; 5.938 ;22.180
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 8QMZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-SEP-23.
REMARK 100 THE DEPOSITION ID IS D_1292133499.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-SEP-23
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 233100
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.470
REMARK 200 RESOLUTION RANGE LOW (A) : 49.470
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.47
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.49
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 6.90
REMARK 200 R MERGE FOR SHELL (I) : 1.12500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG6000, 10% ETHYLENE GLYCOL, 0.1M
REMARK 280 HEPES PH 7.0, 0.1M CALCIUM CHLORIDE, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 40.14500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 94.20800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.32100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 94.20800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 40.14500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.32100
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 198
REMARK 465 GLY A 199
REMARK 465 SER A 200
REMARK 465 SER A 201
REMARK 465 HIS A 202
REMARK 465 HIS A 203
REMARK 465 HIS A 204
REMARK 465 HIS A 205
REMARK 465 HIS A 206
REMARK 465 HIS A 207
REMARK 465 SER A 208
REMARK 465 SER A 209
REMARK 465 GLY A 210
REMARK 465 LEU A 211
REMARK 465 VAL A 212
REMARK 465 PRO A 213
REMARK 465 ARG A 214
REMARK 465 GLY A 215
REMARK 465 SER A 216
REMARK 465 HIS A 217
REMARK 465 MET A 218
REMARK 465 ALA A 219
REMARK 465 SER A 220
REMARK 465 MET A 221
REMARK 465 LEU A 222
REMARK 465 ASN A 223
REMARK 465 THR A 224
REMARK 465 PRO A 225
REMARK 465 ALA A 226
REMARK 465 PRO A 227
REMARK 465 ASN A 548
REMARK 465 PRO A 549
REMARK 465 PRO A 550
REMARK 465 VAL A 551
REMARK 465 VAL A 552
REMARK 465 SER A 553
REMARK 465 LYS A 554
REMARK 465 MET A 555
REMARK 465 LEU A 556
REMARK 465 LEU A 557
REMARK 465 GLU A 558
REMARK 465 HIS A 559
REMARK 465 HIS A 560
REMARK 465 HIS A 561
REMARK 465 HIS A 562
REMARK 465 HIS A 563
REMARK 465 HIS A 564
REMARK 465 MET B 198
REMARK 465 GLY B 199
REMARK 465 SER B 200
REMARK 465 SER B 201
REMARK 465 HIS B 202
REMARK 465 HIS B 203
REMARK 465 HIS B 204
REMARK 465 HIS B 205
REMARK 465 HIS B 206
REMARK 465 HIS B 207
REMARK 465 SER B 208
REMARK 465 SER B 209
REMARK 465 GLY B 210
REMARK 465 LEU B 211
REMARK 465 VAL B 212
REMARK 465 PRO B 213
REMARK 465 ARG B 214
REMARK 465 GLY B 215
REMARK 465 SER B 216
REMARK 465 HIS B 217
REMARK 465 MET B 218
REMARK 465 ALA B 219
REMARK 465 SER B 220
REMARK 465 MET B 221
REMARK 465 LEU B 222
REMARK 465 ASN B 223
REMARK 465 THR B 224
REMARK 465 PRO B 225
REMARK 465 ALA B 226
REMARK 465 PRO B 227
REMARK 465 ALA B 546
REMARK 465 ARG B 547
REMARK 465 ASN B 548
REMARK 465 PRO B 549
REMARK 465 PRO B 550
REMARK 465 VAL B 551
REMARK 465 VAL B 552
REMARK 465 SER B 553
REMARK 465 LYS B 554
REMARK 465 MET B 555
REMARK 465 LEU B 556
REMARK 465 LEU B 557
REMARK 465 GLU B 558
REMARK 465 HIS B 559
REMARK 465 HIS B 560
REMARK 465 HIS B 561
REMARK 465 HIS B 562
REMARK 465 HIS B 563
REMARK 465 HIS B 564
REMARK 465 MET C 198
REMARK 465 GLY C 199
REMARK 465 SER C 200
REMARK 465 SER C 201
REMARK 465 HIS C 202
REMARK 465 HIS C 203
REMARK 465 HIS C 204
REMARK 465 HIS C 205
REMARK 465 HIS C 206
REMARK 465 HIS C 207
REMARK 465 SER C 208
REMARK 465 SER C 209
REMARK 465 GLY C 210
REMARK 465 LEU C 211
REMARK 465 VAL C 212
REMARK 465 PRO C 213
REMARK 465 ARG C 214
REMARK 465 GLY C 215
REMARK 465 SER C 216
REMARK 465 HIS C 217
REMARK 465 MET C 218
REMARK 465 ALA C 219
REMARK 465 SER C 220
REMARK 465 MET C 221
REMARK 465 LEU C 222
REMARK 465 ASN C 223
REMARK 465 THR C 224
REMARK 465 PRO C 225
REMARK 465 ALA C 226
REMARK 465 PRO C 227
REMARK 465 ASN C 548
REMARK 465 PRO C 549
REMARK 465 PRO C 550
REMARK 465 VAL C 551
REMARK 465 VAL C 552
REMARK 465 SER C 553
REMARK 465 LYS C 554
REMARK 465 MET C 555
REMARK 465 LEU C 556
REMARK 465 LEU C 557
REMARK 465 GLU C 558
REMARK 465 HIS C 559
REMARK 465 HIS C 560
REMARK 465 HIS C 561
REMARK 465 HIS C 562
REMARK 465 HIS C 563
REMARK 465 HIS C 564
REMARK 465 MET D 198
REMARK 465 GLY D 199
REMARK 465 SER D 200
REMARK 465 SER D 201
REMARK 465 HIS D 202
REMARK 465 HIS D 203
REMARK 465 HIS D 204
REMARK 465 HIS D 205
REMARK 465 HIS D 206
REMARK 465 HIS D 207
REMARK 465 SER D 208
REMARK 465 SER D 209
REMARK 465 GLY D 210
REMARK 465 LEU D 211
REMARK 465 VAL D 212
REMARK 465 PRO D 213
REMARK 465 ARG D 214
REMARK 465 GLY D 215
REMARK 465 SER D 216
REMARK 465 HIS D 217
REMARK 465 MET D 218
REMARK 465 ALA D 219
REMARK 465 SER D 220
REMARK 465 MET D 221
REMARK 465 LEU D 222
REMARK 465 ASN D 223
REMARK 465 THR D 224
REMARK 465 PRO D 225
REMARK 465 ALA D 226
REMARK 465 PRO D 227
REMARK 465 ASN D 548
REMARK 465 PRO D 549
REMARK 465 PRO D 550
REMARK 465 VAL D 551
REMARK 465 VAL D 552
REMARK 465 SER D 553
REMARK 465 LYS D 554
REMARK 465 MET D 555
REMARK 465 LEU D 556
REMARK 465 LEU D 557
REMARK 465 GLU D 558
REMARK 465 HIS D 559
REMARK 465 HIS D 560
REMARK 465 HIS D 561
REMARK 465 HIS D 562
REMARK 465 HIS D 563
REMARK 465 HIS D 564
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 ARG A 247 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 283 CG CD OE1 NE2
REMARK 470 LYS A 315 CG CD CE NZ
REMARK 470 LYS A 376 CG CD CE NZ
REMARK 470 HIS A 420 CG ND1 CD2 CE1 NE2
REMARK 470 GLU A 424 CG CD OE1 OE2
REMARK 470 GLU A 434 CG CD OE1 OE2
REMARK 470 GLU A 470 CG CD OE1 OE2
REMARK 470 GLN B 283 CG CD OE1 NE2
REMARK 470 LYS B 376 CG CD CE NZ
REMARK 470 ASN B 378 CG OD1 ND2
REMARK 470 GLU B 424 CG CD OE1 OE2
REMARK 470 GLN C 283 CG CD OE1 NE2
REMARK 470 LYS C 376 CG CD CE NZ
REMARK 470 ASN C 378 CG OD1 ND2
REMARK 470 VAL C 380 CG1 CG2
REMARK 470 GLU C 424 CG CD OE1 OE2
REMARK 470 GLN D 283 CG CD OE1 NE2
REMARK 470 LYS D 315 CE NZ
REMARK 470 LYS D 376 CG CD CE NZ
REMARK 470 SER D 418 OG
REMARK 470 LYS D 421 CG CD CE NZ
REMARK 470 GLU D 424 CG CD OE1 OE2
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 OD2 ASP D 382 O HOH D 701 1.96
REMARK 500 O1 EDO D 604 O HOH D 702 1.98
REMARK 500 O SER D 544 O HOH D 703 2.10
REMARK 500 O1 EDO C 603 O HOH C 701 2.14
REMARK 500 CB LYS B 376 O HOH B 899 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 494 CD GLU A 494 OE2 0.072
REMARK 500 LEU C 228 CA LEU C 228 CB 0.633
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG B 249 NE - CZ - NH1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG B 249 NE - CZ - NH2 ANGL. DEV. = 3.6 DEGREES
REMARK 500 LEU C 228 CB - CA - C ANGL. DEV. = -18.4 DEGREES
REMARK 500 LEU C 228 N - CA - CB ANGL. DEV. = 41.6 DEGREES
REMARK 500 ARG C 482 CB - CA - C ANGL. DEV. = 13.8 DEGREES
REMARK 500 HIS C 513 CA - CB - CG ANGL. DEV. = -13.0 DEGREES
REMARK 500 ARG D 516 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 231 -168.74 -104.50
REMARK 500 GLU A 269 -150.87 -120.55
REMARK 500 ASP A 335 -126.98 61.43
REMARK 500 ASN A 359 -41.10 78.56
REMARK 500 PRO A 379 38.21 -85.00
REMARK 500 ASN A 400 88.18 -154.33
REMARK 500 HIS A 506 6.08 80.33
REMARK 500 HIS A 506 6.21 80.33
REMARK 500 HIS A 513 43.91 -91.45
REMARK 500 SER B 231 -166.26 -107.78
REMARK 500 GLU B 269 -146.44 -121.42
REMARK 500 ASP B 335 -132.45 59.64
REMARK 500 ASN B 359 -44.63 78.59
REMARK 500 ASN B 378 89.02 -154.62
REMARK 500 PRO B 379 37.71 -80.95
REMARK 500 HIS B 513 37.02 -97.85
REMARK 500 SER C 231 -166.87 -107.12
REMARK 500 GLU C 269 -145.70 -121.47
REMARK 500 ASP C 335 -134.52 65.17
REMARK 500 ASN C 359 -42.55 79.95
REMARK 500 PRO C 379 33.44 -89.49
REMARK 500 SER D 231 -167.74 -106.71
REMARK 500 GLU D 269 -139.93 -118.11
REMARK 500 ASP D 335 -134.75 63.88
REMARK 500 ASN D 359 -42.29 82.50
REMARK 500 ASN D 378 84.93 -160.46
REMARK 500 PRO D 379 25.96 -70.52
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 MET A 291 ASP A 292 145.89
REMARK 500 MET B 291 ASP B 292 142.60
REMARK 500 SER B 479 LEU B 480 -148.88
REMARK 500 MET C 291 ASP C 292 145.12
REMARK 500 MET D 291 ASP D 292 142.11
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 B 353 0.08 SIDE CHAIN
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 915 DISTANCE = 6.34 ANGSTROMS
DBREF 8QMZ A 222 555 UNP P34913 HYES_HUMAN 222 555
DBREF 8QMZ B 222 555 UNP P34913 HYES_HUMAN 222 555
DBREF 8QMZ C 222 555 UNP P34913 HYES_HUMAN 222 555
DBREF 8QMZ D 222 555 UNP P34913 HYES_HUMAN 222 555
SEQADV 8QMZ MET A 198 UNP P34913 INITIATING METHIONINE
SEQADV 8QMZ GLY A 199 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ SER A 200 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ SER A 201 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS A 202 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS A 203 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS A 204 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS A 205 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS A 206 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS A 207 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ SER A 208 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ SER A 209 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ GLY A 210 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ LEU A 211 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ VAL A 212 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ PRO A 213 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ ARG A 214 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ GLY A 215 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ SER A 216 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS A 217 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ MET A 218 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ ALA A 219 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ SER A 220 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ MET A 221 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ LEU A 556 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ LEU A 557 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ GLU A 558 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS A 559 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS A 560 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS A 561 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS A 562 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS A 563 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS A 564 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ MET B 198 UNP P34913 INITIATING METHIONINE
SEQADV 8QMZ GLY B 199 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ SER B 200 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ SER B 201 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS B 202 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS B 203 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS B 204 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS B 205 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS B 206 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS B 207 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ SER B 208 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ SER B 209 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ GLY B 210 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ LEU B 211 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ VAL B 212 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ PRO B 213 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ ARG B 214 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ GLY B 215 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ SER B 216 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS B 217 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ MET B 218 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ ALA B 219 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ SER B 220 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ MET B 221 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ LEU B 556 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ LEU B 557 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ GLU B 558 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS B 559 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS B 560 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS B 561 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS B 562 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS B 563 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS B 564 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ MET C 198 UNP P34913 INITIATING METHIONINE
SEQADV 8QMZ GLY C 199 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ SER C 200 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ SER C 201 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS C 202 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS C 203 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS C 204 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS C 205 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS C 206 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS C 207 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ SER C 208 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ SER C 209 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ GLY C 210 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ LEU C 211 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ VAL C 212 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ PRO C 213 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ ARG C 214 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ GLY C 215 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ SER C 216 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS C 217 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ MET C 218 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ ALA C 219 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ SER C 220 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ MET C 221 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ LEU C 556 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ LEU C 557 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ GLU C 558 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS C 559 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS C 560 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS C 561 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS C 562 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS C 563 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS C 564 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ MET D 198 UNP P34913 INITIATING METHIONINE
SEQADV 8QMZ GLY D 199 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ SER D 200 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ SER D 201 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS D 202 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS D 203 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS D 204 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS D 205 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS D 206 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS D 207 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ SER D 208 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ SER D 209 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ GLY D 210 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ LEU D 211 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ VAL D 212 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ PRO D 213 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ ARG D 214 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ GLY D 215 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ SER D 216 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS D 217 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ MET D 218 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ ALA D 219 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ SER D 220 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ MET D 221 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ LEU D 556 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ LEU D 557 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ GLU D 558 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS D 559 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS D 560 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS D 561 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS D 562 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS D 563 UNP P34913 EXPRESSION TAG
SEQADV 8QMZ HIS D 564 UNP P34913 EXPRESSION TAG
SEQRES 1 A 367 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 367 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET LEU ASN
SEQRES 3 A 367 THR PRO ALA PRO LEU PRO THR SER CYS ASN PRO SER ASP
SEQRES 4 A 367 MET SER HIS GLY TYR VAL THR VAL LYS PRO ARG VAL ARG
SEQRES 5 A 367 LEU HIS PHE VAL GLU LEU GLY SER GLY PRO ALA VAL CYS
SEQRES 6 A 367 LEU CYS HIS GLY PHE PRO GLU SER TRP TYR SER TRP ARG
SEQRES 7 A 367 TYR GLN ILE PRO ALA LEU ALA GLN ALA GLY TYR ARG VAL
SEQRES 8 A 367 LEU ALA MET ASP MET LYS GLY TYR GLY GLU SER SER ALA
SEQRES 9 A 367 PRO PRO GLU ILE GLU GLU TYR CYS MET GLU VAL LEU CYS
SEQRES 10 A 367 LYS GLU MET VAL THR PHE LEU ASP LYS LEU GLY LEU SER
SEQRES 11 A 367 GLN ALA VAL PHE ILE GLY HIS ASP TRP GLY GLY MET LEU
SEQRES 12 A 367 VAL TRP TYR MET ALA LEU PHE TYR PRO GLU ARG VAL ARG
SEQRES 13 A 367 ALA VAL ALA SER LEU ASN THR PRO PHE ILE PRO ALA ASN
SEQRES 14 A 367 PRO ASN MET SER PRO LEU GLU SER ILE LYS ALA ASN PRO
SEQRES 15 A 367 VAL PHE ASP TYR GLN LEU TYR PHE GLN GLU PRO GLY VAL
SEQRES 16 A 367 ALA GLU ALA GLU LEU GLU GLN ASN LEU SER ARG THR PHE
SEQRES 17 A 367 LYS SER LEU PHE ARG ALA SER ASP GLU SER VAL LEU SER
SEQRES 18 A 367 MET HIS LYS VAL CYS GLU ALA GLY GLY LEU PHE VAL ASN
SEQRES 19 A 367 SER PRO GLU GLU PRO SER LEU SER ARG MET VAL THR GLU
SEQRES 20 A 367 GLU GLU ILE GLN PHE TYR VAL GLN GLN PHE LYS LYS SER
SEQRES 21 A 367 GLY PHE ARG GLY PRO LEU ASN TRP TYR ARG ASN MET GLU
SEQRES 22 A 367 ARG ASN TRP LYS TRP ALA CYS LYS SER LEU GLY ARG LYS
SEQRES 23 A 367 ILE LEU ILE PRO ALA LEU MET VAL THR ALA GLU LYS ASP
SEQRES 24 A 367 PHE VAL LEU VAL PRO GLN MET SER GLN HIS MET GLU ASP
SEQRES 25 A 367 TRP ILE PRO HIS LEU LYS ARG GLY HIS ILE GLU ASP CYS
SEQRES 26 A 367 GLY HIS TRP THR GLN MET ASP LYS PRO THR GLU VAL ASN
SEQRES 27 A 367 GLN ILE LEU ILE LYS TRP LEU ASP SER ASP ALA ARG ASN
SEQRES 28 A 367 PRO PRO VAL VAL SER LYS MET LEU LEU GLU HIS HIS HIS
SEQRES 29 A 367 HIS HIS HIS
SEQRES 1 B 367 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 367 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET LEU ASN
SEQRES 3 B 367 THR PRO ALA PRO LEU PRO THR SER CYS ASN PRO SER ASP
SEQRES 4 B 367 MET SER HIS GLY TYR VAL THR VAL LYS PRO ARG VAL ARG
SEQRES 5 B 367 LEU HIS PHE VAL GLU LEU GLY SER GLY PRO ALA VAL CYS
SEQRES 6 B 367 LEU CYS HIS GLY PHE PRO GLU SER TRP TYR SER TRP ARG
SEQRES 7 B 367 TYR GLN ILE PRO ALA LEU ALA GLN ALA GLY TYR ARG VAL
SEQRES 8 B 367 LEU ALA MET ASP MET LYS GLY TYR GLY GLU SER SER ALA
SEQRES 9 B 367 PRO PRO GLU ILE GLU GLU TYR CYS MET GLU VAL LEU CYS
SEQRES 10 B 367 LYS GLU MET VAL THR PHE LEU ASP LYS LEU GLY LEU SER
SEQRES 11 B 367 GLN ALA VAL PHE ILE GLY HIS ASP TRP GLY GLY MET LEU
SEQRES 12 B 367 VAL TRP TYR MET ALA LEU PHE TYR PRO GLU ARG VAL ARG
SEQRES 13 B 367 ALA VAL ALA SER LEU ASN THR PRO PHE ILE PRO ALA ASN
SEQRES 14 B 367 PRO ASN MET SER PRO LEU GLU SER ILE LYS ALA ASN PRO
SEQRES 15 B 367 VAL PHE ASP TYR GLN LEU TYR PHE GLN GLU PRO GLY VAL
SEQRES 16 B 367 ALA GLU ALA GLU LEU GLU GLN ASN LEU SER ARG THR PHE
SEQRES 17 B 367 LYS SER LEU PHE ARG ALA SER ASP GLU SER VAL LEU SER
SEQRES 18 B 367 MET HIS LYS VAL CYS GLU ALA GLY GLY LEU PHE VAL ASN
SEQRES 19 B 367 SER PRO GLU GLU PRO SER LEU SER ARG MET VAL THR GLU
SEQRES 20 B 367 GLU GLU ILE GLN PHE TYR VAL GLN GLN PHE LYS LYS SER
SEQRES 21 B 367 GLY PHE ARG GLY PRO LEU ASN TRP TYR ARG ASN MET GLU
SEQRES 22 B 367 ARG ASN TRP LYS TRP ALA CYS LYS SER LEU GLY ARG LYS
SEQRES 23 B 367 ILE LEU ILE PRO ALA LEU MET VAL THR ALA GLU LYS ASP
SEQRES 24 B 367 PHE VAL LEU VAL PRO GLN MET SER GLN HIS MET GLU ASP
SEQRES 25 B 367 TRP ILE PRO HIS LEU LYS ARG GLY HIS ILE GLU ASP CYS
SEQRES 26 B 367 GLY HIS TRP THR GLN MET ASP LYS PRO THR GLU VAL ASN
SEQRES 27 B 367 GLN ILE LEU ILE LYS TRP LEU ASP SER ASP ALA ARG ASN
SEQRES 28 B 367 PRO PRO VAL VAL SER LYS MET LEU LEU GLU HIS HIS HIS
SEQRES 29 B 367 HIS HIS HIS
SEQRES 1 C 367 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 367 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET LEU ASN
SEQRES 3 C 367 THR PRO ALA PRO LEU PRO THR SER CYS ASN PRO SER ASP
SEQRES 4 C 367 MET SER HIS GLY TYR VAL THR VAL LYS PRO ARG VAL ARG
SEQRES 5 C 367 LEU HIS PHE VAL GLU LEU GLY SER GLY PRO ALA VAL CYS
SEQRES 6 C 367 LEU CYS HIS GLY PHE PRO GLU SER TRP TYR SER TRP ARG
SEQRES 7 C 367 TYR GLN ILE PRO ALA LEU ALA GLN ALA GLY TYR ARG VAL
SEQRES 8 C 367 LEU ALA MET ASP MET LYS GLY TYR GLY GLU SER SER ALA
SEQRES 9 C 367 PRO PRO GLU ILE GLU GLU TYR CYS MET GLU VAL LEU CYS
SEQRES 10 C 367 LYS GLU MET VAL THR PHE LEU ASP LYS LEU GLY LEU SER
SEQRES 11 C 367 GLN ALA VAL PHE ILE GLY HIS ASP TRP GLY GLY MET LEU
SEQRES 12 C 367 VAL TRP TYR MET ALA LEU PHE TYR PRO GLU ARG VAL ARG
SEQRES 13 C 367 ALA VAL ALA SER LEU ASN THR PRO PHE ILE PRO ALA ASN
SEQRES 14 C 367 PRO ASN MET SER PRO LEU GLU SER ILE LYS ALA ASN PRO
SEQRES 15 C 367 VAL PHE ASP TYR GLN LEU TYR PHE GLN GLU PRO GLY VAL
SEQRES 16 C 367 ALA GLU ALA GLU LEU GLU GLN ASN LEU SER ARG THR PHE
SEQRES 17 C 367 LYS SER LEU PHE ARG ALA SER ASP GLU SER VAL LEU SER
SEQRES 18 C 367 MET HIS LYS VAL CYS GLU ALA GLY GLY LEU PHE VAL ASN
SEQRES 19 C 367 SER PRO GLU GLU PRO SER LEU SER ARG MET VAL THR GLU
SEQRES 20 C 367 GLU GLU ILE GLN PHE TYR VAL GLN GLN PHE LYS LYS SER
SEQRES 21 C 367 GLY PHE ARG GLY PRO LEU ASN TRP TYR ARG ASN MET GLU
SEQRES 22 C 367 ARG ASN TRP LYS TRP ALA CYS LYS SER LEU GLY ARG LYS
SEQRES 23 C 367 ILE LEU ILE PRO ALA LEU MET VAL THR ALA GLU LYS ASP
SEQRES 24 C 367 PHE VAL LEU VAL PRO GLN MET SER GLN HIS MET GLU ASP
SEQRES 25 C 367 TRP ILE PRO HIS LEU LYS ARG GLY HIS ILE GLU ASP CYS
SEQRES 26 C 367 GLY HIS TRP THR GLN MET ASP LYS PRO THR GLU VAL ASN
SEQRES 27 C 367 GLN ILE LEU ILE LYS TRP LEU ASP SER ASP ALA ARG ASN
SEQRES 28 C 367 PRO PRO VAL VAL SER LYS MET LEU LEU GLU HIS HIS HIS
SEQRES 29 C 367 HIS HIS HIS
SEQRES 1 D 367 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 367 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET LEU ASN
SEQRES 3 D 367 THR PRO ALA PRO LEU PRO THR SER CYS ASN PRO SER ASP
SEQRES 4 D 367 MET SER HIS GLY TYR VAL THR VAL LYS PRO ARG VAL ARG
SEQRES 5 D 367 LEU HIS PHE VAL GLU LEU GLY SER GLY PRO ALA VAL CYS
SEQRES 6 D 367 LEU CYS HIS GLY PHE PRO GLU SER TRP TYR SER TRP ARG
SEQRES 7 D 367 TYR GLN ILE PRO ALA LEU ALA GLN ALA GLY TYR ARG VAL
SEQRES 8 D 367 LEU ALA MET ASP MET LYS GLY TYR GLY GLU SER SER ALA
SEQRES 9 D 367 PRO PRO GLU ILE GLU GLU TYR CYS MET GLU VAL LEU CYS
SEQRES 10 D 367 LYS GLU MET VAL THR PHE LEU ASP LYS LEU GLY LEU SER
SEQRES 11 D 367 GLN ALA VAL PHE ILE GLY HIS ASP TRP GLY GLY MET LEU
SEQRES 12 D 367 VAL TRP TYR MET ALA LEU PHE TYR PRO GLU ARG VAL ARG
SEQRES 13 D 367 ALA VAL ALA SER LEU ASN THR PRO PHE ILE PRO ALA ASN
SEQRES 14 D 367 PRO ASN MET SER PRO LEU GLU SER ILE LYS ALA ASN PRO
SEQRES 15 D 367 VAL PHE ASP TYR GLN LEU TYR PHE GLN GLU PRO GLY VAL
SEQRES 16 D 367 ALA GLU ALA GLU LEU GLU GLN ASN LEU SER ARG THR PHE
SEQRES 17 D 367 LYS SER LEU PHE ARG ALA SER ASP GLU SER VAL LEU SER
SEQRES 18 D 367 MET HIS LYS VAL CYS GLU ALA GLY GLY LEU PHE VAL ASN
SEQRES 19 D 367 SER PRO GLU GLU PRO SER LEU SER ARG MET VAL THR GLU
SEQRES 20 D 367 GLU GLU ILE GLN PHE TYR VAL GLN GLN PHE LYS LYS SER
SEQRES 21 D 367 GLY PHE ARG GLY PRO LEU ASN TRP TYR ARG ASN MET GLU
SEQRES 22 D 367 ARG ASN TRP LYS TRP ALA CYS LYS SER LEU GLY ARG LYS
SEQRES 23 D 367 ILE LEU ILE PRO ALA LEU MET VAL THR ALA GLU LYS ASP
SEQRES 24 D 367 PHE VAL LEU VAL PRO GLN MET SER GLN HIS MET GLU ASP
SEQRES 25 D 367 TRP ILE PRO HIS LEU LYS ARG GLY HIS ILE GLU ASP CYS
SEQRES 26 D 367 GLY HIS TRP THR GLN MET ASP LYS PRO THR GLU VAL ASN
SEQRES 27 D 367 GLN ILE LEU ILE LYS TRP LEU ASP SER ASP ALA ARG ASN
SEQRES 28 D 367 PRO PRO VAL VAL SER LYS MET LEU LEU GLU HIS HIS HIS
SEQRES 29 D 367 HIS HIS HIS
HET W6O A 601 30
HET EDO A 602 4
HET EDO A 603 4
HET EDO A 604 4
HET EDO A 605 4
HET W6O B 601 30
HET EDO B 602 4
HET EDO B 603 4
HET EDO B 604 4
HET EDO B 605 4
HET EDO B 606 4
HET W6O C 601 30
HET EDO C 602 4
HET EDO C 603 4
HET W6O D 601 30
HET EDO D 602 4
HET EDO D 603 4
HET EDO D 604 4
HET EDO D 605 4
HET EDO D 606 4
HETNAM W6O (3~{A}~{R},6~{A}~{S})-~{N}-[(2,4-DICHLOROPHENYL)
HETNAM 2 W6O METHYL]-2-(4-METHYLPHENYL)SULFONYL-3,3~{A},4,5,6,
HETNAM 3 W6O 6~{A}-HEXAHYDRO-1~{H}-CYCLOPENTA[C]PYRROLE-5-
HETNAM 4 W6O CARBOXAMIDE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 5 W6O 4(C22 H24 CL2 N2 O3 S)
FORMUL 6 EDO 16(C2 H6 O2)
FORMUL 25 HOH *841(H2 O)
HELIX 1 AA1 ASN A 233 MET A 237 5 5
HELIX 2 AA2 SER A 270 ARG A 275 5 6
HELIX 3 AA3 TYR A 276 ALA A 284 1 9
HELIX 4 AA4 GLU A 304 TYR A 308 5 5
HELIX 5 AA5 CYS A 309 GLY A 325 1 17
HELIX 6 AA6 ASP A 335 TYR A 348 1 14
HELIX 7 AA7 SER A 370 ASN A 378 1 9
HELIX 8 AA8 PRO A 379 PHE A 381 5 3
HELIX 9 AA9 ASP A 382 PHE A 387 1 6
HELIX 10 AB1 GLY A 391 GLN A 399 1 9
HELIX 11 AB2 ASN A 400 PHE A 409 1 10
HELIX 12 AB3 ALA A 411 SER A 415 5 5
HELIX 13 AB4 SER A 418 HIS A 420 5 3
HELIX 14 AB5 LYS A 421 GLY A 426 1 6
HELIX 15 AB6 THR A 443 LYS A 456 1 14
HELIX 16 AB7 PHE A 459 TRP A 465 1 7
HELIX 17 AB8 ASN A 468 LYS A 478 1 11
HELIX 18 AB9 VAL A 500 GLN A 505 5 6
HELIX 19 AC1 HIS A 506 TRP A 510 5 5
HELIX 20 AC2 TRP A 525 LYS A 530 1 6
HELIX 21 AC3 LYS A 530 ALA A 546 1 17
HELIX 22 AC4 ASN B 233 MET B 237 5 5
HELIX 23 AC5 SER B 270 ARG B 275 5 6
HELIX 24 AC6 GLN B 277 ALA B 284 1 8
HELIX 25 AC7 GLU B 304 TYR B 308 5 5
HELIX 26 AC8 CYS B 309 GLY B 325 1 17
HELIX 27 AC9 ASP B 335 TYR B 348 1 14
HELIX 28 AD1 SER B 370 ASN B 378 1 9
HELIX 29 AD2 PRO B 379 PHE B 381 5 3
HELIX 30 AD3 ASP B 382 PHE B 387 1 6
HELIX 31 AD4 GLY B 391 ASN B 400 1 10
HELIX 32 AD5 ASN B 400 PHE B 409 1 10
HELIX 33 AD6 ALA B 411 SER B 415 5 5
HELIX 34 AD7 SER B 418 HIS B 420 5 3
HELIX 35 AD8 LYS B 421 GLY B 426 1 6
HELIX 36 AD9 THR B 443 GLY B 458 1 16
HELIX 37 AE1 PHE B 459 TRP B 465 1 7
HELIX 38 AE2 ASN B 468 LYS B 478 1 11
HELIX 39 AE3 VAL B 500 GLN B 505 5 6
HELIX 40 AE4 HIS B 506 TRP B 510 5 5
HELIX 41 AE5 TRP B 525 LYS B 530 1 6
HELIX 42 AE6 LYS B 530 ASP B 545 1 16
HELIX 43 AE7 ASN C 233 MET C 237 5 5
HELIX 44 AE8 SER C 270 ARG C 275 5 6
HELIX 45 AE9 TYR C 276 ALA C 284 1 9
HELIX 46 AF1 GLU C 304 TYR C 308 5 5
HELIX 47 AF2 CYS C 309 GLY C 325 1 17
HELIX 48 AF3 ASP C 335 TYR C 348 1 14
HELIX 49 AF4 SER C 370 ASN C 378 1 9
HELIX 50 AF5 PRO C 379 PHE C 381 5 3
HELIX 51 AF6 ASP C 382 PHE C 387 1 6
HELIX 52 AF7 GLY C 391 GLN C 399 1 9
HELIX 53 AF8 ASN C 400 PHE C 409 1 10
HELIX 54 AF9 ALA C 411 SER C 415 5 5
HELIX 55 AG1 SER C 418 HIS C 420 5 3
HELIX 56 AG2 LYS C 421 GLY C 426 1 6
HELIX 57 AG3 THR C 443 LYS C 455 1 13
HELIX 58 AG4 PHE C 459 TRP C 465 1 7
HELIX 59 AG5 ASN C 468 LYS C 478 1 11
HELIX 60 AG6 VAL C 500 GLN C 505 5 6
HELIX 61 AG7 HIS C 506 TRP C 510 5 5
HELIX 62 AG8 TRP C 525 LYS C 530 1 6
HELIX 63 AG9 LYS C 530 ALA C 546 1 17
HELIX 64 AH1 ASN D 233 MET D 237 5 5
HELIX 65 AH2 SER D 270 ARG D 275 5 6
HELIX 66 AH3 GLN D 277 ALA D 284 1 8
HELIX 67 AH4 GLU D 304 TYR D 308 5 5
HELIX 68 AH5 CYS D 309 GLY D 325 1 17
HELIX 69 AH6 ASP D 335 TYR D 348 1 14
HELIX 70 AH7 SER D 370 ASN D 378 1 9
HELIX 71 AH8 PRO D 379 PHE D 381 5 3
HELIX 72 AH9 ASP D 382 PHE D 387 1 6
HELIX 73 AI1 GLY D 391 GLN D 399 1 9
HELIX 74 AI2 ASN D 400 PHE D 409 1 10
HELIX 75 AI3 ALA D 411 SER D 415 5 5
HELIX 76 AI4 SER D 418 HIS D 420 5 3
HELIX 77 AI5 LYS D 421 GLY D 426 1 6
HELIX 78 AI6 THR D 443 LYS D 456 1 14
HELIX 79 AI7 PHE D 459 TRP D 465 1 7
HELIX 80 AI8 ASN D 468 LYS D 478 1 11
HELIX 81 AI9 VAL D 500 GLN D 505 5 6
HELIX 82 AJ1 HIS D 506 TRP D 510 5 5
HELIX 83 AJ2 TRP D 525 LYS D 530 1 6
HELIX 84 AJ3 LYS D 530 ALA D 546 1 17
SHEET 1 AA116 LEU A 514 ILE A 519 0
SHEET 2 AA116 ALA A 488 ALA A 493 1 N ALA A 488 O LYS A 515
SHEET 3 AA116 VAL A 352 LEU A 358 1 N SER A 357 O VAL A 491
SHEET 4 AA116 ALA A 329 HIS A 334 1 N GLY A 333 O LEU A 358
SHEET 5 AA116 ALA A 260 CYS A 264 1 N CYS A 262 O VAL A 330
SHEET 6 AA116 ARG A 287 MET A 291 1 O LEU A 289 N VAL A 261
SHEET 7 AA116 VAL A 248 LEU A 255 -1 N LEU A 255 O VAL A 288
SHEET 8 AA116 SER A 238 LYS A 245 -1 N GLY A 240 O PHE A 252
SHEET 9 AA116 SER C 238 LYS C 245 -1 O TYR C 241 N HIS A 239
SHEET 10 AA116 VAL C 248 LEU C 255 -1 O PHE C 252 N GLY C 240
SHEET 11 AA116 ARG C 287 MET C 291 -1 O VAL C 288 N LEU C 255
SHEET 12 AA116 ALA C 260 CYS C 264 1 N VAL C 261 O LEU C 289
SHEET 13 AA116 ALA C 329 HIS C 334 1 O VAL C 330 N CYS C 262
SHEET 14 AA116 VAL C 352 LEU C 358 1 O LEU C 358 N GLY C 333
SHEET 15 AA116 ALA C 488 ALA C 493 1 O VAL C 491 N SER C 357
SHEET 16 AA116 LEU C 514 ILE C 519 1 O LYS C 515 N ALA C 488
SHEET 1 AA216 LEU B 514 ILE B 519 0
SHEET 2 AA216 ALA B 488 ALA B 493 1 N ALA B 488 O LYS B 515
SHEET 3 AA216 VAL B 352 LEU B 358 1 N SER B 357 O VAL B 491
SHEET 4 AA216 ALA B 329 HIS B 334 1 N GLY B 333 O LEU B 358
SHEET 5 AA216 ALA B 260 CYS B 264 1 N CYS B 262 O VAL B 330
SHEET 6 AA216 ARG B 287 MET B 291 1 O LEU B 289 N VAL B 261
SHEET 7 AA216 VAL B 248 LEU B 255 -1 N LEU B 255 O VAL B 288
SHEET 8 AA216 SER B 238 LYS B 245 -1 N GLY B 240 O PHE B 252
SHEET 9 AA216 SER D 238 LYS D 245 -1 O TYR D 241 N HIS B 239
SHEET 10 AA216 VAL D 248 LEU D 255 -1 O PHE D 252 N GLY D 240
SHEET 11 AA216 ARG D 287 MET D 291 -1 O VAL D 288 N LEU D 255
SHEET 12 AA216 ALA D 260 CYS D 264 1 N VAL D 261 O LEU D 289
SHEET 13 AA216 ALA D 329 HIS D 334 1 O VAL D 330 N CYS D 262
SHEET 14 AA216 VAL D 352 LEU D 358 1 O LEU D 358 N GLY D 333
SHEET 15 AA216 ALA D 488 ALA D 493 1 O VAL D 491 N SER D 357
SHEET 16 AA216 LEU D 514 ILE D 519 1 O ILE D 519 N THR D 492
CISPEP 1 PHE A 267 PRO A 268 0 -12.05
CISPEP 2 PHE B 267 PRO B 268 0 -7.12
CISPEP 3 PHE C 267 PRO C 268 0 -13.21
CISPEP 4 PHE D 267 PRO D 268 0 -13.32
CRYST1 80.290 90.642 188.416 90.00 90.00 90.00 P 21 21 21 16
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 0.012455 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011032 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005307 0.00000
TER 2627 ARG A 547
TER 5268 ASP B 545
TER 7910 ARG C 547
TER 10546 ARG D 547
MASTER 630 0 20 84 32 0 0 611231 4 184 116
END |