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HEADER HYDROLASE 27-APR-15 4ZI5
TITLE CRYSTAL STRUCTURE OF DIENELACTONE HYDROLASE-LIKE PROMISCUOUS
TITLE 2 PHOSPOTRIESTERASE P91 FROM METAGENOMIC LIBRARIES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: P91;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.8.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METAGENOME;
SOURCE 3 ORGANISM_TAXID: 256318;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PASKIBA5+
KEYWDS METAGENOMIC LIBRARIES, ALPHA/BETA HYDROLASE, PROMISCUITY,
KEYWDS 2 PHOSPHOTRIESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.-Y.COLIN,G.FISCHER,M.HYVONEN,F.HOLLFELDER
REVDAT 1 17-FEB-16 4ZI5 0
JRNL AUTH P.Y.COLIN,B.KINTSES,F.GIELEN,C.M.MITON,G.FISCHER,
JRNL AUTH 2 M.F.MOHAMED,M.HYVONEN,D.P.MORGAVI,D.B.JANSSEN,F.HOLLFELDER
JRNL TITL ULTRAHIGH-THROUGHPUT DISCOVERY OF PROMISCUOUS ENZYMES BY
JRNL TITL 2 PICODROPLET FUNCTIONAL METAGENOMICS.
JRNL REF NAT COMMUN V. 6 10008 2015
JRNL REFN ESSN 2041-1723
JRNL PMID 26639611
JRNL DOI 10.1038/NCOMMS10008
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0107
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 61.57
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 87.6
REMARK 3 NUMBER OF REFLECTIONS : 42939
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) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 2180
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.75
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2650
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 73.83
REMARK 3 BIN R VALUE (WORKING SET) : 0.3180
REMARK 3 BIN FREE R VALUE SET COUNT : 137
REMARK 3 BIN FREE R VALUE : 0.3310
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3586
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 3
REMARK 3 SOLVENT ATOMS : 456
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.25
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.48000
REMARK 3 B22 (A**2) : 0.26000
REMARK 3 B33 (A**2) : 1.21000
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): 0.131
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.117
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.082
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.654
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.963
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A -1 237 B -1 237 28118 0.06 0.05
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 4ZI5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-APR-15.
REMARK 100 THE DEPOSITION ID IS D_1000209341.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-JUN-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91882
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS (VERSION JANUARY 10,
REMARK 200 AUTOPROC
REMARK 200 DATA SCALING SOFTWARE : AIMLESS (VERSION 0.3.8), CCP4
REMARK 200 6.4
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45156
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.702
REMARK 200 RESOLUTION RANGE LOW (A) : 61.570
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87.6
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : 0.06300
REMARK 200 FOR THE DATA SET : 12.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.71
REMARK 200 COMPLETENESS FOR SHELL (%) : 55.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.45400
REMARK 200 R SYM FOR SHELL (I) : 0.45400
REMARK 200 FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3F67
REMARK 200
REMARK 200 REMARK: SHARD-LIKE PLATES
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS PH=8.5, 0.2M MGCL2, 20%
REMARK 280 PEG8000, PH 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 292K
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 27.80650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.52850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.70700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 56.52850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.80650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.70700
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: 2100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 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 -12
REMARK 465 ALA A -11
REMARK 465 SER A -10
REMARK 465 TRP A -9
REMARK 465 SER A -8
REMARK 465 HIS A -7
REMARK 465 PRO A -6
REMARK 465 GLN A -5
REMARK 465 PHE A -4
REMARK 465 GLU A -3
REMARK 465 LYS A -2
REMARK 465 MET B -12
REMARK 465 ALA B -11
REMARK 465 SER B -10
REMARK 465 TRP B -9
REMARK 465 SER B -8
REMARK 465 HIS B -7
REMARK 465 PRO B -6
REMARK 465 GLN B -5
REMARK 465 PHE B -4
REMARK 465 GLU B -3
REMARK 465 LYS B -2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 561 O HOH B 425 3555 1.48
REMARK 500 O HOH A 633 O HOH B 619 1655 1.93
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 LEU A 76 CA - CB - CG ANGL. DEV. = 18.7 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 86 82.64 -151.43
REMARK 500 CYS A 118 -120.12 61.15
REMARK 500 CYS A 118 -119.70 61.05
REMARK 500 VAL A 198 -157.33 -116.16
REMARK 500 ASP B 86 82.39 -151.27
REMARK 500 CYS B 118 -120.69 60.86
REMARK 500 CYS B 118 -120.64 60.45
REMARK 500 HIS B 141 49.06 38.73
REMARK 500 VAL B 198 -156.90 -117.12
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 MG A 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 611 O
REMARK 620 2 HOH A 438 O 95.5
REMARK 620 3 HOH A 606 O 92.9 91.2
REMARK 620 4 HOH A 450 O 89.5 93.1 174.9
REMARK 620 5 HOH A 635 O 91.8 172.7 88.0 87.4
REMARK 620 6 HOH A 548 O 173.1 85.1 94.0 83.6 87.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 591 O
REMARK 620 2 HOH B 445 O 91.7
REMARK 620 3 HOH B 603 O 94.2 97.2
REMARK 620 4 HOH B 462 O 90.6 82.7 175.1
REMARK 620 5 HOH B 458 O 176.1 91.3 87.8 87.3
REMARK 620 6 HOH B 620 O 91.2 173.7 88.1 91.7 85.5
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 302
DBREF 4ZI5 A -12 237 PDB 4ZI5 4ZI5 -12 237
DBREF 4ZI5 B -12 237 PDB 4ZI5 4ZI5 -12 237
SEQRES 1 A 250 MET ALA SER TRP SER HIS PRO GLN PHE GLU LYS GLY ALA
SEQRES 2 A 250 MET THR ALA ARG LYS VAL ASP TYR THR ASP GLY ALA THR
SEQRES 3 A 250 ARG CYS ILE GLY GLU PHE HIS TRP ASP GLU GLY LYS SER
SEQRES 4 A 250 GLY PRO ARG PRO GLY VAL VAL VAL PHE PRO GLU ALA PHE
SEQRES 5 A 250 GLY LEU ASN ASP HIS ALA LYS GLU ARG ALA ARG ARG LEU
SEQRES 6 A 250 ALA ASP LEU GLY PHE ALA ALA LEU ALA ALA ASP MET HIS
SEQRES 7 A 250 GLY ASP ALA GLN VAL PHE ASP ALA ALA SER LEU SER SER
SEQRES 8 A 250 THR ILE GLN GLY TYR TYR GLY ASP ARG ALA HIS TRP ARG
SEQRES 9 A 250 ARG ARG ALA GLN ALA ALA LEU ASP ALA LEU THR ALA GLN
SEQRES 10 A 250 PRO GLU VAL ASP GLY SER LYS VAL ALA ALA ILE GLY PHE
SEQRES 11 A 250 CYS PHE GLY GLY ALA THR CYS LEU GLU LEU ALA ARG THR
SEQRES 12 A 250 GLY ALA PRO LEU THR ALA ILE VAL THR PHE HIS GLY GLY
SEQRES 13 A 250 LEU LEU PRO GLU MET ALA GLY ASP ALA GLY ARG ILE GLN
SEQRES 14 A 250 SER SER VAL LEU VAL CYS HIS GLY ALA ASP ASP PRO LEU
SEQRES 15 A 250 VAL GLN ASP GLU THR MET LYS ALA VAL MET ASP GLU PHE
SEQRES 16 A 250 ARG ARG ASP LYS VAL ASP TRP GLN VAL LEU TYR LEU GLY
SEQRES 17 A 250 ASN ALA VAL HIS SER PHE THR ASP PRO LEU ALA GLY SER
SEQRES 18 A 250 HIS GLY ILE PRO GLY LEU ALA TYR ASP ALA THR ALA GLU
SEQRES 19 A 250 ALA ARG SER TRP THR ALA MET CYS ASN LEU PHE SER GLU
SEQRES 20 A 250 LEU PHE GLY
SEQRES 1 B 250 MET ALA SER TRP SER HIS PRO GLN PHE GLU LYS GLY ALA
SEQRES 2 B 250 MET THR ALA ARG LYS VAL ASP TYR THR ASP GLY ALA THR
SEQRES 3 B 250 ARG CYS ILE GLY GLU PHE HIS TRP ASP GLU GLY LYS SER
SEQRES 4 B 250 GLY PRO ARG PRO GLY VAL VAL VAL PHE PRO GLU ALA PHE
SEQRES 5 B 250 GLY LEU ASN ASP HIS ALA LYS GLU ARG ALA ARG ARG LEU
SEQRES 6 B 250 ALA ASP LEU GLY PHE ALA ALA LEU ALA ALA ASP MET HIS
SEQRES 7 B 250 GLY ASP ALA GLN VAL PHE ASP ALA ALA SER LEU SER SER
SEQRES 8 B 250 THR ILE GLN GLY TYR TYR GLY ASP ARG ALA HIS TRP ARG
SEQRES 9 B 250 ARG ARG ALA GLN ALA ALA LEU ASP ALA LEU THR ALA GLN
SEQRES 10 B 250 PRO GLU VAL ASP GLY SER LYS VAL ALA ALA ILE GLY PHE
SEQRES 11 B 250 CYS PHE GLY GLY ALA THR CYS LEU GLU LEU ALA ARG THR
SEQRES 12 B 250 GLY ALA PRO LEU THR ALA ILE VAL THR PHE HIS GLY GLY
SEQRES 13 B 250 LEU LEU PRO GLU MET ALA GLY ASP ALA GLY ARG ILE GLN
SEQRES 14 B 250 SER SER VAL LEU VAL CYS HIS GLY ALA ASP ASP PRO LEU
SEQRES 15 B 250 VAL GLN ASP GLU THR MET LYS ALA VAL MET ASP GLU PHE
SEQRES 16 B 250 ARG ARG ASP LYS VAL ASP TRP GLN VAL LEU TYR LEU GLY
SEQRES 17 B 250 ASN ALA VAL HIS SER PHE THR ASP PRO LEU ALA GLY SER
SEQRES 18 B 250 HIS GLY ILE PRO GLY LEU ALA TYR ASP ALA THR ALA GLU
SEQRES 19 B 250 ALA ARG SER TRP THR ALA MET CYS ASN LEU PHE SER GLU
SEQRES 20 B 250 LEU PHE GLY
HET MG A 301 1
HET CL B 301 1
HET MG B 302 1
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
FORMUL 3 MG 2(MG 2+)
FORMUL 4 CL CL 1-
FORMUL 6 HOH *456(H2 O)
HELIX 1 AA1 ASN A 42 LEU A 55 1 14
HELIX 2 AA2 ASP A 72 SER A 75 5 4
HELIX 3 AA3 LEU A 76 GLY A 85 1 10
HELIX 4 AA4 ASP A 86 ALA A 103 1 18
HELIX 5 AA5 CYS A 118 THR A 130 1 13
HELIX 6 AA6 GLN A 171 LYS A 186 1 16
HELIX 7 AA7 LEU A 205 GLY A 210 5 6
HELIX 8 AA8 ASP A 217 PHE A 236 1 20
HELIX 9 AA9 ASN B 42 LEU B 55 1 14
HELIX 10 AB1 LEU B 76 GLY B 85 1 10
HELIX 11 AB2 ASP B 86 ALA B 103 1 18
HELIX 12 AB3 CYS B 118 THR B 130 1 13
HELIX 13 AB4 GLN B 171 LYS B 186 1 16
HELIX 14 AB5 LEU B 205 GLY B 210 5 6
HELIX 15 AB6 ASP B 217 PHE B 236 1 20
SHEET 1 AA116 THR A 2 ASP A 10 0
SHEET 2 AA116 THR A 13 TRP A 21 -1 O CYS A 15 N TYR A 8
SHEET 3 AA116 ALA A 58 ALA A 61 -1 O ALA A 59 N HIS A 20
SHEET 4 AA116 ARG A 29 PHE A 35 1 N VAL A 34 O LEU A 60
SHEET 5 AA116 VAL A 107 PHE A 117 1 O ILE A 115 N PHE A 35
SHEET 6 AA116 ALA A 136 PHE A 140 1 O PHE A 140 N GLY A 116
SHEET 7 AA116 SER A 158 GLY A 164 1 O CYS A 162 N THR A 139
SHEET 8 AA116 TRP A 189 LEU A 194 1 O LEU A 194 N HIS A 163
SHEET 9 AA116 TRP B 189 LEU B 194 -1 O TYR B 193 N VAL A 191
SHEET 10 AA116 SER B 158 GLY B 164 1 N HIS B 163 O LEU B 194
SHEET 11 AA116 ALA B 136 PHE B 140 1 N THR B 139 O CYS B 162
SHEET 12 AA116 VAL B 107 PHE B 117 1 N GLY B 116 O PHE B 140
SHEET 13 AA116 ARG B 29 PHE B 35 1 N VAL B 33 O ILE B 115
SHEET 14 AA116 ALA B 58 ALA B 61 1 O LEU B 60 N VAL B 34
SHEET 15 AA116 THR B 13 TRP B 21 -1 N HIS B 20 O ALA B 59
SHEET 16 AA116 THR B 2 ASP B 10 -1 N TYR B 8 O CYS B 15
LINK MG MG A 301 O HOH A 611 1555 1555 2.07
LINK MG MG A 301 O HOH A 438 1555 1555 2.00
LINK MG MG A 301 O HOH A 606 1555 1555 2.02
LINK MG MG A 301 O HOH A 450 1555 1555 2.07
LINK MG MG A 301 O HOH A 635 1555 1555 2.14
LINK MG MG A 301 O HOH A 548 1555 1555 2.10
LINK MG MG B 302 O HOH B 591 1555 1555 2.10
LINK MG MG B 302 O HOH B 445 1555 1555 2.02
LINK MG MG B 302 O HOH B 603 1555 1555 2.02
LINK MG MG B 302 O HOH B 462 1555 1555 2.14
LINK MG MG B 302 O HOH B 458 1555 1555 2.14
LINK MG MG B 302 O HOH B 620 1555 1555 2.11
CISPEP 1 SER B 78 THR B 79 0 24.13
SITE 1 AC1 6 HOH A 438 HOH A 450 HOH A 548 HOH A 606
SITE 2 AC1 6 HOH A 611 HOH A 635
SITE 1 AC2 6 HOH B 445 HOH B 458 HOH B 462 HOH B 591
SITE 2 AC2 6 HOH B 603 HOH B 620
CRYST1 55.613 73.414 113.057 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 0.017981 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013621 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008845 0.00000
TER 1845 GLY A 237
TER 3690 GLY B 237
MASTER 372 0 3 15 16 0 4 6 4045 2 16 40
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