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HEADER HYDROLASE 30-JUN-20 6ZL7
TITLE CRYSTAL STRUCTURE OF C173S MUTATION IN THE PMGL2 ESTERASE FROM
TITLE 2 PERMAFROST METAGENOMIC LIBRARY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PMGL2;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.3;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: 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 PMGL2, ESTERASE, PERMAFROST, METAGENOMIC LIBRARY, LIPASE, MUTANT,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.A.GORYAYNOVA,K.M.BOYKO,A.Y.NIKOLAEVA,D.A.KORZHENEVSKIY,
AUTHOR 2 M.V.KRYUKOVA,L.E.PETROVSKAYA,K.A.NOVOTOTSKAYA-VLASOVA,E.M.RIVKINA,
AUTHOR 3 D.A.DOLGIKH,M.P.KIRPICHNIKOV,V.O.POPOV
REVDAT 1 08-JUL-20 6ZL7 0
JRNL AUTH D.A.GORYAYNOVA,K.M.BOYKO,A.Y.NIKOLAEVA,D.A.KORZHENEVSKIY,
JRNL AUTH 2 M.V.KRYUKOVA,L.E.PETROVSKAYA,K.A.NOVOTOTSKAYA-VLASOVA,
JRNL AUTH 3 E.M.RIVKINA,D.A.DOLGIKH,M.P.KIRPICHNIKOV,V.O.POPOV
JRNL TITL CRYSTAL STRUCTURE OF C173S MUTATION IN THE PMGL2 ESTERASE
JRNL TITL 2 FROM PERMAFROST METAGENOMIC LIBRARY
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0258
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) : 56.54
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 90444
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) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4737
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) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6558
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.82
REMARK 3 BIN R VALUE (WORKING SET) : 0.2340
REMARK 3 BIN FREE R VALUE SET COUNT : 335
REMARK 3 BIN FREE R VALUE : 0.2500
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4751
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 25
REMARK 3 SOLVENT ATOMS : 453
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.29
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.08000
REMARK 3 B22 (A**2) : 0.25000
REMARK 3 B33 (A**2) : -0.51000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.44000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.072
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.073
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.048
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.302
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.956
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4960 ; 0.012 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6783 ; 1.891 ; 1.634
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 652 ; 6.455 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 249 ;26.241 ;20.120
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 682 ;12.810 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 45 ;19.077 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 629 ; 0.119 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3952 ; 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 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: U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 6ZL7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-JUN-20.
REMARK 100 THE DEPOSITION ID IS D_1292109711.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-JUN-17
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 : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.31
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 95216
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 56.540
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : 0.06700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.1000
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) : 1.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.30
REMARK 200 R MERGE FOR SHELL (I) : 0.56100
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: MOLREP
REMARK 200 STARTING MODEL: 6QIN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 250MM MAGNESIUM CHLORIDE, 12-18%
REMARK 280 PEG3350, 100MM HEPES PH 7.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 288K
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 46.26500
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23310 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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 ALA A 2
REMARK 465 SER A 3
REMARK 465 GLY A 4
REMARK 465 SER A 5
REMARK 465 ALA A 6
REMARK 465 SER A 7
REMARK 465 SER A 8
REMARK 465 ALA A 9
REMARK 465 GLN A 10
REMARK 465 THR A 11
REMARK 465 PRO A 12
REMARK 465 GLY A 13
REMARK 465 LEU A 14
REMARK 465 MET A 15
REMARK 465 SER A 16
REMARK 465 SER A 334
REMARK 465 SER A 335
REMARK 465 ILE A 336
REMARK 465 PRO A 337
REMARK 465 THR A 338
REMARK 465 PRO A 339
REMARK 465 ARG A 340
REMARK 465 SER A 341
REMARK 465 PRO A 342
REMARK 465 SER A 343
REMARK 465 LEU A 344
REMARK 465 GLU A 345
REMARK 465 HIS A 346
REMARK 465 HIS A 347
REMARK 465 HIS A 348
REMARK 465 HIS A 349
REMARK 465 HIS A 350
REMARK 465 HIS A 351
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 SER B 3
REMARK 465 GLY B 4
REMARK 465 SER B 5
REMARK 465 ALA B 6
REMARK 465 SER B 7
REMARK 465 SER B 8
REMARK 465 ALA B 9
REMARK 465 GLN B 10
REMARK 465 THR B 11
REMARK 465 PRO B 12
REMARK 465 GLY B 13
REMARK 465 SER B 334
REMARK 465 SER B 335
REMARK 465 ILE B 336
REMARK 465 PRO B 337
REMARK 465 THR B 338
REMARK 465 PRO B 339
REMARK 465 ARG B 340
REMARK 465 SER B 341
REMARK 465 PRO B 342
REMARK 465 SER B 343
REMARK 465 LEU B 344
REMARK 465 GLU B 345
REMARK 465 HIS B 346
REMARK 465 HIS B 347
REMARK 465 HIS B 348
REMARK 465 HIS B 349
REMARK 465 HIS B 350
REMARK 465 HIS B 351
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 LYS A 39 CG CD CE NZ
REMARK 470 GLU A 42 CG CD OE1 OE2
REMARK 470 ASN A 44 CG OD1 ND2
REMARK 470 ARG A 49 CD NE CZ NH1 NH2
REMARK 470 ARG A 72 CZ NH1 NH2
REMARK 470 ARG A 144 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 221 CG1 CG2
REMARK 470 GLU A 240 CD OE1 OE2
REMARK 470 ALA A 256 CB
REMARK 470 SER A 333 C O CB OG
REMARK 470 LEU B 14 CG CD1 CD2
REMARK 470 LYS B 39 CD CE NZ
REMARK 470 ARG B 67 CZ NH1 NH2
REMARK 470 ARG B 97 CD NE CZ NH1 NH2
REMARK 470 ARG B 157 NE CZ NH1 NH2
REMARK 470 ARG B 162 CD NE CZ NH1 NH2
REMARK 470 PRO B 220 CG CD
REMARK 470 SER B 333 CA C O CB OG
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 34 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 TYR A 208 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG A 283 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG B 66 NE - CZ - NH2 ANGL. DEV. = -4.5 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 174 -123.99 64.74
REMARK 500 SER A 174 -123.99 57.18
REMARK 500 SER B 174 -124.12 62.98
REMARK 500 SER B 174 -124.12 58.70
REMARK 500 VAL B 221 -50.94 -124.14
REMARK 500 PRO B 223 111.67 -32.00
REMARK 500 ASP B 309 57.63 -90.85
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 PRO B 220 VAL B 221 -138.35
REMARK 500 VAL B 221 GLY B 222 -147.29
REMARK 500
REMARK 500 REMARK: NULL
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 PG6 A 402
REMARK 610 PG6 B 401
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 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG6 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG6 B 401
DBREF1 6ZL7 A 1 343 UNP A0A142J6I6_9BACT
DBREF2 6ZL7 A A0A142J6I6 1 343
DBREF1 6ZL7 B 1 343 UNP A0A142J6I6_9BACT
DBREF2 6ZL7 B A0A142J6I6 1 343
SEQADV 6ZL7 SER A 173 UNP A0A142J6I CYS 173 ENGINEERED MUTATION
SEQADV 6ZL7 LEU A 344 UNP A0A142J6I EXPRESSION TAG
SEQADV 6ZL7 GLU A 345 UNP A0A142J6I EXPRESSION TAG
SEQADV 6ZL7 HIS A 346 UNP A0A142J6I EXPRESSION TAG
SEQADV 6ZL7 HIS A 347 UNP A0A142J6I EXPRESSION TAG
SEQADV 6ZL7 HIS A 348 UNP A0A142J6I EXPRESSION TAG
SEQADV 6ZL7 HIS A 349 UNP A0A142J6I EXPRESSION TAG
SEQADV 6ZL7 HIS A 350 UNP A0A142J6I EXPRESSION TAG
SEQADV 6ZL7 HIS A 351 UNP A0A142J6I EXPRESSION TAG
SEQADV 6ZL7 SER B 173 UNP A0A142J6I CYS 173 ENGINEERED MUTATION
SEQADV 6ZL7 LEU B 344 UNP A0A142J6I EXPRESSION TAG
SEQADV 6ZL7 GLU B 345 UNP A0A142J6I EXPRESSION TAG
SEQADV 6ZL7 HIS B 346 UNP A0A142J6I EXPRESSION TAG
SEQADV 6ZL7 HIS B 347 UNP A0A142J6I EXPRESSION TAG
SEQADV 6ZL7 HIS B 348 UNP A0A142J6I EXPRESSION TAG
SEQADV 6ZL7 HIS B 349 UNP A0A142J6I EXPRESSION TAG
SEQADV 6ZL7 HIS B 350 UNP A0A142J6I EXPRESSION TAG
SEQADV 6ZL7 HIS B 351 UNP A0A142J6I EXPRESSION TAG
SEQRES 1 A 351 MET ALA SER GLY SER ALA SER SER ALA GLN THR PRO GLY
SEQRES 2 A 351 LEU MET SER TRP LEU PRO PRO SER ASN GLN LEU SER PRO
SEQRES 3 A 351 GLU ALA ARG SER VAL LEU ASP ARG MET ASP ALA ALA LYS
SEQRES 4 A 351 ALA PRO GLU PHE ASN GLY ASP LEU VAL ARG GLN ARG ALA
SEQRES 5 A 351 PHE TYR GLN GLN PHE ASN ASP ASP ARG LEU VAL GLU MET
SEQRES 6 A 351 ARG ARG VAL PHE ARG THR ARG GLU ARG HIS GLU THR LEU
SEQRES 7 A 351 ASN ALA VAL HIS VAL GLN VAL VAL GLU PRO ALA ASP GLY
SEQRES 8 A 351 VAL SER ALA ARG ASN ARG ASP ARG VAL LEU ILE ASN VAL
SEQRES 9 A 351 HIS GLY GLY ALA PHE MET TRP GLY ALA GLY SER GLY ALA
SEQRES 10 A 351 LEU VAL GLU ALA ILE PRO ILE ALA ALA THR MET GLY VAL
SEQRES 11 A 351 SER VAL VAL THR VAL ASP TYR ARG LEU ALA PRO GLU ASN
SEQRES 12 A 351 ARG TYR PRO ALA ALA SER GLU ASP VAL THR ALA VAL TYR
SEQRES 13 A 351 ARG ALA LEU LEU GLU ARG TYR PRO ALA ALA ASN ILE GLY
SEQRES 14 A 351 ILE PHE GLY SER SER ALA GLY GLY VAL ILE THR ALA GLN
SEQRES 15 A 351 ALA VAL THR TRP ILE ARG ARG GLU GLY LEU PRO ARG PRO
SEQRES 16 A 351 GLY ALA ILE GLY THR LEU CYS GLY THR GLY ALA PRO TYR
SEQRES 17 A 351 SER GLY ASP SER PRO TYR LEU ALA GLY VAL VAL PRO VAL
SEQRES 18 A 351 GLY PRO GLY VAL LYS ALA PRO PRO LEU PRO GLY LEU LEU
SEQRES 19 A 351 PRO THR ALA TYR MET GLU GLY VAL GLY ALA ASP ASP ALA
SEQRES 20 A 351 ARG ALA TYR PRO LEU THR SER ASP ALA GLU THR VAL PHE
SEQRES 21 A 351 MET PRO PRO THR LEU LEU LEU ALA GLY GLY ARG ASP PHE
SEQRES 22 A 351 ALA VAL SER ALA LEU SER LEU ALA HIS ARG ARG LEU ALA
SEQRES 23 A 351 ARG ALA GLY VAL ASP SER GLU LEU HIS LEU PHE ASP GLY
SEQRES 24 A 351 LEU PRO HIS ALA PHE PHE VAL TRP PRO ASP MET PRO GLU
SEQRES 25 A 351 SER LEU GLU ALA TYR ALA LEU ILE ALA GLY PHE PHE ASP
SEQRES 26 A 351 SER ARG LEU GLY LEU THR PRO SER SER SER ILE PRO THR
SEQRES 27 A 351 PRO ARG SER PRO SER LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 351 MET ALA SER GLY SER ALA SER SER ALA GLN THR PRO GLY
SEQRES 2 B 351 LEU MET SER TRP LEU PRO PRO SER ASN GLN LEU SER PRO
SEQRES 3 B 351 GLU ALA ARG SER VAL LEU ASP ARG MET ASP ALA ALA LYS
SEQRES 4 B 351 ALA PRO GLU PHE ASN GLY ASP LEU VAL ARG GLN ARG ALA
SEQRES 5 B 351 PHE TYR GLN GLN PHE ASN ASP ASP ARG LEU VAL GLU MET
SEQRES 6 B 351 ARG ARG VAL PHE ARG THR ARG GLU ARG HIS GLU THR LEU
SEQRES 7 B 351 ASN ALA VAL HIS VAL GLN VAL VAL GLU PRO ALA ASP GLY
SEQRES 8 B 351 VAL SER ALA ARG ASN ARG ASP ARG VAL LEU ILE ASN VAL
SEQRES 9 B 351 HIS GLY GLY ALA PHE MET TRP GLY ALA GLY SER GLY ALA
SEQRES 10 B 351 LEU VAL GLU ALA ILE PRO ILE ALA ALA THR MET GLY VAL
SEQRES 11 B 351 SER VAL VAL THR VAL ASP TYR ARG LEU ALA PRO GLU ASN
SEQRES 12 B 351 ARG TYR PRO ALA ALA SER GLU ASP VAL THR ALA VAL TYR
SEQRES 13 B 351 ARG ALA LEU LEU GLU ARG TYR PRO ALA ALA ASN ILE GLY
SEQRES 14 B 351 ILE PHE GLY SER SER ALA GLY GLY VAL ILE THR ALA GLN
SEQRES 15 B 351 ALA VAL THR TRP ILE ARG ARG GLU GLY LEU PRO ARG PRO
SEQRES 16 B 351 GLY ALA ILE GLY THR LEU CYS GLY THR GLY ALA PRO TYR
SEQRES 17 B 351 SER GLY ASP SER PRO TYR LEU ALA GLY VAL VAL PRO VAL
SEQRES 18 B 351 GLY PRO GLY VAL LYS ALA PRO PRO LEU PRO GLY LEU LEU
SEQRES 19 B 351 PRO THR ALA TYR MET GLU GLY VAL GLY ALA ASP ASP ALA
SEQRES 20 B 351 ARG ALA TYR PRO LEU THR SER ASP ALA GLU THR VAL PHE
SEQRES 21 B 351 MET PRO PRO THR LEU LEU LEU ALA GLY GLY ARG ASP PHE
SEQRES 22 B 351 ALA VAL SER ALA LEU SER LEU ALA HIS ARG ARG LEU ALA
SEQRES 23 B 351 ARG ALA GLY VAL ASP SER GLU LEU HIS LEU PHE ASP GLY
SEQRES 24 B 351 LEU PRO HIS ALA PHE PHE VAL TRP PRO ASP MET PRO GLU
SEQRES 25 B 351 SER LEU GLU ALA TYR ALA LEU ILE ALA GLY PHE PHE ASP
SEQRES 26 B 351 SER ARG LEU GLY LEU THR PRO SER SER SER ILE PRO THR
SEQRES 27 B 351 PRO ARG SER PRO SER LEU GLU HIS HIS HIS HIS HIS HIS
HET MG A 401 1
HET PG6 A 402 13
HET PG6 B 401 11
HETNAM MG MAGNESIUM ION
HETNAM PG6 1-(2-METHOXY-ETHOXY)-2-{2-[2-(2-METHOXY-ETHOXY]-
HETNAM 2 PG6 ETHOXY}-ETHANE
FORMUL 3 MG MG 2+
FORMUL 4 PG6 2(C12 H26 O6)
FORMUL 6 HOH *453(H2 O)
HELIX 1 AA1 SER A 25 ALA A 38 1 14
HELIX 2 AA2 ASP A 46 PHE A 69 1 24
HELIX 3 AA3 SER A 93 ARG A 97 5 5
HELIX 4 AA4 GLY A 114 GLY A 129 1 16
HELIX 5 AA5 PRO A 146 LEU A 160 1 15
HELIX 6 AA6 PRO A 164 ALA A 166 5 3
HELIX 7 AA7 SER A 174 GLU A 190 1 17
HELIX 8 AA8 ASP A 211 ALA A 216 1 6
HELIX 9 AA9 THR A 236 GLU A 240 5 5
HELIX 10 AB1 TYR A 250 THR A 253 5 4
HELIX 11 AB2 SER A 254 PHE A 260 1 7
HELIX 12 AB3 ALA A 274 ALA A 288 1 15
HELIX 13 AB4 ALA A 303 TRP A 307 5 5
HELIX 14 AB5 MET A 310 LEU A 328 1 19
HELIX 15 AB6 LEU B 14 LEU B 18 5 5
HELIX 16 AB7 SER B 25 ALA B 38 1 14
HELIX 17 AB8 ASP B 46 PHE B 69 1 24
HELIX 18 AB9 SER B 93 ARG B 97 5 5
HELIX 19 AC1 GLY B 114 GLY B 129 1 16
HELIX 20 AC2 PRO B 146 LEU B 160 1 15
HELIX 21 AC3 PRO B 164 ALA B 166 5 3
HELIX 22 AC4 SER B 174 GLU B 190 1 17
HELIX 23 AC5 ASP B 211 ALA B 216 1 6
HELIX 24 AC6 THR B 236 GLU B 240 5 5
HELIX 25 AC7 TYR B 250 THR B 253 5 4
HELIX 26 AC8 SER B 254 PHE B 260 1 7
HELIX 27 AC9 ALA B 274 ALA B 288 1 15
HELIX 28 AD1 ALA B 303 TRP B 307 5 5
HELIX 29 AD2 MET B 310 LEU B 328 1 19
SHEET 1 AA1 8 THR A 71 LEU A 78 0
SHEET 2 AA1 8 VAL A 81 PRO A 88 -1 O VAL A 85 N ARG A 74
SHEET 3 AA1 8 VAL A 132 VAL A 135 -1 O VAL A 132 N VAL A 86
SHEET 4 AA1 8 VAL A 100 VAL A 104 1 N LEU A 101 O VAL A 133
SHEET 5 AA1 8 ILE A 168 SER A 173 1 O PHE A 171 N ILE A 102
SHEET 6 AA1 8 ALA A 197 LEU A 201 1 O LEU A 201 N GLY A 172
SHEET 7 AA1 8 THR A 264 GLY A 269 1 O LEU A 265 N ILE A 198
SHEET 8 AA1 8 SER A 292 PHE A 297 1 O GLU A 293 N LEU A 266
SHEET 1 AA2 8 THR B 71 LEU B 78 0
SHEET 2 AA2 8 VAL B 81 PRO B 88 -1 O VAL B 85 N ARG B 74
SHEET 3 AA2 8 VAL B 132 VAL B 135 -1 O VAL B 132 N VAL B 86
SHEET 4 AA2 8 VAL B 100 VAL B 104 1 N LEU B 101 O VAL B 133
SHEET 5 AA2 8 ILE B 168 SER B 173 1 O GLY B 169 N ILE B 102
SHEET 6 AA2 8 ALA B 197 LEU B 201 1 O LEU B 201 N GLY B 172
SHEET 7 AA2 8 THR B 264 GLY B 269 1 O LEU B 265 N ILE B 198
SHEET 8 AA2 8 SER B 292 PHE B 297 1 O GLU B 293 N LEU B 266
LINK MG MG A 401 O HOH A 667 1555 1555 2.99
CISPEP 1 ALA A 140 PRO A 141 0 -2.38
CISPEP 2 TYR A 145 PRO A 146 0 2.63
CISPEP 3 ALA B 140 PRO B 141 0 -2.54
CISPEP 4 TYR B 145 PRO B 146 0 5.56
SITE 1 AC1 7 HIS A 282 GLU A 293 LEU A 294 HOH A 667
SITE 2 AC1 7 HIS B 282 GLU B 293 LEU B 294
SITE 1 AC2 9 SER A 174 ALA A 175 GLY A 203 THR A 204
SITE 2 AC2 9 ALA A 206 TYR A 208 PHE A 273 ALA A 274
SITE 3 AC2 9 ALA A 277
SITE 1 AC3 9 SER B 174 ALA B 175 CYS B 202 GLY B 203
SITE 2 AC3 9 THR B 204 ALA B 206 PHE B 273 ALA B 274
SITE 3 AC3 9 ALA B 277
CRYST1 47.149 92.530 74.410 90.00 106.61 90.00 P 1 21 1 4
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 0.021209 0.000000 0.006327 0.00000
SCALE2 0.000000 0.010807 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014024 0.00000
TER 2381 SER A 333
TER 4808 SER B 333
MASTER 407 0 3 29 16 0 8 6 5229 2 26 54
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