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HEADER HYDROLASE 15-DEC-17 6F9O
TITLE CRYSTAL STRUCTURE OF COLD-ADAPTED HALOALKANE DEHALOGENASE DPCA FROM
TITLE 2 PSYCHROBACTER CRYOHALOLENTIS K5
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: PSYCHROBACTER CRYOHALOLENTIS (STRAIN K5);
SOURCE 3 ORGANISM_TAXID: 335284;
SOURCE 4 STRAIN: K5;
SOURCE 5 GENE: DHMA, PCRYO_1253;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 866768;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: DE3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21B
KEYWDS MICROBIAL ENZYMES, HALOALKANE DEHALOGENASES, HLDS, ALPHA/BETA-
KEYWDS 2 HYDROLASE FOLD ENZYMES, HYDROLASE, 2 DOMAINS, THE HIGHEST ACTIVITY
KEYWDS 3 TOWARDS 1-BROMOBUTANE, 1-BROMOHEXANE AND 1, 3-DIBROMOPROPANE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.TRATSIAK,T.PRUDNIKOVA,I.DRIENOVSKA,J.DAMBORSKY,J.BRYNDA,P.PACHL,
AUTHOR 2 M.KUTY,R.CHALOUPKOVA,I.KUTA SMATANOVA,P.REZACOVA
REVDAT 1 27-FEB-19 6F9O 0
JRNL AUTH K.TRATSIAK,P.MALOY REZACOVA,R.CHALUPKOVA,I.KUTA SMATANOVA,
JRNL AUTH 2 J.DAMBORSKY
JRNL TITL CRYSTAL STRUCTURE OF COLD-ADAPTED HALOALKANE DEHALOGENASE
JRNL TITL 2 DPCA FROM PSYCHROBACTER CRYOHALOLENTIS K5
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.TRATSIAK,O.DEGTJARIK,I.DRIENOVSKA,L.CHRAST,P.REZACOVA,
REMARK 1 AUTH 2 M.KUTY,R.CHALOUPKOVA,J.DAMBORSKY,I.KUTA SMATANOVA
REMARK 1 TITL CRYSTALLOGRAPHIC ANALYSIS OF NEW PSYCHROPHILIC HALOALKANE
REMARK 1 TITL 2 DEHALOGENASES: DPCA FROM PSYCHROBACTER CRYOHALOLENTIS K5 AND
REMARK 1 TITL 3 DMXA FROM MARINOBACTER SP. ELB17.
REMARK 1 REF ACTA CRYSTALLOGR. SECT. F V. 69 683 2013
REMARK 1 REF 2 STRUCT. BIOL. CRYST. COMMUN.
REMARK 1 REFN ESSN 1744-3091
REMARK 1 PMID 23722854
REMARK 1 DOI 10.1107/S1744309113012979
REMARK 1 REFERENCE 2
REMARK 1 AUTH I.DRIENOVSKA,E.CHOVANCOVA,T.KOUDELAKOVA,J.DAMBORSKY,
REMARK 1 AUTH 2 R.CHALOUPKOVA
REMARK 1 TITL BIOCHEMICAL CHARACTERIZATION OF A NOVEL HALOALKANE
REMARK 1 TITL 2 DEHALOGENASE FROM A COLD-ADAPTED BACTERIUM.
REMARK 1 REF APPL. ENVIRON. MICROBIOL. V. 78 4995 2012
REMARK 1 REFN ESSN 1098-5336
REMARK 1 PMID 22582053
REMARK 1 DOI 10.1128/AEM.00485-12
REMARK 2
REMARK 2 RESOLUTION. 1.05 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) : 1.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.0
REMARK 3 NUMBER OF REFLECTIONS : 114202
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) : 0.111
REMARK 3 R VALUE (WORKING SET) : 0.110
REMARK 3 FREE R VALUE : 0.132
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6066
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) : 1.05
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.08
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4716
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 51.27
REMARK 3 BIN R VALUE (WORKING SET) : 0.2180
REMARK 3 BIN FREE R VALUE SET COUNT : 244
REMARK 3 BIN FREE R VALUE : 0.2380
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2465
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 576
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.72
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 8.67
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): 0.024
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.024
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.013
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.543
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.982
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.976
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2740 ; 0.012 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2445 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3748 ; 1.634 ; 1.945
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5721 ; 1.030 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 352 ; 6.086 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 138 ;33.671 ;24.058
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 442 ;12.244 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;16.682 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 390 ; 0.097 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3156 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 570 ; 0.003 ; 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): 1324 ; 0.710 ; 0.645
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1323 ; 0.710 ; 0.645
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1683 ; 1.023 ; 0.978
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1684 ; 1.022 ; 0.979
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1416 ; 1.083 ; 0.804
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1416 ; 1.082 ; 0.804
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2059 ; 1.322 ; 1.147
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3451 ; 2.693 ;10.367
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 3452 ; 2.693 ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 5182 ; 2.273 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 305 ;22.761 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 5399 ; 7.178 ; 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 : NULL
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 6F9O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-DEC-17.
REMARK 100 THE DEPOSITION ID IS D_1200007830.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-FEB-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6-5.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.978260
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : SAGITALLY BENDED SI111 CRYSTAL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-225
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000 VERSION NOVEMBER 1,
REMARK 200 2011
REMARK 200 DATA SCALING SOFTWARE : HKL-3000 VERSION NOVEMBER 1,
REMARK 200 2011
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 120315
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.050
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.2
REMARK 200 DATA REDUNDANCY : 5.700
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 39.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.09
REMARK 200 COMPLETENESS FOR SHELL (%) : 56.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.30700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.400
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: 1B6G
REMARK 200
REMARK 200 REMARK: NEEDLE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM ACETATE, 30%(W/V) PEG
REMARK 280 4000 AND 0.1 M SODIUM ACETATE TRIHYDRATE PH 4.6 AND WITH THE
REMARK 280 ADDITION OF 0.6 UL OF 0.1M L-PROLINE (ADDITIVE SCREEN KIT,
REMARK 280 HAMPTON RESEARCH) TO THE CRYSTALLIZATION DROP, PH 5.88, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 39.72550
REMARK 290 SMTRY3 2 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 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 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 1054 O HOH A 1057 1.51
REMARK 500 O HOH A 727 O HOH A 906 1.60
REMARK 500 O HOH A 961 O HOH A 1054 1.68
REMARK 500 O HOH A 781 O HOH A 1019 2.13
REMARK 500 OE1 GLN A 173 O HOH A 502 2.16
REMARK 500 O HOH A 522 O HOH A 861 2.17
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 ASN A 18 33.00 -144.49
REMARK 500 SER A 29 -4.99 77.94
REMARK 500 SER A 32 -154.59 -141.13
REMARK 500 PRO A 56 57.73 -98.65
REMARK 500 SER A 57 -166.47 -102.09
REMARK 500 ASP A 123 -139.00 56.76
REMARK 500 ASP A 123 -134.04 48.30
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 A1076 DISTANCE = 5.82 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 PEG A 405
REMARK 610 PEG A 406
REMARK 610 PEG A 407
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 408 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 261 O
REMARK 620 2 THR A 267 OG1 64.0
REMARK 620 3 HOH A 727 O 63.5 122.6
REMARK 620 4 HOH A 892 O 154.8 125.9 111.5
REMARK 620 5 HOH A 906 O 80.0 143.5 33.3 84.8
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 408
DBREF 6F9O A 1 303 UNP Q1QBB9 DHMA_PSYCK 1 303
SEQADV 6F9O HIS A 304 UNP Q1QBB9 EXPRESSION TAG
SEQADV 6F9O HIS A 305 UNP Q1QBB9 EXPRESSION TAG
SEQADV 6F9O HIS A 306 UNP Q1QBB9 EXPRESSION TAG
SEQADV 6F9O HIS A 307 UNP Q1QBB9 EXPRESSION TAG
SEQADV 6F9O HIS A 308 UNP Q1QBB9 EXPRESSION TAG
SEQADV 6F9O HIS A 309 UNP Q1QBB9 EXPRESSION TAG
SEQRES 1 A 309 MET LYS ILE LEU ARG THR PRO ASP SER ARG PHE ALA ASN
SEQRES 2 A 309 LEU PRO ASP TYR ASN PHE ASP PRO HIS TYR LEU MET VAL
SEQRES 3 A 309 ASP ASP SER GLU ASP SER GLU LEU ARG VAL HIS TYR LEU
SEQRES 4 A 309 ASP GLU GLY PRO ARG ASP ALA ASP PRO VAL LEU LEU LEU
SEQRES 5 A 309 HIS GLY GLU PRO SER TRP CYS TYR LEU TYR ARG LYS MET
SEQRES 6 A 309 ILE PRO ILE LEU THR ALA ALA GLY HIS ARG VAL ILE ALA
SEQRES 7 A 309 PRO ASP LEU PRO GLY PHE GLY ARG SER ASP LYS PRO ALA
SEQRES 8 A 309 SER ARG THR ASP TYR THR TYR GLN ARG HIS VAL ASN TRP
SEQRES 9 A 309 MET GLN SER VAL LEU ASP GLN LEU ASP LEU ASN ASN ILE
SEQRES 10 A 309 THR LEU PHE CYS GLN ASP TRP GLY GLY LEU ILE GLY LEU
SEQRES 11 A 309 ARG LEU VAL ALA GLU ASN PRO ASP ARG PHE ALA ARG VAL
SEQRES 12 A 309 ALA ALA GLY ASN THR MET LEU PRO THR GLY ASP HIS ASP
SEQRES 13 A 309 LEU GLY GLU GLY PHE ARG LYS TRP GLN GLN PHE SER GLN
SEQRES 14 A 309 GLU ILE PRO GLN PHE HIS VAL GLY GLY THR ILE LYS SER
SEQRES 15 A 309 GLY THR VAL THR LYS LEU SER GLN ALA VAL ILE ASP ALA
SEQRES 16 A 309 TYR ASN ALA PRO PHE PRO ASP GLU SER TYR LYS GLU GLY
SEQRES 17 A 309 ALA ARG GLN PHE PRO LEU LEU VAL PRO SER THR PRO ASP
SEQRES 18 A 309 ASP PRO ALA SER GLU ASN ASN ARG ALA ALA TRP ILE GLU
SEQRES 19 A 309 LEU SER LYS TRP THR LYS PRO PHE ILE THR LEU PHE SER
SEQRES 20 A 309 ASP SER ASP PRO VAL THR ALA GLY GLY ASP ARG ILE MET
SEQRES 21 A 309 GLN LYS ILE ILE PRO GLY THR LYS GLY GLN ALA HIS THR
SEQRES 22 A 309 THR ILE ALA ASN GLY GLY HIS PHE LEU GLN GLU ASP GLN
SEQRES 23 A 309 GLY GLU LYS VAL ALA LYS LEU LEU VAL GLN PHE ILE HIS
SEQRES 24 A 309 ASP ASN PRO ARG HIS HIS HIS HIS HIS HIS
HET CL A 401 1
HET CL A 402 1
HET PEG A 403 7
HET PEG A 404 7
HET PEG A 405 4
HET PEG A 406 3
HET PEG A 407 4
HET NA A 408 1
HETNAM CL CHLORIDE ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM NA SODIUM ION
FORMUL 2 CL 2(CL 1-)
FORMUL 4 PEG 5(C4 H10 O3)
FORMUL 9 NA NA 1+
FORMUL 10 HOH *576(H2 O)
HELIX 1 AA1 PRO A 7 ALA A 12 5 6
HELIX 2 AA2 TRP A 58 ARG A 63 5 6
HELIX 3 AA3 MET A 65 ALA A 72 1 8
HELIX 4 AA4 SER A 92 TYR A 96 5 5
HELIX 5 AA5 THR A 97 ASP A 113 1 17
HELIX 6 AA6 ASP A 123 ASN A 136 1 14
HELIX 7 AA7 GLY A 158 ILE A 171 1 14
HELIX 8 AA8 HIS A 175 GLY A 183 1 9
HELIX 9 AA9 SER A 189 ALA A 198 1 10
HELIX 10 AB1 ASP A 202 TYR A 205 5 4
HELIX 11 AB2 LYS A 206 PHE A 212 1 7
HELIX 12 AB3 PRO A 213 VAL A 216 5 4
HELIX 13 AB4 ALA A 224 SER A 236 1 13
HELIX 14 AB5 GLY A 255 ILE A 264 1 10
HELIX 15 AB6 PRO A 265 LYS A 268 5 4
HELIX 16 AB7 PHE A 281 ASP A 300 1 20
SHEET 1 AA1 2 ILE A 3 LEU A 4 0
SHEET 2 AA1 2 LYS A 89 PRO A 90 -1 O LYS A 89 N LEU A 4
SHEET 1 AA2 7 HIS A 22 ASP A 27 0
SHEET 2 AA2 7 GLU A 33 GLU A 41 -1 O VAL A 36 N LEU A 24
SHEET 3 AA2 7 ARG A 75 PRO A 79 -1 O VAL A 76 N GLU A 41
SHEET 4 AA2 7 PRO A 48 LEU A 52 1 N LEU A 51 O ILE A 77
SHEET 5 AA2 7 ILE A 117 CYS A 121 1 O PHE A 120 N LEU A 50
SHEET 6 AA2 7 PHE A 140 ALA A 145 1 O ALA A 144 N LEU A 119
SHEET 7 AA2 7 PHE A 242 THR A 244 1 O ILE A 243 N VAL A 143
SHEET 1 AA3 2 SER A 247 SER A 249 0
SHEET 2 AA3 2 ILE A 275 GLY A 279 1 O ILE A 275 N ASP A 248
LINK O GLN A 261 NA NA A 408 1555 1555 3.02
LINK OG1 THR A 267 NA NA A 408 1555 1555 2.82
LINK NA NA A 408 O HOH A 727 1555 1555 2.92
LINK NA NA A 408 O HOH A 892 1555 1555 2.56
LINK NA NA A 408 O HOH A 906 1555 1555 2.43
CISPEP 1 GLU A 55 PRO A 56 0 -28.57
SITE 1 AC1 4 TRP A 124 TRP A 164 PRO A 213 HOH A 610
SITE 1 AC2 3 GLY A 177 GLY A 178 ASN A 197
SITE 1 AC3 5 THR A 94 HOH A 708 HOH A 782 HOH A 793
SITE 2 AC3 5 HOH A1058
SITE 1 AC4 10 ARG A 93 LEU A 214 HOH A 519 HOH A 528
SITE 2 AC4 10 HOH A 578 HOH A 713 HOH A 785 HOH A 851
SITE 3 AC4 10 HOH A 900 HOH A 934
SITE 1 AC5 4 GLU A 135 HOH A 693 HOH A 849 HOH A 860
SITE 1 AC6 3 PRO A 43 HOH A 573 HOH A 608
SITE 1 AC7 7 PRO A 21 ARG A 86 HOH A 506 HOH A 589
SITE 2 AC7 7 HOH A 597 HOH A 618 HOH A 916
SITE 1 AC8 6 GLN A 261 THR A 267 LYS A 268 HOH A 727
SITE 2 AC8 6 HOH A 892 HOH A 906
CRYST1 41.332 79.451 43.489 90.00 94.98 90.00 P 1 21 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 0.024194 0.000000 0.002109 0.00000
SCALE2 0.000000 0.012586 0.000000 0.00000
SCALE3 0.000000 0.000000 0.023081 0.00000
TER 2625 HIS A 309
MASTER 365 0 8 16 11 0 13 6 3069 1 32 24
END |