HEADER TOXIN 10-AUG-13 4C18
TITLE THE STRUCTURE OF THE TSI2 DIMER WITH A DISULFIDE BOND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TSI2;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 287;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET28A
KEYWDS TOXIN, IMMUNITY PROTEIN, T6SS, ANTI-TOXIN
EXPDTA X-RAY DIFFRACTION
AUTHOR C.S.ROBB,F.E.NANO,A.B.BORASTON
REVDAT 1 27-AUG-14 4C18 0
JRNL AUTH C.S.ROBB,M.CID,F.E.NANO,A.B.BORASTON
JRNL TITL THE STRUCTURE OF TSE2 IN COMPLEX WITH TSI2
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.49 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,
REMARK 3 STEINER,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) : 1.49
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.59
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.91
REMARK 3 NUMBER OF REFLECTIONS : 19974
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) : 0.22445
REMARK 3 R VALUE (WORKING SET) : 0.22262
REMARK 3 FREE R VALUE : 0.25886
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.1
REMARK 3 FREE R VALUE TEST SET COUNT : 1076
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) : 1.494
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.533
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1379
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.41
REMARK 3 BIN R VALUE (WORKING SET) : 0.270
REMARK 3 BIN FREE R VALUE SET COUNT : 90
REMARK 3 BIN FREE R VALUE : 0.367
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1153
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 88
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.916
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.55
REMARK 3 B22 (A**2) : -1.61
REMARK 3 B33 (A**2) : 2.16
REMARK 3 B12 (A**2) : 0.49
REMARK 3 B13 (A**2) : 0.52
REMARK 3 B23 (A**2) : 1.39
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.100
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.101
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.079
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.068
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.943
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.926
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1170 ; 0.018 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 1118 ; 0.006 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1595 ; 1.812 ; 2.000
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2561 ; 1.353 ; 3.002
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 151 ; 6.563 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 58 ;35.818 ;26.897
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 195 ;13.502 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 5 ;15.889 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 183 ; 0.115 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1376 ; 0.011 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 241 ; 0.005 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 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 : 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
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 4C18 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-AUG-13.
REMARK 100 THE PDBE ID CODE IS EBI-57971.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JUL-11
REMARK 200 TEMPERATURE (KELVIN) : 113
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : RH COATED FLAT MIRROR,
REMARK 200 TOROIDAL FOCUSING MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21050
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.49
REMARK 200 RESOLUTION RANGE LOW (A) : 35.93
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.0
REMARK 200 DATA REDUNDANCY : 3.8
REMARK 200 R MERGE (I) : 0.11
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.30
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.49
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.57
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.8
REMARK 200 R MERGE FOR SHELL (I) : 0.24
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.70
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: PDB ENTRY 3VPV
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM CITRATE PH 5.6, 35%
REMARK 280 T-BUTANOL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.2 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 MET A -20
REMARK 465 GLY A -19
REMARK 465 SER A -18
REMARK 465 SER A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 SER A -10
REMARK 465 SER A -9
REMARK 465 GLY A -8
REMARK 465 LEU A -7
REMARK 465 VAL A -6
REMARK 465 PRO A -5
REMARK 465 ARG A -4
REMARK 465 GLY A -3
REMARK 465 SER A -2
REMARK 465 HIS A -1
REMARK 465 ALA A 76
REMARK 465 SER A 77
REMARK 465 MET B -20
REMARK 465 GLY B -19
REMARK 465 SER B -18
REMARK 465 SER B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 SER B -10
REMARK 465 SER B -9
REMARK 465 GLY B -8
REMARK 465 LEU B -7
REMARK 465 VAL B -6
REMARK 465 PRO B -5
REMARK 465 ARG B -4
REMARK 465 GLY B -3
REMARK 465 SER B -2
REMARK 465 GLU B 74
REMARK 465 PRO B 75
REMARK 465 ALA B 76
REMARK 465 SER B 77
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 MET A 0 CG SD CE
REMARK 470 GLU A 21 CD OE1 OE2
REMARK 470 ASN A 28 CG OD1 ND2
REMARK 470 ASP A 29 CG OD1 OD2
REMARK 470 ASP A 30 CG OD1 OD2
REMARK 470 ARG A 70 CZ NH1 NH2
REMARK 470 GLU A 74 CG CD OE1 OE2
REMARK 470 PRO A 75 C O
REMARK 470 HIS B -1 CG ND1 CD2 CE1 NE2
REMARK 470 MET B 0 CG SD CE
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 NH1 ARG A 18 O HOH A 2022 1.95
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG B 70 NE - CZ - NH1 ANGL. DEV. = 3.3 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 MET B 0 -41.23 -150.23
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 HIS B -1 MET B 0 -148.98
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 MET A 0 22.8 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4C15 RELATED DB: PDB
REMARK 900 THE COMPLEX OF TSE2 AND TSI2 FROM PSEUDOMONAS
REMARK 900 AERUGINOSA
DBREF 4C18 A 1 77 UNP Q9I0D9 Q9I0D9_PSEAE 1 77
DBREF 4C18 B 1 77 UNP Q9I0D9 Q9I0D9_PSEAE 1 77
SEQADV 4C18 MET A -20 UNP Q9I0D9 EXPRESSION TAG
SEQADV 4C18 GLY A -19 UNP Q9I0D9 EXPRESSION TAG
SEQADV 4C18 SER A -18 UNP Q9I0D9 EXPRESSION TAG
SEQADV 4C18 SER A -17 UNP Q9I0D9 EXPRESSION TAG
SEQADV 4C18 HIS A -16 UNP Q9I0D9 EXPRESSION TAG
SEQADV 4C18 HIS A -15 UNP Q9I0D9 EXPRESSION TAG
SEQADV 4C18 HIS A -14 UNP Q9I0D9 EXPRESSION TAG
SEQADV 4C18 HIS A -13 UNP Q9I0D9 EXPRESSION TAG
SEQADV 4C18 HIS A -12 UNP Q9I0D9 EXPRESSION TAG
SEQADV 4C18 HIS A -11 UNP Q9I0D9 EXPRESSION TAG
SEQADV 4C18 SER A -10 UNP Q9I0D9 EXPRESSION TAG
SEQADV 4C18 SER A -9 UNP Q9I0D9 EXPRESSION TAG
SEQADV 4C18 GLY A -8 UNP Q9I0D9 EXPRESSION TAG
SEQADV 4C18 LEU A -7 UNP Q9I0D9 EXPRESSION TAG
SEQADV 4C18 VAL A -6 UNP Q9I0D9 EXPRESSION TAG
SEQADV 4C18 PRO A -5 UNP Q9I0D9 EXPRESSION TAG
SEQADV 4C18 ARG A -4 UNP Q9I0D9 EXPRESSION TAG
SEQADV 4C18 GLY A -3 UNP Q9I0D9 EXPRESSION TAG
SEQADV 4C18 SER A -2 UNP Q9I0D9 EXPRESSION TAG
SEQADV 4C18 HIS A -1 UNP Q9I0D9 EXPRESSION TAG
SEQADV 4C18 MET A 0 UNP Q9I0D9 EXPRESSION TAG
SEQADV 4C18 MET B -20 UNP Q9I0D9 EXPRESSION TAG
SEQADV 4C18 GLY B -19 UNP Q9I0D9 EXPRESSION TAG
SEQADV 4C18 SER B -18 UNP Q9I0D9 EXPRESSION TAG
SEQADV 4C18 SER B -17 UNP Q9I0D9 EXPRESSION TAG
SEQADV 4C18 HIS B -16 UNP Q9I0D9 EXPRESSION TAG
SEQADV 4C18 HIS B -15 UNP Q9I0D9 EXPRESSION TAG
SEQADV 4C18 HIS B -14 UNP Q9I0D9 EXPRESSION TAG
SEQADV 4C18 HIS B -13 UNP Q9I0D9 EXPRESSION TAG
SEQADV 4C18 HIS B -12 UNP Q9I0D9 EXPRESSION TAG
SEQADV 4C18 HIS B -11 UNP Q9I0D9 EXPRESSION TAG
SEQADV 4C18 SER B -10 UNP Q9I0D9 EXPRESSION TAG
SEQADV 4C18 SER B -9 UNP Q9I0D9 EXPRESSION TAG
SEQADV 4C18 GLY B -8 UNP Q9I0D9 EXPRESSION TAG
SEQADV 4C18 LEU B -7 UNP Q9I0D9 EXPRESSION TAG
SEQADV 4C18 VAL B -6 UNP Q9I0D9 EXPRESSION TAG
SEQADV 4C18 PRO B -5 UNP Q9I0D9 EXPRESSION TAG
SEQADV 4C18 ARG B -4 UNP Q9I0D9 EXPRESSION TAG
SEQADV 4C18 GLY B -3 UNP Q9I0D9 EXPRESSION TAG
SEQADV 4C18 SER B -2 UNP Q9I0D9 EXPRESSION TAG
SEQADV 4C18 HIS B -1 UNP Q9I0D9 EXPRESSION TAG
SEQADV 4C18 MET B 0 UNP Q9I0D9 EXPRESSION TAG
SEQRES 1 A 98 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 98 LEU VAL PRO ARG GLY SER HIS MET MET ASN LEU LYS PRO
SEQRES 3 A 98 GLN THR LEU MET VAL ALA ILE GLN CYS VAL ALA ALA ARG
SEQRES 4 A 98 THR ARG GLU LEU ASP ALA GLN LEU GLN ASN ASP ASP PRO
SEQRES 5 A 98 GLN ASN ALA ALA GLU LEU GLU GLN LEU LEU VAL GLY TYR
SEQRES 6 A 98 ASP LEU ALA ALA ASP ASP LEU LYS ASN ALA TYR GLU GLN
SEQRES 7 A 98 ALA LEU GLY GLN TYR SER GLY LEU PRO PRO TYR ASP ARG
SEQRES 8 A 98 LEU ILE GLU GLU PRO ALA SER
SEQRES 1 B 98 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 98 LEU VAL PRO ARG GLY SER HIS MET MET ASN LEU LYS PRO
SEQRES 3 B 98 GLN THR LEU MET VAL ALA ILE GLN CYS VAL ALA ALA ARG
SEQRES 4 B 98 THR ARG GLU LEU ASP ALA GLN LEU GLN ASN ASP ASP PRO
SEQRES 5 B 98 GLN ASN ALA ALA GLU LEU GLU GLN LEU LEU VAL GLY TYR
SEQRES 6 B 98 ASP LEU ALA ALA ASP ASP LEU LYS ASN ALA TYR GLU GLN
SEQRES 7 B 98 ALA LEU GLY GLN TYR SER GLY LEU PRO PRO TYR ASP ARG
SEQRES 8 B 98 LEU ILE GLU GLU PRO ALA SER
FORMUL 3 HOH *88(H2 O)
HELIX 1 1 LYS A 4 GLN A 27 1 24
HELIX 2 2 ASN A 33 GLY A 60 1 28
HELIX 3 3 PRO A 67 ILE A 72 1 6
HELIX 4 4 LYS B 4 LEU B 26 1 23
HELIX 5 5 ASN B 33 TYR B 62 1 30
HELIX 6 6 PRO B 67 GLU B 73 1 7
SSBOND 1 CYS A 14 CYS B 14 1555 1555 2.14
CRYST1 27.970 36.300 37.860 107.37 95.23 92.11 P 1 2
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 0.035753 0.001317 0.003854 0.00000
SCALE2 0.000000 0.027567 0.008776 0.00000
SCALE3 0.000000 0.000000 0.027835 0.00000
(ATOM LINES ARE NOT SHOWN.)
END