HEADER PERIPLASMIC BINDING PROTEIN 10-APR-89 2LBP
TITLE STRUCTURE OF THE L-LEUCINE-BINDING PROTEIN REFINED AT 2.4
TITLE 2 ANGSTROMS RESOLUTION AND COMPARISON WITH THE LEU(SLASH)
TITLE 3 ILE(SLASH)VAL-BINDING PROTEIN STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LEUCINE-BINDING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM_STRAIN: K12
KEYWDS PERIPLASMIC BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.S.SACK,S.D.TRAKHANOV,I.H.TSIGANNIK,F.A.QUIOCHO
REVDAT 3 24-FEB-09 2LBP 1 VERSN
REVDAT 2 01-APR-03 2LBP 1 JRNL
REVDAT 1 12-JUL-89 2LBP 0
JRNL AUTH J.S.SACK,S.D.TRAKHANOV,I.H.TSIGANNIK,F.A.QUIOCHO
JRNL TITL STRUCTURE OF THE L-LEUCINE-BINDING PROTEIN REFINED
JRNL TITL 2 AT 2.4 A RESOLUTION AND COMPARISON WITH THE
JRNL TITL 3 LEU/ILE/VAL-BINDING PROTEIN STRUCTURE.
JRNL REF J.MOL.BIOL. V. 206 193 1989
JRNL REFN ISSN 0022-2836
JRNL PMID 2649683
JRNL DOI 10.1016/0022-2836(89)90532-9
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.S.SACK,M.A.SAPER,F.A.QUIOCHO
REMARK 1 TITL PERIPLASMIC BINDING PROTEIN STRUCTURE AND
REMARK 1 TITL 2 FUNCTION. REFINED X-RAY STRUCTURES OF THE
REMARK 1 TITL 3 LEUCINE(SLASH)ISOLEUCINE(SLASH)VALINE-BINDING
REMARK 1 TITL 4 PROTEIN AND ITS COMPLEX WITH LEUCINE
REMARK 1 REF J.MOL.BIOL. V. 206 171 1989
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROLSQ
REMARK 3 AUTHORS : KONNERT,HENDRICKSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 13797
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.213
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2600
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 91
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.019 ; 0.020
REMARK 3 ANGLE DISTANCE (A) : 0.045 ; 0.030
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.067 ; 0.050
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.014 ; 0.020
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.235 ; 0.150
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.230 ; 0.500
REMARK 3 MULTIPLE TORSION (A) : 0.326 ; 0.500
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : 0.289 ; 0.500
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : 9.200 ; 3.000
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 0.662 ; 1.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.152 ; 1.500
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.203 ; 1.500
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 1.896 ; 2.000
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2LBP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 34.40000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 37.14000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.67000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 37.14000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.40000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.67000
REMARK 290 SMTRY3 4 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: 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 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 OD1 ASP A 32 OH TYR A 281 1.82
REMARK 500 OE2 GLU A 27 OE2 GLU A 48 2.00
REMARK 500 O SER A 286 O ALA A 290 2.08
REMARK 500 O THR A 289 N LEU A 291 2.09
REMARK 500 O ALA A 103 NH2 ARG A 116 2.17
REMARK 500 O HOH A 547 O HOH A 549 2.19
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 GLY A 13 N GLY A 13 CA 0.112
REMARK 500 GLU A 22 CB GLU A 22 CG -0.144
REMARK 500 GLU A 27 CG GLU A 27 CD -0.107
REMARK 500 GLU A 90 CD GLU A 90 OE1 -0.066
REMARK 500 GLU A 292 CD GLU A 292 OE1 -0.068
REMARK 500 GLY A 310 N GLY A 310 CA 0.098
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 2 CB - CG - OD2 ANGL. DEV. = -6.9 DEGREES
REMARK 500 VAL A 5 CB - CA - C ANGL. DEV. = -16.9 DEGREES
REMARK 500 VAL A 5 C - N - CA ANGL. DEV. = 17.4 DEGREES
REMARK 500 MET A 11 CA - CB - CG ANGL. DEV. = 11.2 DEGREES
REMARK 500 SER A 12 CA - C - N ANGL. DEV. = 17.2 DEGREES
REMARK 500 SER A 12 O - C - N ANGL. DEV. = -10.3 DEGREES
REMARK 500 GLU A 22 CA - CB - CG ANGL. DEV. = 36.6 DEGREES
REMARK 500 GLU A 22 CB - CG - CD ANGL. DEV. = 46.3 DEGREES
REMARK 500 ASN A 24 N - CA - CB ANGL. DEV. = -15.0 DEGREES
REMARK 500 GLU A 27 CB - CG - CD ANGL. DEV. = 40.7 DEGREES
REMARK 500 GLU A 27 OE1 - CD - OE2 ANGL. DEV. = -10.7 DEGREES
REMARK 500 GLU A 27 CG - CD - OE1 ANGL. DEV. = 20.6 DEGREES
REMARK 500 ASN A 34 CB - CA - C ANGL. DEV. = 25.7 DEGREES
REMARK 500 ASN A 34 CA - CB - CG ANGL. DEV. = 16.8 DEGREES
REMARK 500 VAL A 47 CB - CA - C ANGL. DEV. = 23.2 DEGREES
REMARK 500 VAL A 47 CA - CB - CG1 ANGL. DEV. = 9.7 DEGREES
REMARK 500 GLU A 48 CG - CD - OE1 ANGL. DEV. = 14.7 DEGREES
REMARK 500 ASP A 50 CB - CG - OD2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ASP A 51 CB - CG - OD1 ANGL. DEV. = 8.4 DEGREES
REMARK 500 ASP A 51 CB - CG - OD2 ANGL. DEV. = -12.0 DEGREES
REMARK 500 HIS A 76 C - N - CA ANGL. DEV. = 29.1 DEGREES
REMARK 500 GLU A 90 CG - CD - OE2 ANGL. DEV. = -12.8 DEGREES
REMARK 500 ASP A 91 N - CA - CB ANGL. DEV. = -11.9 DEGREES
REMARK 500 ASP A 91 C - N - CA ANGL. DEV. = 18.1 DEGREES
REMARK 500 GLN A 108 CA - CB - CG ANGL. DEV. = 17.3 DEGREES
REMARK 500 ARG A 109 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG A 116 CA - CB - CG ANGL. DEV. = 13.2 DEGREES
REMARK 500 ARG A 116 CD - NE - CZ ANGL. DEV. = 18.1 DEGREES
REMARK 500 ARG A 116 NE - CZ - NH1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP A 146 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 ARG A 156 NE - CZ - NH1 ANGL. DEV. = 7.1 DEGREES
REMARK 500 ARG A 156 NE - CZ - NH2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 LYS A 163 N - CA - CB ANGL. DEV. = 10.9 DEGREES
REMARK 500 ASP A 173 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP A 173 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 THR A 176 CA - CB - CG2 ANGL. DEV. = 8.4 DEGREES
REMARK 500 ALA A 177 CB - CA - C ANGL. DEV. = 9.4 DEGREES
REMARK 500 ARG A 188 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ARG A 188 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 ARG A 211 CD - NE - CZ ANGL. DEV. = -9.7 DEGREES
REMARK 500 ARG A 211 NE - CZ - NH1 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG A 214 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 MET A 223 N - CA - CB ANGL. DEV. = 14.9 DEGREES
REMARK 500 GLU A 226 CA - CB - CG ANGL. DEV. = 16.6 DEGREES
REMARK 500 ASN A 235 CA - CB - CG ANGL. DEV. = 19.6 DEGREES
REMARK 500 ASP A 239 CB - CG - OD2 ANGL. DEV. = -8.7 DEGREES
REMARK 500 VAL A 246 CB - CA - C ANGL. DEV. = -12.7 DEGREES
REMARK 500 VAL A 246 CA - CB - CG2 ANGL. DEV. = 11.6 DEGREES
REMARK 500 TYR A 252 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 LEU A 287 CA - C - O ANGL. DEV. = 14.0 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 66 ANGLE DEVIATIONS.
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 SER A 12 -32.02 -146.04
REMARK 500 ALA A 52 3.18 55.20
REMARK 500 VAL A 66 -72.38 -61.74
REMARK 500 ASN A 67 26.76 -64.73
REMARK 500 HIS A 76 133.81 -16.47
REMARK 500 TYR A 150 -82.90 -50.17
REMARK 500 ALA A 164 94.70 -63.20
REMARK 500 ALA A 165 6.48 138.63
REMARK 500 GLN A 285 2.99 -69.78
REMARK 500 THR A 289 -111.35 107.40
REMARK 500 LEU A 291 -55.90 86.81
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 GLY A 75 HIS A 76 -86.81
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 A 140 0.10 SIDE_CHAIN
REMARK 500 ARG A 214 0.09 SIDE_CHAIN
REMARK 500 ARG A 293 0.12 SIDE_CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 GLY A 75 -14.95
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 501 DISTANCE = 5.62 ANGSTROMS
REMARK 525 HOH A 509 DISTANCE = 5.64 ANGSTROMS
REMARK 525 HOH A 514 DISTANCE = 5.05 ANGSTROMS
REMARK 525 HOH A 517 DISTANCE = 5.00 ANGSTROMS
REMARK 525 HOH A 522 DISTANCE = 6.79 ANGSTROMS
REMARK 525 HOH A 523 DISTANCE = 5.17 ANGSTROMS
REMARK 525 HOH A 527 DISTANCE = 5.41 ANGSTROMS
REMARK 525 HOH A 537 DISTANCE = 8.16 ANGSTROMS
REMARK 525 HOH A 540 DISTANCE = 5.77 ANGSTROMS
REMARK 525 HOH A 541 DISTANCE = 7.88 ANGSTROMS
REMARK 525 HOH A 555 DISTANCE = 5.98 ANGSTROMS
REMARK 525 HOH A 568 DISTANCE = 9.55 ANGSTROMS
REMARK 525 HOH A 572 DISTANCE = 6.72 ANGSTROMS
REMARK 525 HOH A 573 DISTANCE = 5.07 ANGSTROMS
REMARK 525 HOH A 576 DISTANCE = 5.11 ANGSTROMS
REMARK 525 HOH A 578 DISTANCE = 5.17 ANGSTROMS
REMARK 525 HOH A 579 DISTANCE = 5.07 ANGSTROMS
REMARK 525 HOH A 581 DISTANCE = 6.23 ANGSTROMS
REMARK 525 HOH A 582 DISTANCE = 5.68 ANGSTROMS
REMARK 525 HOH A 583 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH A 585 DISTANCE = 7.37 ANGSTROMS
REMARK 525 HOH A 586 DISTANCE = 6.20 ANGSTROMS
DBREF 2LBP A 1 346 UNP P04816 LIVK_ECOLI 24 369
SEQADV 2LBP LYS A 344 UNP P04816 ALA 367 CONFLICT
SEQRES 1 A 346 ASP ASP ILE LYS VAL ALA VAL VAL GLY ALA MET SER GLY
SEQRES 2 A 346 PRO ILE ALA GLN TRP GLY ILE MET GLU PHE ASN GLY ALA
SEQRES 3 A 346 GLU GLN ALA ILE LYS ASP ILE ASN ALA LYS GLY GLY ILE
SEQRES 4 A 346 LYS GLY ASP LYS LEU VAL GLY VAL GLU TYR ASP ASP ALA
SEQRES 5 A 346 CYS ASP PRO LYS GLN ALA VAL ALA VAL ALA ASN LYS ILE
SEQRES 6 A 346 VAL ASN ASP GLY ILE LYS TYR VAL ILE GLY HIS LEU CYS
SEQRES 7 A 346 SER SER SER THR GLN PRO ALA SER ASP ILE TYR GLU ASP
SEQRES 8 A 346 GLU GLY ILE LEU MET ILE SER PRO GLY ALA THR ALA PRO
SEQRES 9 A 346 GLU LEU THR GLN ARG GLY TYR GLN HIS ILE MET ARG THR
SEQRES 10 A 346 ALA GLY LEU ASP SER SER GLN GLY PRO THR ALA ALA LYS
SEQRES 11 A 346 TYR ILE LEU GLU THR VAL LYS PRO GLN ARG ILE ALA ILE
SEQRES 12 A 346 ILE HIS ASP LYS GLN GLN TYR GLY GLU GLY LEU ALA ARG
SEQRES 13 A 346 SER VAL GLN ASP GLY LEU LYS ALA ALA ASN ALA ASN VAL
SEQRES 14 A 346 VAL PHE PHE ASP GLY ILE THR ALA GLY GLU LYS ASP PHE
SEQRES 15 A 346 SER ALA LEU ILE ALA ARG LEU LYS LYS GLU ASN ILE ASP
SEQRES 16 A 346 PHE VAL TYR TYR GLY GLY TYR TYR PRO GLU MET GLY GLN
SEQRES 17 A 346 MET LEU ARG GLN ALA ARG SER VAL GLY LEU LYS THR GLN
SEQRES 18 A 346 PHE MET GLY PRO GLU GLY VAL GLY ASN ALA SER LEU SER
SEQRES 19 A 346 ASN ILE ALA GLY ASP ALA ALA GLU GLY MET LEU VAL THR
SEQRES 20 A 346 MET PRO LYS ARG TYR ASP GLN ASP PRO ALA ASN GLN GLY
SEQRES 21 A 346 ILE VAL ASP ALA LEU LYS ALA ASP LYS LYS ASP PRO SER
SEQRES 22 A 346 GLY PRO TYR VAL TRP ILE THR TYR ALA ALA VAL GLN SER
SEQRES 23 A 346 LEU ALA THR ALA LEU GLU ARG THR GLY SER ASP GLU PRO
SEQRES 24 A 346 LEU ALA LEU VAL LYS ASP LEU LYS ALA ASN GLY ALA ASN
SEQRES 25 A 346 THR VAL ILE GLY PRO LEU ASN TRP ASP GLU LYS GLY ASP
SEQRES 26 A 346 LEU LYS GLY PHE ASP PHE GLY VAL PHE GLN TRP HIS ALA
SEQRES 27 A 346 ASP GLY SER SER THR LYS ALA LYS
FORMUL 2 HOH *91(H2 O)
HELIX 1 A TRP A 18 GLY A 37 1 20
HELIX 2 B ASP A 54 GLY A 69 1 16
HELIX 3 C ALA A 85 GLY A 93 1 9
HELIX 4 D GLN A 124 THR A 135 1 12
HELIX 5 E GLN A 148 ALA A 164 1 17
HELIX 6 F PHE A 182 LYS A 191 1 10
HELIX 7 G TYR A 202 VAL A 216 1 15
HELIX 8 H ASN A 258 ALA A 267 1 10
HELIX 9 I PRO A 275 ARG A 293 1 19
HELIX 10 J GLU A 298 ASN A 309 1 12
SHEET 1 I 7 LYS A 43 ASP A 51 0
SHEET 2 I 7 ILE A 3 GLY A 9 1 N ILE A 3 O LYS A 43
SHEET 3 I 7 LYS A 71 GLY A 75 1 O TYR A 72 N ALA A 6
SHEET 4 I 7 LEU A 95 SER A 98 1 N LEU A 95 O LYS A 71
SHEET 5 I 7 HIS A 113 THR A 117 1 O HIS A 113 N MET A 96
SHEET 6 I 7 GLY A 324 LYS A 327 1 O GLY A 324 N ARG A 116
SHEET 7 I 7 ASN A 319 ASP A 321 -1 O ASN A 319 N LYS A 327
SHEET 1 II 7 ASN A 168 ILE A 175 0
SHEET 2 II 7 ARG A 140 ASP A 146 1 N ILE A 141 O ASN A 168
SHEET 3 II 7 ASP A 195 GLY A 200 1 N PHE A 196 O ARG A 140
SHEET 4 II 7 GLN A 221 GLU A 226 1 N GLN A 221 O ASP A 195
SHEET 5 II 7 GLY A 243 THR A 247 1 N LEU A 245 O PHE A 222
SHEET 6 II 7 GLY A 332 HIS A 337 -1 N TRP A 336 O MET A 244
SHEET 7 II 7 SER A 341 ALA A 345 1 O SER A 341 N HIS A 337
SSBOND 1 CYS A 53 CYS A 78 1555 1555 2.02
CRYST1 68.800 69.340 74.280 90.00 90.00 90.00 P 21 21 21 4
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 0.014535 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014422 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013463 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
