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HEADER TOXIN 23-OCT-18 6IMP
TITLE CRYSTAL STRUCTURE OF ALPHA-BETA HYDROLASE (ABH) FROM VIBRIO VULNIFICUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RTX TOXIN RTXA;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: HYDROLASE FOLD DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VIBRIO VULNIFICUS MO6-24/O;
SOURCE 3 ORGANISM_TAXID: 914127;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS VIRULENCE, HYDROLASE, ALPHA-BETA FOLD, TOXINS, TOXIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.H.KIM,J.HWANG
REVDAT 1 21-AUG-19 6IMP 0
JRNL AUTH M.H.KIM,J.HWANG
JRNL TITL PATHOGENIC BACTERIAL PROTEIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.62 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0103
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) : 2.62
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.84
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 21082
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) : 0.240
REMARK 3 R VALUE (WORKING SET) : 0.237
REMARK 3 FREE R VALUE : 0.287
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1071
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) : 2.62
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.69
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1366
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.76
REMARK 3 BIN R VALUE (WORKING SET) : 0.4200
REMARK 3 BIN FREE R VALUE SET COUNT : 71
REMARK 3 BIN FREE R VALUE : 0.4730
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4277
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 21
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 92.55
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.19000
REMARK 3 B22 (A**2) : -0.12000
REMARK 3 B33 (A**2) : 0.32000
REMARK 3 B12 (A**2) : 0.00000
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): 0.669
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.348
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.944
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.919
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4344 ; 0.009 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5856 ; 1.430 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 560 ;10.838 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 203 ;38.183 ;25.222
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 752 ;18.428 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;17.372 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 638 ; 0.078 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3313 ; 0.014 ; 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): 2252 ; 6.666 ; 9.065
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2808 ; 9.932 ;13.575
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2092 ; 7.326 ; 9.405
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): 6577 ;14.801 ;75.234
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: NULL
REMARK 4
REMARK 4 6IMP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-NOV-18.
REMARK 100 THE DEPOSITION ID IS D_1300009490.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-DEC-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 7A (6B, 6C1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22210
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 6.100
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : 0.07700
REMARK 200 FOR THE DATA SET : 23.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.4
REMARK 200 DATA REDUNDANCY IN SHELL : 5.30
REMARK 200 R MERGE FOR SHELL (I) : 0.59700
REMARK 200 R SYM FOR SHELL (I) : 0.59700
REMARK 200 FOR SHELL : 1.870
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: AUTOSOL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM FORMATE, 25% PEG 3350,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 22.05300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.44500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.84050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 82.44500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.05300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 49.84050
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 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 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 ALA A 2898
REMARK 465 MET A 2899
REMARK 465 ALA A 2900
REMARK 465 LEU A 2901
REMARK 465 SER A 2902
REMARK 465 GLY A 2903
REMARK 465 ASN A 2904
REMARK 465 GLU A 2905
REMARK 465 LYS A 2906
REMARK 465 HIS A 2907
REMARK 465 ALA A 2984
REMARK 465 ALA A 2985
REMARK 465 SER A 2986
REMARK 465 SER A 2987
REMARK 465 GLU A 2988
REMARK 465 GLY A 2989
REMARK 465 GLU A 2990
REMARK 465 THR A 2991
REMARK 465 SER A 2992
REMARK 465 ALA A 2993
REMARK 465 THR A 2994
REMARK 465 SER A 2995
REMARK 465 GLY A 2996
REMARK 465 ASN A 3205
REMARK 465 ALA A 3206
REMARK 465 GLU A 3207
REMARK 465 GLN A 3208
REMARK 465 ALA A 3209
REMARK 465 ALA A 3210
REMARK 465 VAL A 3211
REMARK 465 GLU A 3212
REMARK 465 ALA A 3213
REMARK 465 GLY A 3214
REMARK 465 GLU A 3215
REMARK 465 VAL A 3216
REMARK 465 LEU A 3217
REMARK 465 LYS A 3218
REMARK 465 GLY A 3219
REMARK 465 LEU A 3220
REMARK 465 ALA B 2898
REMARK 465 MET B 2899
REMARK 465 ALA B 2900
REMARK 465 LEU B 2901
REMARK 465 SER B 2902
REMARK 465 GLY B 2903
REMARK 465 ASN B 2904
REMARK 465 GLU B 2905
REMARK 465 LYS B 2906
REMARK 465 HIS B 2907
REMARK 465 LYS B 2908
REMARK 465 GLU B 2909
REMARK 465 ASN B 2910
REMARK 465 ALA B 2984
REMARK 465 ALA B 2985
REMARK 465 SER B 2986
REMARK 465 SER B 2987
REMARK 465 GLU B 2988
REMARK 465 GLY B 2989
REMARK 465 GLU B 2990
REMARK 465 THR B 2991
REMARK 465 SER B 2992
REMARK 465 ALA B 2993
REMARK 465 THR B 2994
REMARK 465 SER B 2995
REMARK 465 GLY B 2996
REMARK 465 PHE B 3204
REMARK 465 ASN B 3205
REMARK 465 ALA B 3206
REMARK 465 GLU B 3207
REMARK 465 GLN B 3208
REMARK 465 ALA B 3209
REMARK 465 ALA B 3210
REMARK 465 VAL B 3211
REMARK 465 GLU B 3212
REMARK 465 ALA B 3213
REMARK 465 GLY B 3214
REMARK 465 GLU B 3215
REMARK 465 VAL B 3216
REMARK 465 LEU B 3217
REMARK 465 LYS B 3218
REMARK 465 GLY B 3219
REMARK 465 LEU B 3220
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 CB ASN B 2915 OD1 ASP B 2916 1.10
REMARK 500 CA ASN B 2915 OD1 ASP B 2916 1.75
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 PRO A2920 C - N - CD ANGL. DEV. = 16.7 DEGREES
REMARK 500 ILE B2913 CB - CA - C ANGL. DEV. = -15.5 DEGREES
REMARK 500 GLU B2914 CB - CA - C ANGL. DEV. = -26.8 DEGREES
REMARK 500 GLU B2914 N - CA - CB ANGL. DEV. = -10.9 DEGREES
REMARK 500 GLU B2914 N - CA - C ANGL. DEV. = 26.7 DEGREES
REMARK 500 PRO B2919 C - N - CA ANGL. DEV. = -14.4 DEGREES
REMARK 500 PRO B2919 C - N - CD ANGL. DEV. = 19.9 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 GLU A2909 44.43 -92.47
REMARK 500 LEU A2926 -86.72 -124.83
REMARK 500 SER A3075 -127.23 55.36
REMARK 500 ALA A3117 -133.41 58.24
REMARK 500 LEU A3203 -42.47 -132.21
REMARK 500 LEU B2926 -157.98 -133.91
REMARK 500 SER B2927 120.97 -34.06
REMARK 500 SER B3075 -124.60 53.26
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 ALA A 2912 ILE A 2913 -148.26
REMARK 500 THR A 2918 PRO A 2919 -140.87
REMARK 500 SER A 2925 LEU A 2926 -129.36
REMARK 500 ASN B 2915 ASP B 2916 -48.44
REMARK 500 ASP B 2916 GLY B 2917 106.80
REMARK 500 GLY B 2917 THR B 2918 103.69
REMARK 500 THR B 2918 PRO B 2919 -84.55
REMARK 500 PRO B 2919 PRO B 2920 -125.36
REMARK 500 LEU B 2926 SER B 2927 -148.81
REMARK 500 SER B 2927 PRO B 2928 -149.24
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A3190 0.28 SIDE CHAIN
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 B3309 DISTANCE = 6.21 ANGSTROMS
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE HAS BEEN DEPOSITED TO DATABASE WITH ACCESSION ID WP_
REMARK 999 015728045.1.
DBREF 6IMP A 2898 3220 PDB 6IMP 6IMP 2898 3220
DBREF 6IMP B 2898 3220 PDB 6IMP 6IMP 2898 3220
SEQRES 1 A 323 ALA MET ALA LEU SER GLY ASN GLU LYS HIS LYS GLU ASN
SEQRES 2 A 323 VAL ALA ILE GLU ASN ASP GLY THR PRO PRO ARG ASP LYS
SEQRES 3 A 323 GLU SER LEU SER PRO LEU THR ARG PHE LEU ASN ASN GLU
SEQRES 4 A 323 LEU TYR GLY GLU LYS ASP ALA ARG ARG LYS ILE GLY GLU
SEQRES 5 A 323 ILE THR GLN THR LEU LEU ASP HIS ALA VAL GLU ASN GLY
SEQRES 6 A 323 GLU SER GLN LYS VAL THR LEU LYS GLY GLU ALA GLY ARG
SEQRES 7 A 323 LEU THR GLY TYR TYR HIS GLN GLY ALA ALA SER SER GLU
SEQRES 8 A 323 GLY GLU THR SER ALA THR SER GLY LYS VAL VAL LEU PHE
SEQRES 9 A 323 LEU HIS GLY SER GLY SER SER ALA GLU GLU GLN ALA SER
SEQRES 10 A 323 GLU ILE ARG ASN HIS TYR GLN LYS GLN GLY ILE ASP MET
SEQRES 11 A 323 LEU ALA VAL ASN LEU ARG GLY TYR GLY GLU SER ASP GLY
SEQRES 12 A 323 GLY PRO SER GLU LYS GLY LEU TYR GLN ASP ALA ARG THR
SEQRES 13 A 323 MET PHE ASN TYR LEU VAL ASN ASP LYS GLY ILE ASP PRO
SEQRES 14 A 323 SER ASN ILE ILE ILE HIS GLY TYR SER MET GLY GLY PRO
SEQRES 15 A 323 ILE ALA ALA ASP LEU ALA ARG TYR ALA ALA GLN ASN GLY
SEQRES 16 A 323 GLN ALA VAL SER GLY LEU LEU LEU ASP ARG PRO MET PRO
SEQRES 17 A 323 SER MET THR LYS ALA ILE THR ALA HIS GLU VAL ALA ASN
SEQRES 18 A 323 PRO ALA GLY ILE VAL GLY ALA ILE ALA LYS ALA VAL ASN
SEQRES 19 A 323 GLY GLN PHE SER VAL GLU LYS ASN LEU LYS GLY LEU PRO
SEQRES 20 A 323 LYS GLU THR PRO ILE LEU LEU LEU THR ASP ASN GLU GLY
SEQRES 21 A 323 LEU GLY GLU GLU GLY GLU LYS LEU ARG ALA LYS LEU ALA
SEQRES 22 A 323 ILE ALA GLY TYR ASN VAL THR GLY GLU GLN THR PHE TYR
SEQRES 23 A 323 GLY HIS GLU ALA SER ASN ARG LEU MET GLY GLN TYR ALA
SEQRES 24 A 323 ASP GLN ILE VAL SER GLY LEU PHE ASN ALA GLU GLN ALA
SEQRES 25 A 323 ALA VAL GLU ALA GLY GLU VAL LEU LYS GLY LEU
SEQRES 1 B 323 ALA MET ALA LEU SER GLY ASN GLU LYS HIS LYS GLU ASN
SEQRES 2 B 323 VAL ALA ILE GLU ASN ASP GLY THR PRO PRO ARG ASP LYS
SEQRES 3 B 323 GLU SER LEU SER PRO LEU THR ARG PHE LEU ASN ASN GLU
SEQRES 4 B 323 LEU TYR GLY GLU LYS ASP ALA ARG ARG LYS ILE GLY GLU
SEQRES 5 B 323 ILE THR GLN THR LEU LEU ASP HIS ALA VAL GLU ASN GLY
SEQRES 6 B 323 GLU SER GLN LYS VAL THR LEU LYS GLY GLU ALA GLY ARG
SEQRES 7 B 323 LEU THR GLY TYR TYR HIS GLN GLY ALA ALA SER SER GLU
SEQRES 8 B 323 GLY GLU THR SER ALA THR SER GLY LYS VAL VAL LEU PHE
SEQRES 9 B 323 LEU HIS GLY SER GLY SER SER ALA GLU GLU GLN ALA SER
SEQRES 10 B 323 GLU ILE ARG ASN HIS TYR GLN LYS GLN GLY ILE ASP MET
SEQRES 11 B 323 LEU ALA VAL ASN LEU ARG GLY TYR GLY GLU SER ASP GLY
SEQRES 12 B 323 GLY PRO SER GLU LYS GLY LEU TYR GLN ASP ALA ARG THR
SEQRES 13 B 323 MET PHE ASN TYR LEU VAL ASN ASP LYS GLY ILE ASP PRO
SEQRES 14 B 323 SER ASN ILE ILE ILE HIS GLY TYR SER MET GLY GLY PRO
SEQRES 15 B 323 ILE ALA ALA ASP LEU ALA ARG TYR ALA ALA GLN ASN GLY
SEQRES 16 B 323 GLN ALA VAL SER GLY LEU LEU LEU ASP ARG PRO MET PRO
SEQRES 17 B 323 SER MET THR LYS ALA ILE THR ALA HIS GLU VAL ALA ASN
SEQRES 18 B 323 PRO ALA GLY ILE VAL GLY ALA ILE ALA LYS ALA VAL ASN
SEQRES 19 B 323 GLY GLN PHE SER VAL GLU LYS ASN LEU LYS GLY LEU PRO
SEQRES 20 B 323 LYS GLU THR PRO ILE LEU LEU LEU THR ASP ASN GLU GLY
SEQRES 21 B 323 LEU GLY GLU GLU GLY GLU LYS LEU ARG ALA LYS LEU ALA
SEQRES 22 B 323 ILE ALA GLY TYR ASN VAL THR GLY GLU GLN THR PHE TYR
SEQRES 23 B 323 GLY HIS GLU ALA SER ASN ARG LEU MET GLY GLN TYR ALA
SEQRES 24 B 323 ASP GLN ILE VAL SER GLY LEU PHE ASN ALA GLU GLN ALA
SEQRES 25 B 323 ALA VAL GLU ALA GLY GLU VAL LEU LYS GLY LEU
FORMUL 3 HOH *21(H2 O)
HELIX 1 AA1 SER A 2927 GLY A 2939 1 13
HELIX 2 AA2 GLU A 2940 LYS A 2946 1 7
HELIX 3 AA3 GLY A 2948 ASN A 2961 1 14
HELIX 4 AA4 SER A 3008 LYS A 3022 1 15
HELIX 5 AA5 SER A 3043 LYS A 3062 1 20
HELIX 6 AA6 ASP A 3065 SER A 3067 5 3
HELIX 7 AA7 MET A 3076 GLN A 3090 1 15
HELIX 8 AA8 SER A 3106 HIS A 3114 1 9
HELIX 9 AA9 ALA A 3120 VAL A 3130 1 11
HELIX 10 AB1 SER A 3135 LYS A 3141 1 7
HELIX 11 AB2 GLU A 3156 ALA A 3172 1 17
HELIX 12 AB3 ALA A 3187 VAL A 3200 1 14
HELIX 13 AB4 SER A 3201 LEU A 3203 5 3
HELIX 14 AB5 SER B 2927 TYR B 2938 1 12
HELIX 15 AB6 GLU B 2940 LYS B 2946 1 7
HELIX 16 AB7 GLY B 2948 GLY B 2962 1 15
HELIX 17 AB8 SER B 3008 GLU B 3015 1 8
HELIX 18 AB9 ILE B 3016 GLN B 3023 1 8
HELIX 19 AC1 SER B 3043 ASP B 3061 1 19
HELIX 20 AC2 ASP B 3065 SER B 3067 5 3
HELIX 21 AC3 MET B 3076 GLN B 3090 1 15
HELIX 22 AC4 SER B 3106 GLU B 3115 1 10
HELIX 23 AC5 ALA B 3120 VAL B 3130 1 11
HELIX 24 AC6 SER B 3135 LYS B 3141 1 7
HELIX 25 AC7 GLU B 3156 GLY B 3173 1 18
HELIX 26 AC8 ALA B 3187 SER B 3201 1 15
SHEET 1 AA1 8 SER A2964 LYS A2970 0
SHEET 2 AA1 8 ARG A2975 HIS A2981 -1 O GLY A2978 N VAL A2967
SHEET 3 AA1 8 ASP A3026 VAL A3030 -1 O MET A3027 N HIS A2981
SHEET 4 AA1 8 VAL A2998 LEU A3002 1 N VAL A2999 O LEU A3028
SHEET 5 AA1 8 ILE A3069 TYR A3074 1 O ILE A3070 N LEU A3000
SHEET 6 AA1 8 GLY A3097 ASP A3101 1 O LEU A3099 N ILE A3071
SHEET 7 AA1 8 ILE A3149 THR A3153 1 O LEU A3150 N LEU A3100
SHEET 8 AA1 8 GLU A3179 GLN A3180 1 O GLU A3179 N THR A3153
SHEET 1 AA2 8 SER B2964 LYS B2970 0
SHEET 2 AA2 8 ARG B2975 HIS B2981 -1 O TYR B2980 N GLN B2965
SHEET 3 AA2 8 ASP B3026 VAL B3030 -1 O MET B3027 N HIS B2981
SHEET 4 AA2 8 VAL B2998 LEU B3002 1 N VAL B2999 O LEU B3028
SHEET 5 AA2 8 ILE B3069 TYR B3074 1 O ILE B3070 N LEU B3000
SHEET 6 AA2 8 GLY B3097 ASP B3101 1 O LEU B3099 N ILE B3071
SHEET 7 AA2 8 ILE B3149 LEU B3152 1 O LEU B3150 N LEU B3098
SHEET 8 AA2 8 VAL B3176 THR B3177 1 O THR B3177 N LEU B3151
CISPEP 1 PRO A 2919 PRO A 2920 0 -28.95
CRYST1 44.106 99.681 164.890 90.00 90.00 90.00 P 21 21 21 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 0.022673 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010032 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006065 0.00000
TER 2158 PHE A3204
TER 4279 LEU B3203
MASTER 444 0 0 26 16 0 0 6 4298 2 0 50
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