HEADER TRANSPORT PROTEIN 28-SEP-18 6HS6
TITLE C-TERMINAL DOMAIN OF THE TSSA COMPONENT OF THE TYPE VI SECRETION
TITLE 2 SYSTEM FROM BURKHOLDERIA CENOCEPACIA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYPE VI SECRETION PROTEIN IMPA;
COMPND 3 CHAIN: A, C, H, G, F, E, D, B;
COMPND 4 FRAGMENT: UNP RESIDUES 303-373;
COMPND 5 SYNONYM: TSSA;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: PURIFICATION BY MALTOSE BINDING PROTEIN CLEAVED AFTER
COMPND 8 IEGRREMAINING TAG RESIDUES ISHM - 299-302CONSTRUCT COMPRISES RESIDUES
COMPND 9 303-373 OF FULL-LENGTH PROTEIN (TOTAL 373 RESIDUES)
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BURKHOLDERIA CENOCEPACIA H111;
SOURCE 3 ORGANISM_TAXID: 1055524;
SOURCE 4 GENE: I35_RS01755;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: NEB EXPRESS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMAL-C5X
KEYWDS ALPHA-HELICAL PROTEIN, TYPE VI SECRETION SYSTEM COMPONENT, TSSA,
KEYWDS 2 TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.R.DIX,H.J.OWEN,R.SUN,A.AHMAD,S.SHASTRI,H.L.SPIEWAK,D.J.MOSBY,
AUTHOR 2 M.J.HARRIS,S.L.BATTERS,T.A.BROOKER,S.B.TZOKOV,S.E.SEDELNIKOVA,
AUTHOR 3 P.J.BAKER,P.A.BULLOUGH,D.W.RICE,M.S.THOMAS
REVDAT 1 21-NOV-18 6HS6 0
JRNL AUTH S.R.DIX,H.J.OWEN,R.SUN,A.AHMAD,S.SHASTRI,H.L.SPIEWAK,
JRNL AUTH 2 D.J.MOSBY,M.J.HARRIS,S.L.BATTERS,T.A.BROOKER,S.B.TZOKOV,
JRNL AUTH 3 S.E.SEDELNIKOVA,P.J.BAKER,P.A.BULLOUGH,D.W.RICE,M.S.THOMAS
JRNL TITL STRUCTURAL INSIGHTS INTO THE FUNCTION OF TYPE VI SECRETION
JRNL TITL 2 SYSTEM TSSA SUBUNITS.
JRNL REF NAT COMMUN V. 9 4765 2018
JRNL REFN ESSN 2041-1723
JRNL PMID 30420757
JRNL DOI 10.1038/S41467-018-07247-1
REMARK 2
REMARK 2 RESOLUTION. 3.08 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.08
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.49
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 22387
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) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1215
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) : 3.08
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.16
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1621
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.94
REMARK 3 BIN R VALUE (WORKING SET) : 0.2830
REMARK 3 BIN FREE R VALUE SET COUNT : 75
REMARK 3 BIN FREE R VALUE : 0.3870
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4401
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 69.71
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.10000
REMARK 3 B22 (A**2) : -2.82000
REMARK 3 B33 (A**2) : -1.28000
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): 0.596
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.337
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.238
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.567
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.932
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.907
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4503 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4340 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6107 ; 1.621 ; 1.941
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9921 ; 0.983 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 540 ; 3.132 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 224 ;31.538 ;22.902
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 761 ;14.281 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 47 ;13.861 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 661 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5066 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1079 ; 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): 2184 ; 4.555 ; 6.658
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2183 ; 4.542 ; 6.657
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2716 ; 7.320 ; 9.964
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2717 ; 7.320 ; 9.966
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2319 ; 4.763 ; 7.194
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2320 ; 4.762 ; 7.196
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3391 ; 7.752 ;10.539
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 4926 ;10.372 ;51.093
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 4927 ;10.372 ;51.106
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 : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 6HS6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-SEP-18.
REMARK 100 THE DEPOSITION ID IS D_1200012162.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-JAN-14
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 : DIAMOND
REMARK 200 BEAMLINE : I24
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.70001
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 : XIA2
REMARK 200 DATA SCALING SOFTWARE : XIA2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23602
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.080
REMARK 200 RESOLUTION RANGE LOW (A) : 41.490
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 12.60
REMARK 200 R MERGE (I) : 0.13100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.08
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.16
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 11.90
REMARK 200 R MERGE FOR SHELL (I) : 0.78600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXCD
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 72.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM CHLORIDE, 0.1M TRIS PH8.0,
REMARK 280 15% (V/V) ETHANOL, 5% (V/V) MPD, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 23.16500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 100.85000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 131.83000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 23.16500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 100.85000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 131.83000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 23.16500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 100.85000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 131.83000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 23.16500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 100.85000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 131.83000
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: 32-MERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 32-MERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 86520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 94560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -622.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, H, G, F, E, D, 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 46.33000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 46.33000
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 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 ILE A 299
REMARK 465 SER A 300
REMARK 465 ASP A 370
REMARK 465 GLU A 371
REMARK 465 GLN A 372
REMARK 465 SER A 373
REMARK 465 ILE C 299
REMARK 465 SER C 300
REMARK 465 HIS C 301
REMARK 465 ASP C 370
REMARK 465 GLU C 371
REMARK 465 GLN C 372
REMARK 465 SER C 373
REMARK 465 ARG H 368
REMARK 465 PRO H 369
REMARK 465 ASP H 370
REMARK 465 GLU H 371
REMARK 465 GLN H 372
REMARK 465 SER H 373
REMARK 465 ILE G 299
REMARK 465 SER G 300
REMARK 465 ASP G 370
REMARK 465 GLU G 371
REMARK 465 GLN G 372
REMARK 465 SER G 373
REMARK 465 ILE F 299
REMARK 465 SER F 300
REMARK 465 ASP F 370
REMARK 465 GLU F 371
REMARK 465 GLN F 372
REMARK 465 SER F 373
REMARK 465 ILE E 299
REMARK 465 SER E 300
REMARK 465 PRO E 369
REMARK 465 ASP E 370
REMARK 465 GLU E 371
REMARK 465 GLN E 372
REMARK 465 SER E 373
REMARK 465 ILE D 299
REMARK 465 SER D 300
REMARK 465 PRO D 369
REMARK 465 ASP D 370
REMARK 465 GLU D 371
REMARK 465 GLN D 372
REMARK 465 SER D 373
REMARK 465 ILE B 299
REMARK 465 SER B 300
REMARK 465 HIS B 301
REMARK 465 ASP B 370
REMARK 465 GLU B 371
REMARK 465 GLN B 372
REMARK 465 SER B 373
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 HIS A 301 CG ND1 CD2 CE1 NE2
REMARK 470 HIS G 301 CG ND1 CD2 CE1 NE2
REMARK 470 HIS F 301 CG ND1 CD2 CE1 NE2
REMARK 470 HIS E 301 CG ND1 CD2 CE1 NE2
REMARK 470 HIS D 301 CG ND1 CD2 CE1 NE2
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 OE1 GLU C 324 NE ARG H 306 3655 2.10
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 MET A 302 78.93 -157.47
REMARK 500 GLN F 304 -83.94 -79.57
REMARK 500 ASN F 305 -156.96 -91.89
REMARK 500 PRO F 325 -5.05 -58.15
REMARK 500 ARG F 368 138.82 -37.94
REMARK 500 ASN E 305 -168.96 -121.57
REMARK 500 ASP E 341 47.17 -102.25
REMARK 500 VAL B 351 -40.18 -139.42
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6HS5 RELATED DB: PDB
REMARK 900 6HS5 CONTAINS THE N-TERMINAL REGION OF THE SAME PROTEIN.
REMARK 900 RELATED ID: 6H8E RELATED DB: PDB
REMARK 900 6H8E - TRUNCATED C-TERMINAL REGION OF THE SAME PROTEIN
REMARK 900 RELATED ID: 6H8F RELATED DB: PDB
REMARK 900 6H8F - FRAGMENT OF THE C-TERMINAL REGION OF THE SAME PROTEIN
DBREF1 6HS6 A 303 373 UNP A0A1V2W6E8_9BURK
DBREF2 6HS6 A A0A1V2W6E8 303 373
DBREF1 6HS6 C 303 373 UNP A0A1V2W6E8_9BURK
DBREF2 6HS6 C A0A1V2W6E8 303 373
DBREF1 6HS6 H 303 373 UNP A0A1V2W6E8_9BURK
DBREF2 6HS6 H A0A1V2W6E8 303 373
DBREF1 6HS6 G 303 373 UNP A0A1V2W6E8_9BURK
DBREF2 6HS6 G A0A1V2W6E8 303 373
DBREF1 6HS6 F 303 373 UNP A0A1V2W6E8_9BURK
DBREF2 6HS6 F A0A1V2W6E8 303 373
DBREF1 6HS6 E 303 373 UNP A0A1V2W6E8_9BURK
DBREF2 6HS6 E A0A1V2W6E8 303 373
DBREF1 6HS6 D 303 373 UNP A0A1V2W6E8_9BURK
DBREF2 6HS6 D A0A1V2W6E8 303 373
DBREF1 6HS6 B 303 373 UNP A0A1V2W6E8_9BURK
DBREF2 6HS6 B A0A1V2W6E8 303 373
SEQADV 6HS6 ILE A 299 UNP A0A1V2W6E EXPRESSION TAG
SEQADV 6HS6 SER A 300 UNP A0A1V2W6E EXPRESSION TAG
SEQADV 6HS6 HIS A 301 UNP A0A1V2W6E EXPRESSION TAG
SEQADV 6HS6 MET A 302 UNP A0A1V2W6E EXPRESSION TAG
SEQADV 6HS6 ILE C 299 UNP A0A1V2W6E EXPRESSION TAG
SEQADV 6HS6 SER C 300 UNP A0A1V2W6E EXPRESSION TAG
SEQADV 6HS6 HIS C 301 UNP A0A1V2W6E EXPRESSION TAG
SEQADV 6HS6 MET C 302 UNP A0A1V2W6E EXPRESSION TAG
SEQADV 6HS6 ILE H 299 UNP A0A1V2W6E EXPRESSION TAG
SEQADV 6HS6 SER H 300 UNP A0A1V2W6E EXPRESSION TAG
SEQADV 6HS6 HIS H 301 UNP A0A1V2W6E EXPRESSION TAG
SEQADV 6HS6 MET H 302 UNP A0A1V2W6E EXPRESSION TAG
SEQADV 6HS6 ILE G 299 UNP A0A1V2W6E EXPRESSION TAG
SEQADV 6HS6 SER G 300 UNP A0A1V2W6E EXPRESSION TAG
SEQADV 6HS6 HIS G 301 UNP A0A1V2W6E EXPRESSION TAG
SEQADV 6HS6 MET G 302 UNP A0A1V2W6E EXPRESSION TAG
SEQADV 6HS6 ILE F 299 UNP A0A1V2W6E EXPRESSION TAG
SEQADV 6HS6 SER F 300 UNP A0A1V2W6E EXPRESSION TAG
SEQADV 6HS6 HIS F 301 UNP A0A1V2W6E EXPRESSION TAG
SEQADV 6HS6 MET F 302 UNP A0A1V2W6E EXPRESSION TAG
SEQADV 6HS6 ILE E 299 UNP A0A1V2W6E EXPRESSION TAG
SEQADV 6HS6 SER E 300 UNP A0A1V2W6E EXPRESSION TAG
SEQADV 6HS6 HIS E 301 UNP A0A1V2W6E EXPRESSION TAG
SEQADV 6HS6 MET E 302 UNP A0A1V2W6E EXPRESSION TAG
SEQADV 6HS6 ILE D 299 UNP A0A1V2W6E EXPRESSION TAG
SEQADV 6HS6 SER D 300 UNP A0A1V2W6E EXPRESSION TAG
SEQADV 6HS6 HIS D 301 UNP A0A1V2W6E EXPRESSION TAG
SEQADV 6HS6 MET D 302 UNP A0A1V2W6E EXPRESSION TAG
SEQADV 6HS6 ILE B 299 UNP A0A1V2W6E EXPRESSION TAG
SEQADV 6HS6 SER B 300 UNP A0A1V2W6E EXPRESSION TAG
SEQADV 6HS6 HIS B 301 UNP A0A1V2W6E EXPRESSION TAG
SEQADV 6HS6 MET B 302 UNP A0A1V2W6E EXPRESSION TAG
SEQRES 1 A 75 ILE SER HIS MET ILE GLN ASN ARG ALA GLN ALA VAL ASP
SEQRES 2 A 75 GLN LEU ARG ALA VAL ALA ARG TYR PHE ARG GLN THR GLU
SEQRES 3 A 75 PRO HIS SER PRO VAL ALA TYR LEU ALA ASP LYS ALA ALA
SEQRES 4 A 75 GLU TRP ALA ASP MET PRO LEU HIS LYS TRP LEU GLU SER
SEQRES 5 A 75 VAL VAL LYS ASP ASP GLY SER LEU SER HIS ILE ARG GLU
SEQRES 6 A 75 LEU LEU GLY VAL ARG PRO ASP GLU GLN SER
SEQRES 1 C 75 ILE SER HIS MET ILE GLN ASN ARG ALA GLN ALA VAL ASP
SEQRES 2 C 75 GLN LEU ARG ALA VAL ALA ARG TYR PHE ARG GLN THR GLU
SEQRES 3 C 75 PRO HIS SER PRO VAL ALA TYR LEU ALA ASP LYS ALA ALA
SEQRES 4 C 75 GLU TRP ALA ASP MET PRO LEU HIS LYS TRP LEU GLU SER
SEQRES 5 C 75 VAL VAL LYS ASP ASP GLY SER LEU SER HIS ILE ARG GLU
SEQRES 6 C 75 LEU LEU GLY VAL ARG PRO ASP GLU GLN SER
SEQRES 1 H 75 ILE SER HIS MET ILE GLN ASN ARG ALA GLN ALA VAL ASP
SEQRES 2 H 75 GLN LEU ARG ALA VAL ALA ARG TYR PHE ARG GLN THR GLU
SEQRES 3 H 75 PRO HIS SER PRO VAL ALA TYR LEU ALA ASP LYS ALA ALA
SEQRES 4 H 75 GLU TRP ALA ASP MET PRO LEU HIS LYS TRP LEU GLU SER
SEQRES 5 H 75 VAL VAL LYS ASP ASP GLY SER LEU SER HIS ILE ARG GLU
SEQRES 6 H 75 LEU LEU GLY VAL ARG PRO ASP GLU GLN SER
SEQRES 1 G 75 ILE SER HIS MET ILE GLN ASN ARG ALA GLN ALA VAL ASP
SEQRES 2 G 75 GLN LEU ARG ALA VAL ALA ARG TYR PHE ARG GLN THR GLU
SEQRES 3 G 75 PRO HIS SER PRO VAL ALA TYR LEU ALA ASP LYS ALA ALA
SEQRES 4 G 75 GLU TRP ALA ASP MET PRO LEU HIS LYS TRP LEU GLU SER
SEQRES 5 G 75 VAL VAL LYS ASP ASP GLY SER LEU SER HIS ILE ARG GLU
SEQRES 6 G 75 LEU LEU GLY VAL ARG PRO ASP GLU GLN SER
SEQRES 1 F 75 ILE SER HIS MET ILE GLN ASN ARG ALA GLN ALA VAL ASP
SEQRES 2 F 75 GLN LEU ARG ALA VAL ALA ARG TYR PHE ARG GLN THR GLU
SEQRES 3 F 75 PRO HIS SER PRO VAL ALA TYR LEU ALA ASP LYS ALA ALA
SEQRES 4 F 75 GLU TRP ALA ASP MET PRO LEU HIS LYS TRP LEU GLU SER
SEQRES 5 F 75 VAL VAL LYS ASP ASP GLY SER LEU SER HIS ILE ARG GLU
SEQRES 6 F 75 LEU LEU GLY VAL ARG PRO ASP GLU GLN SER
SEQRES 1 E 75 ILE SER HIS MET ILE GLN ASN ARG ALA GLN ALA VAL ASP
SEQRES 2 E 75 GLN LEU ARG ALA VAL ALA ARG TYR PHE ARG GLN THR GLU
SEQRES 3 E 75 PRO HIS SER PRO VAL ALA TYR LEU ALA ASP LYS ALA ALA
SEQRES 4 E 75 GLU TRP ALA ASP MET PRO LEU HIS LYS TRP LEU GLU SER
SEQRES 5 E 75 VAL VAL LYS ASP ASP GLY SER LEU SER HIS ILE ARG GLU
SEQRES 6 E 75 LEU LEU GLY VAL ARG PRO ASP GLU GLN SER
SEQRES 1 D 75 ILE SER HIS MET ILE GLN ASN ARG ALA GLN ALA VAL ASP
SEQRES 2 D 75 GLN LEU ARG ALA VAL ALA ARG TYR PHE ARG GLN THR GLU
SEQRES 3 D 75 PRO HIS SER PRO VAL ALA TYR LEU ALA ASP LYS ALA ALA
SEQRES 4 D 75 GLU TRP ALA ASP MET PRO LEU HIS LYS TRP LEU GLU SER
SEQRES 5 D 75 VAL VAL LYS ASP ASP GLY SER LEU SER HIS ILE ARG GLU
SEQRES 6 D 75 LEU LEU GLY VAL ARG PRO ASP GLU GLN SER
SEQRES 1 B 75 ILE SER HIS MET ILE GLN ASN ARG ALA GLN ALA VAL ASP
SEQRES 2 B 75 GLN LEU ARG ALA VAL ALA ARG TYR PHE ARG GLN THR GLU
SEQRES 3 B 75 PRO HIS SER PRO VAL ALA TYR LEU ALA ASP LYS ALA ALA
SEQRES 4 B 75 GLU TRP ALA ASP MET PRO LEU HIS LYS TRP LEU GLU SER
SEQRES 5 B 75 VAL VAL LYS ASP ASP GLY SER LEU SER HIS ILE ARG GLU
SEQRES 6 B 75 LEU LEU GLY VAL ARG PRO ASP GLU GLN SER
HELIX 1 AA1 ASN A 305 GLU A 324 1 20
HELIX 2 AA2 PRO A 328 ASP A 341 1 14
HELIX 3 AA3 PRO A 343 VAL A 352 1 10
HELIX 4 AA4 ASP A 354 GLY A 366 1 13
HELIX 5 AA5 ASN C 305 GLU C 324 1 20
HELIX 6 AA6 PRO C 328 ASP C 341 1 14
HELIX 7 AA7 PRO C 343 VAL C 352 1 10
HELIX 8 AA8 ASP C 354 GLY C 366 1 13
HELIX 9 AA9 SER H 300 GLU H 324 1 25
HELIX 10 AB1 PRO H 328 ASP H 341 1 14
HELIX 11 AB2 PRO H 343 VAL H 352 1 10
HELIX 12 AB3 ASP H 354 GLY H 366 1 13
HELIX 13 AB4 ASN G 305 GLU G 324 1 20
HELIX 14 AB5 PRO G 328 ASP G 341 1 14
HELIX 15 AB6 PRO G 343 VAL G 352 1 10
HELIX 16 AB7 ASP G 354 GLY G 366 1 13
HELIX 17 AB8 ASN F 305 GLU F 324 1 20
HELIX 18 AB9 PRO F 328 ASP F 341 1 14
HELIX 19 AC1 PRO F 343 VAL F 352 1 10
HELIX 20 AC2 ASP F 354 GLY F 366 1 13
HELIX 21 AC3 ASN E 305 GLU E 324 1 20
HELIX 22 AC4 PRO E 328 ASP E 341 1 14
HELIX 23 AC5 PRO E 343 SER E 350 1 8
HELIX 24 AC6 ASP E 354 GLY E 366 1 13
HELIX 25 AC7 ASN D 305 GLU D 324 1 20
HELIX 26 AC8 SER D 327 ASP D 341 1 15
HELIX 27 AC9 PRO D 343 VAL D 352 1 10
HELIX 28 AD1 ASP D 354 GLY D 366 1 13
HELIX 29 AD2 ASN B 305 GLU B 324 1 20
HELIX 30 AD3 PRO B 328 ASP B 341 1 14
HELIX 31 AD4 PRO B 343 SER B 350 1 8
HELIX 32 AD5 ASP B 354 GLY B 366 1 13
CRYST1 46.330 201.700 263.660 90.00 90.00 90.00 I 2 2 2 64
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 0.021584 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004958 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003793 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
