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HEADER HYDROLASE 05-OCT-21 7PW1
TITLE CRYSTAL STRUCTURE OF ANCESTRAL HALOALKANE DEHALOGENASE ANCLINB-DMBA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.8.1.5;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 3 ORGANISM_TAXID: 32630;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS ANCESTRAL ENZYME, BALBES, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.MAZUR,P.GRINKEVICH,T.PRUDNIKOVA
REVDAT 1 06-APR-22 7PW1 0
JRNL AUTH A.MAZUR,P.GRINKEVICH,R.CHALOUPKOVA,P.HAVLICKOVA,B.KASCAKOVA,
JRNL AUTH 2 M.KUTY,J.DAMBORSKY,I.KUTA SMATANOVA,T.PRUDNIKOVA
JRNL TITL STRUCTURAL ANALYSIS OF THE ANCESTRAL HALOALKANE DEHALOGENASE
JRNL TITL 2 ANCLINB-DMBA
JRNL REF INT J MOL SCI 2021
JRNL REFN ESSN 1422-0067
JRNL DOI 10.3390/IJMS222111992
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0189
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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 63.04
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 58297
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) : 0.140
REMARK 3 R VALUE (WORKING SET) : 0.138
REMARK 3 FREE R VALUE : 0.174
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3064
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4064
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.86
REMARK 3 BIN R VALUE (WORKING SET) : 0.2290
REMARK 3 BIN FREE R VALUE SET COUNT : 215
REMARK 3 BIN FREE R VALUE : 0.2540
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2331
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 9
REMARK 3 SOLVENT ATOMS : 317
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.27
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.10000
REMARK 3 B22 (A**2) : 0.10000
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): 0.061
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.058
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.041
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.495
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.978
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.966
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2509 ; 0.046 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2274 ; 0.006 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3418 ; 2.968 ; 1.951
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5268 ; 1.357 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 314 ; 6.784 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 131 ;34.622 ;23.435
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 406 ;12.107 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 25 ;17.662 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 350 ; 0.205 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2877 ; 0.016 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 552 ; 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): 1220 ; 1.463 ; 1.868
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1219 ; 1.459 ; 1.865
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1537 ; 1.459 ; 2.801
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1538 ; 1.460 ; 2.803
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1289 ; 2.770 ; 2.188
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1289 ; 2.770 ; 2.188
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1879 ; 2.429 ; 3.172
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3006 ; 2.228 ;24.038
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2924 ; 2.126 ;23.260
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 4783 ; 6.979 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 207 ;10.499 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 4829 ; 4.045 ; 5.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 7PW1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-OCT-21.
REMARK 100 THE DEPOSITION ID IS D_1292118257.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-JAN-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91841
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 61367
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 63.040
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 10.45
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.6800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.650
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 2QVB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 4000, 0.1 M SODIUM CITRATE PH
REMARK 280 5.6, 0.2 M AMMONIUM ACETATE, PH 7.5, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 78.12950
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 34.44850
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 34.44850
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 117.19425
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 34.44850
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 34.44850
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 39.06475
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 34.44850
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 34.44850
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 117.19425
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 34.44850
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 34.44850
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 39.06475
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 78.12950
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 690 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ALA A 297
REMARK 465 ALA A 298
REMARK 465 GLY A 299
REMARK 465 VAL A 300
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 A 16 CD GLU A 16 OE2 0.153
REMARK 500 ARG A 87 CZ ARG A 87 NH1 -0.139
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 PRO A 40 52.58 -101.69
REMARK 500 THR A 41 -160.44 -107.90
REMARK 500 ASP A 109 -134.84 51.72
REMARK 500 ARG A 156 47.73 -88.69
REMARK 500 ALA A 248 -65.68 -149.35
REMARK 500 ALA A 272 -99.73 -97.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 816 DISTANCE = 6.21 ANGSTROMS
REMARK 525 HOH A 817 DISTANCE = 6.24 ANGSTROMS
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 402 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE A 35 O
REMARK 620 2 GLN A 36 OE1 92.3
REMARK 620 N 1
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 PHE A 35 O
REMARK 620 2 CYS A 62 O 115.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 405 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 81 O
REMARK 620 2 PRO A 204 O 140.6
REMARK 620 N 1
DBREF 7PW1 A 5 300 PDB 7PW1 7PW1 5 300
SEQRES 1 A 296 GLY ALA GLU PRO TYR GLY GLN LYS LYS PHE ILE GLU ILE
SEQRES 2 A 296 ALA GLY LYS ARG MET ALA TYR ILE ASP GLU GLY GLU GLY
SEQRES 3 A 296 ASP PRO ILE VAL PHE GLN HIS GLY ASN PRO THR SER SER
SEQRES 4 A 296 TYR LEU TRP ARG ASN ILE MET PRO HIS LEU GLU GLY LEU
SEQRES 5 A 296 GLY ARG LEU ILE ALA CYS ASP LEU ILE GLY MET GLY ASP
SEQRES 6 A 296 SER ASP LYS LEU SER PRO SER GLY PRO ASP ARG TYR SER
SEQRES 7 A 296 TYR ALA GLU HIS ARG ASP TYR LEU PHE ALA LEU TRP GLU
SEQRES 8 A 296 ALA LEU ASP LEU GLY ASP ASN VAL VAL LEU VAL ILE HIS
SEQRES 9 A 296 ASP TRP GLY SER ALA LEU GLY PHE ASP TRP ALA ASN GLN
SEQRES 10 A 296 HIS ARG ASP ARG VAL GLN GLY ILE ALA TYR MET GLU ALA
SEQRES 11 A 296 ILE VAL THR PRO LEU GLU TRP ALA ASP TRP PRO GLU GLU
SEQRES 12 A 296 VAL ARG ASP ILE PHE GLN GLY PHE ARG SER PRO ALA GLY
SEQRES 13 A 296 GLU GLU MET VAL LEU GLU ASN ASN ILE PHE VAL GLU ARG
SEQRES 14 A 296 VAL LEU PRO GLY ALA ILE LEU ARG GLN LEU SER ASP GLU
SEQRES 15 A 296 GLU MET ALA GLU TYR ARG ARG PRO PHE LEU ASN ALA GLY
SEQRES 16 A 296 GLU ASP ARG ARG PRO THR LEU SER TRP PRO ARG GLN ILE
SEQRES 17 A 296 PRO ILE ASP GLY GLU PRO ALA ASP VAL VAL ALA ILE VAL
SEQRES 18 A 296 SER ASP TYR ALA SER TRP LEU ALA GLU SER ASP ILE PRO
SEQRES 19 A 296 LYS LEU PHE ILE ASN ALA GLU PRO GLY ALA ILE VAL THR
SEQRES 20 A 296 GLY ARG MET ARG ASP PHE CYS ARG SER TRP PRO ASN GLN
SEQRES 21 A 296 THR GLU ILE THR VAL LYS GLY ALA HIS PHE ILE GLN GLU
SEQRES 22 A 296 ASP SER PRO ASP GLU ILE GLY ALA ALA ILE ALA GLU PHE
SEQRES 23 A 296 VAL ARG ARG LEU ARG VAL ALA ALA GLY VAL
HET CL A 401 1
HET NA A 402 1
HET NA A 403 1
HET NA A 404 1
HET NA A 405 1
HET EDO A 406 8
HETNAM CL CHLORIDE ION
HETNAM NA SODIUM ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 CL CL 1-
FORMUL 3 NA 4(NA 1+)
FORMUL 7 EDO C2 H6 O2
FORMUL 8 HOH *317(H2 O)
HELIX 1 AA1 SER A 42 ARG A 47 5 6
HELIX 2 AA2 ILE A 49 GLU A 54 5 6
HELIX 3 AA3 SER A 82 LEU A 97 1 16
HELIX 4 AA4 ASP A 109 HIS A 122 1 14
HELIX 5 AA5 GLU A 140 TRP A 144 5 5
HELIX 6 AA6 PRO A 145 ARG A 156 1 12
HELIX 7 AA7 ALA A 159 LEU A 165 1 7
HELIX 8 AA8 ASN A 168 ARG A 173 1 6
HELIX 9 AA9 ARG A 173 ALA A 178 1 6
HELIX 10 AB1 SER A 184 ARG A 193 1 10
HELIX 11 AB2 PRO A 194 LEU A 196 5 3
HELIX 12 AB3 GLY A 199 ASP A 201 5 3
HELIX 13 AB4 ARG A 202 TRP A 208 1 7
HELIX 14 AB5 PRO A 209 ILE A 212 5 4
HELIX 15 AB6 PRO A 218 SER A 235 1 18
HELIX 16 AB7 THR A 251 SER A 260 1 10
HELIX 17 AB8 PHE A 274 ASP A 278 5 5
HELIX 18 AB9 SER A 279 VAL A 296 1 18
SHEET 1 AA1 8 LYS A 13 ILE A 17 0
SHEET 2 AA1 8 LYS A 20 GLU A 27 -1 O LYS A 20 N ILE A 17
SHEET 3 AA1 8 ARG A 58 CYS A 62 -1 O LEU A 59 N GLU A 27
SHEET 4 AA1 8 PRO A 32 GLN A 36 1 N PHE A 35 O ILE A 60
SHEET 5 AA1 8 VAL A 103 HIS A 108 1 O VAL A 104 N VAL A 34
SHEET 6 AA1 8 VAL A 126 MET A 132 1 O ALA A 130 N LEU A 105
SHEET 7 AA1 8 LYS A 239 PRO A 246 1 O LEU A 240 N TYR A 131
SHEET 8 AA1 8 GLN A 264 GLY A 271 1 O THR A 265 N PHE A 241
LINK O PHE A 35 NA NA A 402 1555 1555 2.88
LINK O PHE A 35 NA NA A 403 1555 1555 2.79
LINK OE1 GLN A 36 NA NA A 402 1555 1555 2.72
LINK O CYS A 62 NA NA A 403 1555 1555 2.87
LINK O TYR A 81 NA NA A 405 1555 1555 2.99
LINK O HIS A 86 NA NA A 404 1555 1555 3.05
LINK O PRO A 204 NA NA A 405 1555 1555 2.89
CISPEP 1 ASN A 39 PRO A 40 0 -13.40
CISPEP 2 SER A 74 PRO A 75 0 -19.25
CISPEP 3 SER A 74 PRO A 75 0 8.23
CISPEP 4 GLU A 217 PRO A 218 0 -3.24
CISPEP 5 GLU A 245 PRO A 246 0 3.51
CISPEP 6 GLU A 245 PRO A 246 0 0.34
CRYST1 68.897 68.897 156.259 90.00 90.00 90.00 P 43 21 2 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 0.014514 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014514 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006400 0.00000
TER 2418 VAL A 296
MASTER 349 0 6 18 8 0 0 6 2657 1 18 23
END |