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HEADER HYDROLASE 11-OCT-11 3VIS
TITLE CRYSTAL STRUCTURE OF CUTINASE EST119 FROM THERMOBIFIDA ALBA AHK119
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOBIFIDA ALBA;
SOURCE 3 ORGANISM_TAXID: 53522;
SOURCE 4 STRAIN: AHK119;
SOURCE 5 GENE: EST2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PQE80L-EST119
KEYWDS ALPHA/BETA-HYDROLASE FOLD, ESTERASE, POLYETHYLENE TEREPHTHALATE,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.KITADOKORO,U.THUMARAT,R.NAKAMURA,K.NISHIMURA,H.KARATANI,H.SUZUKI,
AUTHOR 2 F.KAWAI
REVDAT 1 11-APR-12 3VIS 0
JRNL AUTH K.KITADOKORO,U.THUMARAT,R.NAKAMURA,K.NISHIMURA,H.KARATANI,
JRNL AUTH 2 H.SUZUKI,F.KAWAI
JRNL TITL CRYSTAL STRUCTURE OF CUTINASE EST119 FROM THERMOBIDA ALBA
JRNL TITL 2 AHK119 THAT CAN DEGRADE MODPOLYETHYLENE TEREPHTHALATE AT
JRNL TITL 3 1.76 A RESOLUTION.
JRNL REF POLYM.DEGRAD.STAB. V. 97 771 2012
JRNL REFN ISSN 0141-3910
JRNL DOI 10.1016/J.POLYMDEGRADSTAB.2012.02.003
REMARK 2
REMARK 2 RESOLUTION. 1.76 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0081
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.76
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 56.75
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 3 NUMBER OF REFLECTIONS : 41770
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) : 0.152
REMARK 3 R VALUE (WORKING SET) : 0.150
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2222
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) : 1.76
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.81
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2955
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.31
REMARK 3 BIN R VALUE (WORKING SET) : 0.1900
REMARK 3 BIN FREE R VALUE SET COUNT : 142
REMARK 3 BIN FREE R VALUE : 0.2590
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4020
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 454
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.82
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.45000
REMARK 3 B22 (A**2) : -1.38000
REMARK 3 B33 (A**2) : 0.99000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.09000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.117
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.073
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.559
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.947
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4146 ; 0.028 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5640 ; 2.174 ; 1.959
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 519 ; 6.927 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 183 ;30.642 ;22.787
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 626 ;12.318 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 36 ;16.767 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 614 ; 0.175 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3206 ; 0.015 ; 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): 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 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED 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 : 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 38 A 300
REMARK 3 ORIGIN FOR THE GROUP (A): 3.4905 -26.7835 23.6601
REMARK 3 T TENSOR
REMARK 3 T11: 0.0322 T22: 0.0526
REMARK 3 T33: 0.0492 T12: -0.0073
REMARK 3 T13: 0.0340 T23: 0.0053
REMARK 3 L TENSOR
REMARK 3 L11: 0.5196 L22: 0.8506
REMARK 3 L33: 0.3642 L12: 0.0388
REMARK 3 L13: 0.3226 L23: -0.0064
REMARK 3 S TENSOR
REMARK 3 S11: -0.0339 S12: -0.0082 S13: 0.0054
REMARK 3 S21: -0.0831 S22: 0.0214 S23: -0.0317
REMARK 3 S31: -0.0103 S32: -0.0106 S33: 0.0125
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 40 B 300
REMARK 3 ORIGIN FOR THE GROUP (A): 22.3826 -0.6778 2.7135
REMARK 3 T TENSOR
REMARK 3 T11: 0.0164 T22: 0.0225
REMARK 3 T33: 0.0228 T12: -0.0079
REMARK 3 T13: 0.0083 T23: 0.0061
REMARK 3 L TENSOR
REMARK 3 L11: 0.5672 L22: 0.4682
REMARK 3 L33: 1.1984 L12: 0.0209
REMARK 3 L13: 0.6487 L23: -0.0080
REMARK 3 S TENSOR
REMARK 3 S11: -0.0224 S12: 0.0014 S13: 0.0064
REMARK 3 S21: -0.0396 S22: 0.0469 S23: 0.0301
REMARK 3 S31: -0.0102 S32: 0.0321 S33: -0.0245
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: NULL
REMARK 4
REMARK 4 3VIS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-OCT-11.
REMARK 100 THE RCSB ID CODE IS RCSB095096.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-JUN-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL44XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41770
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.760
REMARK 200 RESOLUTION RANGE LOW (A) : 56.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.09900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.76
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.82
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: SAD+MR
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% (W/V) PEG 1000, 0.2M SODIUM
REMARK 280 CHLORIDE, 0.1M SODIUM POTASSIUM PHOSPHATE, PH 6.2, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 50.49450
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.36600
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 50.49450
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 44.36600
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
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 VAL A 3
REMARK 465 THR A 4
REMARK 465 THR A 5
REMARK 465 PRO A 6
REMARK 465 ARG A 7
REMARK 465 ARG A 8
REMARK 465 GLU A 9
REMARK 465 THR A 10
REMARK 465 SER A 11
REMARK 465 LEU A 12
REMARK 465 LEU A 13
REMARK 465 SER A 14
REMARK 465 ARG A 15
REMARK 465 ALA A 16
REMARK 465 LEU A 17
REMARK 465 ARG A 18
REMARK 465 ALA A 19
REMARK 465 THR A 20
REMARK 465 ALA A 21
REMARK 465 ALA A 22
REMARK 465 ALA A 23
REMARK 465 ALA A 24
REMARK 465 THR A 25
REMARK 465 ALA A 26
REMARK 465 VAL A 27
REMARK 465 VAL A 28
REMARK 465 ALA A 29
REMARK 465 THR A 30
REMARK 465 VAL A 31
REMARK 465 ALA A 32
REMARK 465 LEU A 33
REMARK 465 ALA A 34
REMARK 465 ALA A 35
REMARK 465 PRO A 36
REMARK 465 ALA A 37
REMARK 465 GLY A 286
REMARK 465 LEU A 287
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 VAL B 3
REMARK 465 THR B 4
REMARK 465 THR B 5
REMARK 465 PRO B 6
REMARK 465 ARG B 7
REMARK 465 ARG B 8
REMARK 465 GLU B 9
REMARK 465 THR B 10
REMARK 465 SER B 11
REMARK 465 LEU B 12
REMARK 465 LEU B 13
REMARK 465 SER B 14
REMARK 465 ARG B 15
REMARK 465 ALA B 16
REMARK 465 LEU B 17
REMARK 465 ARG B 18
REMARK 465 ALA B 19
REMARK 465 THR B 20
REMARK 465 ALA B 21
REMARK 465 ALA B 22
REMARK 465 ALA B 23
REMARK 465 ALA B 24
REMARK 465 THR B 25
REMARK 465 ALA B 26
REMARK 465 VAL B 27
REMARK 465 VAL B 28
REMARK 465 ALA B 29
REMARK 465 THR B 30
REMARK 465 VAL B 31
REMARK 465 ALA B 32
REMARK 465 LEU B 33
REMARK 465 ALA B 34
REMARK 465 ALA B 35
REMARK 465 PRO B 36
REMARK 465 ALA B 37
REMARK 465 GLN B 38
REMARK 465 ALA B 39
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 A 440 O HOH A 464 1.80
REMARK 500 O PHE A 300 O HOH A 454 1.98
REMARK 500 O HOH B 348 O HOH B 430 2.13
REMARK 500 O ALA B 73 O HOH B 374 2.17
REMARK 500 OG SER B 69 O PHE B 71 2.17
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 NE2 GLN A 38 OG1 THR B 216 4546 1.87
REMARK 500 OE2 GLU A 292 OE2 GLU A 292 2656 2.04
REMARK 500 O HOH B 374 O HOH B 392 4545 2.15
REMARK 500 O HOH A 393 O HOH A 393 2656 2.17
REMARK 500
REMARK 500 REMARK: NULL
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 ARG A 67 CB ARG A 67 CG -0.214
REMARK 500 GLU A 241 CB GLU A 241 CG 0.134
REMARK 500 TRP A 264 CZ3 TRP A 264 CH2 0.105
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 THR A 100 -5.98 71.03
REMARK 500 SER A 169 -114.67 57.42
REMARK 500 THR A 192 52.85 37.28
REMARK 500 HIS A 223 -86.66 -123.15
REMARK 500 THR A 297 40.20 -104.94
REMARK 500 THR B 100 -10.59 71.47
REMARK 500 SER B 169 -122.56 59.49
REMARK 500 THR B 192 53.75 34.01
REMARK 500 HIS B 223 -81.39 -123.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE4 A 557
DBREF 3VIS A 1 300 UNP F7IX06 F7IX06_9ACTO 1 300
DBREF 3VIS B 1 300 UNP F7IX06 F7IX06_9ACTO 1 300
SEQADV 3VIS HIS A -5 UNP F7IX06 EXPRESSION TAG
SEQADV 3VIS HIS A -4 UNP F7IX06 EXPRESSION TAG
SEQADV 3VIS HIS A -3 UNP F7IX06 EXPRESSION TAG
SEQADV 3VIS HIS A -2 UNP F7IX06 EXPRESSION TAG
SEQADV 3VIS HIS A -1 UNP F7IX06 EXPRESSION TAG
SEQADV 3VIS HIS A 0 UNP F7IX06 EXPRESSION TAG
SEQADV 3VIS HIS B -5 UNP F7IX06 EXPRESSION TAG
SEQADV 3VIS HIS B -4 UNP F7IX06 EXPRESSION TAG
SEQADV 3VIS HIS B -3 UNP F7IX06 EXPRESSION TAG
SEQADV 3VIS HIS B -2 UNP F7IX06 EXPRESSION TAG
SEQADV 3VIS HIS B -1 UNP F7IX06 EXPRESSION TAG
SEQADV 3VIS HIS B 0 UNP F7IX06 EXPRESSION TAG
SEQRES 1 A 306 HIS HIS HIS HIS HIS HIS MET SER VAL THR THR PRO ARG
SEQRES 2 A 306 ARG GLU THR SER LEU LEU SER ARG ALA LEU ARG ALA THR
SEQRES 3 A 306 ALA ALA ALA ALA THR ALA VAL VAL ALA THR VAL ALA LEU
SEQRES 4 A 306 ALA ALA PRO ALA GLN ALA ALA ASN PRO TYR GLU ARG GLY
SEQRES 5 A 306 PRO ASN PRO THR GLU SER MET LEU GLU ALA ARG SER GLY
SEQRES 6 A 306 PRO PHE SER VAL SER GLU GLU ARG ALA SER ARG PHE GLY
SEQRES 7 A 306 ALA ASP GLY PHE GLY GLY GLY THR ILE TYR TYR PRO ARG
SEQRES 8 A 306 GLU ASN ASN THR TYR GLY ALA ILE ALA ILE SER PRO GLY
SEQRES 9 A 306 TYR THR GLY THR GLN SER SER ILE ALA TRP LEU GLY GLU
SEQRES 10 A 306 ARG ILE ALA SER HIS GLY PHE VAL VAL ILE ALA ILE ASP
SEQRES 11 A 306 THR ASN THR THR LEU ASP GLN PRO ASP SER ARG ALA ARG
SEQRES 12 A 306 GLN LEU ASN ALA ALA LEU ASP TYR MET LEU THR ASP ALA
SEQRES 13 A 306 SER SER ALA VAL ARG ASN ARG ILE ASP ALA SER ARG LEU
SEQRES 14 A 306 ALA VAL MET GLY HIS SER MET GLY GLY GLY GLY THR LEU
SEQRES 15 A 306 ARG LEU ALA SER GLN ARG PRO ASP LEU LYS ALA ALA ILE
SEQRES 16 A 306 PRO LEU THR PRO TRP HIS LEU ASN LYS SER TRP ARG ASP
SEQRES 17 A 306 ILE THR VAL PRO THR LEU ILE ILE GLY ALA GLU TYR ASP
SEQRES 18 A 306 THR ILE ALA SER VAL THR LEU HIS SER LYS PRO PHE TYR
SEQRES 19 A 306 ASN SER ILE PRO SER PRO THR ASP LYS ALA TYR LEU GLU
SEQRES 20 A 306 LEU ASP GLY ALA SER HIS PHE ALA PRO ASN ILE THR ASN
SEQRES 21 A 306 LYS THR ILE GLY MET TYR SER VAL ALA TRP LEU LYS ARG
SEQRES 22 A 306 PHE VAL ASP GLU ASP THR ARG TYR THR GLN PHE LEU CYS
SEQRES 23 A 306 PRO GLY PRO ARG THR GLY LEU LEU SER ASP VAL GLU GLU
SEQRES 24 A 306 TYR ARG SER THR CYS PRO PHE
SEQRES 1 B 306 HIS HIS HIS HIS HIS HIS MET SER VAL THR THR PRO ARG
SEQRES 2 B 306 ARG GLU THR SER LEU LEU SER ARG ALA LEU ARG ALA THR
SEQRES 3 B 306 ALA ALA ALA ALA THR ALA VAL VAL ALA THR VAL ALA LEU
SEQRES 4 B 306 ALA ALA PRO ALA GLN ALA ALA ASN PRO TYR GLU ARG GLY
SEQRES 5 B 306 PRO ASN PRO THR GLU SER MET LEU GLU ALA ARG SER GLY
SEQRES 6 B 306 PRO PHE SER VAL SER GLU GLU ARG ALA SER ARG PHE GLY
SEQRES 7 B 306 ALA ASP GLY PHE GLY GLY GLY THR ILE TYR TYR PRO ARG
SEQRES 8 B 306 GLU ASN ASN THR TYR GLY ALA ILE ALA ILE SER PRO GLY
SEQRES 9 B 306 TYR THR GLY THR GLN SER SER ILE ALA TRP LEU GLY GLU
SEQRES 10 B 306 ARG ILE ALA SER HIS GLY PHE VAL VAL ILE ALA ILE ASP
SEQRES 11 B 306 THR ASN THR THR LEU ASP GLN PRO ASP SER ARG ALA ARG
SEQRES 12 B 306 GLN LEU ASN ALA ALA LEU ASP TYR MET LEU THR ASP ALA
SEQRES 13 B 306 SER SER ALA VAL ARG ASN ARG ILE ASP ALA SER ARG LEU
SEQRES 14 B 306 ALA VAL MET GLY HIS SER MET GLY GLY GLY GLY THR LEU
SEQRES 15 B 306 ARG LEU ALA SER GLN ARG PRO ASP LEU LYS ALA ALA ILE
SEQRES 16 B 306 PRO LEU THR PRO TRP HIS LEU ASN LYS SER TRP ARG ASP
SEQRES 17 B 306 ILE THR VAL PRO THR LEU ILE ILE GLY ALA GLU TYR ASP
SEQRES 18 B 306 THR ILE ALA SER VAL THR LEU HIS SER LYS PRO PHE TYR
SEQRES 19 B 306 ASN SER ILE PRO SER PRO THR ASP LYS ALA TYR LEU GLU
SEQRES 20 B 306 LEU ASP GLY ALA SER HIS PHE ALA PRO ASN ILE THR ASN
SEQRES 21 B 306 LYS THR ILE GLY MET TYR SER VAL ALA TRP LEU LYS ARG
SEQRES 22 B 306 PHE VAL ASP GLU ASP THR ARG TYR THR GLN PHE LEU CYS
SEQRES 23 B 306 PRO GLY PRO ARG THR GLY LEU LEU SER ASP VAL GLU GLU
SEQRES 24 B 306 TYR ARG SER THR CYS PRO PHE
HET PE4 A 557 24
HETNAM PE4 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-
HETNAM 2 PE4 ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL
HETSYN PE4 POLYETHYLENE GLYCOL PEG4000
FORMUL 3 PE4 C16 H34 O8
FORMUL 4 HOH *454(H2 O)
HELIX 1 1 THR A 50 ALA A 56 1 7
HELIX 2 2 THR A 102 SER A 115 1 14
HELIX 3 3 GLN A 131 ASP A 149 1 19
HELIX 4 4 SER A 151 ASN A 156 1 6
HELIX 5 5 SER A 169 ARG A 182 1 14
HELIX 6 6 HIS A 223 SER A 230 1 8
HELIX 7 7 PHE A 248 ILE A 252 5 5
HELIX 8 8 ASN A 254 ASP A 270 1 17
HELIX 9 9 ASP A 272 ARG A 274 5 3
HELIX 10 10 TYR A 275 CYS A 280 1 6
HELIX 11 11 THR B 50 ALA B 56 1 7
HELIX 12 12 THR B 102 SER B 115 1 14
HELIX 13 13 GLN B 131 ASP B 149 1 19
HELIX 14 14 SER B 151 ASN B 156 1 6
HELIX 15 15 SER B 169 ARG B 182 1 14
HELIX 16 16 HIS B 223 ILE B 231 1 9
HELIX 17 17 PHE B 248 ILE B 252 5 5
HELIX 18 18 ASN B 254 ASP B 270 1 17
HELIX 19 19 ASP B 272 ARG B 274 5 3
HELIX 20 20 TYR B 275 CYS B 280 1 6
SHEET 1 A 6 VAL A 63 ALA A 68 0
SHEET 2 A 6 GLY A 79 PRO A 84 -1 O ILE A 81 N GLU A 66
SHEET 3 A 6 PHE A 118 ILE A 123 -1 O VAL A 120 N TYR A 82
SHEET 4 A 6 TYR A 90 SER A 96 1 N ILE A 95 O ILE A 121
SHEET 5 A 6 ILE A 158 HIS A 168 1 O ASP A 159 N TYR A 90
SHEET 6 A 6 ALA A 187 LEU A 191 1 O LEU A 191 N GLY A 167
SHEET 1 B 3 THR A 207 ALA A 212 0
SHEET 2 B 3 LYS A 237 LEU A 242 1 O LEU A 242 N GLY A 211
SHEET 3 B 3 VAL A 291 SER A 296 -1 O ARG A 295 N TYR A 239
SHEET 1 C 6 VAL B 63 ALA B 68 0
SHEET 2 C 6 GLY B 79 PRO B 84 -1 O ILE B 81 N GLU B 66
SHEET 3 C 6 VAL B 119 ILE B 123 -1 O VAL B 120 N TYR B 82
SHEET 4 C 6 TYR B 90 SER B 96 1 N ILE B 95 O ILE B 121
SHEET 5 C 6 ILE B 158 HIS B 168 1 O ASP B 159 N TYR B 90
SHEET 6 C 6 ALA B 187 LEU B 191 1 O LEU B 191 N GLY B 167
SHEET 1 D 3 THR B 207 ALA B 212 0
SHEET 2 D 3 LYS B 237 LEU B 242 1 O LEU B 242 N GLY B 211
SHEET 3 D 3 VAL B 291 SER B 296 -1 O GLU B 292 N GLU B 241
SSBOND 1 CYS A 280 CYS A 298 1555 1555 2.07
SSBOND 2 CYS B 280 CYS B 298 1555 1555 2.13
CISPEP 1 SER A 233 PRO A 234 0 6.43
CISPEP 2 CYS A 280 PRO A 281 0 9.17
CISPEP 3 CYS A 298 PRO A 299 0 4.25
CISPEP 4 CYS B 280 PRO B 281 0 -0.44
CISPEP 5 CYS B 298 PRO B 299 0 -0.29
SITE 1 AC1 9 TYR A 99 THR A 100 ILE A 217 PHE A 248
SITE 2 AC1 9 HOH A 304 HOH A 448 HOH A 499 THR B 216
SITE 3 AC1 9 ILE B 217
CRYST1 100.989 88.732 71.794 90.00 133.03 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 0.009902 0.000000 0.009242 0.00000
SCALE2 0.000000 0.011270 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019053 0.00000
TER 2012 PHE A 300
TER 4022 PHE B 300
MASTER 460 0 1 20 18 0 3 6 4498 2 28 48
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