HEADER TRANSPORT PROTEIN 22-JUL-13 4LSH
TITLE ION SELECTIVITY OF OMPF PORIN SOAKED IN 0.2M KBR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OUTER MEMBRANE PROTEIN F;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 23-362;
COMPND 5 SYNONYM: OUTER MEMBRANE PROTEIN 1A, OUTER MEMBRANE PROTEIN B, OUTER
COMPND 6 MEMBRANE PROTEIN IA, PORIN OMPF;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: B0929, CMLB, COA, CRY, JW0912, OMPF, TOLF;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: K12;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPR272
KEYWDS PORIN, OUTER MEMBRANE PROTEIN, BETA-BARREL, ION TRANSPORT, TRANSPORT
KEYWDS 2 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR D.BALASUNDARESAN,L.BLACHOWICZ,B.ROUX
REVDAT 3 20-SEP-23 4LSH 1 REMARK SEQADV LINK
REVDAT 2 15-JAN-14 4LSH 1 JRNL
REVDAT 1 23-OCT-13 4LSH 0
JRNL AUTH B.DHAKSHNAMOORTHY,B.K.ZIERVOGEL,L.BLACHOWICZ,B.ROUX
JRNL TITL A STRUCTURAL STUDY OF ION PERMEATION IN OMPF PORIN FROM
JRNL TITL 2 ANOMALOUS X-RAY DIFFRACTION AND MOLECULAR DYNAMICS
JRNL TITL 3 SIMULATIONS.
JRNL REF J.AM.CHEM.SOC. V. 135 16561 2013
JRNL REFN ISSN 0002-7863
JRNL PMID 24106986
JRNL DOI 10.1021/JA407783A
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.89
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 38062
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) : 0.247
REMARK 3 R VALUE (WORKING SET) : 0.245
REMARK 3 FREE R VALUE : 0.293
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2011
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.25
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2779
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.43
REMARK 3 BIN R VALUE (WORKING SET) : 0.3070
REMARK 3 BIN FREE R VALUE SET COUNT : 143
REMARK 3 BIN FREE R VALUE : 0.3300
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5153
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 13
REMARK 3 SOLVENT ATOMS : 325
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.75
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.46000
REMARK 3 B22 (A**2) : -1.46000
REMARK 3 B33 (A**2) : 4.74000
REMARK 3 B12 (A**2) : -1.46000
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): 0.320
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.249
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.210
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.238
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.909
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.881
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5257 ; 0.015 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 4665 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7106 ; 1.615 ; 1.931
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10665 ; 0.961 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 663 ; 7.206 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 284 ;38.109 ;24.930
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 780 ;16.532 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;13.603 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 722 ; 0.093 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6345 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1353 ; 0.003 ; 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 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 1 340 B 1 340 18175 0.10 0.05
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 4LSH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-AUG-13.
REMARK 100 THE DEPOSITION ID IS D_1000081029.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-JUN-11
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91956
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40073
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.14000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.4400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.24
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.79200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
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 2OMF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50% PEG200, 0.1 M SODIUM CACODYLATE,
REMARK 280 0.2 M MAGNESIUM CHLORIDE, PH 6.5, CRYSTALS SOAKED IN 0.2 M
REMARK 280 POTASSIUM BROMIDE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,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 -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 0.00000
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 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41220 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.0 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 350 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40680 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.0 KCAL/MOL
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 350 BIOMT1 2 -0.500000 -0.866025 0.000000 116.98100
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 58.49050
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 101.30852
REMARK 350 BIOMT3 3 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 GLY A 0
REMARK 465 TYR A 4
REMARK 465 ASN A 5
REMARK 465 LYS A 6
REMARK 465 ASP A 7
REMARK 465 ASN A 27
REMARK 465 GLY B 0
REMARK 465 ILE B 3
REMARK 465 TYR B 4
REMARK 465 ASN B 5
REMARK 465 LYS B 6
REMARK 465 ASP B 7
REMARK 465 ASN B 27
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 ILE A 3 CG1 CG2 CD1
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 NZ LYS A 25 O HOH A 615 1.79
REMARK 500 O ASP B 121 O HOH B 511 2.14
REMARK 500 NH2 ARG B 167 BR BR B 404 2.14
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 THR B 81 BR BR B 403 2655 2.05
REMARK 500 BR BR A 402 O HOH A 572 3555 2.15
REMARK 500 O HOH A 545 O HOH A 621 3555 2.18
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 ASP A 172 CB - CG - OD1 ANGL. DEV. = 5.5 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 ALA A 84 98.00 -163.03
REMARK 500 ALA A 91 -114.83 51.05
REMARK 500 GLU A 117 -47.03 -132.76
REMARK 500 PHE A 118 -147.59 -97.25
REMARK 500 PHE A 128 -116.15 60.28
REMARK 500 PHE A 144 73.67 45.05
REMARK 500 GLU A 183 68.15 39.10
REMARK 500 ILE A 286 -22.35 -143.66
REMARK 500 ASN A 304 -157.57 -158.14
REMARK 500 SER A 320 -9.61 -59.42
REMARK 500 ASN A 322 131.34 -38.20
REMARK 500 ALA B 84 95.98 -165.70
REMARK 500 ALA B 91 -115.55 49.32
REMARK 500 GLU B 117 -46.33 -130.67
REMARK 500 PHE B 118 -159.48 -100.36
REMARK 500 ALA B 123 60.00 -91.59
REMARK 500 PHE B 128 -113.27 58.90
REMARK 500 PHE B 144 72.87 45.51
REMARK 500 GLU B 183 69.04 36.47
REMARK 500 ILE B 286 -23.48 -144.37
REMARK 500 ASN B 304 -159.04 -158.58
REMARK 500 ASN B 322 130.44 -38.20
REMARK 500
REMARK 500 REMARK: NULL
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 407 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 63 OH
REMARK 620 2 HOH A 543 O 89.8
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 406
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4LSE RELATED DB: PDB
REMARK 900 RELATED ID: 4LSF RELATED DB: PDB
REMARK 900 RELATED ID: 4LSI RELATED DB: PDB
DBREF 4LSH A 1 340 UNP P02931 OMPF_ECOLI 23 362
DBREF 4LSH B 1 340 UNP P02931 OMPF_ECOLI 23 362
SEQADV 4LSH GLY A 0 UNP P02931 EXPRESSION TAG
SEQADV 4LSH GLY B 0 UNP P02931 EXPRESSION TAG
SEQRES 1 A 341 GLY ALA GLU ILE TYR ASN LYS ASP GLY ASN LYS VAL ASP
SEQRES 2 A 341 LEU TYR GLY LYS ALA VAL GLY LEU HIS TYR PHE SER LYS
SEQRES 3 A 341 GLY ASN GLY GLU ASN SER TYR GLY GLY ASN GLY ASP MET
SEQRES 4 A 341 THR TYR ALA ARG LEU GLY PHE LYS GLY GLU THR GLN ILE
SEQRES 5 A 341 ASN SER ASP LEU THR GLY TYR GLY GLN TRP GLU TYR ASN
SEQRES 6 A 341 PHE GLN GLY ASN ASN SER GLU GLY ALA ASP ALA GLN THR
SEQRES 7 A 341 GLY ASN LYS THR ARG LEU ALA PHE ALA GLY LEU LYS TYR
SEQRES 8 A 341 ALA ASP VAL GLY SER PHE ASP TYR GLY ARG ASN TYR GLY
SEQRES 9 A 341 VAL VAL TYR ASP ALA LEU GLY TYR THR ASP MET LEU PRO
SEQRES 10 A 341 GLU PHE GLY GLY ASP THR ALA TYR SER ASP ASP PHE PHE
SEQRES 11 A 341 VAL GLY ARG VAL GLY GLY VAL ALA THR TYR ARG ASN SER
SEQRES 12 A 341 ASN PHE PHE GLY LEU VAL ASP GLY LEU ASN PHE ALA VAL
SEQRES 13 A 341 GLN TYR LEU GLY LYS ASN GLU ARG ASP THR ALA ARG ARG
SEQRES 14 A 341 SER ASN GLY ASP GLY VAL GLY GLY SER ILE SER TYR GLU
SEQRES 15 A 341 TYR GLU GLY PHE GLY ILE VAL GLY ALA TYR GLY ALA ALA
SEQRES 16 A 341 ASP ARG THR ASN LEU GLN GLU ALA GLN PRO LEU GLY ASN
SEQRES 17 A 341 GLY LYS LYS ALA GLU GLN TRP ALA THR GLY LEU LYS TYR
SEQRES 18 A 341 ASP ALA ASN ASN ILE TYR LEU ALA ALA ASN TYR GLY GLU
SEQRES 19 A 341 THR ARG ASN ALA THR PRO ILE THR ASN LYS PHE THR ASN
SEQRES 20 A 341 THR SER GLY PHE ALA ASN LYS THR GLN ASP VAL LEU LEU
SEQRES 21 A 341 VAL ALA GLN TYR GLN PHE ASP PHE GLY LEU ARG PRO SER
SEQRES 22 A 341 ILE ALA TYR THR LYS SER LYS ALA LYS ASP VAL GLU GLY
SEQRES 23 A 341 ILE GLY ASP VAL ASP LEU VAL ASN TYR PHE GLU VAL GLY
SEQRES 24 A 341 ALA THR TYR TYR PHE ASN LYS ASN MET SER THR TYR VAL
SEQRES 25 A 341 ASP TYR ILE ILE ASN GLN ILE ASP SER ASP ASN LYS LEU
SEQRES 26 A 341 GLY VAL GLY SER ASP ASP THR VAL ALA VAL GLY ILE VAL
SEQRES 27 A 341 TYR GLN PHE
SEQRES 1 B 341 GLY ALA GLU ILE TYR ASN LYS ASP GLY ASN LYS VAL ASP
SEQRES 2 B 341 LEU TYR GLY LYS ALA VAL GLY LEU HIS TYR PHE SER LYS
SEQRES 3 B 341 GLY ASN GLY GLU ASN SER TYR GLY GLY ASN GLY ASP MET
SEQRES 4 B 341 THR TYR ALA ARG LEU GLY PHE LYS GLY GLU THR GLN ILE
SEQRES 5 B 341 ASN SER ASP LEU THR GLY TYR GLY GLN TRP GLU TYR ASN
SEQRES 6 B 341 PHE GLN GLY ASN ASN SER GLU GLY ALA ASP ALA GLN THR
SEQRES 7 B 341 GLY ASN LYS THR ARG LEU ALA PHE ALA GLY LEU LYS TYR
SEQRES 8 B 341 ALA ASP VAL GLY SER PHE ASP TYR GLY ARG ASN TYR GLY
SEQRES 9 B 341 VAL VAL TYR ASP ALA LEU GLY TYR THR ASP MET LEU PRO
SEQRES 10 B 341 GLU PHE GLY GLY ASP THR ALA TYR SER ASP ASP PHE PHE
SEQRES 11 B 341 VAL GLY ARG VAL GLY GLY VAL ALA THR TYR ARG ASN SER
SEQRES 12 B 341 ASN PHE PHE GLY LEU VAL ASP GLY LEU ASN PHE ALA VAL
SEQRES 13 B 341 GLN TYR LEU GLY LYS ASN GLU ARG ASP THR ALA ARG ARG
SEQRES 14 B 341 SER ASN GLY ASP GLY VAL GLY GLY SER ILE SER TYR GLU
SEQRES 15 B 341 TYR GLU GLY PHE GLY ILE VAL GLY ALA TYR GLY ALA ALA
SEQRES 16 B 341 ASP ARG THR ASN LEU GLN GLU ALA GLN PRO LEU GLY ASN
SEQRES 17 B 341 GLY LYS LYS ALA GLU GLN TRP ALA THR GLY LEU LYS TYR
SEQRES 18 B 341 ASP ALA ASN ASN ILE TYR LEU ALA ALA ASN TYR GLY GLU
SEQRES 19 B 341 THR ARG ASN ALA THR PRO ILE THR ASN LYS PHE THR ASN
SEQRES 20 B 341 THR SER GLY PHE ALA ASN LYS THR GLN ASP VAL LEU LEU
SEQRES 21 B 341 VAL ALA GLN TYR GLN PHE ASP PHE GLY LEU ARG PRO SER
SEQRES 22 B 341 ILE ALA TYR THR LYS SER LYS ALA LYS ASP VAL GLU GLY
SEQRES 23 B 341 ILE GLY ASP VAL ASP LEU VAL ASN TYR PHE GLU VAL GLY
SEQRES 24 B 341 ALA THR TYR TYR PHE ASN LYS ASN MET SER THR TYR VAL
SEQRES 25 B 341 ASP TYR ILE ILE ASN GLN ILE ASP SER ASP ASN LYS LEU
SEQRES 26 B 341 GLY VAL GLY SER ASP ASP THR VAL ALA VAL GLY ILE VAL
SEQRES 27 B 341 TYR GLN PHE
HET BR A 401 1
HET BR A 402 1
HET BR A 403 1
HET BR A 404 1
HET BR A 405 1
HET BR A 406 1
HET MG A 407 1
HET BR B 401 1
HET BR B 402 1
HET BR B 403 1
HET BR B 404 1
HET BR B 405 1
HET BR B 406 1
HETNAM BR BROMIDE ION
HETNAM MG MAGNESIUM ION
FORMUL 3 BR 12(BR 1-)
FORMUL 9 MG MG 2+
FORMUL 16 HOH *325(H2 O)
HELIX 1 1 VAL A 105 GLY A 110 1 6
HELIX 2 2 SER A 142 LEU A 147 1 6
HELIX 3 3 THR A 197 ALA A 202 1 6
HELIX 4 4 VAL B 105 GLY B 110 1 6
HELIX 5 5 SER B 142 LEU B 147 1 6
HELIX 6 6 THR B 197 ALA B 202 1 6
SHEET 1 A18 GLY A 36 ASP A 37 0
SHEET 2 A18 ASN A 9 PHE A 23 -1 N TYR A 22 O GLY A 36
SHEET 3 A18 THR A 331 PHE A 340 -1 O VAL A 332 N PHE A 23
SHEET 4 A18 MET A 307 ASN A 316 -1 N SER A 308 O VAL A 337
SHEET 5 A18 GLY A 287 TYR A 302 -1 N PHE A 295 O ILE A 315
SHEET 6 A18 LEU A 269 VAL A 283 -1 N SER A 272 O GLY A 298
SHEET 7 A18 LYS A 253 TYR A 263 -1 N LEU A 259 O TYR A 275
SHEET 8 A18 ILE A 225 ARG A 235 -1 N GLY A 232 O ASP A 256
SHEET 9 A18 LYS A 210 ALA A 222 -1 N TYR A 220 O LEU A 227
SHEET 10 A18 PHE A 185 ASP A 195 -1 N VAL A 188 O GLY A 217
SHEET 11 A18 GLY A 173 TYR A 182 -1 N GLY A 176 O TYR A 191
SHEET 12 A18 LEU A 151 LEU A 158 -1 N LEU A 158 O GLY A 173
SHEET 13 A18 ARG A 132 ASN A 141 -1 N ASN A 141 O PHE A 153
SHEET 14 A18 GLY A 94 TYR A 102 -1 N ASP A 97 O THR A 138
SHEET 15 A18 LYS A 80 TYR A 90 -1 N LEU A 88 O PHE A 96
SHEET 16 A18 LEU A 55 GLN A 66 -1 N THR A 56 O LYS A 89
SHEET 17 A18 TYR A 40 ASN A 52 -1 N THR A 49 O GLY A 57
SHEET 18 A18 ASN A 9 PHE A 23 -1 N LYS A 10 O GLU A 48
SHEET 1 B 2 PRO A 239 ASN A 242 0
SHEET 2 B 2 THR A 247 PHE A 250 -1 O THR A 247 N ASN A 242
SHEET 1 C18 GLY B 36 ASP B 37 0
SHEET 2 C18 ASN B 9 PHE B 23 -1 N TYR B 22 O GLY B 36
SHEET 3 C18 THR B 331 PHE B 340 -1 O VAL B 332 N PHE B 23
SHEET 4 C18 MET B 307 ASN B 316 -1 N ILE B 314 O THR B 331
SHEET 5 C18 GLY B 287 TYR B 302 -1 N PHE B 295 O ILE B 315
SHEET 6 C18 LEU B 269 VAL B 283 -1 N SER B 272 O GLY B 298
SHEET 7 C18 LYS B 253 TYR B 263 -1 N LEU B 259 O TYR B 275
SHEET 8 C18 ILE B 225 ARG B 235 -1 N TYR B 226 O GLN B 262
SHEET 9 C18 LYS B 210 ALA B 222 -1 N TYR B 220 O LEU B 227
SHEET 10 C18 PHE B 185 ASP B 195 -1 N VAL B 188 O GLY B 217
SHEET 11 C18 GLY B 173 TYR B 182 -1 N GLY B 176 O TYR B 191
SHEET 12 C18 LEU B 151 LEU B 158 -1 N LEU B 158 O GLY B 173
SHEET 13 C18 ARG B 132 ASN B 141 -1 N ASN B 141 O PHE B 153
SHEET 14 C18 GLY B 94 TYR B 102 -1 N ASP B 97 O THR B 138
SHEET 15 C18 LYS B 80 TYR B 90 -1 N LEU B 88 O PHE B 96
SHEET 16 C18 LEU B 55 GLN B 66 -1 N THR B 56 O LYS B 89
SHEET 17 C18 TYR B 40 ASN B 52 -1 N THR B 49 O GLY B 57
SHEET 18 C18 ASN B 9 PHE B 23 -1 N ASP B 12 O LYS B 46
SHEET 1 D 2 PRO B 239 ASN B 242 0
SHEET 2 D 2 THR B 247 PHE B 250 -1 O THR B 247 N ASN B 242
LINK OH TYR A 63 MG MG A 407 1555 1555 2.72
LINK MG MG A 407 O HOH A 543 1555 1555 2.61
SITE 1 AC1 2 ALA A 123 HOH A 659
SITE 1 AC2 6 ASN A 69 ARG A 100 ASP A 126 GLY A 134
SITE 2 AC2 6 ARG A 163 HOH A 572
SITE 1 AC3 2 ALA A 261 ILE A 273
SITE 1 AC4 2 ARG A 167 HOH A 553
SITE 1 AC5 3 ASN A 69 SER A 70 ALA A 75
SITE 1 AC6 6 LYS A 89 ARG A 140 ASN A 141 SER A 142
SITE 2 AC6 6 HOH A 607 HOH A 610
SITE 1 AC7 3 TYR A 63 GLN A 76 HOH A 543
SITE 1 AC8 2 GLN B 262 ARG B 270
SITE 1 AC9 2 SER B 125 BR B 404
SITE 1 BC1 5 ASN B 69 GLU B 71 THR B 81 BR B 405
SITE 2 BC1 5 HOH B 638
SITE 1 BC2 5 SER B 125 ARG B 167 ARG B 168 BR B 402
SITE 2 BC2 5 HOH B 610
SITE 1 BC3 5 GLN B 66 GLY B 67 ASN B 68 ASN B 69
SITE 2 BC3 5 BR B 403
SITE 1 BC4 2 ASP B 113 HOH B 566
CRYST1 116.981 116.981 51.411 90.00 90.00 120.00 P 3 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 0.008548 0.004935 0.000000 0.00000
SCALE2 0.000000 0.009871 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019451 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
