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HEADER HYDROLASE 24-JAN-17 5MXP
TITLE HALOALKANE DEHALOGENASE DMXA FROM MARINOBACTER SP. ELB17 POSSESSING A
TITLE 2 UNIQUE CATALYTIC RESIDUE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: DMXA;
COMPND 5 EC: 3.8.1.5;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MARINOBACTER SP. ELB17;
SOURCE 3 ORGANISM_TAXID: 270374;
SOURCE 4 GENE: MELB17_23105;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: DH5A;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21B
KEYWDS HYDROLASE, THERMOSTABLE ENZYME, DISULFIDE BRIDGE, UNIQUE CATALYTIC
KEYWDS 2 RESIDUE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.TRATSIAK,P.REZACOVA,T.PRUDNIKOVA
REVDAT 1 25-JUL-18 5MXP 0
JRNL AUTH L.CHRAST,K.TRATSIAK,L.DANIEL,T.PRUDNIKOVA,J.BREZOVSKY,
JRNL AUTH 2 I.K.SMATANOVA,R.CHALOUPKOVA,J.DAMBORSKY
JRNL TITL STRUCTURAL BASIS OF PARADOXICALLY HIGH THERMOSTABILITY OF
JRNL TITL 2 DEHALOGENASE FROM PSYCHROPHILIC BACTERIUM
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 75.26
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 86980
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) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.173
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4589
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) : 1.45
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.49
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6373
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.91
REMARK 3 BIN R VALUE (WORKING SET) : 0.2800
REMARK 3 BIN FREE R VALUE SET COUNT : 329
REMARK 3 BIN FREE R VALUE : 0.3050
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4770
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 599
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.05
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.62
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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): 0.074
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.079
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.062
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.379
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5017 ; 0.019 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4500 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6827 ; 1.927 ; 1.950
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10461 ; 1.098 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 610 ; 5.845 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 258 ;31.769 ;23.566
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 810 ;13.151 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 38 ;19.918 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 698 ; 0.125 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5649 ; 0.012 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1081 ; 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): 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 : 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 3 A 296
REMARK 3 ORIGIN FOR THE GROUP (A): -40.3560 18.3730 55.9660
REMARK 3 T TENSOR
REMARK 3 T11: 0.1447 T22: 0.0013
REMARK 3 T33: 0.0193 T12: 0.0006
REMARK 3 T13: 0.0026 T23: -0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 0.8133 L22: 0.8861
REMARK 3 L33: 1.0560 L12: 0.0100
REMARK 3 L13: -0.2043 L23: -0.1097
REMARK 3 S TENSOR
REMARK 3 S11: -0.0010 S12: -0.0115 S13: 0.0270
REMARK 3 S21: 0.0504 S22: 0.0276 S23: -0.0631
REMARK 3 S31: -0.1091 S32: 0.0071 S33: -0.0267
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 3 B 296
REMARK 3 ORIGIN FOR THE GROUP (A): -19.3180 17.5140 19.6250
REMARK 3 T TENSOR
REMARK 3 T11: 0.1300 T22: 0.0009
REMARK 3 T33: 0.0293 T12: 0.0076
REMARK 3 T13: 0.0041 T23: -0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 1.3004 L22: 0.9037
REMARK 3 L33: 1.4580 L12: 0.2021
REMARK 3 L13: -0.5626 L23: -0.2397
REMARK 3 S TENSOR
REMARK 3 S11: 0.0220 S12: -0.0206 S13: 0.0581
REMARK 3 S21: 0.0276 S22: -0.0081 S23: 0.0310
REMARK 3 S31: 0.0176 S32: 0.0211 S33: -0.0138
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.70
REMARK 3 SHRINKAGE RADIUS : 0.70
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: U VALUES : WITH TLS ADDED HYDROGENS
REMARK 3 HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 4
REMARK 4 5MXP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-JAN-17.
REMARK 100 THE DEPOSITION ID IS D_1200003057.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-JUL-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9724
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : SILICON PIXEL ARRAY DETECTOR
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS 2013-03-30
REMARK 200 DATA SCALING SOFTWARE : XDS 2013-03-30
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 86980
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 5.280
REMARK 200 R MERGE (I) : 0.11200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.0200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.52
REMARK 200 R MERGE FOR SHELL (I) : 0.62100
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: NULL
REMARK 200 STARTING MODEL: 4E46
REMARK 200
REMARK 200 REMARK: RHOMBOHEDRAL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 34.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM ACETATE, 30%(W/V) PEG
REMARK 280 4000 AND 0.1M SODIUM CITRATE TRIBASIC DIHYDRATE, ADDITIONALLY
REMARK 280 ADDED SARCOSINE, PH 5.6, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 21.68550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 75.25700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.17150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 75.25700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.68550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.17150
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: 3270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -96.0 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 THR A 2
REMARK 465 HIS A 297
REMARK 465 HIS A 298
REMARK 465 HIS A 299
REMARK 465 HIS A 300
REMARK 465 HIS A 301
REMARK 465 HIS A 302
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 HIS B 297
REMARK 465 HIS B 298
REMARK 465 HIS B 299
REMARK 465 HIS B 300
REMARK 465 HIS B 301
REMARK 465 HIS B 302
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 O HOH A 555 O HOH A 577 2.12
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 TYR A 190 CE1 TYR A 190 CZ -0.082
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 48 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ASP A 72 CB - CG - OD1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ARG A 85 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ASP A 97 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 TYR A 190 CB - CG - CD2 ANGL. DEV. = 4.8 DEGREES
REMARK 500 TYR A 190 CB - CG - CD1 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ASP B 17 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP B 75 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ASP B 81 CB - CG - OD1 ANGL. DEV. = 5.6 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 A 8 30.85 -98.14
REMARK 500 PRO A 10 48.54 -93.88
REMARK 500 PRO A 41 55.34 -106.52
REMARK 500 THR A 42 -159.75 -104.16
REMARK 500 LYS A 73 77.18 -113.53
REMARK 500 ASP A 105 -134.06 52.68
REMARK 500 LEU A 132 -106.24 -107.73
REMARK 500 ASN A 172 -60.05 -122.86
REMARK 500 PHE A 246 -74.16 -147.00
REMARK 500 LEU A 272 -95.19 -112.86
REMARK 500 PRO B 10 46.42 -93.84
REMARK 500 PRO B 41 55.89 -110.92
REMARK 500 THR B 42 -159.82 -104.15
REMARK 500 LYS B 73 75.17 -115.55
REMARK 500 ASP B 105 -132.81 49.54
REMARK 500 LEU B 132 -102.42 -107.45
REMARK 500 PHE B 246 -74.89 -147.12
REMARK 500 LEU B 272 -97.02 -117.79
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 A 403 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU A 19 O
REMARK 620 2 SER A 21 OG 120.9
REMARK 620 3 TYR A 86 OH 100.3 110.8
REMARK 620 4 HOH A 796 O 109.7 107.2 107.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 404 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 142 OD2
REMARK 620 2 PHE A 246 O 101.9
REMARK 620 3 HOH A 720 O 99.6 120.1
REMARK 620 4 HOH A 799 O 111.5 112.1 110.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 407 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU B 19 O
REMARK 620 2 SER B 21 OG 119.3
REMARK 620 3 TYR B 86 OH 97.3 115.8
REMARK 620 4 HOH B 778 O 112.1 104.0 108.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 404 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR B 114 OH
REMARK 620 2 HOH B 595 O 126.3
REMARK 620 3 HOH B 529 O 95.5 124.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 402 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 142 OD2
REMARK 620 2 THR B 145 OG1 100.5
REMARK 620 3 HOH B 678 O 83.1 92.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 403 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG B 257 O
REMARK 620 2 LEU B 260 O 95.8
REMARK 620 3 HOH B 703 O 127.7 105.9
REMARK 620 4 HOH B 759 O 107.0 131.3 93.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 403 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG B 257 O
REMARK 620 2 LEU B 260 O 87.2
REMARK 620 3 HOH B 759 O 98.5 134.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 405 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU B 263 O
REMARK 620 2 HOH B 730 O 109.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 406 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 606 O
REMARK 620 2 HOH A 589 O 119.5
REMARK 620 3 HOH A 592 O 130.6 108.1
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 407
DBREF 5MXP A 1 296 UNP A3JB27 A3JB27_9ALTE 1 296
DBREF 5MXP B 1 296 UNP A3JB27 A3JB27_9ALTE 1 296
SEQADV 5MXP HIS A 297 UNP A3JB27 EXPRESSION TAG
SEQADV 5MXP HIS A 298 UNP A3JB27 EXPRESSION TAG
SEQADV 5MXP HIS A 299 UNP A3JB27 EXPRESSION TAG
SEQADV 5MXP HIS A 300 UNP A3JB27 EXPRESSION TAG
SEQADV 5MXP HIS A 301 UNP A3JB27 EXPRESSION TAG
SEQADV 5MXP HIS A 302 UNP A3JB27 EXPRESSION TAG
SEQADV 5MXP HIS B 297 UNP A3JB27 EXPRESSION TAG
SEQADV 5MXP HIS B 298 UNP A3JB27 EXPRESSION TAG
SEQADV 5MXP HIS B 299 UNP A3JB27 EXPRESSION TAG
SEQADV 5MXP HIS B 300 UNP A3JB27 EXPRESSION TAG
SEQADV 5MXP HIS B 301 UNP A3JB27 EXPRESSION TAG
SEQADV 5MXP HIS B 302 UNP A3JB27 EXPRESSION TAG
SEQRES 1 A 302 MET THR THR GLN LYS PRO ALA ASP PHE PRO TYR PRO SER
SEQRES 2 A 302 HIS PHE ALA ASP VAL LEU GLY SER ARG MET HIS TYR VAL
SEQRES 3 A 302 GLU HIS GLY ASN GLY ASP PRO LEU LEU PHE LEU HIS GLY
SEQRES 4 A 302 GLN PRO THR TRP SER TYR LEU TRP ARG LYS VAL LEU PRO
SEQRES 5 A 302 GLU LEU GLU GLY LYS GLY ARG LEU ILE ALA VAL ASP LEU
SEQRES 6 A 302 ILE GLY TYR GLY MET SER ASP LYS PRO ASP ILE PRO TYR
SEQRES 7 A 302 ASP ILE ASP ASP HIS ILE ARG TYR LEU ASP GLY PHE ILE
SEQRES 8 A 302 GLU ALA LEU GLY LEU ASP ARG ILE THR ILE VAL CYS HIS
SEQRES 9 A 302 ASP TRP GLY SER PHE PHE GLY PHE HIS TYR ALA HIS ARG
SEQRES 10 A 302 HIS PRO GLU ARG ILE LYS GLY LEU ALA PHE MET GLU ALA
SEQRES 11 A 302 MET LEU ASN PRO ILE PRO GLY TYR ASP ALA PHE ASP PRO
SEQRES 12 A 302 GLN THR ARG ALA PHE PHE GLN THR LEU ARG SER SER GLN
SEQRES 13 A 302 ALA ASN ALA GLU ARG MET MET MET ASP GLU ASN GLN PHE
SEQRES 14 A 302 VAL GLU ASN ILE LEU PRO ALA MET ILE CYS ARG PRO LEU
SEQRES 15 A 302 GLU ARG GLN GLU LEU ASP ALA TYR ARG ALA PRO TRP THR
SEQRES 16 A 302 ASP ARG GLN SER ARG ARG ILE LEU CYS THR PHE PRO GLN
SEQRES 17 A 302 ASN LEU CYS ILE GLY LYS GLU PRO ALA SER VAL TYR ARG
SEQRES 18 A 302 MET GLN THR ALA TYR ILE GLU TRP LEU GLY GLN THR ASP
SEQRES 19 A 302 LEU PRO LYS LEU LEU ILE HIS ALA GLU PRO GLY PHE LEU
SEQRES 20 A 302 ILE PRO ALA PRO ALA VAL ASP GLN TYR ARG GLN GLN LEU
SEQRES 21 A 302 PRO ASN LEU GLU THR ALA PHE VAL GLY SER GLY LEU HIS
SEQRES 22 A 302 TYR ILE GLN GLU ASP GLN PRO GLN LYS ILE GLY GLN ALA
SEQRES 23 A 302 ILE ALA GLN TRP MET ASP ARG CYS GLY LEU HIS HIS HIS
SEQRES 24 A 302 HIS HIS HIS
SEQRES 1 B 302 MET THR THR GLN LYS PRO ALA ASP PHE PRO TYR PRO SER
SEQRES 2 B 302 HIS PHE ALA ASP VAL LEU GLY SER ARG MET HIS TYR VAL
SEQRES 3 B 302 GLU HIS GLY ASN GLY ASP PRO LEU LEU PHE LEU HIS GLY
SEQRES 4 B 302 GLN PRO THR TRP SER TYR LEU TRP ARG LYS VAL LEU PRO
SEQRES 5 B 302 GLU LEU GLU GLY LYS GLY ARG LEU ILE ALA VAL ASP LEU
SEQRES 6 B 302 ILE GLY TYR GLY MET SER ASP LYS PRO ASP ILE PRO TYR
SEQRES 7 B 302 ASP ILE ASP ASP HIS ILE ARG TYR LEU ASP GLY PHE ILE
SEQRES 8 B 302 GLU ALA LEU GLY LEU ASP ARG ILE THR ILE VAL CYS HIS
SEQRES 9 B 302 ASP TRP GLY SER PHE PHE GLY PHE HIS TYR ALA HIS ARG
SEQRES 10 B 302 HIS PRO GLU ARG ILE LYS GLY LEU ALA PHE MET GLU ALA
SEQRES 11 B 302 MET LEU ASN PRO ILE PRO GLY TYR ASP ALA PHE ASP PRO
SEQRES 12 B 302 GLN THR ARG ALA PHE PHE GLN THR LEU ARG SER SER GLN
SEQRES 13 B 302 ALA ASN ALA GLU ARG MET MET MET ASP GLU ASN GLN PHE
SEQRES 14 B 302 VAL GLU ASN ILE LEU PRO ALA MET ILE CYS ARG PRO LEU
SEQRES 15 B 302 GLU ARG GLN GLU LEU ASP ALA TYR ARG ALA PRO TRP THR
SEQRES 16 B 302 ASP ARG GLN SER ARG ARG ILE LEU CYS THR PHE PRO GLN
SEQRES 17 B 302 ASN LEU CYS ILE GLY LYS GLU PRO ALA SER VAL TYR ARG
SEQRES 18 B 302 MET GLN THR ALA TYR ILE GLU TRP LEU GLY GLN THR ASP
SEQRES 19 B 302 LEU PRO LYS LEU LEU ILE HIS ALA GLU PRO GLY PHE LEU
SEQRES 20 B 302 ILE PRO ALA PRO ALA VAL ASP GLN TYR ARG GLN GLN LEU
SEQRES 21 B 302 PRO ASN LEU GLU THR ALA PHE VAL GLY SER GLY LEU HIS
SEQRES 22 B 302 TYR ILE GLN GLU ASP GLN PRO GLN LYS ILE GLY GLN ALA
SEQRES 23 B 302 ILE ALA GLN TRP MET ASP ARG CYS GLY LEU HIS HIS HIS
SEQRES 24 B 302 HIS HIS HIS
HET ACT A 401 4
HET ACT A 402 4
HET NA A 403 1
HET NA A 404 1
HET ACT B 401 4
HET NA B 402 1
HET NA B 403 2
HET NA B 404 1
HET NA B 405 1
HET NA B 406 1
HET NA B 407 1
HETNAM ACT ACETATE ION
HETNAM NA SODIUM ION
FORMUL 3 ACT 3(C2 H3 O2 1-)
FORMUL 5 NA 8(NA 1+)
FORMUL 14 HOH *599(H2 O)
HELIX 1 AA1 TRP A 43 ARG A 48 5 6
HELIX 2 AA2 VAL A 50 GLU A 55 5 6
HELIX 3 AA3 ASP A 79 GLY A 95 1 17
HELIX 4 AA4 ASP A 105 HIS A 118 1 14
HELIX 5 AA5 ASP A 142 SER A 155 1 14
HELIX 6 AA6 SER A 155 MET A 164 1 10
HELIX 7 AA7 ASN A 167 ASN A 172 1 6
HELIX 8 AA8 ASN A 172 MET A 177 1 6
HELIX 9 AA9 GLU A 183 ALA A 192 1 10
HELIX 10 AB1 PRO A 193 THR A 195 5 3
HELIX 11 AB2 ARG A 197 LEU A 203 5 7
HELIX 12 AB3 CYS A 204 LEU A 210 1 7
HELIX 13 AB4 PRO A 216 GLY A 231 1 16
HELIX 14 AB5 PRO A 249 LEU A 260 1 12
HELIX 15 AB6 TYR A 274 ASP A 278 5 5
HELIX 16 AB7 GLN A 279 ARG A 293 1 15
HELIX 17 AB8 CYS A 294 LEU A 296 5 3
HELIX 18 AB9 TRP B 43 ARG B 48 5 6
HELIX 19 AC1 VAL B 50 GLU B 55 5 6
HELIX 20 AC2 ASP B 79 GLY B 95 1 17
HELIX 21 AC3 ASP B 105 HIS B 118 1 14
HELIX 22 AC4 GLY B 137 PHE B 141 5 5
HELIX 23 AC5 ASP B 142 SER B 155 1 14
HELIX 24 AC6 SER B 155 MET B 164 1 10
HELIX 25 AC7 ASN B 167 ASN B 172 1 6
HELIX 26 AC8 ASN B 172 MET B 177 1 6
HELIX 27 AC9 GLU B 183 ALA B 192 1 10
HELIX 28 AD1 PRO B 193 THR B 195 5 3
HELIX 29 AD2 ARG B 197 LEU B 203 5 7
HELIX 30 AD3 CYS B 204 LEU B 210 1 7
HELIX 31 AD4 PRO B 216 GLY B 231 1 16
HELIX 32 AD5 PRO B 249 LEU B 260 1 12
HELIX 33 AD6 TYR B 274 ASP B 278 5 5
HELIX 34 AD7 GLN B 279 CYS B 294 1 16
SHEET 1 AA1 8 SER A 13 VAL A 18 0
SHEET 2 AA1 8 SER A 21 HIS A 28 -1 O TYR A 25 N HIS A 14
SHEET 3 AA1 8 ARG A 59 VAL A 63 -1 O LEU A 60 N HIS A 28
SHEET 4 AA1 8 PRO A 33 LEU A 37 1 N LEU A 34 O ILE A 61
SHEET 5 AA1 8 ILE A 99 HIS A 104 1 O VAL A 102 N LEU A 35
SHEET 6 AA1 8 ILE A 122 MET A 128 1 O ALA A 126 N ILE A 101
SHEET 7 AA1 8 LYS A 237 PRO A 244 1 O LEU A 238 N PHE A 127
SHEET 8 AA1 8 LEU A 263 GLY A 271 1 O GLU A 264 N LEU A 239
SHEET 1 AA2 8 SER B 13 VAL B 18 0
SHEET 2 AA2 8 SER B 21 HIS B 28 -1 O SER B 21 N VAL B 18
SHEET 3 AA2 8 ARG B 59 VAL B 63 -1 O LEU B 60 N HIS B 28
SHEET 4 AA2 8 PRO B 33 LEU B 37 1 N PHE B 36 O ILE B 61
SHEET 5 AA2 8 ILE B 99 HIS B 104 1 O VAL B 102 N LEU B 35
SHEET 6 AA2 8 ILE B 122 MET B 128 1 O ALA B 126 N ILE B 101
SHEET 7 AA2 8 LYS B 237 PRO B 244 1 O LEU B 238 N PHE B 127
SHEET 8 AA2 8 LEU B 263 GLY B 271 1 O GLU B 264 N LEU B 239
SSBOND 1 CYS A 294 CYS B 294 1555 1555 2.04
LINK O LEU A 19 NA NA A 403 1555 1555 2.51
LINK OG SER A 21 NA NA A 403 1555 1555 2.66
LINK OH TYR A 86 NA NA A 403 1555 1555 2.69
LINK OD2 ASP A 142 NA NA A 404 1555 1555 2.68
LINK O PHE A 246 NA NA A 404 1555 1555 2.83
LINK O LEU B 19 NA NA B 407 1555 1555 2.51
LINK OG SER B 21 NA NA B 407 1555 1555 2.80
LINK OH TYR B 86 NA NA B 407 1555 1555 2.68
LINK OH TYR B 114 NA NA B 404 1555 1555 2.81
LINK OD2 ASP B 142 NA NA B 402 1555 1555 2.80
LINK OG1 THR B 145 NA NA B 402 1555 1555 2.71
LINK O ARG B 257 NA A NA B 403 1555 1555 2.52
LINK O ARG B 257 NA B NA B 403 1555 1555 2.89
LINK O LEU B 260 NA A NA B 403 1555 1555 2.76
LINK O LEU B 260 NA B NA B 403 1555 1555 2.79
LINK O LEU B 263 NA NA B 405 1555 1555 2.77
LINK NA NA A 403 O HOH A 796 1555 1555 2.73
LINK NA NA A 404 O HOH A 720 1555 1555 2.45
LINK NA NA A 404 O HOH A 799 1555 1555 2.59
LINK NA NA B 402 O HOH B 678 1555 1555 2.53
LINK NA A NA B 403 O HOH B 703 1555 1555 2.45
LINK NA A NA B 403 O HOH B 759 1555 1555 2.46
LINK NA B NA B 403 O HOH B 759 1555 1555 2.37
LINK NA NA B 404 O HOH B 595 1555 1555 2.91
LINK NA NA B 404 O HOH B 529 1555 1555 2.92
LINK NA NA B 405 O HOH B 730 1555 1555 2.80
LINK NA NA B 406 O HOH A 606 1555 1555 2.14
LINK NA NA B 406 O HOH A 589 1555 1555 2.66
LINK NA NA B 406 O HOH A 592 1555 1555 2.81
LINK NA NA B 407 O HOH B 778 1555 1555 2.73
CISPEP 1 GLN A 40 PRO A 41 0 -10.91
CISPEP 2 GLU A 215 PRO A 216 0 -1.59
CISPEP 3 GLU A 243 PRO A 244 0 9.16
CISPEP 4 GLN B 40 PRO B 41 0 -4.41
CISPEP 5 GLU B 215 PRO B 216 0 0.36
CISPEP 6 GLU B 243 PRO B 244 0 7.70
SITE 1 AC1 6 GLN A 40 ASP A 105 MET A 131 PHE A 149
SITE 2 AC1 6 PHE A 169 HOH A 511
SITE 1 AC2 8 THR A 265 ALA A 266 PHE A 267 HOH A 592
SITE 2 AC2 8 HOH A 656 HOH A 692 GLN B 289 HOH B 515
SITE 1 AC3 4 LEU A 19 SER A 21 TYR A 86 HOH A 796
SITE 1 AC4 4 ASP A 142 PHE A 246 HOH A 720 HOH A 799
SITE 1 AC5 4 ASP B 105 PHE B 149 PHE B 169 HOH B 548
SITE 1 AC6 3 ASP B 142 THR B 145 HOH B 678
SITE 1 AC7 6 ARG B 257 LEU B 260 ASN B 262 LEU B 263
SITE 2 AC7 6 HOH B 703 HOH B 759
SITE 1 AC8 5 GLU B 92 TYR B 114 ARG B 121 HOH B 529
SITE 2 AC8 5 HOH B 595
SITE 1 AC9 4 GLN A 289 ARG B 257 LEU B 263 HOH B 730
SITE 1 AD1 4 HOH A 589 HOH A 592 HOH A 606 THR B 265
SITE 1 AD2 4 LEU B 19 SER B 21 TYR B 86 HOH B 778
CRYST1 43.371 78.343 150.514 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 0.023057 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012764 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006644 0.00000
TER 2426 LEU A 296
TER 4851 LEU B 296
MASTER 515 0 11 34 16 0 15 6 5389 2 50 48
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