HEADER CHEMOTAXIS 09-MAR-93 1WAS
TITLE THE THREE-DIMENSIONAL STRUCTURE OF THE LIGAND-BINDING DOMAIN OF A
TITLE 2 WILD-TYPE BACTERIAL CHEMOTAXIS RECEPTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BACTERIAL ASPARTATE RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM;
SOURCE 3 ORGANISM_TAXID: 602;
SOURCE 4 EXPRESSION_SYSTEM_VECTOR_TYPE: BACTERIAL
KEYWDS CHEMOTAXIS
EXPDTA X-RAY DIFFRACTION
AUTHOR S.-H.KIM
REVDAT 5 14-FEB-24 1WAS 1 REMARK
REVDAT 4 24-FEB-09 1WAS 1 VERSN
REVDAT 3 01-APR-03 1WAS 1 JRNL
REVDAT 2 15-JAN-95 1WAS 1 COMPND
REVDAT 1 20-DEC-94 1WAS 0
JRNL AUTH J.I.YEH,H.P.BIEMANN,J.PANDIT,D.E.KOSHLAND,S.H.KIM
JRNL TITL THE THREE-DIMENSIONAL STRUCTURE OF THE LIGAND-BINDING DOMAIN
JRNL TITL 2 OF A WILD-TYPE BACTERIAL CHEMOTAXIS RECEPTOR. STRUCTURAL
JRNL TITL 3 COMPARISON TO THE CROSS-LINKED MUTANT FORMS AND
JRNL TITL 4 CONFORMATIONAL CHANGES UPON LIGAND BINDING.
JRNL REF J.BIOL.CHEM. V. 268 9787 1993
JRNL REFN ISSN 0021-9258
JRNL PMID 8486661
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.V.MILBURN,G.G.PRIVE,D.L.MILLIGAN,W.G.SCOTT,J.I.YEH,
REMARK 1 AUTH 2 J.JANCARIK,D.E.KOSHLAND JUNIOR,S.-H.KIM
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURES OF THE LIGAND-BINDING DOMAIN OF
REMARK 1 TITL 2 THE BACTERIAL ASPARTATE RECEPTOR WITH AND WITHOUT A LIGAND
REMARK 1 REF SCIENCE V. 254 1342 1991
REMARK 1 REFN ISSN 0036-8075
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 4005
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 SET) : 0.192
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 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1144
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) : 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 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.019
REMARK 3 BOND ANGLES (DEGREES) : 3.797
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE LOOP REGION (RESIDUES 77 - 83) IS
REMARK 3 DISORDERED.
REMARK 4
REMARK 4 1WAS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000177168.
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: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 3555 -Y,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X,Z+3/4
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y,Z
REMARK 290 7555 -Y+1/2,X,Z+3/4
REMARK 290 8555 Y,-X+1/2,Z+1/4
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 32.52500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 32.52500
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 36.18500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 32.52500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 18.09250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 32.52500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 54.27750
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 32.52500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 32.52500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 36.18500
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 32.52500
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 54.27750
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 32.52500
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 18.09250
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 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 MET A 35 SD CE
REMARK 480 ASN A 36 CG OD1 ND2
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 HIS A 103 NE2 HIS A 103 CD2 -0.068
REMARK 500 TYR A 127 CZ TYR A 127 CE2 -0.104
REMARK 500 PHE A 150 CB PHE A 150 CG 0.115
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 ASN A 36 CA - C - N ANGL. DEV. = -13.8 DEGREES
REMARK 500 PHE A 40 CA - CB - CG ANGL. DEV. = -16.6 DEGREES
REMARK 500 ARG A 47 CA - CB - CG ANGL. DEV. = 15.0 DEGREES
REMARK 500 ARG A 47 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 47 NE - CZ - NH2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 GLU A 52 OE1 - CD - OE2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 THR A 54 CA - C - N ANGL. DEV. = 15.6 DEGREES
REMARK 500 TRP A 57 CE2 - CD2 - CG ANGL. DEV. = -5.5 DEGREES
REMARK 500 ALA A 85 CA - C - N ANGL. DEV. = -14.5 DEGREES
REMARK 500 LYS A 86 N - CA - C ANGL. DEV. = 17.5 DEGREES
REMARK 500 THR A 87 CA - CB - CG2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 LEU A 90 CB - CG - CD1 ANGL. DEV. = -10.4 DEGREES
REMARK 500 TYR A 104 CG - CD2 - CE2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 TYR A 127 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 TYR A 130 CB - CG - CD2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 TYR A 130 CB - CG - CD1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 MET A 157 CG - SD - CE ANGL. DEV. = -11.8 DEGREES
REMARK 500 LEU A 161 CA - CB - CG ANGL. DEV. = 14.1 DEGREES
REMARK 500 TYR A 168 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG A 170 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 LEU A 175 CA - CB - CG ANGL. DEV. = 17.6 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 ASN A 36 54.49 75.14
REMARK 500 GLN A 37 -119.25 77.22
REMARK 500 GLN A 38 -69.75 16.88
REMARK 500 PHE A 40 -63.08 -165.12
REMARK 500 GLN A 50 11.24 -66.85
REMARK 500 SER A 51 -60.30 -93.58
REMARK 500 ASN A 66 -7.85 -58.16
REMARK 500 ARG A 73 31.41 -83.81
REMARK 500 MET A 76 65.41 -69.35
REMARK 500 ASP A 77 -57.12 -139.39
REMARK 500 ALA A 78 -18.63 53.98
REMARK 500 ASN A 80 85.64 -67.59
REMARK 500 SER A 84 -67.38 73.40
REMARK 500 ALA A 85 147.59 -22.22
REMARK 500 THR A 87 -36.08 -10.86
REMARK 500 ASP A 88 -59.32 -142.92
REMARK 500 ALA A 117 -71.44 -62.31
REMARK 500 ALA A 119 -63.28 -142.31
REMARK 500 ASN A 145 52.36 -61.34
REMARK 500 PHE A 150 46.10 -90.29
REMARK 500 GLN A 178 -25.31 -168.94
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 LEU A 113 PRO A 114 -114.20
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1WAS A 36 180 UNP P02941 MCP2_SALTY 36 180
SEQRES 1 A 146 MET ASN GLN GLN GLY PHE VAL ILE SER ASN GLU LEU ARG
SEQRES 2 A 146 GLN GLN GLN SER GLU LEU THR SER THR TRP ASP LEU MET
SEQRES 3 A 146 LEU GLN THR ARG ILE ASN LEU SER ARG SER ALA ALA ARG
SEQRES 4 A 146 MET MET MET ASP ALA SER ASN GLN GLN SER SER ALA LYS
SEQRES 5 A 146 THR ASP LEU LEU GLN ASN ALA LYS THR THR LEU ALA GLN
SEQRES 6 A 146 ALA ALA ALA HIS TYR ALA ASN PHE LYS ASN MET THR PRO
SEQRES 7 A 146 LEU PRO ALA MET ALA GLU ALA SER ALA ASN VAL ASP GLU
SEQRES 8 A 146 LYS TYR GLN ARG TYR GLN ALA ALA LEU ALA GLU LEU ILE
SEQRES 9 A 146 GLN PHE LEU ASP ASN GLY ASN MET ASP ALA TYR PHE ALA
SEQRES 10 A 146 GLN PRO THR GLN GLY MET GLN ASN ALA LEU GLY GLU ALA
SEQRES 11 A 146 LEU GLY ASN TYR ALA ARG VAL SER GLU ASN LEU TYR ARG
SEQRES 12 A 146 GLN THR PHE
HELIX 1 H1 MET A 35 MET A 75 1 41
HELIX 2 H2 LYS A 86 ASN A 109 1 24
HELIX 3 H3 MET A 116 GLY A 144 1 29
HELIX 4 H4 MET A 146 PHE A 180 1 35
CRYST1 65.050 65.050 72.370 90.00 90.00 90.00 I 41 8
ORIGX1 0.015373 0.000000 0.000000 0.00000
ORIGX2 0.000000 0.015373 0.000000 0.00000
ORIGX3 0.000000 0.000000 0.013818 0.00000
SCALE1 0.015373 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015373 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013818 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
