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HEADER HYDROLASE 25-NOV-20 7B1X
TITLE CRYSTAL STRUCTURE OF COLD-ACTIVE ESTERASE PMGL3 FROM PERMAFROST
TITLE 2 METAGENOMIC LIBRARY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE PMGL3;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;
SOURCE 3 ORGANISM_TAXID: 77133;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ESTERASE, HSL, PERMAFROST, COLD-ACTIVE, PSYCHROPHILIC, TETRAMER,
KEYWDS 2 DIMER, LIPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.M.BOYKO,A.Y.NIKOLAEVA,L.E.PETROVSKAYA,M.V.KRYUKOVA,E.A.KRYUKOVA,
AUTHOR 2 D.A.KORZHENEVSKY,G.Y.LOMAKINA,K.A.NOVOTOTSKAYA-VLASOVA,E.M.RIVKINA,
AUTHOR 3 D.A.DOLGIKH,M.P.KIRPICHNIKOV,V.O.POPOV
REVDAT 1 03-NOV-21 7B1X 0
JRNL AUTH K.M.BOYKO,M.V.KRYUKOVA,L.E.PETROVSKAYA,E.A.KRYUKOVA,
JRNL AUTH 2 A.Y.NIKOLAEVA,D.A.KORZHENEVSKY,G.Y.LOMAKINA,
JRNL AUTH 3 K.A.NOVOTOTSKAYA-VLASOVA,E.M.RIVKINA,D.A.DOLGIKH,
JRNL AUTH 4 M.P.KIRPICHNIKOV,V.O.POPOV
JRNL TITL STRUCTURAL AND BIOCHEMICAL CHARACTERIZATION OF A COLD-ACTIVE
JRNL TITL 2 PMGL3 ESTERASE WITH UNUSUAL OLIGOMERIC STRUCTURE.
JRNL REF BIOMOLECULES V. 11 2021
JRNL REFN ESSN 2218-273X
JRNL PMID 33466452
JRNL DOI 10.3390/BIOM11010057
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0267
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.28
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.2
REMARK 3 NUMBER OF REFLECTIONS : 22446
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) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.162
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1182
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1666
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.21
REMARK 3 BIN R VALUE (WORKING SET) : 0.2410
REMARK 3 BIN FREE R VALUE SET COUNT : 98
REMARK 3 BIN FREE R VALUE : 0.3070
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4507
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 197
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 44.04
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.74
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.50000
REMARK 3 B22 (A**2) : 1.32000
REMARK 3 B33 (A**2) : -0.95000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.20000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.450
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.257
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.182
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.695
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.929
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4632 ; 0.012 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6310 ; 2.074 ; 1.622
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 602 ; 7.109 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 230 ;35.540 ;21.957
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 684 ;19.578 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;17.175 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 593 ; 0.146 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3620 ; 0.012 ; 0.020
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 1 302 B 1 302 9755 0.080 0.050
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 1 A 302
REMARK 3 ORIGIN FOR THE GROUP (A): -29.1198 0.6853 5.0134
REMARK 3 T TENSOR
REMARK 3 T11: 0.0691 T22: 0.1510
REMARK 3 T33: 0.0154 T12: 0.0320
REMARK 3 T13: -0.0200 T23: 0.0118
REMARK 3 L TENSOR
REMARK 3 L11: 1.2237 L22: 0.5197
REMARK 3 L33: 0.7971 L12: 0.0132
REMARK 3 L13: 0.1046 L23: 0.0307
REMARK 3 S TENSOR
REMARK 3 S11: 0.0637 S12: 0.3387 S13: 0.0384
REMARK 3 S21: 0.0018 S22: 0.0082 S23: -0.0437
REMARK 3 S31: 0.0937 S32: 0.0167 S33: -0.0719
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 1 B 302
REMARK 3 ORIGIN FOR THE GROUP (A): -48.4461 15.1620 29.6386
REMARK 3 T TENSOR
REMARK 3 T11: 0.0230 T22: 0.1104
REMARK 3 T33: 0.1001 T12: 0.0281
REMARK 3 T13: 0.0009 T23: -0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 0.9504 L22: 0.5354
REMARK 3 L33: 0.7949 L12: -0.0105
REMARK 3 L13: 0.0318 L23: 0.0594
REMARK 3 S TENSOR
REMARK 3 S11: 0.0493 S12: -0.0740 S13: 0.2219
REMARK 3 S21: 0.0227 S22: 0.0116 S23: 0.0235
REMARK 3 S31: -0.0213 S32: -0.2404 S33: -0.0609
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: U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 7B1X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-NOV-20.
REMARK 100 THE DEPOSITION ID IS D_1292112509.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-SEP-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : MASSIF-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9677
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33658
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 37.280
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 200 DATA REDUNDANCY : 6.034
REMARK 200 R MERGE (I) : 0.10900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.5800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.26
REMARK 200 R MERGE FOR SHELL (I) : 0.52900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.540
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: 3FAK
REMARK 200
REMARK 200 REMARK: NULL
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 SODIUM CITRATE TRIBASIC DIHYDRATE
REMARK 280 PH 5.6; 20% ISOPROPANOL; 20% PEG4000, VAPOR DIFFUSION,
REMARK 280 TEMPERATURE 288K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 51.90000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.20000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 51.90000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 49.20000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 -46.40110
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 59.17751
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 43880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 3 1.000000 0.000000 0.000000 46.40110
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 -59.17751
REMARK 350 BIOMT1 4 -1.000000 0.000000 0.000000 -46.40110
REMARK 350 BIOMT2 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 59.17751
REMARK 350
REMARK 350 BIOMOLECULE: 3
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: 1860 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22380 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 GLY A 303
REMARK 465 HIS A 304
REMARK 465 LEU A 305
REMARK 465 GLU A 306
REMARK 465 HIS A 307
REMARK 465 HIS A 308
REMARK 465 HIS A 309
REMARK 465 HIS A 310
REMARK 465 HIS A 311
REMARK 465 HIS A 312
REMARK 465 GLY B 303
REMARK 465 HIS B 304
REMARK 465 LEU B 305
REMARK 465 GLU B 306
REMARK 465 HIS B 307
REMARK 465 HIS B 308
REMARK 465 HIS B 309
REMARK 465 HIS B 310
REMARK 465 HIS B 311
REMARK 465 HIS B 312
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 22 NE CZ NH1 NH2
REMARK 470 ILE A 29 CD1
REMARK 470 GLU A 30 CD OE1 OE2
REMARK 470 ILE A 31 CD1
REMARK 470 ASN A 202 CG OD1 ND2
REMARK 470 GLU B 30 CG CD OE1 OE2
REMARK 470 LYS B 73 CE NZ
REMARK 470 LYS B 139 CD CE NZ
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 47 CD GLU A 47 OE1 0.075
REMARK 500 GLU A 47 CD GLU A 47 OE2 0.092
REMARK 500 GLU B 47 CD GLU B 47 OE2 0.088
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 GLU A 62 CB - CA - C ANGL. DEV. = -14.0 DEGREES
REMARK 500 ARG A 254 CG - CD - NE ANGL. DEV. = -17.2 DEGREES
REMARK 500 ARG A 254 NE - CZ - NH2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 ARG A 255 NE - CZ - NH1 ANGL. DEV. = -4.4 DEGREES
REMARK 500 GLU B 62 CB - CA - C ANGL. DEV. = -13.7 DEGREES
REMARK 500 ARG B 192 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ASP B 228 CB - CA - C ANGL. DEV. = 14.0 DEGREES
REMARK 500 ARG B 254 CG - CD - NE ANGL. DEV. = -19.1 DEGREES
REMARK 500 ARG B 254 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG B 254 NE - CZ - NH2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 ARG B 255 NE - CZ - NH1 ANGL. DEV. = 4.0 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 SER A 55 86.16 -155.02
REMARK 500 HIS A 83 12.81 58.28
REMARK 500 PRO A 120 32.09 -97.02
REMARK 500 SER A 149 -112.53 40.39
REMARK 500 SER A 177 51.88 36.31
REMARK 500 ASP A 242 54.60 -97.57
REMARK 500 SER B 55 78.89 -155.22
REMARK 500 HIS B 83 16.92 56.67
REMARK 500 SER B 149 -114.00 40.74
REMARK 500 SER B 177 49.40 38.45
REMARK 500 ALA B 213 58.60 38.37
REMARK 500 ASP B 231 2.29 80.68
REMARK 500 ASP B 242 58.88 -100.71
REMARK 500 ASN B 270 -2.00 71.29
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LEU A 301 GLY A 302 145.56
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 498 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH B 499 DISTANCE = 6.06 ANGSTROMS
DBREF 7B1X A 1 312 PDB 7B1X 7B1X 1 312
DBREF 7B1X B 1 312 PDB 7B1X 7B1X 1 312
SEQRES 1 A 312 MET ASN GLY ASN ASP PRO ASP ILE ALA GLY PHE LYS GLN
SEQRES 2 A 312 GLN LEU VAL GLN MET THR ALA MET ARG GLU SER GLN PRO
SEQRES 3 A 312 PRO SER ILE GLU ILE GLU ARG GLN MET PHE ASP ALA GLN
SEQRES 4 A 312 HIS GLY ALA VAL PRO PRO ALA GLU GLY CYS LEU ILE GLU
SEQRES 5 A 312 PRO ILE SER THR GLY GLY VAL ARG GLY GLU ARG ILE THR
SEQRES 6 A 312 PRO LYS SER ALA ASP THR SER LYS ALA LEU ILE TYR PHE
SEQRES 7 A 312 HIS GLY GLY GLY HIS LEU PHE GLY SER ALA LEU SER HIS
SEQRES 8 A 312 ARG HIS LEU VAL SER ARG LEU ALA ALA ALA ALA GLY VAL
SEQRES 9 A 312 VAL ALA TYR ASN MET GLU TYR ARG LEU ALA PRO GLU ASN
SEQRES 10 A 312 PRO TYR PRO ALA GLY LEU ASP ASP ALA GLU GLN ALA TYR
SEQRES 11 A 312 ARG PHE VAL LEU ALA GLN GLY PHE LYS PRO GLU ASP ILE
SEQRES 12 A 312 ILE VAL ALA GLY GLU SER ALA GLY GLY ASN LEU ALA ALA
SEQRES 13 A 312 ALA LEU LEU LEU LYS LEU ARG ASP GLN ASP LEU PRO GLN
SEQRES 14 A 312 PRO ALA GLY ALA TYR LEU LEU SER PRO TRP LEU ASP MET
SEQRES 15 A 312 SER GLN SER GLY ALA SER TYR GLU ALA ARG GLY PRO HIS
SEQRES 16 A 312 ASP PRO MET ILE THR HIS ASN ALA LEU THR GLY CYS SER
SEQRES 17 A 312 ALA ALA TYR ARG ALA GLY ALA SER ALA GLU ASP PRO LEU
SEQRES 18 A 312 ILE SER PRO ALA LYS ALA ASP LEU ALA ASP LEU PRO SER
SEQRES 19 A 312 LEU PHE ILE GLN VAL GLY ALA ASP GLU VAL LEU LEU SER
SEQRES 20 A 312 ASP SER VAL GLU PHE THR ARG ARG ALA ALA LEU ALA GLY
SEQRES 21 A 312 LEU ASP VAL ARG LEU HIS VAL TRP ALA ASN MET VAL HIS
SEQRES 22 A 312 ALA TRP PRO LEU PHE HIS PHE ALA LEU PRO VAL SER GLY
SEQRES 23 A 312 LEU ALA ALA ILE ASP GLU ALA GLY ALA TRP ILE SER ARG
SEQRES 24 A 312 GLN LEU GLY GLY HIS LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 312 MET ASN GLY ASN ASP PRO ASP ILE ALA GLY PHE LYS GLN
SEQRES 2 B 312 GLN LEU VAL GLN MET THR ALA MET ARG GLU SER GLN PRO
SEQRES 3 B 312 PRO SER ILE GLU ILE GLU ARG GLN MET PHE ASP ALA GLN
SEQRES 4 B 312 HIS GLY ALA VAL PRO PRO ALA GLU GLY CYS LEU ILE GLU
SEQRES 5 B 312 PRO ILE SER THR GLY GLY VAL ARG GLY GLU ARG ILE THR
SEQRES 6 B 312 PRO LYS SER ALA ASP THR SER LYS ALA LEU ILE TYR PHE
SEQRES 7 B 312 HIS GLY GLY GLY HIS LEU PHE GLY SER ALA LEU SER HIS
SEQRES 8 B 312 ARG HIS LEU VAL SER ARG LEU ALA ALA ALA ALA GLY VAL
SEQRES 9 B 312 VAL ALA TYR ASN MET GLU TYR ARG LEU ALA PRO GLU ASN
SEQRES 10 B 312 PRO TYR PRO ALA GLY LEU ASP ASP ALA GLU GLN ALA TYR
SEQRES 11 B 312 ARG PHE VAL LEU ALA GLN GLY PHE LYS PRO GLU ASP ILE
SEQRES 12 B 312 ILE VAL ALA GLY GLU SER ALA GLY GLY ASN LEU ALA ALA
SEQRES 13 B 312 ALA LEU LEU LEU LYS LEU ARG ASP GLN ASP LEU PRO GLN
SEQRES 14 B 312 PRO ALA GLY ALA TYR LEU LEU SER PRO TRP LEU ASP MET
SEQRES 15 B 312 SER GLN SER GLY ALA SER TYR GLU ALA ARG GLY PRO HIS
SEQRES 16 B 312 ASP PRO MET ILE THR HIS ASN ALA LEU THR GLY CYS SER
SEQRES 17 B 312 ALA ALA TYR ARG ALA GLY ALA SER ALA GLU ASP PRO LEU
SEQRES 18 B 312 ILE SER PRO ALA LYS ALA ASP LEU ALA ASP LEU PRO SER
SEQRES 19 B 312 LEU PHE ILE GLN VAL GLY ALA ASP GLU VAL LEU LEU SER
SEQRES 20 B 312 ASP SER VAL GLU PHE THR ARG ARG ALA ALA LEU ALA GLY
SEQRES 21 B 312 LEU ASP VAL ARG LEU HIS VAL TRP ALA ASN MET VAL HIS
SEQRES 22 B 312 ALA TRP PRO LEU PHE HIS PHE ALA LEU PRO VAL SER GLY
SEQRES 23 B 312 LEU ALA ALA ILE ASP GLU ALA GLY ALA TRP ILE SER ARG
SEQRES 24 B 312 GLN LEU GLY GLY HIS LEU GLU HIS HIS HIS HIS HIS HIS
FORMUL 3 HOH *197(H2 O)
HELIX 1 AA1 ASP A 7 GLN A 25 1 19
HELIX 2 AA2 SER A 28 GLY A 41 1 14
HELIX 3 AA3 SER A 87 GLY A 103 1 17
HELIX 4 AA4 PRO A 120 GLN A 136 1 17
HELIX 5 AA5 LYS A 139 GLU A 141 5 3
HELIX 6 AA6 ALA A 150 GLN A 165 1 16
HELIX 7 AA7 GLY A 186 GLY A 193 1 8
HELIX 8 AA8 PRO A 194 ASP A 196 5 3
HELIX 9 AA9 THR A 200 ALA A 213 1 14
HELIX 10 AB1 SER A 223 ALA A 227 5 5
HELIX 11 AB2 LEU A 245 ALA A 259 1 15
HELIX 12 AB3 ALA A 274 HIS A 279 5 6
HELIX 13 AB4 LEU A 282 LEU A 301 1 20
HELIX 14 AB5 ASP B 7 GLN B 25 1 19
HELIX 15 AB6 SER B 28 GLY B 41 1 14
HELIX 16 AB7 SER B 87 GLY B 103 1 17
HELIX 17 AB8 PRO B 120 GLN B 136 1 17
HELIX 18 AB9 LYS B 139 GLU B 141 5 3
HELIX 19 AC1 SER B 149 GLN B 165 1 17
HELIX 20 AC2 ALA B 187 GLY B 193 1 7
HELIX 21 AC3 PRO B 194 ASP B 196 5 3
HELIX 22 AC4 THR B 200 ALA B 213 1 14
HELIX 23 AC5 SER B 223 ALA B 227 5 5
HELIX 24 AC6 LEU B 245 ALA B 259 1 15
HELIX 25 AC7 ALA B 274 HIS B 279 5 6
HELIX 26 AC8 LEU B 282 LEU B 301 1 20
SHEET 1 AA116 CYS A 49 THR A 56 0
SHEET 2 AA116 VAL A 59 PRO A 66 -1 O THR A 65 N LEU A 50
SHEET 3 AA116 VAL A 104 MET A 109 -1 O ALA A 106 N ILE A 64
SHEET 4 AA116 ASP A 70 PHE A 78 1 N LEU A 75 O TYR A 107
SHEET 5 AA116 ILE A 143 SER A 149 1 O ILE A 144 N ILE A 76
SHEET 6 AA116 GLY A 172 PRO A 178 1 O TYR A 174 N VAL A 145
SHEET 7 AA116 SER A 234 GLY A 240 1 O GLN A 238 N SER A 177
SHEET 8 AA116 VAL A 263 TRP A 268 1 O ARG A 264 N ILE A 237
SHEET 9 AA116 VAL B 263 TRP B 268 -1 O VAL B 267 N VAL A 263
SHEET 10 AA116 SER B 234 GLY B 240 1 N ILE B 237 O ARG B 264
SHEET 11 AA116 GLY B 172 LEU B 176 1 N LEU B 175 O PHE B 236
SHEET 12 AA116 ILE B 143 GLU B 148 1 N VAL B 145 O TYR B 174
SHEET 13 AA116 ASP B 70 PHE B 78 1 N ILE B 76 O ILE B 144
SHEET 14 AA116 VAL B 104 MET B 109 1 O TYR B 107 N LEU B 75
SHEET 15 AA116 VAL B 59 PRO B 66 -1 N ILE B 64 O ALA B 106
SHEET 16 AA116 CYS B 49 THR B 56 -1 N LEU B 50 O THR B 65
CISPEP 1 ALA A 114 PRO A 115 0 3.50
CISPEP 2 TYR A 119 PRO A 120 0 1.17
CISPEP 3 ALA B 114 PRO B 115 0 0.17
CISPEP 4 TYR B 119 PRO B 120 0 4.49
CRYST1 103.800 98.400 75.200 90.00 128.10 90.00 C 1 2 1 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 0.009634 0.000000 0.007554 0.00000
SCALE2 0.000000 0.010163 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016898 0.00000
TER 2260 GLY A 302
TER 4521 GLY B 302
MASTER 463 0 0 26 16 0 0 6 4704 2 0 48
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