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HEADER BIOSYNTHETIC PROTEIN 12-OCT-21 7VO4
TITLE PIMARICIN TYPE I PKS THIOESTERASE DOMAIN (APO PIM TE)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SCNS4;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: PIMARICIN TYPE I PKS THIOESTERASE DOMAIN (PIM TE);
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES CHATTANOOGENSIS;
SOURCE 3 ORGANISM_TAXID: 66876;
SOURCE 4 GENE: SCNS4;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS THIOESTERASE, TYPE I THIOESTERASE, PIMARICIN, POLYKETIDE SYNTHASE
KEYWDS 2 THIOESTERASE DOMAIN, BIOSYNTHETIC PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR L.BAI,Y.ZHOU
REVDAT 1 19-JAN-22 7VO4 0
JRNL AUTH Y.ZHOU,W.TAO,Z.QI,J.WEI,T.SHI,Q.KANG,J.ZHENG,Y.ZHAO,L.BAI
JRNL TITL STRUCTURAL AND MECHANISTIC INSIGHTS INTO CHAIN RELEASE OF
JRNL TITL 2 THE POLYENE PKS THIOESTERASE DOMAIN
JRNL REF ACS CATALYSIS V. 12 762 2022
JRNL REFN ESSN 2155-5435
JRNL DOI 10.1021/ACSCATAL.1C04991
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 83.46
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 28306
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) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1465
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2083
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.91
REMARK 3 BIN R VALUE (WORKING SET) : 0.3200
REMARK 3 BIN FREE R VALUE SET COUNT : 104
REMARK 3 BIN FREE R VALUE : 0.3680
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3597
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 62
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.11
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.13000
REMARK 3 B22 (A**2) : -0.53000
REMARK 3 B33 (A**2) : 0.15000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.63000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.226
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.192
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.146
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.661
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.938
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.905
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3664 ; 0.018 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3486 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4992 ; 1.870 ; 1.973
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7953 ; 1.132 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 483 ; 6.908 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 137 ;30.596 ;22.117
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 540 ;17.653 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 36 ;19.296 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 600 ; 0.121 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4132 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 796 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 7VO4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-OCT-21.
REMARK 100 THE DEPOSITION ID IS D_1300025019.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-JAN-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5-9.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97852
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29474
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 83.460
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.06700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.8000
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) : 2.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.46000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 0.771
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: 2H7X
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH 7.5, 18%-25% W/V
REMARK 280 POLYETHYLENE GLYCOL 6000, 5% V/V (+/-)-2-METHYL-2,4-PENTANEDIOL,
REMARK 280 PH 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.15K
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 29.43350
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: 1700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 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 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 -51.94600
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 29.43350
REMARK 350 BIOMT3 2 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 PHE A 1
REMARK 465 LEU A 2
REMARK 465 PRO A 3
REMARK 465 ALA A 4
REMARK 465 ALA A 5
REMARK 465 ALA A 6
REMARK 465 PRO A 7
REMARK 465 LEU A 168
REMARK 465 SER A 169
REMARK 465 LEU A 170
REMARK 465 ARG A 171
REMARK 465 HIS A 172
REMARK 465 GLU A 173
REMARK 465 GLN A 174
REMARK 465 ASN A 175
REMARK 465 GLU A 176
REMARK 465 THR A 177
REMARK 465 ILE A 178
REMARK 465 ASP A 179
REMARK 465 TYR A 180
REMARK 465 VAL A 190
REMARK 465 GLU A 192
REMARK 465 GLY A 236
REMARK 465 ILE A 237
REMARK 465 GLY A 238
REMARK 465 THR A 239
REMARK 465 ASP A 240
REMARK 465 THR A 241
REMARK 465 GLY A 242
REMARK 465 ILE A 243
REMARK 465 TYR A 244
REMARK 465 GLY A 245
REMARK 465 GLU A 246
REMARK 465 ASP A 247
REMARK 465 HIS A 248
REMARK 465 GLY A 249
REMARK 465 SER A 250
REMARK 465 PRO A 251
REMARK 465 GLY A 284
REMARK 465 ASN A 285
REMARK 465 ALA A 286
REMARK 465 PHE B 1
REMARK 465 LEU B 2
REMARK 465 PRO B 3
REMARK 465 ALA B 4
REMARK 465 ALA B 5
REMARK 465 ALA B 6
REMARK 465 PRO B 7
REMARK 465 LEU B 170
REMARK 465 ARG B 171
REMARK 465 HIS B 172
REMARK 465 GLU B 173
REMARK 465 GLN B 174
REMARK 465 ASN B 175
REMARK 465 GLU B 176
REMARK 465 THR B 177
REMARK 465 ILE B 178
REMARK 465 ASP B 179
REMARK 465 TYR B 180
REMARK 465 ASP B 191
REMARK 465 GLU B 192
REMARK 465 VAL B 193
REMARK 465 PHE B 235
REMARK 465 GLY B 236
REMARK 465 ILE B 237
REMARK 465 GLY B 238
REMARK 465 THR B 239
REMARK 465 ASP B 240
REMARK 465 THR B 241
REMARK 465 GLY B 242
REMARK 465 ILE B 243
REMARK 465 TYR B 244
REMARK 465 GLY B 245
REMARK 465 GLU B 246
REMARK 465 ASP B 247
REMARK 465 HIS B 248
REMARK 465 GLY B 249
REMARK 465 GLY B 284
REMARK 465 ASN B 285
REMARK 465 ALA B 286
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 GLU A 21 CG CD OE1 OE2
REMARK 470 ARG A 24 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 43 CG CD OE1 OE2
REMARK 470 GLU A 49 CG CD OE1 OE2
REMARK 470 LEU A 183 CG CD1 CD2
REMARK 470 MET A 184 CG SD CE
REMARK 470 ARG A 186 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 191 CG OD1 OD2
REMARK 470 VAL A 193 CG1 CG2
REMARK 470 SER A 194 OG
REMARK 470 ASN A 214 CG OD1 ND2
REMARK 470 GLU A 217 CG CD OE1 OE2
REMARK 470 HIS A 220 CG ND1 CD2 CE1 NE2
REMARK 470 PHE A 235 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A 274 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 277 CG CD CE NZ
REMARK 470 ARG B 14 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 21 CG CD OE1 OE2
REMARK 470 ILE B 25 CG1 CG2 CD1
REMARK 470 GLN B 29 CG CD OE1 NE2
REMARK 470 ARG B 30 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 43 CG CD OE1 OE2
REMARK 470 GLU B 49 CG CD OE1 OE2
REMARK 470 ARG B 89 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 168 CG CD1 CD2
REMARK 470 MET B 184 CG SD CE
REMARK 470 ARG B 185 CG CD NE CZ NH1 NH2
REMARK 470 MET B 189 CG SD CE
REMARK 470 PRO B 195 CG CD
REMARK 470 ARG B 197 CG CD NE CZ NH1 NH2
REMARK 470 VAL B 218 CG1 CG2
REMARK 470 HIS B 220 CG ND1 CD2 CE1 NE2
REMARK 470 THR B 234 OG1 CG2
REMARK 470 SER B 250 OG
REMARK 470 ASP B 258 CG OD1 OD2
REMARK 470 GLU B 271 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH B 316 O HOH B 317 2.00
REMARK 500 O HOH B 327 O HOH B 329 2.00
REMARK 500
REMARK 500 REMARK: NULL
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 427 O HOH B 307 2455 1.81
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 ARG B 39 NE - CZ - NH2 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG B 65 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG B 65 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ARG B 92 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG B 186 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ARG B 186 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG B 202 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG B 202 NE - CZ - NH2 ANGL. DEV. = 3.4 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 PRO A 72 41.21 -78.52
REMARK 500 SER A 87 0.97 -69.67
REMARK 500 SER A 138 -133.74 58.28
REMARK 500 ARG A 266 -105.06 -121.23
REMARK 500 ASP B 10 40.16 -106.29
REMARK 500 ARG B 24 48.64 -91.87
REMARK 500 PRO B 72 49.47 -77.14
REMARK 500 SER B 138 -128.10 57.30
REMARK 500 ARG B 266 -109.65 -128.45
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 GLY A 105 GLU A 106 -142.68
REMARK 500
REMARK 500 REMARK: NULL
DBREF 7VO4 A 1 286 UNP F1CLA7 F1CLA7_9ACTN 1736 2021
DBREF 7VO4 B 1 286 UNP F1CLA7 F1CLA7_9ACTN 1736 2021
SEQRES 1 A 286 PHE LEU PRO ALA ALA ALA PRO GLU THR ASP SER LEU GLU
SEQRES 2 A 286 ARG MET PHE LEU ASP ALA LEU GLU SER GLY ARG ILE PRO
SEQRES 3 A 286 GLU ALA GLN ARG MET LEU SER ALA LEU GLY ALA LEU ARG
SEQRES 4 A 286 PRO SER PHE GLU ASN THR ALA GLU LEU GLU ASP LEU PRO
SEQRES 5 A 286 LEU PRO ALA THR LEU ALA GLU GLY PRO GLY ALA PRO ARG
SEQRES 6 A 286 LEU ILE CYS VAL SER THR PRO THR ALA ASN GLY GLY VAL
SEQRES 7 A 286 HIS GLU TYR ALA ARG LEU ALA ALA SER PHE ARG GLY GLU
SEQRES 8 A 286 ARG HIS VAL SER ALA LEU PRO LEU VAL GLY PHE ALA ALA
SEQRES 9 A 286 GLY GLU ARG LEU PRO ALA THR PRO GLU THR ALA VAL ARG
SEQRES 10 A 286 VAL VAL ALA GLU SER THR LEU ARG ALA SER ASP GLY ASN
SEQRES 11 A 286 PRO PHE VAL LEU VAL GLY HIS SER SER ALA GLY ALA PHE
SEQRES 12 A 286 ALA TYR LEU ALA ALA ALA LEU LEU GLU ASN THR TRP GLY
SEQRES 13 A 286 ILE ARG PRO GLU ALA VAL VAL LEU LEU ASP THR LEU SER
SEQRES 14 A 286 LEU ARG HIS GLU GLN ASN GLU THR ILE ASP TYR ALA GLY
SEQRES 15 A 286 LEU MET ARG ARG HIS PHE MET VAL ASP GLU VAL SER PRO
SEQRES 16 A 286 VAL ARG MET THR ASN SER ARG LEU SER ALA MET ALA ARG
SEQRES 17 A 286 TRP MET GLY MET LEU ASN GLN LEU GLU VAL ARG HIS THR
SEQRES 18 A 286 THR VAL PRO VAL LEU ILE ILE ARG ALA ALA LYS GLU THR
SEQRES 19 A 286 PHE GLY ILE GLY THR ASP THR GLY ILE TYR GLY GLU ASP
SEQRES 20 A 286 HIS GLY SER PRO VAL ASP VAL ARG SER VAL ASP ALA ASP
SEQRES 21 A 286 HIS PHE SER MET VAL ARG ASP ASP ALA PRO GLU THR ALA
SEQRES 22 A 286 ARG ILE VAL LYS GLU TRP LEU ASP SER LEU GLY ASN ALA
SEQRES 1 B 286 PHE LEU PRO ALA ALA ALA PRO GLU THR ASP SER LEU GLU
SEQRES 2 B 286 ARG MET PHE LEU ASP ALA LEU GLU SER GLY ARG ILE PRO
SEQRES 3 B 286 GLU ALA GLN ARG MET LEU SER ALA LEU GLY ALA LEU ARG
SEQRES 4 B 286 PRO SER PHE GLU ASN THR ALA GLU LEU GLU ASP LEU PRO
SEQRES 5 B 286 LEU PRO ALA THR LEU ALA GLU GLY PRO GLY ALA PRO ARG
SEQRES 6 B 286 LEU ILE CYS VAL SER THR PRO THR ALA ASN GLY GLY VAL
SEQRES 7 B 286 HIS GLU TYR ALA ARG LEU ALA ALA SER PHE ARG GLY GLU
SEQRES 8 B 286 ARG HIS VAL SER ALA LEU PRO LEU VAL GLY PHE ALA ALA
SEQRES 9 B 286 GLY GLU ARG LEU PRO ALA THR PRO GLU THR ALA VAL ARG
SEQRES 10 B 286 VAL VAL ALA GLU SER THR LEU ARG ALA SER ASP GLY ASN
SEQRES 11 B 286 PRO PHE VAL LEU VAL GLY HIS SER SER ALA GLY ALA PHE
SEQRES 12 B 286 ALA TYR LEU ALA ALA ALA LEU LEU GLU ASN THR TRP GLY
SEQRES 13 B 286 ILE ARG PRO GLU ALA VAL VAL LEU LEU ASP THR LEU SER
SEQRES 14 B 286 LEU ARG HIS GLU GLN ASN GLU THR ILE ASP TYR ALA GLY
SEQRES 15 B 286 LEU MET ARG ARG HIS PHE MET VAL ASP GLU VAL SER PRO
SEQRES 16 B 286 VAL ARG MET THR ASN SER ARG LEU SER ALA MET ALA ARG
SEQRES 17 B 286 TRP MET GLY MET LEU ASN GLN LEU GLU VAL ARG HIS THR
SEQRES 18 B 286 THR VAL PRO VAL LEU ILE ILE ARG ALA ALA LYS GLU THR
SEQRES 19 B 286 PHE GLY ILE GLY THR ASP THR GLY ILE TYR GLY GLU ASP
SEQRES 20 B 286 HIS GLY SER PRO VAL ASP VAL ARG SER VAL ASP ALA ASP
SEQRES 21 B 286 HIS PHE SER MET VAL ARG ASP ASP ALA PRO GLU THR ALA
SEQRES 22 B 286 ARG ILE VAL LYS GLU TRP LEU ASP SER LEU GLY ASN ALA
HET SO4 A 301 5
HETNAM SO4 SULFATE ION
FORMUL 3 SO4 O4 S 2-
FORMUL 4 HOH *62(H2 O)
HELIX 1 AA1 SER A 11 GLY A 23 1 13
HELIX 2 AA2 ARG A 24 LEU A 38 1 15
HELIX 3 AA3 ASN A 44 LEU A 48 5 5
HELIX 4 AA4 GLY A 77 GLU A 80 5 4
HELIX 5 AA5 TYR A 81 SER A 87 1 7
HELIX 6 AA6 THR A 111 ASP A 128 1 18
HELIX 7 AA7 SER A 139 THR A 154 1 16
HELIX 8 AA8 GLY A 182 PHE A 188 1 7
HELIX 9 AA9 THR A 199 MET A 212 1 14
HELIX 10 AB1 LYS A 232 THR A 234 5 3
HELIX 11 AB2 PHE A 262 ARG A 266 5 5
HELIX 12 AB3 ASP A 268 LEU A 283 1 16
HELIX 13 AB4 SER B 11 SER B 22 1 12
HELIX 14 AB5 ARG B 24 LEU B 38 1 15
HELIX 15 AB6 ASN B 44 LEU B 48 5 5
HELIX 16 AB7 GLY B 77 GLU B 80 5 4
HELIX 17 AB8 TYR B 81 SER B 87 1 7
HELIX 18 AB9 THR B 111 ASP B 128 1 18
HELIX 19 AC1 SER B 139 GLY B 156 1 18
HELIX 20 AC2 GLY B 182 VAL B 190 1 9
HELIX 21 AC3 THR B 199 ASN B 214 1 16
HELIX 22 AC4 PHE B 262 ARG B 266 5 5
HELIX 23 AC5 ASP B 268 SER B 282 1 15
SHEET 1 AA1 2 SER A 41 PHE A 42 0
SHEET 2 AA1 2 LEU A 108 PRO A 109 1 O LEU A 108 N PHE A 42
SHEET 1 AA2 7 ALA A 55 PRO A 61 0
SHEET 2 AA2 7 ARG A 92 LEU A 97 -1 O VAL A 94 N LEU A 57
SHEET 3 AA2 7 ARG A 65 VAL A 69 1 N CYS A 68 O LEU A 97
SHEET 4 AA2 7 PHE A 132 HIS A 137 1 O VAL A 135 N ILE A 67
SHEET 5 AA2 7 ALA A 161 LEU A 165 1 O VAL A 163 N LEU A 134
SHEET 6 AA2 7 VAL A 225 ALA A 230 1 O ILE A 228 N LEU A 164
SHEET 7 AA2 7 ASP A 253 VAL A 257 1 O ARG A 255 N ARG A 229
SHEET 1 AA3 2 SER B 41 PHE B 42 0
SHEET 2 AA3 2 LEU B 108 PRO B 109 1 O LEU B 108 N PHE B 42
SHEET 1 AA4 7 ALA B 55 ALA B 58 0
SHEET 2 AA4 7 ARG B 92 LEU B 97 -1 O VAL B 94 N LEU B 57
SHEET 3 AA4 7 GLY B 62 VAL B 69 1 N CYS B 68 O SER B 95
SHEET 4 AA4 7 PHE B 132 HIS B 137 1 O VAL B 135 N ILE B 67
SHEET 5 AA4 7 ALA B 161 LEU B 165 1 O VAL B 163 N LEU B 134
SHEET 6 AA4 7 VAL B 225 ALA B 230 1 O LEU B 226 N LEU B 164
SHEET 7 AA4 7 VAL B 252 VAL B 257 1 O ARG B 255 N ARG B 229
CISPEP 1 ALA A 63 PRO A 64 0 -4.54
CISPEP 2 ALA B 63 PRO B 64 0 3.41
CRYST1 51.946 58.867 85.043 90.00 101.07 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 0.019251 0.000000 0.003766 0.00000
SCALE2 0.000000 0.016987 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011982 0.00000
TER 1802 LEU A 283
TER 3599 LEU B 283
MASTER 459 0 1 23 18 0 0 6 3664 2 5 44
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