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HEADER HYDROLASE 16-JUL-22 7YII
TITLE CARBOXYLESTERASE - ROCE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NON-HEME HALOPEROXIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 1.11.1.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS OPACUS;
SOURCE 3 ORGANISM_TAXID: 37919;
SOURCE 4 GENE: R1CP_28090;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS ALPHA/BETA HYDROLASE, DIMER, ESTER HYDROLASE, ACYLTRANSFERASE,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.DOU,P.JIA,Y.NI,G.C.XU
REVDAT 1 19-JUL-23 7YII 0
JRNL AUTH Z.DOU,P.JIA,Y.NI,G.C.XU
JRNL TITL CARBOXYLESTERASE - ROCE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.78 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0267
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) : 1.78
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.34
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 52737
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) : 0.158
REMARK 3 R VALUE (WORKING SET) : 0.157
REMARK 3 FREE R VALUE : 0.189
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2731
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) : 1.78
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.83
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3309
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 84.11
REMARK 3 BIN R VALUE (WORKING SET) : 0.1890
REMARK 3 BIN FREE R VALUE SET COUNT : 158
REMARK 3 BIN FREE R VALUE : 0.2310
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3967
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 455
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.43
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.22000
REMARK 3 B22 (A**2) : -0.04000
REMARK 3 B33 (A**2) : -0.19000
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): 0.102
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.100
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.062
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.988
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.944
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4082 ; 0.013 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 3798 ; 0.001 ; 0.015
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5566 ; 1.789 ; 1.627
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8722 ; 1.589 ; 1.576
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 548 ; 9.156 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 198 ;28.480 ;21.111
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 578 ;15.613 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 32 ;22.187 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 516 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4766 ; 0.011 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 914 ; 0.001 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 7YII COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-JUL-22.
REMARK 100 THE DEPOSITION ID IS D_1300030931.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-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 : APS
REMARK 200 BEAMLINE : 18-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.987
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : AGILENT ATLAS CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55437
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.780
REMARK 200 RESOLUTION RANGE LOW (A) : 24.340
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 1.000
REMARK 200 R MERGE (I) : 0.02900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.78
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.82
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.01000
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: HKL-3000
REMARK 200 STARTING MODEL: 4RNC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS BUFFER (PH 6.5), 25%
REMARK 280 PEG 300 (W/V), VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289.15K
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 24.33850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 65.67900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.23600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 65.67900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.33850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.23600
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ARG A 133
REMARK 465 MET B 1
REMARK 465 GLY B 275
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 GLN A 35 -158.26 -110.35
REMARK 500 SER A 101 -124.44 64.96
REMARK 500 ASP A 252 -137.99 -96.96
REMARK 500 ASP A 259 76.16 -151.57
REMARK 500 GLN B 35 -154.99 -116.73
REMARK 500 SER B 101 -120.45 57.95
REMARK 500 GLN B 242 62.26 -115.85
REMARK 500 ASP B 252 -135.58 -95.72
REMARK 500 ASP B 259 77.36 -150.77
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 7YII A 1 275 UNP A0A1B1KCC1_RHOOP
DBREF2 7YII A A0A1B1KCC1 1 275
DBREF1 7YII B 1 275 UNP A0A1B1KCC1_RHOOP
DBREF2 7YII B A0A1B1KCC1 1 275
SEQRES 1 A 275 MET ALA ILE ARG GLU THR VAL GLY VAL ASP GLY THR PRO
SEQRES 2 A 275 LEU VAL TYR SER VAL THR GLY ASP PRO ASP ALA ARG ALA
SEQRES 3 A 275 LEU VAL LEU LEU HIS GLY TRP ALA GLN SER SER LYS CYS
SEQRES 4 A 275 TRP GLY PRO GLY VAL LEU ASP GLU LEU ALA ALA ARG TYR
SEQRES 5 A 275 ARG VAL ILE ALA VAL ASP LEU ARG GLY HIS GLY TYR SER
SEQRES 6 A 275 GLY ALA PRO ASP THR GLY TYR ASP ASP SER ALA VAL TRP
SEQRES 7 A 275 ALA GLY ASP VAL ASP ALA VAL LEU THR ALA GLU GLY VAL
SEQRES 8 A 275 THR SER GLY ALA VAL LEU LEU GLY TRP SER TYR GLY GLY
SEQRES 9 A 275 LEU VAL ILE CYS ASP TYR LEU ALA SER ASN GLY THR SER
SEQRES 10 A 275 ALA VAL ASP GLY VAL VAL LEU VAL GLY ALA ILE THR SER
SEQRES 11 A 275 ILE GLY ARG GLY GLU ALA GLY GLY LYS VAL GLY ALA ALA
SEQRES 12 A 275 MET ARG ALA ALA ILE PRO GLY ALA MET SER GLU GLU PRO
SEQRES 13 A 275 ARG GLU ALA ILE ARG ALA LEU GLY ALA PHE GLY ASN ALA
SEQRES 14 A 275 LEU THR GLY PRO PRO GLU GLY LYS GLY ALA GLN SER GLN
SEQRES 15 A 275 ALA LEU PHE GLY ALA SER LEU THR THR PRO PRO ARG VAL
SEQRES 16 A 275 ARG ALA ALA LEU PHE ASN ARG SER ALA SER HIS ASP ASP
SEQRES 17 A 275 LEU LEU ARG SER LEU ASP VAL PRO VAL LEU VAL LEU HIS
SEQRES 18 A 275 GLY THR GLU ASP SER VAL VAL ASP VAL SER ALA GLY ARG
SEQRES 19 A 275 HIS ALA ALA GLU LEU ILE PRO GLN ALA ARG ALA SER PHE
SEQRES 20 A 275 TRP GLU GLY CYS ASP HIS GLY PRO PHE VAL GLU ASP PRO
SEQRES 21 A 275 GLU ARG PHE VAL LYS GLU VAL GLY GLU PHE VAL ASP ASN
SEQRES 22 A 275 LEU GLY
SEQRES 1 B 275 MET ALA ILE ARG GLU THR VAL GLY VAL ASP GLY THR PRO
SEQRES 2 B 275 LEU VAL TYR SER VAL THR GLY ASP PRO ASP ALA ARG ALA
SEQRES 3 B 275 LEU VAL LEU LEU HIS GLY TRP ALA GLN SER SER LYS CYS
SEQRES 4 B 275 TRP GLY PRO GLY VAL LEU ASP GLU LEU ALA ALA ARG TYR
SEQRES 5 B 275 ARG VAL ILE ALA VAL ASP LEU ARG GLY HIS GLY TYR SER
SEQRES 6 B 275 GLY ALA PRO ASP THR GLY TYR ASP ASP SER ALA VAL TRP
SEQRES 7 B 275 ALA GLY ASP VAL ASP ALA VAL LEU THR ALA GLU GLY VAL
SEQRES 8 B 275 THR SER GLY ALA VAL LEU LEU GLY TRP SER TYR GLY GLY
SEQRES 9 B 275 LEU VAL ILE CYS ASP TYR LEU ALA SER ASN GLY THR SER
SEQRES 10 B 275 ALA VAL ASP GLY VAL VAL LEU VAL GLY ALA ILE THR SER
SEQRES 11 B 275 ILE GLY ARG GLY GLU ALA GLY GLY LYS VAL GLY ALA ALA
SEQRES 12 B 275 MET ARG ALA ALA ILE PRO GLY ALA MET SER GLU GLU PRO
SEQRES 13 B 275 ARG GLU ALA ILE ARG ALA LEU GLY ALA PHE GLY ASN ALA
SEQRES 14 B 275 LEU THR GLY PRO PRO GLU GLY LYS GLY ALA GLN SER GLN
SEQRES 15 B 275 ALA LEU PHE GLY ALA SER LEU THR THR PRO PRO ARG VAL
SEQRES 16 B 275 ARG ALA ALA LEU PHE ASN ARG SER ALA SER HIS ASP ASP
SEQRES 17 B 275 LEU LEU ARG SER LEU ASP VAL PRO VAL LEU VAL LEU HIS
SEQRES 18 B 275 GLY THR GLU ASP SER VAL VAL ASP VAL SER ALA GLY ARG
SEQRES 19 B 275 HIS ALA ALA GLU LEU ILE PRO GLN ALA ARG ALA SER PHE
SEQRES 20 B 275 TRP GLU GLY CYS ASP HIS GLY PRO PHE VAL GLU ASP PRO
SEQRES 21 B 275 GLU ARG PHE VAL LYS GLU VAL GLY GLU PHE VAL ASP ASN
SEQRES 22 B 275 LEU GLY
FORMUL 3 HOH *455(H2 O)
HELIX 1 AA1 GLY A 41 ALA A 50 1 10
HELIX 2 AA2 ASP A 74 GLU A 89 1 16
HELIX 3 AA3 TYR A 102 GLY A 115 1 14
HELIX 4 AA4 GLU A 135 LYS A 139 5 5
HELIX 5 AA5 GLY A 141 ILE A 148 1 8
HELIX 6 AA6 PRO A 149 SER A 153 5 5
HELIX 7 AA7 GLU A 155 ALA A 165 1 11
HELIX 8 AA8 LYS A 177 THR A 191 1 15
HELIX 9 AA9 PRO A 192 LEU A 199 1 8
HELIX 10 AB1 HIS A 206 LEU A 213 1 8
HELIX 11 AB2 ASP A 229 ILE A 240 1 12
HELIX 12 AB3 GLY A 254 ASP A 259 1 6
HELIX 13 AB4 ASP A 259 ASN A 273 1 15
HELIX 14 AB5 GLY B 41 ALA B 50 1 10
HELIX 15 AB6 ASP B 74 GLU B 89 1 16
HELIX 16 AB7 TYR B 102 GLY B 115 1 14
HELIX 17 AB8 GLU B 135 LYS B 139 5 5
HELIX 18 AB9 GLY B 141 ILE B 148 1 8
HELIX 19 AC1 PRO B 149 SER B 153 5 5
HELIX 20 AC2 GLU B 155 ALA B 165 1 11
HELIX 21 AC3 LYS B 177 THR B 191 1 15
HELIX 22 AC4 PRO B 192 ASN B 201 1 10
HELIX 23 AC5 HIS B 206 SER B 212 1 7
HELIX 24 AC6 ASP B 229 ILE B 240 1 12
HELIX 25 AC7 GLY B 254 ASP B 259 1 6
HELIX 26 AC8 ASP B 259 ASN B 273 1 15
SHEET 1 AA1 8 ILE A 3 VAL A 7 0
SHEET 2 AA1 8 PRO A 13 THR A 19 -1 O TYR A 16 N ARG A 4
SHEET 3 AA1 8 ARG A 53 VAL A 57 -1 O ALA A 56 N SER A 17
SHEET 4 AA1 8 ALA A 26 LEU A 30 1 N LEU A 29 O ILE A 55
SHEET 5 AA1 8 ALA A 95 TRP A 100 1 O LEU A 98 N VAL A 28
SHEET 6 AA1 8 VAL A 119 VAL A 125 1 O VAL A 125 N GLY A 99
SHEET 7 AA1 8 VAL A 217 GLY A 222 1 O LEU A 220 N LEU A 124
SHEET 8 AA1 8 ALA A 243 TRP A 248 1 O SER A 246 N VAL A 219
SHEET 1 AA2 8 ILE B 3 VAL B 7 0
SHEET 2 AA2 8 PRO B 13 THR B 19 -1 O TYR B 16 N ARG B 4
SHEET 3 AA2 8 ARG B 53 VAL B 57 -1 O ALA B 56 N SER B 17
SHEET 4 AA2 8 ALA B 26 LEU B 30 1 N LEU B 29 O ILE B 55
SHEET 5 AA2 8 ALA B 95 TRP B 100 1 O LEU B 98 N VAL B 28
SHEET 6 AA2 8 VAL B 119 VAL B 125 1 O VAL B 125 N GLY B 99
SHEET 7 AA2 8 VAL B 217 GLY B 222 1 O LEU B 220 N LEU B 124
SHEET 8 AA2 8 ALA B 243 TRP B 248 1 O SER B 246 N VAL B 219
CISPEP 1 ILE A 148 PRO A 149 0 1.31
CISPEP 2 ILE B 148 PRO B 149 0 2.73
CRYST1 48.677 90.472 131.358 90.00 90.00 90.00 P 21 21 21 8
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 0.020544 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011053 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007613 0.00000
TER 1981 GLY A 275
TER 3969 LEU B 274
MASTER 276 0 0 26 16 0 0 6 4422 2 0 44
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