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HEADER HYDROLASE 24-NOV-25 9XUI
TITLE CRYSTAL STRUCTURE OF THE DEEP-SEA HALOPHILIC PET HYDROLASE DSPETASE06
TITLE 2 C23A MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PET HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONADOTA BACTERIUM;
SOURCE 3 ORGANISM_TAXID: 1977087;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS HYDROLASE, PET HYDROLASE, PET DEGRADATION ENZYME
EXPDTA X-RAY DIFFRACTION
AUTHOR X.LI,M.Z.ZHANG,S.Q.HUANG,C.ZENG,J.-W.HUANG,C.-C.CHEN,R.-T.GUO
REVDAT 1 23-SEP-26 9XUI 0
JRNL AUTH X.LI,M.Z.ZHANG,S.Q.HUANG,C.ZENG,J.-W.HUANG,C.-C.CHEN,
JRNL AUTH 2 R.-T.GUO
JRNL TITL CRYSTAL STRUCTURE OF THE DEEP-SEA HALOPHILIC PET HYDROLASE
JRNL TITL 2 DSPETASE06 C23A MUTANT
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.38 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0238
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) : 1.38
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.74
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 75309
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) : 0.132
REMARK 3 R VALUE (WORKING SET) : 0.131
REMARK 3 FREE R VALUE : 0.151
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3970
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) : 1.38
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.42
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5359
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.36
REMARK 3 BIN R VALUE (WORKING SET) : 0.2190
REMARK 3 BIN FREE R VALUE SET COUNT : 273
REMARK 3 BIN FREE R VALUE : 0.2130
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1995
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 393
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.27
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.33000
REMARK 3 B22 (A**2) : 0.33000
REMARK 3 B33 (A**2) : -1.08000
REMARK 3 B12 (A**2) : 0.17000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.036
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.038
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.024
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.617
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.982
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.977
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2083 ; 0.017 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 1779 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2842 ; 2.080 ; 1.644
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4156 ; 1.657 ; 1.568
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 267 ; 6.449 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 110 ;34.576 ;24.545
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 312 ;10.498 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 6 ;23.081 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 263 ; 0.126 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2409 ; 0.012 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 433 ; 0.001 ; 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): 1041 ; 1.422 ; 1.751
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1040 ; 1.396 ; 1.749
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1302 ; 2.206 ; 2.625
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1303 ; 2.214 ; 2.627
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1042 ; 2.935 ; 2.011
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1043 ; 2.936 ; 2.016
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1536 ; 4.335 ; 2.921
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2560 ; 5.527 ;23.474
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2436 ; 5.178 ;22.071
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
REMARK 4
REMARK 4 9XUI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 28-NOV-25.
REMARK 100 THE DEPOSITION ID IS D_1300066364.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-JUL-24
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSRRC
REMARK 200 BEAMLINE : TPS 07A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9762
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 79329
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.380
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.38
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.43
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.4
REMARK 200 DATA REDUNDANCY IN SHELL : 6.10
REMARK 200 R MERGE FOR SHELL (I) : 0.62600
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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M MAGNESIUM CHLORIDE HEXAHYDRATE;
REMARK 280 0.1M SODIUM HEPES PH 7.5; 30% PEG 400, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 38.76667
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 77.53333
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 58.15000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 96.91667
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 19.38333
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9910 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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 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 22
REMARK 465 ALA A 23
REMARK 465 PHE A 24
REMARK 465 GLY A 25
REMARK 465 GLY A 26
REMARK 465 GLY A 27
REMARK 465 ASP A 28
REMARK 465 PRO A 29
REMARK 465 GLU A 30
REMARK 465 PRO A 31
REMARK 465 GLY A 32
REMARK 465 PRO A 33
REMARK 465 ASP A 34
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 605 O HOH A 611 1.51
REMARK 500 O HOH A 485 O HOH A 730 1.84
REMARK 500 O HOH A 403 O HOH A 630 1.95
REMARK 500 ND2 ASN A 241 O HOH A 401 1.99
REMARK 500 O HOH A 470 O HOH A 741 2.03
REMARK 500 NE2 GLN A 291 O HOH A 402 2.03
REMARK 500 O HOH A 455 O HOH A 741 2.04
REMARK 500 OE1 GLU A 91 O HOH A 403 2.05
REMARK 500 O HOH A 484 O HOH A 730 2.06
REMARK 500 O HOH A 428 O HOH A 735 2.06
REMARK 500 O HOH A 403 O HOH A 433 2.09
REMARK 500 O HOH A 598 O HOH A 753 2.10
REMARK 500 O HOH A 424 O HOH A 741 2.10
REMARK 500 O HOH A 403 O HOH A 745 2.10
REMARK 500 O HOH A 403 O HOH A 510 2.11
REMARK 500 O HOH A 402 O HOH A 535 2.12
REMARK 500 O HOH A 457 O HOH A 747 2.14
REMARK 500 O HOH A 402 O HOH A 660 2.14
REMARK 500 N GLY A 35 O HOH A 404 2.15
REMARK 500 O HOH A 403 O HOH A 519 2.17
REMARK 500 O HOH A 402 O HOH A 644 2.17
REMARK 500 ND2 ASN A 187 O HOH A 405 2.18
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 741 O HOH A 787 3544 1.97
REMARK 500 O HOH A 402 O HOH A 486 2445 1.99
REMARK 500 O HOH A 426 O HOH A 741 2445 2.07
REMARK 500 O HOH A 402 O HOH A 586 2445 2.11
REMARK 500 O HOH A 543 O HOH A 741 2445 2.12
REMARK 500 O HOH A 422 O HOH A 735 5554 2.18
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 GLU A 194 CD GLU A 194 OE2 -0.083
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 A 62 NE - CZ - NH2 ANGL. DEV. = 4.0 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 THR A 84 -8.58 77.31
REMARK 500 SER A 156 -120.89 70.56
REMARK 500 ASP A 272 18.78 -146.90
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 793 DISTANCE = 5.95 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 304 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 52 O
REMARK 620 2 GLU A 129 OE2 95.2
REMARK 620 3 ASP A 132 OD2 171.3 93.2
REMARK 620 4 GLU A 133 OE2 83.9 96.5 92.9
REMARK 620 5 HOH A 585 O 84.0 86.7 98.7 167.8
REMARK 620 6 HOH A 670 O 85.0 168.3 87.2 95.1 81.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 413 O
REMARK 620 2 HOH A 421 O 168.8
REMARK 620 3 HOH A 422 O 78.1 96.6
REMARK 620 4 HOH A 462 O 87.3 97.8 165.4
REMARK 620 5 HOH A 733 O 92.4 98.1 95.8 84.2
REMARK 620 6 HOH A 735 O 78.3 90.5 68.5 109.3 163.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 303 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 444 O
REMARK 620 2 HOH A 477 O 84.6
REMARK 620 3 HOH A 616 O 172.0 87.9
REMARK 620 4 HOH A 676 O 96.7 101.5 87.6
REMARK 620 5 HOH A 699 O 89.9 170.7 97.1 86.6
REMARK 620 6 HOH A 759 O 91.3 89.7 85.7 166.8 82.9
REMARK 620 N 1 2 3 4 5
DBREF 9XUI A 22 292 PDB 9XUI 9XUI 22 292
SEQRES 1 A 271 MET ALA PHE GLY GLY GLY ASP PRO GLU PRO GLY PRO ASP
SEQRES 2 A 271 GLY GLN ALA LEU THR ASN PRO GLY GLU TYR GLU ILE CYS
SEQRES 3 A 271 SER TYR GLU THR ASP LEU GLU ASN SER GLY TYR ALA SER
SEQRES 4 A 271 ALA ARG MET THR TYR PRO CYS ASP LEU SER ASP GLY PRO
SEQRES 5 A 271 TYR PRO ALA THR THR LEU THR GLY GLY PHE THR ASN THR
SEQRES 6 A 271 LYS GLU GLN MET GLU TRP LEU ALA GLU HIS LEU THR THR
SEQRES 7 A 271 HIS GLY TYR VAL VAL LEU THR MET THR PRO ASN ASN THR
SEQRES 8 A 271 LEU GLY VAL PRO PRO GLY TRP ARG ASP ALA GLN LEU GLY
SEQRES 9 A 271 GLY PHE ALA GLU LEU ALA ASP GLU ASN ALA ARG SER ASN
SEQRES 10 A 271 SER PRO LEU LYS GLY LYS ILE ASP LEU SER LYS ARG ASN
SEQRES 11 A 271 ILE MET GLY PHE SER MET GLY GLY GLY GLY VAL ILE LEU
SEQRES 12 A 271 ALA ALA GLU GLU MET GLY ASP ALA PRO THR SER ALA ILE
SEQRES 13 A 271 ALA LEU ALA PRO TRP LEU GLY ALA TYR ASN VAL ASP TYR
SEQRES 14 A 271 SER GLN ILE GLU THR PRO MET LEU MET LEU GLY SER GLU
SEQRES 15 A 271 ASN ASP GLU LEU ALA TYR TYR THR GLU ASP TYR TYR ALA
SEQRES 16 A 271 GLN LEU PRO ALA ASP LEU GLU ARG GLY VAL ALA ILE TYR
SEQRES 17 A 271 ALA GLY ALA SER HIS PHE ASP TRP TYR GLY VAL ASN ASN
SEQRES 18 A 271 GLN ASP GLN LYS ALA GLN PHE ARG THR LEU VAL THR ALA
SEQRES 19 A 271 PHE LEU GLU VAL GLN LEU LYS GLY ASP THR SER ALA TYR
SEQRES 20 A 271 SER TYR PHE ASP GLY ALA GLU HIS ASP GLU HIS VAL GLN
SEQRES 21 A 271 GLU GLY TRP PHE SER ALA PHE ASP TYR GLN LYS
HET PEG A 301 7
HET MG A 302 1
HET MG A 303 1
HET MG A 304 1
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM MG MAGNESIUM ION
FORMUL 2 PEG C4 H10 O3
FORMUL 3 MG 3(MG 2+)
FORMUL 6 HOH *393(H2 O)
HELIX 1 AA1 THR A 86 GLN A 89 5 4
HELIX 2 AA2 MET A 90 HIS A 100 1 11
HELIX 3 AA3 VAL A 115 ARG A 136 1 22
HELIX 4 AA4 SER A 156 GLY A 170 1 15
HELIX 5 AA5 ASP A 189 ILE A 193 5 5
HELIX 6 AA6 LEU A 207 GLN A 217 1 11
HELIX 7 AA7 HIS A 234 TYR A 238 5 5
HELIX 8 AA8 ASN A 242 GLY A 263 1 22
HELIX 9 AA9 ASP A 264 ALA A 267 5 4
HELIX 10 AB1 TYR A 268 GLY A 273 1 6
HELIX 11 AB2 GLY A 273 GLU A 282 1 10
SHEET 1 AA1 9 ILE A 46 TYR A 49 0
SHEET 2 AA1 9 SER A 60 PRO A 66 -1 O MET A 63 N TYR A 49
SHEET 3 AA1 9 VAL A 103 THR A 108 -1 O VAL A 104 N THR A 64
SHEET 4 AA1 9 TYR A 74 THR A 80 1 N PRO A 75 O VAL A 103
SHEET 5 AA1 9 ILE A 145 PHE A 155 1 O ASP A 146 N TYR A 74
SHEET 6 AA1 9 SER A 175 LEU A 179 1 O LEU A 179 N GLY A 154
SHEET 7 AA1 9 MET A 197 SER A 202 1 O LEU A 198 N ALA A 178
SHEET 8 AA1 9 ARG A 224 TYR A 229 1 O TYR A 229 N GLY A 201
SHEET 9 AA1 9 PHE A 285 GLN A 291 -1 O GLN A 291 N ARG A 224
SSBOND 1 CYS A 47 CYS A 67 1555 1555 2.20
LINK O ASP A 52 MG MG A 304 1555 1555 2.32
LINK OE2 GLU A 129 MG MG A 304 1555 1555 2.21
LINK OD2 ASP A 132 MG MG A 304 1555 1555 2.27
LINK OE2 GLU A 133 MG MG A 304 1555 1555 2.35
LINK MG MG A 302 O HOH A 413 1555 1555 2.21
LINK MG MG A 302 O HOH A 421 1555 5554 1.89
LINK MG MG A 302 O HOH A 422 1555 1555 1.92
LINK MG MG A 302 O HOH A 462 1555 5554 2.16
LINK MG MG A 302 O HOH A 733 1555 1555 2.00
LINK MG MG A 302 O HOH A 735 1555 5554 1.95
LINK MG MG A 303 O HOH A 444 1555 1555 2.21
LINK MG MG A 303 O HOH A 477 1555 1555 2.07
LINK MG MG A 303 O HOH A 616 1555 1555 2.10
LINK MG MG A 303 O HOH A 676 1555 5554 2.26
LINK MG MG A 303 O HOH A 699 1555 5554 2.05
LINK MG MG A 303 O HOH A 759 1555 1555 1.83
LINK MG MG A 304 O HOH A 585 1555 1555 2.37
LINK MG MG A 304 O HOH A 670 1555 1555 2.32
CISPEP 1 GLY A 72 PRO A 73 0 0.56
CRYST1 77.315 77.315 116.300 90.00 90.00 120.00 P 61 6
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 0.012934 0.007468 0.000000 0.00000
SCALE2 0.000000 0.014935 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008598 0.00000
TER 2020 LYS A 292
MASTER 431 0 4 11 9 0 0 6 2398 1 26 21
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