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HEADER HYDROLASE 17-MAR-17 5NG7
TITLE NOVEL EPOXIDE HYDROLASES BELONGING TO THE ALPHA/BETA HYDROLASES
TITLE 2 SUPERFAMILY IN METAGENOMES FROM HOT ENVIRONMENTS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPOXIDE HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.3.2.10;
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: 562
KEYWDS EPOXIDE HYDROLASES, METAGENOMICS, INDUSTRIAL BIOCATALYSIS,
KEYWDS 2 STEREOSELECTIVITY, PROTEIN STRUCTURE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.E.FERRANDI,S.A.DE ROSE,C.SAYER,E.GUAZZELLI,C.MARCHESI,V.SANEEI,
AUTHOR 2 M.N.ISUPOV,J.A.LITTLECHILD,D.MONTI
REVDAT 1 16-MAY-18 5NG7 0
JRNL AUTH E.E.FERRANDI,S.A.DE ROSE,C.SAYER,E.GUAZZELLI,C.MARCHESI,
JRNL AUTH 2 V.SANEEI,M.N.ISUPOV,J.A.LITTLECHILD,D.MONTI
JRNL TITL NOVEL EPOXIDE HYDROLASES BELONGING TO THE ALPHA/BETA
JRNL TITL 2 HYDROLASES SUPERFAMILY IN METAGENOMES FROM HOT ENVIRONMENTS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.39 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) : 1.39
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.51
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 99619
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) : 0.174
REMARK 3 R VALUE (WORKING SET) : 0.173
REMARK 3 FREE R VALUE : 0.204
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5200
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) : 1.39
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.43
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6061
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 81.44
REMARK 3 BIN R VALUE (WORKING SET) : 0.3150
REMARK 3 BIN FREE R VALUE SET COUNT : 323
REMARK 3 BIN FREE R VALUE : 0.3250
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4792
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 29
REMARK 3 SOLVENT ATOMS : 616
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.81
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.67000
REMARK 3 B22 (A**2) : 0.61000
REMARK 3 B33 (A**2) : 0.14000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.18000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.069
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.071
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.057
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.473
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.975
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.965
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5664 ; 0.013 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7809 ; 1.637 ; 1.964
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 758 ; 5.772 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 277 ;35.458 ;24.079
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1095 ;16.150 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 33 ;22.742 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 856 ; 0.114 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4351 ; 0.009 ; 0.021
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): 2554 ; 3.716 ; 5.533
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3239 ; 5.274 ; 9.286
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3110 ; 5.055 ; 6.580
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): 24805 ; 8.232 ;41.363
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 2 290 B 2 290 21536 0.12 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 : 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: NULL
REMARK 4
REMARK 4 5NG7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-MAR-17.
REMARK 100 THE DEPOSITION ID IS D_1200004049.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-AUG-16
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 : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
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, XIA2
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 104819
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.390
REMARK 200 RESOLUTION RANGE LOW (A) : 39.510
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.03500
REMARK 200 FOR THE DATA SET : 15.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.39
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.41
REMARK 200 COMPLETENESS FOR SHELL (%) : 79.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.77000
REMARK 200 FOR SHELL : 1.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MORDA
REMARK 200 STARTING MODEL: 4INZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM MAGNESIUM FORMATE DEHYDRATE,
REMARK 280 100MM SODIUM HEPES 7.5 20 % W/V PEG 3350, PH 7.5, MICROBATCH,
REMARK 280 TEMPERATURE 291K
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 81.97000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.11000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 81.97000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 23.11000
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: 3580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 425 LIES ON A SPECIAL POSITION.
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 HIS A 294
REMARK 465 HIS A 295
REMARK 465 HIS A 296
REMARK 465 HIS A 297
REMARK 465 HIS A 298
REMARK 465 HIS A 299
REMARK 465 MET B 1
REMARK 465 ASP B 292
REMARK 465 ILE B 293
REMARK 465 HIS B 294
REMARK 465 HIS B 295
REMARK 465 HIS B 296
REMARK 465 HIS B 297
REMARK 465 HIS B 298
REMARK 465 HIS B 299
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 559 O HOH B 633 4555 1.98
REMARK 500 O HOH A 405 O HOH B 426 4555 1.99
REMARK 500 O HOH A 496 O HOH B 446 3455 2.16
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 35 59.46 -103.18
REMARK 500 ASP A 36 -159.52 -103.76
REMARK 500 PHE A 37 -166.66 -172.39
REMARK 500 ASN A 63 -109.34 44.70
REMARK 500 ASP A 101 -131.06 58.06
REMARK 500 ASN A 156 -45.53 68.86
REMARK 500 LYS A 240 40.50 -89.79
REMARK 500 LYS A 240 40.50 -89.77
REMARK 500 ASN A 251 73.17 60.55
REMARK 500 ASN A 251 72.73 61.39
REMARK 500 TRP A 271 53.82 -92.17
REMARK 500 ASP A 292 -143.64 -90.48
REMARK 500 ASN B 13 -118.41 46.35
REMARK 500 PRO B 35 60.19 -104.78
REMARK 500 ASP B 36 -158.98 -103.48
REMARK 500 PHE B 37 -167.99 -172.80
REMARK 500 ASN B 63 -110.90 45.72
REMARK 500 ASP B 101 -133.01 58.32
REMARK 500 ASN B 156 -45.39 70.90
REMARK 500 LYS B 240 39.26 -89.67
REMARK 500 ASN B 251 73.37 47.38
REMARK 500 GLU B 257 64.25 -107.62
REMARK 500 GLU B 257 69.07 -111.15
REMARK 500 TRP B 271 55.78 -91.53
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 ASP A 254 PHE A 255 145.16
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 747 DISTANCE = 6.37 ANGSTROMS
REMARK 525 HOH B 669 DISTANCE = 5.95 ANGSTROMS
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 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SER B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 305
DBREF 5NG7 A 1 299 PDB 5NG7 5NG7 1 299
DBREF 5NG7 B 1 299 PDB 5NG7 5NG7 1 299
SEQRES 1 A 299 MET ASN GLU MET LEU LYS HIS GLU TYR VAL LYS VAL ASN
SEQRES 2 A 299 GLY ILE LYS MET HIS TYR VAL THR GLN GLY LYS GLY LYS
SEQRES 3 A 299 LEU LEU LEU LEU LEU HIS GLY PHE PRO ASP PHE TRP TYR
SEQRES 4 A 299 VAL TRP ARG PHE GLN ILE PRO ALA LEU ALA LYS HIS PHE
SEQRES 5 A 299 ARG VAL VAL ALA PRO ASP LEU ARG GLY TYR ASN GLU THR
SEQRES 6 A 299 ASP LYS PRO GLU GLY VAL GLU ASN TYR ARG LEU ASP LEU
SEQRES 7 A 299 LEU ALA LYS ASP ILE LEU GLY LEU ILE LYS ALA LEU GLY
SEQRES 8 A 299 GLU GLU HIS ALA VAL VAL VAL GLY HIS ASP TRP GLY GLY
SEQRES 9 A 299 ILE ILE SER TRP THR LEU THR ALA PHE ASN PRO GLN ALA
SEQRES 10 A 299 VAL GLU LYS LEU VAL ILE LEU ASN ALA PRO HIS PRO LYS
SEQRES 11 A 299 ALA TYR MET THR ARG THR LYS ASN SER LEU ARG GLN LEU
SEQRES 12 A 299 GLN LYS SER TRP TYR VAL PHE PHE PHE GLN VAL ALA ASN
SEQRES 13 A 299 ILE PRO GLU LYS ILE LEU SER ARG ASN GLU PHE ALA PHE
SEQRES 14 A 299 LEU LYS ASN MET LEU ILE GLN SER PHE VAL ARG ARG ASP
SEQRES 15 A 299 LEU LEU THR GLU GLU ASP LEU ARG ILE TYR VAL ASP ALA
SEQRES 16 A 299 TRP SER LYS SER GLY ALA LEU THR SER ALA LEU ASN TYR
SEQRES 17 A 299 TYR ARG ALA ASN LEU ASN PRO ASP ILE ILE PHE SER GLU
SEQRES 18 A 299 LYS THR VAL VAL PHE PRO LYS ILE LYS VAL PRO THR LEU
SEQRES 19 A 299 VAL ILE TRP GLY GLU LYS ASP VAL ALA ILE SER LYS ASP
SEQRES 20 A 299 LEU ILE VAL ASN MET GLU ASP PHE ILE GLU ALA PRO TYR
SEQRES 21 A 299 SER ILE LYS TYR PHE PRO GLU CYS GLY HIS TRP VAL GLN
SEQRES 22 A 299 LEU GLU GLU PRO GLU LEU VAL ARG LYS HIS ILE GLU GLU
SEQRES 23 A 299 PHE ILE LEU LYS SER ASP ILE HIS HIS HIS HIS HIS HIS
SEQRES 1 B 299 MET ASN GLU MET LEU LYS HIS GLU TYR VAL LYS VAL ASN
SEQRES 2 B 299 GLY ILE LYS MET HIS TYR VAL THR GLN GLY LYS GLY LYS
SEQRES 3 B 299 LEU LEU LEU LEU LEU HIS GLY PHE PRO ASP PHE TRP TYR
SEQRES 4 B 299 VAL TRP ARG PHE GLN ILE PRO ALA LEU ALA LYS HIS PHE
SEQRES 5 B 299 ARG VAL VAL ALA PRO ASP LEU ARG GLY TYR ASN GLU THR
SEQRES 6 B 299 ASP LYS PRO GLU GLY VAL GLU ASN TYR ARG LEU ASP LEU
SEQRES 7 B 299 LEU ALA LYS ASP ILE LEU GLY LEU ILE LYS ALA LEU GLY
SEQRES 8 B 299 GLU GLU HIS ALA VAL VAL VAL GLY HIS ASP TRP GLY GLY
SEQRES 9 B 299 ILE ILE SER TRP THR LEU THR ALA PHE ASN PRO GLN ALA
SEQRES 10 B 299 VAL GLU LYS LEU VAL ILE LEU ASN ALA PRO HIS PRO LYS
SEQRES 11 B 299 ALA TYR MET THR ARG THR LYS ASN SER LEU ARG GLN LEU
SEQRES 12 B 299 GLN LYS SER TRP TYR VAL PHE PHE PHE GLN VAL ALA ASN
SEQRES 13 B 299 ILE PRO GLU LYS ILE LEU SER ARG ASN GLU PHE ALA PHE
SEQRES 14 B 299 LEU LYS ASN MET LEU ILE GLN SER PHE VAL ARG ARG ASP
SEQRES 15 B 299 LEU LEU THR GLU GLU ASP LEU ARG ILE TYR VAL ASP ALA
SEQRES 16 B 299 TRP SER LYS SER GLY ALA LEU THR SER ALA LEU ASN TYR
SEQRES 17 B 299 TYR ARG ALA ASN LEU ASN PRO ASP ILE ILE PHE SER GLU
SEQRES 18 B 299 LYS THR VAL VAL PHE PRO LYS ILE LYS VAL PRO THR LEU
SEQRES 19 B 299 VAL ILE TRP GLY GLU LYS ASP VAL ALA ILE SER LYS ASP
SEQRES 20 B 299 LEU ILE VAL ASN MET GLU ASP PHE ILE GLU ALA PRO TYR
SEQRES 21 B 299 SER ILE LYS TYR PHE PRO GLU CYS GLY HIS TRP VAL GLN
SEQRES 22 B 299 LEU GLU GLU PRO GLU LEU VAL ARG LYS HIS ILE GLU GLU
SEQRES 23 B 299 PHE ILE LEU LYS SER ASP ILE HIS HIS HIS HIS HIS HIS
HET CL A 301 1
HET EDO A 302 4
HET EDO A 303 4
HET CL B 301 1
HET CL B 302 1
HET SER B 303 7
HET EDO B 304 4
HET PEG B 305 7
HETNAM CL CHLORIDE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM SER SERINE
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 CL 3(CL 1-)
FORMUL 4 EDO 3(C2 H6 O2)
FORMUL 8 SER C3 H7 N O3
FORMUL 10 PEG C4 H10 O3
FORMUL 11 HOH *616(H2 O)
HELIX 1 AA1 PHE A 37 ARG A 42 5 6
HELIX 2 AA2 PHE A 43 ALA A 49 1 7
HELIX 3 AA3 GLY A 70 TYR A 74 5 5
HELIX 4 AA4 ARG A 75 LEU A 90 1 16
HELIX 5 AA5 ASP A 101 ASN A 114 1 14
HELIX 6 AA6 HIS A 128 THR A 136 1 9
HELIX 7 AA7 SER A 139 SER A 146 1 8
HELIX 8 AA8 SER A 146 PHE A 152 1 7
HELIX 9 AA9 ASN A 156 PHE A 178 1 23
HELIX 10 AB1 THR A 185 SER A 197 1 13
HELIX 11 AB2 GLY A 200 LEU A 213 1 14
HELIX 12 AB3 ASN A 214 SER A 220 1 7
HELIX 13 AB4 SER A 245 ILE A 249 5 5
HELIX 14 AB5 TRP A 271 GLU A 276 1 6
HELIX 15 AB6 GLU A 276 LYS A 290 1 15
HELIX 16 AB7 PHE B 37 ARG B 42 5 6
HELIX 17 AB8 PHE B 43 ALA B 49 1 7
HELIX 18 AB9 GLY B 70 TYR B 74 5 5
HELIX 19 AC1 ARG B 75 LEU B 90 1 16
HELIX 20 AC2 ASP B 101 ASN B 114 1 14
HELIX 21 AC3 HIS B 128 THR B 136 1 9
HELIX 22 AC4 SER B 139 SER B 146 1 8
HELIX 23 AC5 SER B 146 PHE B 152 1 7
HELIX 24 AC6 ASN B 156 PHE B 178 1 23
HELIX 25 AC7 THR B 185 SER B 197 1 13
HELIX 26 AC8 GLY B 200 LEU B 213 1 14
HELIX 27 AC9 ASN B 214 PHE B 219 1 6
HELIX 28 AD1 SER B 245 ILE B 249 5 5
HELIX 29 AD2 MET B 252 ILE B 256 5 5
HELIX 30 AD3 TRP B 271 GLU B 276 1 6
HELIX 31 AD4 GLU B 276 LYS B 290 1 15
SHEET 1 AA1 8 LYS A 6 VAL A 12 0
SHEET 2 AA1 8 ILE A 15 GLN A 22 -1 O MET A 17 N VAL A 10
SHEET 3 AA1 8 PHE A 52 PRO A 57 -1 O VAL A 54 N GLN A 22
SHEET 4 AA1 8 LYS A 26 LEU A 31 1 N LEU A 28 O ARG A 53
SHEET 5 AA1 8 ALA A 95 HIS A 100 1 O VAL A 96 N LEU A 29
SHEET 6 AA1 8 VAL A 118 LEU A 124 1 O LEU A 124 N GLY A 99
SHEET 7 AA1 8 THR A 233 GLY A 238 1 O ILE A 236 N ILE A 123
SHEET 8 AA1 8 TYR A 260 PHE A 265 1 O PHE A 265 N TRP A 237
SHEET 1 AA2 8 LYS B 6 VAL B 12 0
SHEET 2 AA2 8 ILE B 15 GLN B 22 -1 O MET B 17 N VAL B 10
SHEET 3 AA2 8 ARG B 53 PRO B 57 -1 O ALA B 56 N VAL B 20
SHEET 4 AA2 8 LEU B 27 LEU B 31 1 N LEU B 28 O ARG B 53
SHEET 5 AA2 8 ALA B 95 HIS B 100 1 O VAL B 96 N LEU B 29
SHEET 6 AA2 8 VAL B 118 LEU B 124 1 O LEU B 124 N GLY B 99
SHEET 7 AA2 8 THR B 233 GLY B 238 1 O ILE B 236 N ILE B 123
SHEET 8 AA2 8 TYR B 260 PHE B 265 1 O PHE B 265 N TRP B 237
CISPEP 1 PHE A 34 PRO A 35 0 -3.61
CISPEP 2 PHE B 34 PRO B 35 0 -0.05
SITE 1 AC1 4 PHE A 265 PRO A 266 GLU A 267 HOH A 436
SITE 1 AC2 3 ALA A 168 HOH A 426 HOH A 438
SITE 1 AC3 5 ASN A 138 LEU A 140 ARG A 141 GLN B 176
SITE 2 AC3 5 PEG B 305
SITE 1 AC4 2 ARG B 135 PHE B 255
SITE 1 AC5 3 PHE B 265 PRO B 266 GLU B 267
SITE 1 AC6 7 ASP B 101 PRO B 127 TYR B 132 TYR B 209
SITE 2 AC6 7 LEU B 213 HOH B 414 HOH B 490
SITE 1 AC7 3 ILE B 191 HOH B 416 HOH B 557
SITE 1 AC8 7 LYS A 137 ASN A 138 EDO A 303 HOH A 419
SITE 2 AC8 7 ASN B 172 GLN B 176 HOH B 545
CRYST1 163.940 46.220 73.870 90.00 106.94 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 0.006100 0.000000 0.001858 0.00000
SCALE2 0.000000 0.021636 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014151 0.00000
TER 2784 ILE A 293
TER 5403 SER B 291
MASTER 394 0 8 31 16 0 11 6 5437 2 19 46
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