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HEADER HYDROLASE 27-OCT-23 8QZD
TITLE SOLUBLE EPOXIDE HYDROLASE IN COMPLEX WITH EPOXYKININ
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BIFUNCTIONAL EPOXIDE HYDROLASE 2;
COMPND 3 CHAIN: A;
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,J.M.H.EHRLER,S.ZIEGLER,L.DOETSCH,E.PROSCHAK,S.KNAPP,
AUTHOR 2 STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 1 28-FEB-24 8QZD 0
JRNL AUTH A.KUMAR,J.M.H.EHRLER,S.ZIEGLER,L.DOETSCH,E.PROSCHAK,S.KNAPP,
JRNL AUTH 2 STRUCTURAL GENOMICS CONSORTIUM (SGC)
JRNL TITL SOLUBLE EPOXIDE HYDROLASE IN COMPLEX WITH EPOXYKININ
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.30 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) : 1.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.54
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 76583
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) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.180
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 4091
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.34
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5354
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.91
REMARK 3 BIN R VALUE (WORKING SET) : 0.2870
REMARK 3 BIN FREE R VALUE SET COUNT : 295
REMARK 3 BIN FREE R VALUE : 0.3040
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2553
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 76
REMARK 3 SOLVENT ATOMS : 258
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.14
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.22000
REMARK 3 B22 (A**2) : -0.82000
REMARK 3 B33 (A**2) : 0.60000
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): 0.047
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.048
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.033
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.800
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.973
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.966
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2837 ; 0.012 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): 2610 ; 0.001 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3853 ; 1.926 ; 1.834
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6039 ; 0.655 ; 1.739
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 350 ; 6.871 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 18 ; 7.199 ; 6.667
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 462 ;12.165 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 393 ; 0.099 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3386 ; 0.011 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 660 ; 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): 1358 ; 1.624 ; 1.778
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1358 ; 1.603 ; 1.777
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1722 ; 2.373 ; 3.183
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1723 ; 2.378 ; 3.185
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1479 ; 2.733 ; 2.052
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1480 ; 2.732 ; 2.053
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2132 ; 3.975 ; 3.637
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3338 ; 5.262 ;20.130
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 3338 ; 5.262 ;20.120
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 8QZD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-OCT-23.
REMARK 100 THE DEPOSITION ID IS D_1292134143.
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 : 80739
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.300
REMARK 200 RESOLUTION RANGE LOW (A) : 44.540
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.33
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 5.80
REMARK 200 R MERGE FOR SHELL (I) : 1.14900
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 (%): 37.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.96
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG SMEAR HIGH, 0.1M PIPES PH 7.0,
REMARK 280 0.1M MAGNESIUM FORMATE, 0.1M RUBIDIUM CHLORIDE, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21
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,Y+1/2,-Z+1/2
REMARK 290 4555 -X,-Y+1/2,Z+1/2
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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.15600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 44.54200
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.15600
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 44.54200
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2400 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 33.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 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 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 MET A 369 CG SD CE
REMARK 470 LEU A 372 CG CD1 CD2
REMARK 470 LYS A 421 CG CD CE NZ
REMARK 470 GLU A 424 CG CD OE1 OE2
REMARK 470 GLN A 502 CG CD OE1 NE2
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 O1 EDO A 610 O HOH A 701 2.15
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 MET A 339 CG - SD - CE ANGL. DEV. = -10.0 DEGREES
REMARK 500 ARG A 482 NE - CZ - NH2 ANGL. DEV. = -4.1 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 -167.95 -105.33
REMARK 500 GLU A 269 -147.91 -123.88
REMARK 500 ASP A 335 -131.96 64.73
REMARK 500 ASN A 359 -42.87 82.17
REMARK 500 SER A 544 -92.62 -129.05
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 292 143.09
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 958 DISTANCE = 6.18 ANGSTROMS
DBREF 8QZD A 222 555 UNP P34913 HYES_HUMAN 222 555
SEQADV 8QZD MET A 198 UNP P34913 INITIATING METHIONINE
SEQADV 8QZD GLY A 199 UNP P34913 EXPRESSION TAG
SEQADV 8QZD SER A 200 UNP P34913 EXPRESSION TAG
SEQADV 8QZD SER A 201 UNP P34913 EXPRESSION TAG
SEQADV 8QZD HIS A 202 UNP P34913 EXPRESSION TAG
SEQADV 8QZD HIS A 203 UNP P34913 EXPRESSION TAG
SEQADV 8QZD HIS A 204 UNP P34913 EXPRESSION TAG
SEQADV 8QZD HIS A 205 UNP P34913 EXPRESSION TAG
SEQADV 8QZD HIS A 206 UNP P34913 EXPRESSION TAG
SEQADV 8QZD HIS A 207 UNP P34913 EXPRESSION TAG
SEQADV 8QZD SER A 208 UNP P34913 EXPRESSION TAG
SEQADV 8QZD SER A 209 UNP P34913 EXPRESSION TAG
SEQADV 8QZD GLY A 210 UNP P34913 EXPRESSION TAG
SEQADV 8QZD LEU A 211 UNP P34913 EXPRESSION TAG
SEQADV 8QZD VAL A 212 UNP P34913 EXPRESSION TAG
SEQADV 8QZD PRO A 213 UNP P34913 EXPRESSION TAG
SEQADV 8QZD ARG A 214 UNP P34913 EXPRESSION TAG
SEQADV 8QZD GLY A 215 UNP P34913 EXPRESSION TAG
SEQADV 8QZD SER A 216 UNP P34913 EXPRESSION TAG
SEQADV 8QZD HIS A 217 UNP P34913 EXPRESSION TAG
SEQADV 8QZD MET A 218 UNP P34913 EXPRESSION TAG
SEQADV 8QZD ALA A 219 UNP P34913 EXPRESSION TAG
SEQADV 8QZD SER A 220 UNP P34913 EXPRESSION TAG
SEQADV 8QZD MET A 221 UNP P34913 EXPRESSION TAG
SEQADV 8QZD LEU A 556 UNP P34913 EXPRESSION TAG
SEQADV 8QZD LEU A 557 UNP P34913 EXPRESSION TAG
SEQADV 8QZD GLU A 558 UNP P34913 EXPRESSION TAG
SEQADV 8QZD HIS A 559 UNP P34913 EXPRESSION TAG
SEQADV 8QZD HIS A 560 UNP P34913 EXPRESSION TAG
SEQADV 8QZD HIS A 561 UNP P34913 EXPRESSION TAG
SEQADV 8QZD HIS A 562 UNP P34913 EXPRESSION TAG
SEQADV 8QZD HIS A 563 UNP P34913 EXPRESSION TAG
SEQADV 8QZD HIS A 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
HET EDO A 601 4
HET EDO A 602 4
HET EDO A 603 4
HET EDO A 604 4
HET EDO A 605 4
HET EDO A 606 4
HET EDO A 607 4
HET EDO A 608 4
HET XDZ A 609 27
HET EDO A 610 4
HET EDO A 611 4
HET BR A 612 1
HET EDO A 613 4
HET EDO A 614 4
HETNAM EDO 1,2-ETHANEDIOL
HETNAM XDZ 2-[5-BROMANYL-3-[2,2,2-TRIS(FLUORANYL)ETHANOYL]INDOL-1-
HETNAM 2 XDZ YL]-N-CYCLOHEPTYL-ETHANAMIDE
HETNAM BR BROMIDE ION
HETSYN EDO ETHYLENE GLYCOL
HETSYN XDZ EPOXYKININ
FORMUL 2 EDO 12(C2 H6 O2)
FORMUL 10 XDZ C19 H20 BR F3 N2 O2
FORMUL 13 BR BR 1-
FORMUL 16 HOH *258(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 GLN A 277 ALA A 284 1 8
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 ALA A 377 1 8
HELIX 8 AA8 ASN A 378 VAL A 380 5 3
HELIX 9 AA9 PHE A 381 PHE A 387 1 7
HELIX 10 AB1 GLY A 391 ASN A 400 1 10
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 LYS A 421 GLY A 426 1 6
HELIX 14 AB5 THR A 443 GLY A 458 1 16
HELIX 15 AB6 PHE A 459 TRP A 465 1 7
HELIX 16 AB7 ASN A 468 LYS A 478 1 11
HELIX 17 AB8 VAL A 500 GLN A 505 5 6
HELIX 18 AB9 HIS A 506 TRP A 510 5 5
HELIX 19 AC1 TRP A 525 LYS A 530 1 6
HELIX 20 AC2 LYS A 530 ASP A 543 1 14
SHEET 1 AA1 8 SER A 238 LYS A 245 0
SHEET 2 AA1 8 VAL A 248 LEU A 255 -1 O PHE A 252 N GLY A 240
SHEET 3 AA1 8 ARG A 287 MET A 291 -1 O VAL A 288 N LEU A 255
SHEET 4 AA1 8 ALA A 260 CYS A 264 1 N VAL A 261 O LEU A 289
SHEET 5 AA1 8 ALA A 329 HIS A 334 1 O VAL A 330 N CYS A 262
SHEET 6 AA1 8 VAL A 352 LEU A 358 1 O LEU A 358 N GLY A 333
SHEET 7 AA1 8 ALA A 488 ALA A 493 1 O VAL A 491 N SER A 357
SHEET 8 AA1 8 LYS A 515 ILE A 519 1 O LYS A 515 N ALA A 488
CISPEP 1 PHE A 267 PRO A 268 0 -10.95
CRYST1 45.924 80.312 89.084 90.00 90.00 90.00 P 2 21 21 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 0.021775 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012451 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011225 0.00000
TER 2680 ARG A 547
MASTER 383 0 14 20 8 0 0 6 2887 1 75 29
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