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HEADER HYDROLASE 21-MAY-08 3D7R
TITLE CRYSTAL STRUCTURE OF A PUTATIVE ESTERASE FROM STAPHYLOCOCCUS
TITLE 2 AUREUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.-.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS
SOURCE 3 USA300_TCH1516;
SOURCE 4 ORGANISM_TAXID: 451516;
SOURCE 5 GENE: USA300HOU_2331;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODONPLUS RIPL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS ESTERASE-LIKE, ALPHA/BETA FOLD, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.LAM,K.P.BATTAILE,T.CHAN,V.ROMANOV,K.LAM,M.SOLOVEYCHIK,
AUTHOR 2 J.WU-BROWN,E.F.PAI,N.Y.CHIRGADZE
REVDAT 1 09-JUN-09 3D7R 0
JRNL AUTH K.P.BATTAILE,R.LAM,T.CHAN,V.ROMANOV,K.LAM,
JRNL AUTH 2 M.SOLOVEYCHIK,J.WU-BROWN,E.F.PAI,N.Y.CHIRGADZE
JRNL TITL CRYSTAL STRUCTURE OF A PUTATIVE ESTERASE FROM
JRNL TITL 2 STAPHYLOCOCCUS AUREUS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.01 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.01
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.56
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 41116
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) : 0.160
REMARK 3 R VALUE (WORKING SET) : 0.158
REMARK 3 FREE R VALUE : 0.192
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2083
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) : 2.01
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.06
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2565
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.23
REMARK 3 BIN R VALUE (WORKING SET) : 0.1470
REMARK 3 BIN FREE R VALUE SET COUNT : 134
REMARK 3 BIN FREE R VALUE : 0.2060
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4837
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 86
REMARK 3 SOLVENT ATOMS : 304
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.45
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01000
REMARK 3 B22 (A**2) : 0.02000
REMARK 3 B33 (A**2) : -0.01000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.01000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.175
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.145
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.093
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.333
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.922
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5039 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6792 ; 1.260 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 593 ; 5.466 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 245 ;34.336 ;24.776
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 898 ;12.701 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;17.643 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 749 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3766 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2365 ; 0.208 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3443 ; 0.306 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 322 ; 0.121 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 1 ; 0.098 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 94 ; 0.226 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 21 ; 0.155 ; 0.200
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): 2985 ; 0.567 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4874 ; 1.140 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2098 ; 2.290 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1916 ; 3.702 ; 4.500
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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 9 A 304
REMARK 3 ORIGIN FOR THE GROUP (A): 39.0390 12.3330 3.4460
REMARK 3 T TENSOR
REMARK 3 T11: -0.0170 T22: -0.0260
REMARK 3 T33: -0.0136 T12: 0.0047
REMARK 3 T13: 0.0009 T23: 0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 0.3577 L22: 0.3662
REMARK 3 L33: 0.3765 L12: 0.0932
REMARK 3 L13: 0.0068 L23: 0.2092
REMARK 3 S TENSOR
REMARK 3 S11: 0.0059 S12: 0.0307 S13: -0.0062
REMARK 3 S21: 0.0242 S22: 0.0031 S23: -0.0046
REMARK 3 S31: -0.0019 S32: -0.0042 S33: -0.0090
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 9 B 303
REMARK 3 ORIGIN FOR THE GROUP (A): 65.1540 20.8500 48.5560
REMARK 3 T TENSOR
REMARK 3 T11: -0.0216 T22: -0.0212
REMARK 3 T33: -0.0166 T12: 0.0026
REMARK 3 T13: -0.0012 T23: 0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 0.4239 L22: 0.3221
REMARK 3 L33: 0.4259 L12: 0.0620
REMARK 3 L13: -0.1214 L23: -0.1171
REMARK 3 S TENSOR
REMARK 3 S11: 0.0082 S12: 0.0292 S13: 0.0170
REMARK 3 S21: 0.0301 S22: 0.0045 S23: 0.0005
REMARK 3 S31: -0.0062 S32: -0.0042 S33: -0.0126
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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: NULL
REMARK 4
REMARK 4 3D7R COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-MAY-08.
REMARK 100 THE RCSB ID CODE IS RCSB047698.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-JUN-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97930
REMARK 200 MONOCHROMATOR : SI(111) DOUBLE-CRYSTAL
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41127
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.010
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 (%) : 97.5
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.06100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 22.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.01
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.08
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.09300
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: SAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG3350, 0.1M NABR, 15MM
REMARK 280 HEXAMINE COBALT(III) CHLORIDE, CRYO-PROTECTED USING 30% DMSO,
REMARK 280 PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 MSE A -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MSE A 1
REMARK 465 ILE A 2
REMARK 465 ARG A 3
REMARK 465 ASN A 4
REMARK 465 ARG A 5
REMARK 465 VAL A 6
REMARK 465 MSE A 7
REMARK 465 ASN A 8
REMARK 465 ASN A 305
REMARK 465 ASN A 306
REMARK 465 MSE B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MSE B 1
REMARK 465 ILE B 2
REMARK 465 ARG B 3
REMARK 465 ASN B 4
REMARK 465 ARG B 5
REMARK 465 VAL B 6
REMARK 465 MSE B 7
REMARK 465 ASN B 8
REMARK 465 GLN B 304
REMARK 465 ASN B 305
REMARK 465 ASN B 306
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 ALA A 88 -34.58 -130.58
REMARK 500 SER B 180 54.97 39.68
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A1200 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 136 OE1
REMARK 620 2 HOH A1510 O 101.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B1201 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN B 136 OE1
REMARK 620 2 HOH B1510 O 101.2
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 1000
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1100
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 1200
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 1001
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 1101
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 1201
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 1400
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 1402
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 1404
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 1407
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 1408
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 1410
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 1411
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 1416
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 1417
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 1418
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 1401
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 1403
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 1405
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 1406
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 1409
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 1412
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 1413
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 1414
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 1415
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 1419
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1300
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1301
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1302
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1303
DBREF 3D7R A 1 306 UNP A8Z540 A8Z540_STAAT 1 306
DBREF 3D7R B 1 306 UNP A8Z540 A8Z540_STAAT 1 306
SEQADV 3D7R MSE A -19 UNP A8Z540 EXPRESSION TAG
SEQADV 3D7R GLY A -18 UNP A8Z540 EXPRESSION TAG
SEQADV 3D7R SER A -17 UNP A8Z540 EXPRESSION TAG
SEQADV 3D7R SER A -16 UNP A8Z540 EXPRESSION TAG
SEQADV 3D7R HIS A -15 UNP A8Z540 EXPRESSION TAG
SEQADV 3D7R HIS A -14 UNP A8Z540 EXPRESSION TAG
SEQADV 3D7R HIS A -13 UNP A8Z540 EXPRESSION TAG
SEQADV 3D7R HIS A -12 UNP A8Z540 EXPRESSION TAG
SEQADV 3D7R HIS A -11 UNP A8Z540 EXPRESSION TAG
SEQADV 3D7R HIS A -10 UNP A8Z540 EXPRESSION TAG
SEQADV 3D7R SER A -9 UNP A8Z540 EXPRESSION TAG
SEQADV 3D7R SER A -8 UNP A8Z540 EXPRESSION TAG
SEQADV 3D7R GLY A -7 UNP A8Z540 EXPRESSION TAG
SEQADV 3D7R LEU A -6 UNP A8Z540 EXPRESSION TAG
SEQADV 3D7R VAL A -5 UNP A8Z540 EXPRESSION TAG
SEQADV 3D7R PRO A -4 UNP A8Z540 EXPRESSION TAG
SEQADV 3D7R ARG A -3 UNP A8Z540 EXPRESSION TAG
SEQADV 3D7R GLY A -2 UNP A8Z540 EXPRESSION TAG
SEQADV 3D7R SER A -1 UNP A8Z540 EXPRESSION TAG
SEQADV 3D7R HIS A 0 UNP A8Z540 EXPRESSION TAG
SEQADV 3D7R MSE B -19 UNP A8Z540 EXPRESSION TAG
SEQADV 3D7R GLY B -18 UNP A8Z540 EXPRESSION TAG
SEQADV 3D7R SER B -17 UNP A8Z540 EXPRESSION TAG
SEQADV 3D7R SER B -16 UNP A8Z540 EXPRESSION TAG
SEQADV 3D7R HIS B -15 UNP A8Z540 EXPRESSION TAG
SEQADV 3D7R HIS B -14 UNP A8Z540 EXPRESSION TAG
SEQADV 3D7R HIS B -13 UNP A8Z540 EXPRESSION TAG
SEQADV 3D7R HIS B -12 UNP A8Z540 EXPRESSION TAG
SEQADV 3D7R HIS B -11 UNP A8Z540 EXPRESSION TAG
SEQADV 3D7R HIS B -10 UNP A8Z540 EXPRESSION TAG
SEQADV 3D7R SER B -9 UNP A8Z540 EXPRESSION TAG
SEQADV 3D7R SER B -8 UNP A8Z540 EXPRESSION TAG
SEQADV 3D7R GLY B -7 UNP A8Z540 EXPRESSION TAG
SEQADV 3D7R LEU B -6 UNP A8Z540 EXPRESSION TAG
SEQADV 3D7R VAL B -5 UNP A8Z540 EXPRESSION TAG
SEQADV 3D7R PRO B -4 UNP A8Z540 EXPRESSION TAG
SEQADV 3D7R ARG B -3 UNP A8Z540 EXPRESSION TAG
SEQADV 3D7R GLY B -2 UNP A8Z540 EXPRESSION TAG
SEQADV 3D7R SER B -1 UNP A8Z540 EXPRESSION TAG
SEQADV 3D7R HIS B 0 UNP A8Z540 EXPRESSION TAG
SEQRES 1 A 326 MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 326 LEU VAL PRO ARG GLY SER HIS MSE ILE ARG ASN ARG VAL
SEQRES 3 A 326 MSE ASN SER VAL VAL ASN LYS TYR LEU LEU HIS ASN ARG
SEQRES 4 A 326 SER ILE MSE PHE LYS ASN ASP GLN ASP VAL GLU ARG PHE
SEQRES 5 A 326 PHE TYR LYS ARG GLU ILE GLU ASN ARG LYS LYS HIS LYS
SEQRES 6 A 326 GLN PRO SER THR LEU ASN VAL LYS ALA ASN LEU GLU LYS
SEQRES 7 A 326 LEU SER LEU ASP ASP MSE GLN VAL PHE ARG PHE ASN PHE
SEQRES 8 A 326 ARG HIS GLN ILE ASP LYS LYS ILE LEU TYR ILE HIS GLY
SEQRES 9 A 326 GLY PHE ASN ALA LEU GLN PRO SER PRO PHE HIS TRP ARG
SEQRES 10 A 326 LEU LEU ASP LYS ILE THR LEU SER THR LEU TYR GLU VAL
SEQRES 11 A 326 VAL LEU PRO ILE TYR PRO LYS THR PRO GLU PHE HIS ILE
SEQRES 12 A 326 ASP ASP THR PHE GLN ALA ILE GLN ARG VAL TYR ASP GLN
SEQRES 13 A 326 LEU VAL SER GLU VAL GLY HIS GLN ASN VAL VAL VAL MSE
SEQRES 14 A 326 GLY ASP GLY SER GLY GLY ALA LEU ALA LEU SER PHE VAL
SEQRES 15 A 326 GLN SER LEU LEU ASP ASN GLN GLN PRO LEU PRO ASN LYS
SEQRES 16 A 326 LEU TYR LEU ILE SER PRO ILE LEU ASP ALA THR LEU SER
SEQRES 17 A 326 ASN LYS ASP ILE SER ASP ALA LEU ILE GLU GLN ASP ALA
SEQRES 18 A 326 VAL LEU SER GLN PHE GLY VAL ASN GLU ILE MSE LYS LYS
SEQRES 19 A 326 TRP ALA ASN GLY LEU PRO LEU THR ASP LYS ARG ILE SER
SEQRES 20 A 326 PRO ILE ASN GLY THR ILE GLU GLY LEU PRO PRO VAL TYR
SEQRES 21 A 326 MSE PHE GLY GLY GLY ARG GLU MSE THR HIS PRO ASP MSE
SEQRES 22 A 326 LYS LEU PHE GLU GLN MSE MSE LEU GLN HIS HIS GLN TYR
SEQRES 23 A 326 ILE GLU PHE TYR ASP TYR PRO LYS MSE VAL HIS ASP PHE
SEQRES 24 A 326 PRO ILE TYR PRO ILE ARG GLN SER HIS LYS ALA ILE LYS
SEQRES 25 A 326 GLN ILE ALA LYS SER ILE ASP GLU ASP VAL THR GLN ASN
SEQRES 26 A 326 ASN
SEQRES 1 B 326 MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 326 LEU VAL PRO ARG GLY SER HIS MSE ILE ARG ASN ARG VAL
SEQRES 3 B 326 MSE ASN SER VAL VAL ASN LYS TYR LEU LEU HIS ASN ARG
SEQRES 4 B 326 SER ILE MSE PHE LYS ASN ASP GLN ASP VAL GLU ARG PHE
SEQRES 5 B 326 PHE TYR LYS ARG GLU ILE GLU ASN ARG LYS LYS HIS LYS
SEQRES 6 B 326 GLN PRO SER THR LEU ASN VAL LYS ALA ASN LEU GLU LYS
SEQRES 7 B 326 LEU SER LEU ASP ASP MSE GLN VAL PHE ARG PHE ASN PHE
SEQRES 8 B 326 ARG HIS GLN ILE ASP LYS LYS ILE LEU TYR ILE HIS GLY
SEQRES 9 B 326 GLY PHE ASN ALA LEU GLN PRO SER PRO PHE HIS TRP ARG
SEQRES 10 B 326 LEU LEU ASP LYS ILE THR LEU SER THR LEU TYR GLU VAL
SEQRES 11 B 326 VAL LEU PRO ILE TYR PRO LYS THR PRO GLU PHE HIS ILE
SEQRES 12 B 326 ASP ASP THR PHE GLN ALA ILE GLN ARG VAL TYR ASP GLN
SEQRES 13 B 326 LEU VAL SER GLU VAL GLY HIS GLN ASN VAL VAL VAL MSE
SEQRES 14 B 326 GLY ASP GLY SER GLY GLY ALA LEU ALA LEU SER PHE VAL
SEQRES 15 B 326 GLN SER LEU LEU ASP ASN GLN GLN PRO LEU PRO ASN LYS
SEQRES 16 B 326 LEU TYR LEU ILE SER PRO ILE LEU ASP ALA THR LEU SER
SEQRES 17 B 326 ASN LYS ASP ILE SER ASP ALA LEU ILE GLU GLN ASP ALA
SEQRES 18 B 326 VAL LEU SER GLN PHE GLY VAL ASN GLU ILE MSE LYS LYS
SEQRES 19 B 326 TRP ALA ASN GLY LEU PRO LEU THR ASP LYS ARG ILE SER
SEQRES 20 B 326 PRO ILE ASN GLY THR ILE GLU GLY LEU PRO PRO VAL TYR
SEQRES 21 B 326 MSE PHE GLY GLY GLY ARG GLU MSE THR HIS PRO ASP MSE
SEQRES 22 B 326 LYS LEU PHE GLU GLN MSE MSE LEU GLN HIS HIS GLN TYR
SEQRES 23 B 326 ILE GLU PHE TYR ASP TYR PRO LYS MSE VAL HIS ASP PHE
SEQRES 24 B 326 PRO ILE TYR PRO ILE ARG GLN SER HIS LYS ALA ILE LYS
SEQRES 25 B 326 GLN ILE ALA LYS SER ILE ASP GLU ASP VAL THR GLN ASN
SEQRES 26 B 326 ASN
MODRES 3D7R MSE A 22 MET SELENOMETHIONINE
MODRES 3D7R MSE A 64 MET SELENOMETHIONINE
MODRES 3D7R MSE A 149 MET SELENOMETHIONINE
MODRES 3D7R MSE A 212 MET SELENOMETHIONINE
MODRES 3D7R MSE A 241 MET SELENOMETHIONINE
MODRES 3D7R MSE A 248 MET SELENOMETHIONINE
MODRES 3D7R MSE A 253 MET SELENOMETHIONINE
MODRES 3D7R MSE A 259 MET SELENOMETHIONINE
MODRES 3D7R MSE A 260 MET SELENOMETHIONINE
MODRES 3D7R MSE A 275 MET SELENOMETHIONINE
MODRES 3D7R MSE B 22 MET SELENOMETHIONINE
MODRES 3D7R MSE B 64 MET SELENOMETHIONINE
MODRES 3D7R MSE B 149 MET SELENOMETHIONINE
MODRES 3D7R MSE B 212 MET SELENOMETHIONINE
MODRES 3D7R MSE B 241 MET SELENOMETHIONINE
MODRES 3D7R MSE B 248 MET SELENOMETHIONINE
MODRES 3D7R MSE B 253 MET SELENOMETHIONINE
MODRES 3D7R MSE B 259 MET SELENOMETHIONINE
MODRES 3D7R MSE B 260 MET SELENOMETHIONINE
MODRES 3D7R MSE B 275 MET SELENOMETHIONINE
HET MSE A 22 8
HET MSE A 64 8
HET MSE A 149 8
HET MSE A 212 8
HET MSE A 241 8
HET MSE A 248 8
HET MSE A 253 8
HET MSE A 259 8
HET MSE A 260 8
HET MSE A 275 8
HET MSE B 22 8
HET MSE B 64 8
HET MSE B 149 8
HET MSE B 212 8
HET MSE B 241 8
HET MSE B 248 8
HET MSE B 253 8
HET MSE B 259 8
HET MSE B 260 8
HET MSE B 275 8
HET BR A1000 1
HET CL A1100 1
HET NA A1200 1
HET BR B1001 1
HET CL B1101 1
HET NA B1201 1
HET DMS A1400 4
HET DMS A1402 4
HET DMS A1404 4
HET DMS A1407 4
HET DMS A1408 4
HET DMS A1410 4
HET DMS A1411 4
HET DMS A1416 4
HET DMS A1417 4
HET DMS A1418 4
HET DMS B1401 4
HET DMS B1403 4
HET DMS B1405 4
HET DMS B1406 4
HET DMS B1409 4
HET DMS B1412 4
HET DMS B1413 4
HET DMS B1414 4
HET DMS B1415 4
HET DMS B1419 4
HET GOL A1300 6
HET GOL A1301 6
HET GOL B1302 6
HET GOL B1303 6
HETNAM MSE SELENOMETHIONINE
HETNAM BR BROMIDE ION
HETNAM CL CHLORIDE ION
HETNAM NA SODIUM ION
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM GOL GLYCEROL
FORMUL 1 MSE 20(C5 H11 N O2 SE)
FORMUL 3 BR 2(BR 1-)
FORMUL 4 CL 2(CL 1-)
FORMUL 5 NA 2(NA 1+)
FORMUL 9 DMS 20(C2 H6 O S)
FORMUL 29 GOL 4(C3 H8 O3)
FORMUL 33 HOH *280(H2 O)
HELIX 1 1 SER A 9 TYR A 14 1 6
HELIX 2 2 LEU A 16 SER A 20 5 5
HELIX 3 3 ASN A 25 LYS A 42 1 18
HELIX 4 4 SER A 92 LEU A 107 1 16
HELIX 5 5 HIS A 122 GLY A 142 1 21
HELIX 6 6 GLY A 152 ASN A 168 1 17
HELIX 7 7 SER A 193 ASP A 200 1 8
HELIX 8 8 SER A 204 ASN A 217 1 14
HELIX 9 9 SER A 227 GLY A 231 5 5
HELIX 10 10 THR A 249 HIS A 263 1 15
HELIX 11 11 ASP A 278 TYR A 282 5 5
HELIX 12 12 ILE A 284 ASP A 299 1 16
HELIX 13 13 SER B 9 TYR B 14 1 6
HELIX 14 14 LEU B 16 SER B 20 5 5
HELIX 15 15 ASN B 25 ASN B 40 1 16
HELIX 16 16 SER B 92 LEU B 107 1 16
HELIX 17 17 HIS B 122 GLY B 142 1 21
HELIX 18 18 GLY B 152 ASN B 168 1 17
HELIX 19 19 SER B 193 ASP B 200 1 8
HELIX 20 20 SER B 204 ASN B 217 1 14
HELIX 21 21 SER B 227 GLY B 231 5 5
HELIX 22 22 THR B 249 HIS B 263 1 15
HELIX 23 23 ASP B 278 TYR B 282 5 5
HELIX 24 24 ILE B 284 ASP B 299 1 16
SHEET 1 A 8 ASN A 55 LEU A 61 0
SHEET 2 A 8 MSE A 64 ASN A 70 -1 O ARG A 68 N GLU A 57
SHEET 3 A 8 GLU A 109 PRO A 113 -1 O LEU A 112 N PHE A 67
SHEET 4 A 8 LYS A 78 ILE A 82 1 N ILE A 79 O VAL A 111
SHEET 5 A 8 VAL A 146 ASP A 151 1 O MSE A 149 N ILE A 82
SHEET 6 A 8 LYS A 175 ILE A 179 1 O TYR A 177 N VAL A 148
SHEET 7 A 8 VAL A 239 GLY A 244 1 O PHE A 242 N LEU A 178
SHEET 8 A 8 ILE A 267 TYR A 272 1 O TYR A 270 N MSE A 241
SHEET 1 B 8 ASN B 55 LEU B 61 0
SHEET 2 B 8 MSE B 64 ASN B 70 -1 O ARG B 68 N GLU B 57
SHEET 3 B 8 GLU B 109 PRO B 113 -1 O LEU B 112 N PHE B 67
SHEET 4 B 8 LYS B 78 ILE B 82 1 N ILE B 79 O VAL B 111
SHEET 5 B 8 VAL B 146 ASP B 151 1 O MSE B 149 N ILE B 82
SHEET 6 B 8 LYS B 175 ILE B 179 1 O TYR B 177 N VAL B 148
SHEET 7 B 8 VAL B 239 GLY B 244 1 O PHE B 242 N LEU B 178
SHEET 8 B 8 ILE B 267 TYR B 272 1 O GLU B 268 N MSE B 241
LINK C ILE A 21 N MSE A 22 1555 1555 1.33
LINK C MSE A 22 N PHE A 23 1555 1555 1.34
LINK C ASP A 63 N MSE A 64 1555 1555 1.33
LINK C MSE A 64 N GLN A 65 1555 1555 1.33
LINK C VAL A 148 N MSE A 149 1555 1555 1.33
LINK C MSE A 149 N GLY A 150 1555 1555 1.33
LINK C ILE A 211 N MSE A 212 1555 1555 1.32
LINK C MSE A 212 N LYS A 213 1555 1555 1.33
LINK C TYR A 240 N MSE A 241 1555 1555 1.32
LINK C MSE A 241 N PHE A 242 1555 1555 1.33
LINK C GLU A 247 N MSE A 248 1555 1555 1.34
LINK C MSE A 248 N THR A 249 1555 1555 1.33
LINK C ASP A 252 N MSE A 253 1555 1555 1.33
LINK C MSE A 253 N LYS A 254 1555 1555 1.33
LINK C GLN A 258 N MSE A 259 1555 1555 1.34
LINK C MSE A 259 N MSE A 260 1555 1555 1.33
LINK C MSE A 260 N LEU A 261 1555 1555 1.33
LINK C LYS A 274 N MSE A 275 1555 1555 1.33
LINK C MSE A 275 N VAL A 276 1555 1555 1.34
LINK C ILE B 21 N MSE B 22 1555 1555 1.33
LINK C MSE B 22 N PHE B 23 1555 1555 1.33
LINK C ASP B 63 N MSE B 64 1555 1555 1.33
LINK C MSE B 64 N GLN B 65 1555 1555 1.33
LINK C VAL B 148 N MSE B 149 1555 1555 1.33
LINK C MSE B 149 N GLY B 150 1555 1555 1.33
LINK C ILE B 211 N MSE B 212 1555 1555 1.33
LINK C MSE B 212 N LYS B 213 1555 1555 1.34
LINK C TYR B 240 N MSE B 241 1555 1555 1.32
LINK C MSE B 241 N PHE B 242 1555 1555 1.33
LINK C GLU B 247 N MSE B 248 1555 1555 1.34
LINK C MSE B 248 N THR B 249 1555 1555 1.34
LINK C ASP B 252 N MSE B 253 1555 1555 1.33
LINK C MSE B 253 N LYS B 254 1555 1555 1.33
LINK C GLN B 258 N MSE B 259 1555 1555 1.33
LINK C MSE B 259 N MSE B 260 1555 1555 1.33
LINK C MSE B 260 N LEU B 261 1555 1555 1.34
LINK C LYS B 274 N MSE B 275 1555 1555 1.33
LINK C MSE B 275 N VAL B 276 1555 1555 1.33
LINK OE1 GLN A 136 NA NA A1200 1555 1555 2.31
LINK OE1 GLN B 136 NA NA B1201 1555 1555 2.58
LINK NA NA A1200 O HOH A1510 1555 1555 2.87
LINK NA NA B1201 O HOH B1510 1555 1555 2.82
CISPEP 1 THR A 118 PRO A 119 0 9.16
CISPEP 2 THR B 118 PRO B 119 0 4.88
SITE 1 AC1 1 LYS A 274
SITE 1 AC2 2 GLN A 205 HOH A1511
SITE 1 AC3 4 VAL A 66 ARG A 68 GLN A 136 HOH A1510
SITE 1 AC4 1 LYS B 274
SITE 1 AC5 1 GLN B 205
SITE 1 AC6 4 VAL B 66 ARG B 68 GLN B 136 HOH B1510
SITE 1 AC7 4 ASP A 271 TYR A 272 LYS A 289 GLN A 293
SITE 1 AC8 5 LEU A 15 LEU A 16 SER A 20 DMS A1407
SITE 2 AC8 5 HOH A1447
SITE 1 AC9 4 PHE A 127 GLN A 131 SER A 164 HOH A1550
SITE 1 BC1 8 TYR A 14 LEU A 16 SER A 92 PHE A 94
SITE 2 BC1 8 ILE A 281 TYR A 282 DMS A1402 HOH A1472
SITE 1 BC2 5 SER A 20 MSE A 22 PHE A 23 ASP A 28
SITE 2 BC2 5 HOH A1489
SITE 1 BC3 7 PRO A 47 THR A 49 PRO A 93 PHE A 94
SITE 2 BC3 7 ASP A 167 ASN A 168 HOH A1560
SITE 1 BC4 3 HIS A 73 ILE A 75 ASP A 76
SITE 1 BC5 4 ILE A 123 ASP A 124 ASN A 217 HOH A1495
SITE 1 BC6 7 ARG A 97 LEU A 98 LYS A 101 PRO A 280
SITE 2 BC6 7 TYR A 282 SER A 287 HIS A 288
SITE 1 BC7 4 LYS A 43 HIS A 44 LYS A 45 HOH A1455
SITE 1 BC8 4 ASP B 271 TYR B 272 LYS B 289 GLN B 293
SITE 1 BC9 5 LEU B 15 LEU B 16 ARG B 19 SER B 20
SITE 2 BC9 5 HOH B1443
SITE 1 CC1 4 PHE B 127 GLN B 131 SER B 164 HOH B1548
SITE 1 CC2 6 ARG B 41 TYR B 240 TYR B 266 GLU B 300
SITE 2 CC2 6 VAL B 302 THR B 303
SITE 1 CC3 6 ASN B 40 LYS B 42 LYS B 43 GLN B 65
SITE 2 CC3 6 GLN B 90 HOH B1454
SITE 1 CC4 9 ARG B 97 LEU B 98 LYS B 101 PRO B 280
SITE 2 CC4 9 ILE B 281 TYR B 282 PRO B 283 SER B 287
SITE 3 CC4 9 HOH B1518
SITE 1 CC5 3 HIS B 73 ILE B 75 ASP B 76
SITE 1 CC6 8 TYR B 14 LEU B 16 SER B 92 PHE B 94
SITE 2 CC6 8 ILE B 281 TYR B 282 GOL B1302 HOH B1488
SITE 1 CC7 5 ILE B 123 ASP B 124 ALA B 216 ASN B 217
SITE 2 CC7 5 HOH B1505
SITE 1 CC8 5 LYS B 42 LYS B 43 HIS B 44 LYS B 45
SITE 2 CC8 5 HOH B1475
SITE 1 CC9 9 ARG A 41 PHE A 121 LEU A 261 HIS A 264
SITE 2 CC9 9 HOH A1448 HOH A1459 HOH A1466 HOH A1479
SITE 3 CC9 9 HOH A1543
SITE 1 DC1 4 SER A 48 LEU A 50 ASN A 51 GLN A 170
SITE 1 DC2 5 TYR B 14 PHE B 94 ASP B 167 LYS B 224
SITE 2 DC2 5 DMS B1414
SITE 1 DC3 5 SER B 48 THR B 49 LEU B 50 ASN B 51
SITE 2 DC3 5 GLN B 170
CRYST1 41.888 46.412 91.688 80.82 89.97 69.51 P 1 2
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 0.023873 -0.008922 0.001528 0.00000
SCALE2 0.000000 0.023002 -0.003972 0.00000
SCALE3 0.000000 0.000000 0.011068 0.00000
TER 2424 GLN A 304
TER 4839 THR B 303
MASTER 462 0 50 24 16 0 47 6 5227 2 306 52
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