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HEADER HYDROLASE 02-JUN-23 8JLV
TITLE BENEFICIAL FLIP OF SUBSTRATE ORIENTATION ENABLE DETERMINE SUBSTRATE
TITLE 2 SPECIFICITY FOR ZEARALENONE LACTONE HYDROLASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AB HYDROLASE-1 DOMAIN-CONTAINING PROTEIN;
COMPND 3 CHAIN: B, A, C, D, E, F;
COMPND 4 SYNONYM: ZEN LACTONE HYDROLASE, ZHDAY3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: EXOPHIALA AQUAMARINA CBS 119918;
SOURCE 3 ORGANISM_TAXID: 1182545;
SOURCE 4 GENE: A1O9_11392;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS MYCOTOXIN, ZEARALENONE HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.XIANG,M.WANG,G.ZHANG,J.ZHOU
REVDAT 1 06-DEC-23 8JLV 0
JRNL AUTH M.WANG,L.XIANG,J.ZHOU,G.ZHANG
JRNL TITL BENEFICIAL FLIP OF SUBSTRATE ORIENTATION ENABLE DETERMINE
JRNL TITL 2 SUBSTRATE SPECIFICITY FOR ZEARALENONE LACTONE HYDROLASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.11.1_2575
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.70
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 3 NUMBER OF REFLECTIONS : 37520
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.877
REMARK 3 FREE R VALUE TEST SET COUNT : 1830
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 8.1300 - 7.0411 0.99 2892 148 0.1802 0.2245
REMARK 3 2 7.0411 - 5.5927 1.00 2865 135 0.1986 0.2346
REMARK 3 3 5.5927 - 4.8869 1.00 2860 131 0.1745 0.2127
REMARK 3 4 4.8869 - 4.4406 1.00 2836 142 0.1605 0.1998
REMARK 3 5 4.4406 - 4.1226 1.00 2866 140 0.1657 0.2104
REMARK 3 6 4.1226 - 3.8797 1.00 2820 163 0.1841 0.2274
REMARK 3 7 3.8797 - 3.6855 1.00 2806 153 0.2028 0.2375
REMARK 3 8 3.6855 - 3.5251 1.00 2805 165 0.2283 0.2585
REMARK 3 9 3.5251 - 3.3895 1.00 2843 142 0.2513 0.3239
REMARK 3 10 3.3895 - 3.2726 0.99 2808 136 0.2576 0.3100
REMARK 3 11 3.2726 - 3.1703 0.97 2726 143 0.2848 0.2943
REMARK 3 12 3.1703 - 3.0797 0.89 2510 132 0.3060 0.3964
REMARK 3 13 3.0797 - 3.0000 0.72 2053 100 0.3149 0.3606
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
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) : 0.405
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.844
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 60.53
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.43
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 : 0.009 12702
REMARK 3 ANGLE : 1.371 17334
REMARK 3 CHIRALITY : 0.074 1914
REMARK 3 PLANARITY : 0.008 2232
REMARK 3 DIHEDRAL : 13.261 7560
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'A'
REMARK 3 SELECTION : CHAIN 'B'
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN 'A'
REMARK 3 SELECTION : CHAIN 'C'
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN 'A'
REMARK 3 SELECTION : CHAIN 'D'
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 4
REMARK 3 REFERENCE SELECTION: CHAIN 'A'
REMARK 3 SELECTION : CHAIN 'E'
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 5
REMARK 3 REFERENCE SELECTION: CHAIN 'A'
REMARK 3 SELECTION : CHAIN 'F'
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 8JLV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 07-JUN-23.
REMARK 100 THE DEPOSITION ID IS D_1300038051.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-NOV-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL18U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38647
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.990
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.31900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.05
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 1.45700
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: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.79
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1M NAH2PO4/K2HPO4, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 60.16300
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
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: 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: 2
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: 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 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
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 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 NZ LYS D 200 CG HIS D 231 1.26
REMARK 500 NZ LYS D 200 CD2 HIS D 231 1.52
REMARK 500 OG1 THR F 8 ND1 HIS F 14 1.99
REMARK 500 NZ LYS D 200 CB HIS D 231 2.13
REMARK 500 O GLY D 60 NH2 ARG D 183 2.13
REMARK 500 CE LYS D 200 CD2 HIS D 231 2.15
REMARK 500 OG1 THR F 76 NE2 GLN F 78 2.18
REMARK 500 NZ LYS D 200 ND1 HIS D 231 2.19
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 B 201 CB GLU B 201 CG 0.117
REMARK 500 GLU B 201 CG GLU B 201 CD 0.107
REMARK 500 LYS D 200 CB LYS D 200 CG -0.182
REMARK 500 GLU F 70 CG GLU F 70 CD 0.189
REMARK 500 GLU F 70 CD GLU F 70 OE1 -0.101
REMARK 500 GLU F 70 CD GLU F 70 OE2 -0.144
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 GLU B 201 CA - CB - CG ANGL. DEV. = 18.8 DEGREES
REMARK 500 ARG B 261 CB - CG - CD ANGL. DEV. = -21.8 DEGREES
REMARK 500 ARG B 261 NE - CZ - NH1 ANGL. DEV. = -4.8 DEGREES
REMARK 500 ARG B 261 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 MET A 1 N - CA - CB ANGL. DEV. = 16.5 DEGREES
REMARK 500 LYS C 41 CD - CE - NZ ANGL. DEV. = -19.7 DEGREES
REMARK 500 ILE D 7 CG1 - CB - CG2 ANGL. DEV. = -27.9 DEGREES
REMARK 500 ASP D 94 CB - CA - C ANGL. DEV. = -13.2 DEGREES
REMARK 500 ASP D 94 CB - CG - OD1 ANGL. DEV. = -5.6 DEGREES
REMARK 500 MET D 132 CB - CA - C ANGL. DEV. = 12.1 DEGREES
REMARK 500 MET D 132 CG - SD - CE ANGL. DEV. = 10.3 DEGREES
REMARK 500 GLU D 133 CA - CB - CG ANGL. DEV. = 14.0 DEGREES
REMARK 500 GLU D 133 CA - C - O ANGL. DEV. = -19.3 DEGREES
REMARK 500 ASP D 134 C - N - CA ANGL. DEV. = 15.8 DEGREES
REMARK 500 LYS D 200 CD - CE - NZ ANGL. DEV. = -16.9 DEGREES
REMARK 500 VAL E 159 CG1 - CB - CG2 ANGL. DEV. = 11.2 DEGREES
REMARK 500 ASP E 161 C - N - CA ANGL. DEV. = -15.5 DEGREES
REMARK 500 ASP E 161 CB - CG - OD1 ANGL. DEV. = -8.9 DEGREES
REMARK 500 ASP E 161 CB - CG - OD2 ANGL. DEV. = 7.1 DEGREES
REMARK 500 ILE E 162 CG1 - CB - CG2 ANGL. DEV. = -25.3 DEGREES
REMARK 500 LYS E 200 CD - CE - NZ ANGL. DEV. = -16.9 DEGREES
REMARK 500 GLU F 70 CA - CB - CG ANGL. DEV. = -18.1 DEGREES
REMARK 500 ASP F 94 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP F 94 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 LYS F 200 N - CA - CB ANGL. DEV. = -12.0 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 ASP B 31 -157.82 -81.83
REMARK 500 SER B 62 -130.86 53.44
REMARK 500 ALA B 102 -121.97 52.56
REMARK 500 GLU B 126 73.24 49.74
REMARK 500 GLU B 163 52.96 -112.94
REMARK 500 TYR B 188 -63.25 -105.88
REMARK 500 TYR B 191 -32.95 -136.49
REMARK 500 LYS B 205 1.68 -68.31
REMARK 500 MET B 241 -100.45 -125.23
REMARK 500 ASP A 31 -158.52 -78.66
REMARK 500 SER A 62 -131.00 54.29
REMARK 500 ALA A 102 -123.00 52.80
REMARK 500 GLU A 126 71.81 49.16
REMARK 500 ILE A 162 17.12 -146.01
REMARK 500 TYR A 191 -35.13 -135.59
REMARK 500 MET A 241 -102.04 -124.41
REMARK 500 ASP C 31 -160.40 -77.28
REMARK 500 SER C 62 -130.40 55.20
REMARK 500 ALA C 102 -122.74 52.57
REMARK 500 ASN C 121 143.51 -171.84
REMARK 500 GLU C 126 72.72 50.08
REMARK 500 TYR C 191 -33.08 -133.75
REMARK 500 LYS C 205 2.54 -68.16
REMARK 500 MET C 241 -99.94 -120.50
REMARK 500 ASP D 31 -157.58 -79.69
REMARK 500 SER D 62 -129.22 55.20
REMARK 500 ALA D 102 -124.83 52.43
REMARK 500 GLU D 126 74.41 48.84
REMARK 500 MET D 132 -118.75 -101.75
REMARK 500 GLU D 133 3.19 -56.09
REMARK 500 ASP D 134 -32.05 86.92
REMARK 500 LEU D 135 3.24 36.59
REMARK 500 ASP D 143 -52.00 -28.30
REMARK 500 ASN D 153 64.48 -106.75
REMARK 500 VAL D 154 -24.54 -145.00
REMARK 500 ILE D 162 75.04 -106.32
REMARK 500 TYR D 191 -35.10 -134.39
REMARK 500 MET D 241 -100.50 -123.69
REMARK 500 ARG E 2 93.52 62.43
REMARK 500 ASP E 31 -159.66 -79.39
REMARK 500 SER E 62 -128.64 55.12
REMARK 500 ALA E 102 -122.57 54.64
REMARK 500 ASN E 121 139.69 -170.25
REMARK 500 GLU E 126 74.36 50.19
REMARK 500 MET E 132 134.60 76.09
REMARK 500 GLU E 133 80.24 16.48
REMARK 500 ASP E 134 147.79 -39.60
REMARK 500 LYS E 136 -50.56 -15.94
REMARK 500 ILE E 162 145.99 75.15
REMARK 500 TYR E 188 -62.41 -105.94
REMARK 500
REMARK 500 THIS ENTRY HAS 60 RAMACHANDRAN OUTLIERS.
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 ASP E 161 ILE E 162 145.25
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 GLU A 66 0.07 SIDE CHAIN
REMARK 500 HIS F 231 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 8JLV B 1 264 UNP A0A072PAD1_9EURO
DBREF2 8JLV B A0A072PAD1 1 264
DBREF1 8JLV A 1 264 UNP A0A072PAD1_9EURO
DBREF2 8JLV A A0A072PAD1 1 264
DBREF1 8JLV C 1 264 UNP A0A072PAD1_9EURO
DBREF2 8JLV C A0A072PAD1 1 264
DBREF1 8JLV D 1 264 UNP A0A072PAD1_9EURO
DBREF2 8JLV D A0A072PAD1 1 264
DBREF1 8JLV E 1 264 UNP A0A072PAD1_9EURO
DBREF2 8JLV E A0A072PAD1 1 264
DBREF1 8JLV F 1 264 UNP A0A072PAD1_9EURO
DBREF2 8JLV F A0A072PAD1 1 264
SEQADV 8JLV ALA B 102 UNP A0A072PAD SER 102 CONFLICT
SEQADV 8JLV ALA A 102 UNP A0A072PAD SER 102 CONFLICT
SEQADV 8JLV ALA C 102 UNP A0A072PAD SER 102 CONFLICT
SEQADV 8JLV ALA D 102 UNP A0A072PAD SER 102 CONFLICT
SEQADV 8JLV ALA E 102 UNP A0A072PAD SER 102 CONFLICT
SEQADV 8JLV ALA F 102 UNP A0A072PAD SER 102 CONFLICT
SEQRES 1 B 264 MET ARG THR ARG SER ASN ILE THR THR LYS ASN GLY ILE
SEQRES 2 B 264 HIS TRP TYR TYR GLU GLN GLU GLY SER GLY PRO HIS VAL
SEQRES 3 B 264 VAL LEU ILE PRO ASP GLY LEU GLY GLU CYS LYS MET PHE
SEQRES 4 B 264 ASP LYS PRO MET SER LEU ILE ALA ASN SER GLY PHE THR
SEQRES 5 B 264 VAL THR THR PHE ASP MET PRO GLY MET SER ARG SER SER
SEQRES 6 B 264 GLU ALA PRO PRO GLU THR TYR GLN GLU ILE THR ALA GLN
SEQRES 7 B 264 LYS LEU ALA SER TYR VAL ILE SER ILE CYS ASP GLU LEU
SEQRES 8 B 264 ALA ILE ASP LYS ALA THR PHE TRP GLY CYS ALA SER GLY
SEQRES 9 B 264 GLY CYS THR VAL LEU ALA LEU VAL ALA ASP TYR PRO THR
SEQRES 10 B 264 ARG VAL ARG ASN ALA LEU ALA HIS GLU VAL PRO THR TYR
SEQRES 11 B 264 LEU MET GLU ASP LEU LYS PRO LEU LEU GLU MET ASP ASP
SEQRES 12 B 264 GLU ALA VAL SER ALA ALA MET SER SER ASN VAL VAL VAL
SEQRES 13 B 264 GLY SER VAL GLY ASP ILE GLU GLY SER TRP GLN GLU LEU
SEQRES 14 B 264 GLY GLU GLU ALA HIS ALA ARG LEU TRP LYS ASN TYR PRO
SEQRES 15 B 264 ARG TRP ALA ARG GLY TYR PRO GLY TYR ILE PRO GLN SER
SEQRES 16 B 264 THR PRO VAL SER LYS GLU ASP LEU ILE LYS ALA PRO LEU
SEQRES 17 B 264 ASP TRP THR VAL GLY ALA SER THR PRO THR ALA ARG PHE
SEQRES 18 B 264 LEU ASP ASN ILE VAL THR ALA THR LYS HIS ASN ILE PRO
SEQRES 19 B 264 PHE GLN THR LEU PRO GLY MET HIS PHE PRO TYR VAL THR
SEQRES 20 B 264 HIS PRO GLU VAL PHE ALA GLU TYR VAL VAL GLU LYS THR
SEQRES 21 B 264 ARG LYS TYR LEU
SEQRES 1 A 264 MET ARG THR ARG SER ASN ILE THR THR LYS ASN GLY ILE
SEQRES 2 A 264 HIS TRP TYR TYR GLU GLN GLU GLY SER GLY PRO HIS VAL
SEQRES 3 A 264 VAL LEU ILE PRO ASP GLY LEU GLY GLU CYS LYS MET PHE
SEQRES 4 A 264 ASP LYS PRO MET SER LEU ILE ALA ASN SER GLY PHE THR
SEQRES 5 A 264 VAL THR THR PHE ASP MET PRO GLY MET SER ARG SER SER
SEQRES 6 A 264 GLU ALA PRO PRO GLU THR TYR GLN GLU ILE THR ALA GLN
SEQRES 7 A 264 LYS LEU ALA SER TYR VAL ILE SER ILE CYS ASP GLU LEU
SEQRES 8 A 264 ALA ILE ASP LYS ALA THR PHE TRP GLY CYS ALA SER GLY
SEQRES 9 A 264 GLY CYS THR VAL LEU ALA LEU VAL ALA ASP TYR PRO THR
SEQRES 10 A 264 ARG VAL ARG ASN ALA LEU ALA HIS GLU VAL PRO THR TYR
SEQRES 11 A 264 LEU MET GLU ASP LEU LYS PRO LEU LEU GLU MET ASP ASP
SEQRES 12 A 264 GLU ALA VAL SER ALA ALA MET SER SER ASN VAL VAL VAL
SEQRES 13 A 264 GLY SER VAL GLY ASP ILE GLU GLY SER TRP GLN GLU LEU
SEQRES 14 A 264 GLY GLU GLU ALA HIS ALA ARG LEU TRP LYS ASN TYR PRO
SEQRES 15 A 264 ARG TRP ALA ARG GLY TYR PRO GLY TYR ILE PRO GLN SER
SEQRES 16 A 264 THR PRO VAL SER LYS GLU ASP LEU ILE LYS ALA PRO LEU
SEQRES 17 A 264 ASP TRP THR VAL GLY ALA SER THR PRO THR ALA ARG PHE
SEQRES 18 A 264 LEU ASP ASN ILE VAL THR ALA THR LYS HIS ASN ILE PRO
SEQRES 19 A 264 PHE GLN THR LEU PRO GLY MET HIS PHE PRO TYR VAL THR
SEQRES 20 A 264 HIS PRO GLU VAL PHE ALA GLU TYR VAL VAL GLU LYS THR
SEQRES 21 A 264 ARG LYS TYR LEU
SEQRES 1 C 264 MET ARG THR ARG SER ASN ILE THR THR LYS ASN GLY ILE
SEQRES 2 C 264 HIS TRP TYR TYR GLU GLN GLU GLY SER GLY PRO HIS VAL
SEQRES 3 C 264 VAL LEU ILE PRO ASP GLY LEU GLY GLU CYS LYS MET PHE
SEQRES 4 C 264 ASP LYS PRO MET SER LEU ILE ALA ASN SER GLY PHE THR
SEQRES 5 C 264 VAL THR THR PHE ASP MET PRO GLY MET SER ARG SER SER
SEQRES 6 C 264 GLU ALA PRO PRO GLU THR TYR GLN GLU ILE THR ALA GLN
SEQRES 7 C 264 LYS LEU ALA SER TYR VAL ILE SER ILE CYS ASP GLU LEU
SEQRES 8 C 264 ALA ILE ASP LYS ALA THR PHE TRP GLY CYS ALA SER GLY
SEQRES 9 C 264 GLY CYS THR VAL LEU ALA LEU VAL ALA ASP TYR PRO THR
SEQRES 10 C 264 ARG VAL ARG ASN ALA LEU ALA HIS GLU VAL PRO THR TYR
SEQRES 11 C 264 LEU MET GLU ASP LEU LYS PRO LEU LEU GLU MET ASP ASP
SEQRES 12 C 264 GLU ALA VAL SER ALA ALA MET SER SER ASN VAL VAL VAL
SEQRES 13 C 264 GLY SER VAL GLY ASP ILE GLU GLY SER TRP GLN GLU LEU
SEQRES 14 C 264 GLY GLU GLU ALA HIS ALA ARG LEU TRP LYS ASN TYR PRO
SEQRES 15 C 264 ARG TRP ALA ARG GLY TYR PRO GLY TYR ILE PRO GLN SER
SEQRES 16 C 264 THR PRO VAL SER LYS GLU ASP LEU ILE LYS ALA PRO LEU
SEQRES 17 C 264 ASP TRP THR VAL GLY ALA SER THR PRO THR ALA ARG PHE
SEQRES 18 C 264 LEU ASP ASN ILE VAL THR ALA THR LYS HIS ASN ILE PRO
SEQRES 19 C 264 PHE GLN THR LEU PRO GLY MET HIS PHE PRO TYR VAL THR
SEQRES 20 C 264 HIS PRO GLU VAL PHE ALA GLU TYR VAL VAL GLU LYS THR
SEQRES 21 C 264 ARG LYS TYR LEU
SEQRES 1 D 264 MET ARG THR ARG SER ASN ILE THR THR LYS ASN GLY ILE
SEQRES 2 D 264 HIS TRP TYR TYR GLU GLN GLU GLY SER GLY PRO HIS VAL
SEQRES 3 D 264 VAL LEU ILE PRO ASP GLY LEU GLY GLU CYS LYS MET PHE
SEQRES 4 D 264 ASP LYS PRO MET SER LEU ILE ALA ASN SER GLY PHE THR
SEQRES 5 D 264 VAL THR THR PHE ASP MET PRO GLY MET SER ARG SER SER
SEQRES 6 D 264 GLU ALA PRO PRO GLU THR TYR GLN GLU ILE THR ALA GLN
SEQRES 7 D 264 LYS LEU ALA SER TYR VAL ILE SER ILE CYS ASP GLU LEU
SEQRES 8 D 264 ALA ILE ASP LYS ALA THR PHE TRP GLY CYS ALA SER GLY
SEQRES 9 D 264 GLY CYS THR VAL LEU ALA LEU VAL ALA ASP TYR PRO THR
SEQRES 10 D 264 ARG VAL ARG ASN ALA LEU ALA HIS GLU VAL PRO THR TYR
SEQRES 11 D 264 LEU MET GLU ASP LEU LYS PRO LEU LEU GLU MET ASP ASP
SEQRES 12 D 264 GLU ALA VAL SER ALA ALA MET SER SER ASN VAL VAL VAL
SEQRES 13 D 264 GLY SER VAL GLY ASP ILE GLU GLY SER TRP GLN GLU LEU
SEQRES 14 D 264 GLY GLU GLU ALA HIS ALA ARG LEU TRP LYS ASN TYR PRO
SEQRES 15 D 264 ARG TRP ALA ARG GLY TYR PRO GLY TYR ILE PRO GLN SER
SEQRES 16 D 264 THR PRO VAL SER LYS GLU ASP LEU ILE LYS ALA PRO LEU
SEQRES 17 D 264 ASP TRP THR VAL GLY ALA SER THR PRO THR ALA ARG PHE
SEQRES 18 D 264 LEU ASP ASN ILE VAL THR ALA THR LYS HIS ASN ILE PRO
SEQRES 19 D 264 PHE GLN THR LEU PRO GLY MET HIS PHE PRO TYR VAL THR
SEQRES 20 D 264 HIS PRO GLU VAL PHE ALA GLU TYR VAL VAL GLU LYS THR
SEQRES 21 D 264 ARG LYS TYR LEU
SEQRES 1 E 264 MET ARG THR ARG SER ASN ILE THR THR LYS ASN GLY ILE
SEQRES 2 E 264 HIS TRP TYR TYR GLU GLN GLU GLY SER GLY PRO HIS VAL
SEQRES 3 E 264 VAL LEU ILE PRO ASP GLY LEU GLY GLU CYS LYS MET PHE
SEQRES 4 E 264 ASP LYS PRO MET SER LEU ILE ALA ASN SER GLY PHE THR
SEQRES 5 E 264 VAL THR THR PHE ASP MET PRO GLY MET SER ARG SER SER
SEQRES 6 E 264 GLU ALA PRO PRO GLU THR TYR GLN GLU ILE THR ALA GLN
SEQRES 7 E 264 LYS LEU ALA SER TYR VAL ILE SER ILE CYS ASP GLU LEU
SEQRES 8 E 264 ALA ILE ASP LYS ALA THR PHE TRP GLY CYS ALA SER GLY
SEQRES 9 E 264 GLY CYS THR VAL LEU ALA LEU VAL ALA ASP TYR PRO THR
SEQRES 10 E 264 ARG VAL ARG ASN ALA LEU ALA HIS GLU VAL PRO THR TYR
SEQRES 11 E 264 LEU MET GLU ASP LEU LYS PRO LEU LEU GLU MET ASP ASP
SEQRES 12 E 264 GLU ALA VAL SER ALA ALA MET SER SER ASN VAL VAL VAL
SEQRES 13 E 264 GLY SER VAL GLY ASP ILE GLU GLY SER TRP GLN GLU LEU
SEQRES 14 E 264 GLY GLU GLU ALA HIS ALA ARG LEU TRP LYS ASN TYR PRO
SEQRES 15 E 264 ARG TRP ALA ARG GLY TYR PRO GLY TYR ILE PRO GLN SER
SEQRES 16 E 264 THR PRO VAL SER LYS GLU ASP LEU ILE LYS ALA PRO LEU
SEQRES 17 E 264 ASP TRP THR VAL GLY ALA SER THR PRO THR ALA ARG PHE
SEQRES 18 E 264 LEU ASP ASN ILE VAL THR ALA THR LYS HIS ASN ILE PRO
SEQRES 19 E 264 PHE GLN THR LEU PRO GLY MET HIS PHE PRO TYR VAL THR
SEQRES 20 E 264 HIS PRO GLU VAL PHE ALA GLU TYR VAL VAL GLU LYS THR
SEQRES 21 E 264 ARG LYS TYR LEU
SEQRES 1 F 264 MET ARG THR ARG SER ASN ILE THR THR LYS ASN GLY ILE
SEQRES 2 F 264 HIS TRP TYR TYR GLU GLN GLU GLY SER GLY PRO HIS VAL
SEQRES 3 F 264 VAL LEU ILE PRO ASP GLY LEU GLY GLU CYS LYS MET PHE
SEQRES 4 F 264 ASP LYS PRO MET SER LEU ILE ALA ASN SER GLY PHE THR
SEQRES 5 F 264 VAL THR THR PHE ASP MET PRO GLY MET SER ARG SER SER
SEQRES 6 F 264 GLU ALA PRO PRO GLU THR TYR GLN GLU ILE THR ALA GLN
SEQRES 7 F 264 LYS LEU ALA SER TYR VAL ILE SER ILE CYS ASP GLU LEU
SEQRES 8 F 264 ALA ILE ASP LYS ALA THR PHE TRP GLY CYS ALA SER GLY
SEQRES 9 F 264 GLY CYS THR VAL LEU ALA LEU VAL ALA ASP TYR PRO THR
SEQRES 10 F 264 ARG VAL ARG ASN ALA LEU ALA HIS GLU VAL PRO THR TYR
SEQRES 11 F 264 LEU MET GLU ASP LEU LYS PRO LEU LEU GLU MET ASP ASP
SEQRES 12 F 264 GLU ALA VAL SER ALA ALA MET SER SER ASN VAL VAL VAL
SEQRES 13 F 264 GLY SER VAL GLY ASP ILE GLU GLY SER TRP GLN GLU LEU
SEQRES 14 F 264 GLY GLU GLU ALA HIS ALA ARG LEU TRP LYS ASN TYR PRO
SEQRES 15 F 264 ARG TRP ALA ARG GLY TYR PRO GLY TYR ILE PRO GLN SER
SEQRES 16 F 264 THR PRO VAL SER LYS GLU ASP LEU ILE LYS ALA PRO LEU
SEQRES 17 F 264 ASP TRP THR VAL GLY ALA SER THR PRO THR ALA ARG PHE
SEQRES 18 F 264 LEU ASP ASN ILE VAL THR ALA THR LYS HIS ASN ILE PRO
SEQRES 19 F 264 PHE GLN THR LEU PRO GLY MET HIS PHE PRO TYR VAL THR
SEQRES 20 F 264 HIS PRO GLU VAL PHE ALA GLU TYR VAL VAL GLU LYS THR
SEQRES 21 F 264 ARG LYS TYR LEU
HELIX 1 AA1 GLU B 35 MET B 38 5 4
HELIX 2 AA2 PHE B 39 ASN B 48 1 10
HELIX 3 AA3 MET B 61 SER B 65 5 5
HELIX 4 AA4 PRO B 68 TYR B 72 5 5
HELIX 5 AA5 THR B 76 LEU B 91 1 16
HELIX 6 AA6 ALA B 102 TYR B 115 1 14
HELIX 7 AA7 MET B 132 LEU B 139 5 8
HELIX 8 AA8 ASP B 143 VAL B 159 1 17
HELIX 9 AA9 TRP B 166 LEU B 169 5 4
HELIX 10 AB1 GLY B 170 TYR B 188 1 19
HELIX 11 AB2 ILE B 192 THR B 196 5 5
HELIX 12 AB3 PHE B 221 LYS B 230 1 10
HELIX 13 AB4 PHE B 243 HIS B 248 1 6
HELIX 14 AB5 HIS B 248 LYS B 262 1 15
HELIX 15 AB6 GLU A 35 MET A 38 5 4
HELIX 16 AB7 PHE A 39 ASN A 48 1 10
HELIX 17 AB8 MET A 61 SER A 65 5 5
HELIX 18 AB9 PRO A 68 TYR A 72 5 5
HELIX 19 AC1 THR A 76 LEU A 91 1 16
HELIX 20 AC2 ALA A 102 TYR A 115 1 14
HELIX 21 AC3 MET A 132 LEU A 139 5 8
HELIX 22 AC4 ASP A 143 SER A 158 1 16
HELIX 23 AC5 TRP A 166 LEU A 169 5 4
HELIX 24 AC6 GLY A 170 TYR A 188 1 19
HELIX 25 AC7 ILE A 192 THR A 196 5 5
HELIX 26 AC8 SER A 199 ILE A 204 1 6
HELIX 27 AC9 PHE A 221 HIS A 231 1 11
HELIX 28 AD1 PHE A 243 HIS A 248 1 6
HELIX 29 AD2 HIS A 248 TYR A 263 1 16
HELIX 30 AD3 GLU C 35 MET C 38 5 4
HELIX 31 AD4 PHE C 39 ASN C 48 1 10
HELIX 32 AD5 MET C 61 SER C 65 5 5
HELIX 33 AD6 PRO C 68 TYR C 72 5 5
HELIX 34 AD7 THR C 76 LEU C 91 1 16
HELIX 35 AD8 ALA C 102 TYR C 115 1 14
HELIX 36 AD9 MET C 132 LEU C 139 5 8
HELIX 37 AE1 ASP C 143 VAL C 156 1 14
HELIX 38 AE2 TRP C 166 LEU C 169 5 4
HELIX 39 AE3 GLY C 170 TYR C 188 1 19
HELIX 40 AE4 ILE C 192 THR C 196 5 5
HELIX 41 AE5 PHE C 221 HIS C 231 1 11
HELIX 42 AE6 PHE C 243 HIS C 248 1 6
HELIX 43 AE7 HIS C 248 TYR C 263 1 16
HELIX 44 AE8 GLU D 35 MET D 38 5 4
HELIX 45 AE9 PHE D 39 SER D 49 1 11
HELIX 46 AF1 MET D 61 SER D 65 5 5
HELIX 47 AF2 PRO D 68 TYR D 72 5 5
HELIX 48 AF3 THR D 76 LEU D 91 1 16
HELIX 49 AF4 ALA D 102 TYR D 115 1 14
HELIX 50 AF5 LEU D 135 MET D 141 1 7
HELIX 51 AF6 ASP D 142 ASN D 153 1 12
HELIX 52 AF7 GLU D 163 GLU D 168 1 6
HELIX 53 AF8 GLY D 170 TYR D 188 1 19
HELIX 54 AF9 TYR D 191 THR D 196 1 6
HELIX 55 AG1 SER D 199 ILE D 204 1 6
HELIX 56 AG2 PHE D 221 HIS D 231 1 11
HELIX 57 AG3 PHE D 243 HIS D 248 1 6
HELIX 58 AG4 HIS D 248 TYR D 263 1 16
HELIX 59 AG5 GLU E 35 MET E 38 5 4
HELIX 60 AG6 PHE E 39 ASN E 48 1 10
HELIX 61 AG7 MET E 61 SER E 65 5 5
HELIX 62 AG8 PRO E 68 TYR E 72 5 5
HELIX 63 AG9 THR E 76 LEU E 91 1 16
HELIX 64 AH1 ALA E 102 TYR E 115 1 14
HELIX 65 AH2 LEU E 135 MET E 141 1 7
HELIX 66 AH3 ASP E 142 SER E 158 1 17
HELIX 67 AH4 TRP E 166 LEU E 169 5 4
HELIX 68 AH5 GLY E 170 TYR E 188 1 19
HELIX 69 AH6 ILE E 192 THR E 196 5 5
HELIX 70 AH7 GLU E 201 LYS E 205 5 5
HELIX 71 AH8 PHE E 221 HIS E 231 1 11
HELIX 72 AH9 PHE E 243 HIS E 248 1 6
HELIX 73 AI1 HIS E 248 LYS E 262 1 15
HELIX 74 AI2 GLU F 35 MET F 38 5 4
HELIX 75 AI3 PHE F 39 ASN F 48 1 10
HELIX 76 AI4 MET F 61 SER F 65 5 5
HELIX 77 AI5 PRO F 68 TYR F 72 5 5
HELIX 78 AI6 THR F 76 LEU F 91 1 16
HELIX 79 AI7 ALA F 102 TYR F 115 1 14
HELIX 80 AI8 MET F 132 LEU F 139 5 8
HELIX 81 AI9 ASP F 143 GLY F 157 1 15
HELIX 82 AJ1 TRP F 166 LEU F 169 5 4
HELIX 83 AJ2 GLY F 170 TYR F 188 1 19
HELIX 84 AJ3 ILE F 192 THR F 196 5 5
HELIX 85 AJ4 PHE F 221 LYS F 230 1 10
HELIX 86 AJ5 PHE F 243 HIS F 248 1 6
HELIX 87 AJ6 HIS F 248 TYR F 263 1 16
SHEET 1 AA1 8 THR B 3 THR B 8 0
SHEET 2 AA1 8 HIS B 14 GLU B 20 -1 O TYR B 17 N SER B 5
SHEET 3 AA1 8 THR B 52 PHE B 56 -1 O THR B 55 N GLU B 18
SHEET 4 AA1 8 HIS B 25 ILE B 29 1 N VAL B 26 O THR B 52
SHEET 5 AA1 8 ALA B 96 CYS B 101 1 O THR B 97 N VAL B 27
SHEET 6 AA1 8 VAL B 119 HIS B 125 1 O LEU B 123 N PHE B 98
SHEET 7 AA1 8 LEU B 208 GLY B 213 1 O ASP B 209 N ALA B 122
SHEET 8 AA1 8 PHE B 235 LEU B 238 1 O GLN B 236 N TRP B 210
SHEET 1 AA2 8 THR A 3 THR A 8 0
SHEET 2 AA2 8 HIS A 14 GLU A 20 -1 O GLN A 19 N THR A 3
SHEET 3 AA2 8 THR A 52 PHE A 56 -1 O THR A 55 N GLU A 18
SHEET 4 AA2 8 HIS A 25 ILE A 29 1 N VAL A 26 O THR A 52
SHEET 5 AA2 8 ALA A 96 CYS A 101 1 O TRP A 99 N ILE A 29
SHEET 6 AA2 8 VAL A 119 HIS A 125 1 O ARG A 120 N ALA A 96
SHEET 7 AA2 8 LEU A 208 GLY A 213 1 O ASP A 209 N ALA A 124
SHEET 8 AA2 8 PHE A 235 LEU A 238 1 O LEU A 238 N VAL A 212
SHEET 1 AA3 8 ARG C 2 THR C 8 0
SHEET 2 AA3 8 HIS C 14 GLU C 20 -1 O GLN C 19 N THR C 3
SHEET 3 AA3 8 THR C 52 PHE C 56 -1 O THR C 55 N GLU C 18
SHEET 4 AA3 8 HIS C 25 ILE C 29 1 N LEU C 28 O THR C 54
SHEET 5 AA3 8 ALA C 96 CYS C 101 1 O TRP C 99 N ILE C 29
SHEET 6 AA3 8 VAL C 119 HIS C 125 1 O ARG C 120 N ALA C 96
SHEET 7 AA3 8 LEU C 208 GLY C 213 1 O ASP C 209 N ALA C 122
SHEET 8 AA3 8 PHE C 235 LEU C 238 1 O LEU C 238 N VAL C 212
SHEET 1 AA4 8 THR D 3 THR D 8 0
SHEET 2 AA4 8 HIS D 14 GLU D 20 -1 O GLN D 19 N THR D 3
SHEET 3 AA4 8 THR D 52 PHE D 56 -1 O THR D 55 N GLU D 18
SHEET 4 AA4 8 HIS D 25 ILE D 29 1 N LEU D 28 O THR D 54
SHEET 5 AA4 8 ALA D 96 CYS D 101 1 O THR D 97 N VAL D 27
SHEET 6 AA4 8 VAL D 119 HIS D 125 1 O ARG D 120 N ALA D 96
SHEET 7 AA4 8 LEU D 208 GLY D 213 1 O ASP D 209 N ALA D 122
SHEET 8 AA4 8 PHE D 235 LEU D 238 1 O LEU D 238 N VAL D 212
SHEET 1 AA5 8 THR E 3 THR E 8 0
SHEET 2 AA5 8 HIS E 14 GLU E 20 -1 O GLN E 19 N THR E 3
SHEET 3 AA5 8 THR E 52 PHE E 56 -1 O THR E 55 N GLU E 18
SHEET 4 AA5 8 HIS E 25 ILE E 29 1 N LEU E 28 O THR E 54
SHEET 5 AA5 8 ALA E 96 CYS E 101 1 O THR E 97 N VAL E 27
SHEET 6 AA5 8 VAL E 119 HIS E 125 1 O ARG E 120 N ALA E 96
SHEET 7 AA5 8 LEU E 208 GLY E 213 1 O ASP E 209 N ALA E 122
SHEET 8 AA5 8 PHE E 235 LEU E 238 1 O LEU E 238 N VAL E 212
SHEET 1 AA6 8 THR F 3 THR F 8 0
SHEET 2 AA6 8 HIS F 14 GLU F 20 -1 O GLN F 19 N THR F 3
SHEET 3 AA6 8 THR F 52 PHE F 56 -1 O THR F 55 N GLU F 18
SHEET 4 AA6 8 HIS F 25 ILE F 29 1 N VAL F 26 O THR F 54
SHEET 5 AA6 8 ALA F 96 CYS F 101 1 O THR F 97 N VAL F 27
SHEET 6 AA6 8 VAL F 119 HIS F 125 1 O ARG F 120 N ALA F 96
SHEET 7 AA6 8 LEU F 208 GLY F 213 1 O ASP F 209 N ALA F 122
SHEET 8 AA6 8 PHE F 235 LEU F 238 1 O LEU F 238 N VAL F 212
CRYST1 79.892 120.326 102.952 90.00 97.42 90.00 P 1 21 1 12
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 0.012517 0.000000 0.001629 0.00000
SCALE2 0.000000 0.008311 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009795 0.00000
TER 2061 LEU B 264
TER 4122 LEU A 264
TER 6183 LEU C 264
TER 8244 LEU D 264
TER 10305 LEU E 264
TER 12366 LEU F 264
MASTER 434 0 0 87 48 0 0 612360 6 0 126
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