HEADER SIGNALLING PROTEIN 12-OCT-94 1NCF
TITLE A NEW PARADIGM FOR TUMOR NECROSIS FACTOR SIGNALLING
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TUMOR NECROSIS FACTOR RECEPTOR;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: TYPE I RECEPTOR, STNFR1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 OTHER_DETAILS: THE CONSTRUCT CONTAINS RESIDUES 12 - 172 OF
COMPND 8 THE MATURE RECEPTOR SEQUENCE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 OTHER_DETAILS: RESIDUE 11 IS MUTATED TO MET AS A RESULT OF
SOURCE 8 THE EXPRESSION SYSTEM
KEYWDS BINDING PROTEIN, CYTOKINE, SIGNALLING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.H.NAISMITH,S.R.SPRANG
REVDAT 2 24-FEB-09 1NCF 1 VERSN
REVDAT 1 07-DEC-95 1NCF 0
JRNL AUTH J.H.NAISMITH,T.Q.DEVINE,B.J.BRANDHUBER,S.R.SPRANG
JRNL TITL CRYSTALLOGRAPHIC EVIDENCE FOR DIMERIZATION OF
JRNL TITL 2 UNLIGANDED TUMOR NECROSIS FACTOR RECEPTOR.
JRNL REF J.BIOL.CHEM. V. 270 13303 1995
JRNL REFN ISSN 0021-9258
JRNL PMID 7768931
JRNL DOI 10.1074/JBC.270.22.13303
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH L.E.RODSETH,B.BRANDHUBER,T.Q.DEVINE,M.J.ECK,K.HALE,
REMARK 1 AUTH 2 J.H.NAISMITH,S.R.SPRANG
REMARK 1 TITL TWO CRYSTAL FORMS OF THE EXTRACELLULAR DOMAIN OF
REMARK 1 TITL 2 TYPE I TUMOR NECROSIS FACTOR RECEPTOR
REMARK 1 REF J.MOL.BIOL. V. 239 332 1994
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 2
REMARK 1 AUTH D.W.BANNER,A.ARCY,W.JANES,R.GENTZ,H.SCHOENFIELD,
REMARK 1 AUTH 2 C.BROGER,H.LOETSCHER,W.LESSLAUER
REMARK 1 TITL CRYSTAL STRUCTURE OF THE SOLUBLE HUMAN 55 KD TNF
REMARK 1 TITL 2 RECEPTOR-HUMAN TNFB COMPLEX: IMPLICATION FOR TNF
REMARK 1 TITL 3 RECEPTOR ACTIVATION
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 73 431 1993
REMARK 1 REFN ISSN 0092-8674
REMARK 2
REMARK 2 RESOLUTION. 2.25 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) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 3.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.0
REMARK 3 NUMBER OF REFLECTIONS : 19343
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) : 0.193
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
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 : 2162
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 260
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.58
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) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.60
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.02
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) : 1.500 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.000 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.000 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.500 ; 2.500
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: NULL
REMARK 4
REMARK 4 1NCF 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 : 24198
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
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 (%): 59.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 92.60000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 34.50000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 34.50000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 46.30000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 34.50000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 34.50000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 138.90000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 34.50000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 34.50000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 46.30000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 34.50000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 34.50000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 138.90000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 92.60000
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 300 REMARK:
REMARK 300 MTRIX
REMARK 300 THE TRANSFORMATIONS PRESENTED ON MTRIX RECORDS BELOW
REMARK 300 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG THE
REMARK 300 VARIOUS DOMAINS IN THIS ENTRY. APPLYING THE APPROPRIATE
REMARK 300 MTRIX TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL
REMARK 300 YIELD APPROXIMATE COORDINATES FOR THE RESIDUES LISTED
REMARK 300 SECOND.
REMARK 300
REMARK 300 APPLIED TO TRANSFORMED TO
REMARK 300 MTRIX CHAIN RESIDUES CHAIN RESIDUES RMSD
REMARK 300 M1 A 15 .. A 52 B 15 .. B 52 0.214
REMARK 300
REMARK 300 THE NCS TRANSFORMATION BETWEEN DOMAIN 1 OF THE TWO
REMARK 300 MONOMERS IN THE ASYMMETRIC UNIT.
REMARK 300
REMARK 300 M2 A 55 .. A 96 B 55 .. B 96 0.314
REMARK 300
REMARK 300 THE NCS TRANSFORMATION BETWEEN DOMAIN 2 OF THE TWO
REMARK 300 MONOMERS IN THE ASYMMETRIC UNIT.
REMARK 300
REMARK 300 M3 A 98 .. A 137 B 98 .. B 137 0.348
REMARK 300
REMARK 300 THE NCS TRANSFORMATION BETWEEN DOMAIN 3 OF THE TWO
REMARK 300 MONOMERS IN THE ASYMMETRIC UNIT.
REMARK 300
REMARK 300 M4 A 139 .. A 150 B 139 .. B 150 0.743
REMARK 300
REMARK 300 THE NCS TRANSFORMATION BETWEEN DOMAIN 4 OF THE TWO
REMARK 300 MONOMERS IN THE ASYMMETRIC UNIT.
REMARK 300
REMARK 300 S1 B 13 .. B 156 ? 13 .. ? 156
REMARK 300
REMARK 300 THIS GENERATES A MOLECULE WHICH MAY FORM AN ALTERNATIVE
REMARK 300 DIMER TO THE ONE DESCRIBED BY THE COORDINATES.
REMARK 300
REMARK 300 SYMMETRY1 1 -1.000000 0.000000 0.000000 34.50000
REMARK 300 SYMMETRY2 1 0.000000 1.000000 0.000000 -34.50000
REMARK 300 SYMMETRY3 1 0.000000 0.000000 -1.000000 46.30000
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: 2080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 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 VAL A 151
REMARK 465 SER A 152
REMARK 465 CYS A 153
REMARK 465 SER A 154
REMARK 465 ASN A 155
REMARK 465 CYS A 156
REMARK 465 LYS A 157
REMARK 465 LYS A 158
REMARK 465 SER A 159
REMARK 465 LEU A 160
REMARK 465 GLU A 161
REMARK 465 CYS A 162
REMARK 465 THR A 163
REMARK 465 LYS A 164
REMARK 465 LEU A 165
REMARK 465 CYS A 166
REMARK 465 LEU A 167
REMARK 465 PRO A 168
REMARK 465 GLN A 169
REMARK 465 ILE A 170
REMARK 465 GLU A 171
REMARK 465 ASN A 172
REMARK 465 MET B 11
REMARK 465 ASP B 12
REMARK 465 SER B 13
REMARK 465 CYS B 156
REMARK 465 LYS B 157
REMARK 465 LYS B 158
REMARK 465 SER B 159
REMARK 465 LEU B 160
REMARK 465 GLU B 161
REMARK 465 CYS B 162
REMARK 465 THR B 163
REMARK 465 LYS B 164
REMARK 465 LEU B 165
REMARK 465 CYS B 166
REMARK 465 LEU B 167
REMARK 465 PRO B 168
REMARK 465 GLN B 169
REMARK 465 ILE B 170
REMARK 465 GLU B 171
REMARK 465 ASN B 172
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 11 CG SD CE
REMARK 470 ARG A 146 CB CG CD NE CZ NH1 NH2
REMARK 470 GLU A 147 CB CG CD OE1 OE2
REMARK 470 ASN A 148 CB CG OD1 ND2
REMARK 470 ARG B 146 CB CG CD NE CZ NH1 NH2
REMARK 470 GLU B 147 CB CG CD OE1 OE2
REMARK 470 ASN B 148 CB CG OD1 ND2
REMARK 470 SER B 154 CB OG
REMARK 470 ASN B 155 CB CG OD1 ND2
REMARK 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 ALA A 141
REMARK 475 PHE A 143
REMARK 475 LEU A 145
REMARK 475 GLU A 147
REMARK 475 ASN A 148
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 LYS A 100 CD CE NZ
REMARK 480 GLU A 109 CD OE1 OE2
REMARK 480 LEU A 121 CG CD1 CD2
REMARK 480 ASN A 122 CG OD1 ND2
REMARK 480 GLU A 149 CD OE1 OE2
REMARK 480 LYS B 75 CD CE NZ
REMARK 480 LYS B 78 CD CE NZ
REMARK 480 LEU B 121 CG CD1 CD2
REMARK 480 ARG B 146 N CA
REMARK 480 ASN B 148 N CA
REMARK 480 CYS B 150 N CA
REMARK 480 VAL B 151 CB CG1 CG2
REMARK 480 ASN B 155 O
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 ASP A 12 134.77 -37.71
REMARK 500 HIS A 66 48.33 -145.85
REMARK 500 CYS A 120 78.91 -113.56
REMARK 500 GLU A 147 -120.26 72.42
REMARK 500 HIS B 66 39.86 -142.90
REMARK 500 VAL B 125 88.79 -67.34
REMARK 500 GLU B 147 -148.91 78.41
REMARK 500 SER B 154 -68.38 111.02
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999
REMARK 999 SOURCE 1
REMARK 999 THE CONSTRUCT CONTAINS RESIDUES 12 - 172 OF THE MATURE
REMARK 999 SEQUENCE OF THE ENTIRE RECEPTOR. RESIDUE 11 IS MUTATED
REMARK 999 TO MET AS A RESULT OF THE EXPRESSION SYSTEM.
DBREF 1NCF A 12 172 UNP P19438 TNR1A_HUMAN 41 201
DBREF 1NCF B 12 172 UNP P19438 TNR1A_HUMAN 41 201
SEQRES 1 A 162 MET ASP SER VAL CYS PRO GLN GLY LYS TYR ILE HIS PRO
SEQRES 2 A 162 GLN ASN ASN SER ILE CYS CYS THR LYS CYS HIS LYS GLY
SEQRES 3 A 162 THR TYR LEU TYR ASN ASP CYS PRO GLY PRO GLY GLN ASP
SEQRES 4 A 162 THR ASP CYS ARG GLU CYS GLU SER GLY SER PHE THR ALA
SEQRES 5 A 162 SER GLU ASN HIS LEU ARG HIS CYS LEU SER CYS SER LYS
SEQRES 6 A 162 CYS ARG LYS GLU MET GLY GLN VAL GLU ILE SER SER CYS
SEQRES 7 A 162 THR VAL ASP ARG ASP THR VAL CYS GLY CYS ARG LYS ASN
SEQRES 8 A 162 GLN TYR ARG HIS TYR TRP SER GLU ASN LEU PHE GLN CYS
SEQRES 9 A 162 PHE ASN CYS SER LEU CYS LEU ASN GLY THR VAL HIS LEU
SEQRES 10 A 162 SER CYS GLN GLU LYS GLN ASN THR VAL CYS THR CYS HIS
SEQRES 11 A 162 ALA GLY PHE PHE LEU ARG GLU ASN GLU CYS VAL SER CYS
SEQRES 12 A 162 SER ASN CYS LYS LYS SER LEU GLU CYS THR LYS LEU CYS
SEQRES 13 A 162 LEU PRO GLN ILE GLU ASN
SEQRES 1 B 162 MET ASP SER VAL CYS PRO GLN GLY LYS TYR ILE HIS PRO
SEQRES 2 B 162 GLN ASN ASN SER ILE CYS CYS THR LYS CYS HIS LYS GLY
SEQRES 3 B 162 THR TYR LEU TYR ASN ASP CYS PRO GLY PRO GLY GLN ASP
SEQRES 4 B 162 THR ASP CYS ARG GLU CYS GLU SER GLY SER PHE THR ALA
SEQRES 5 B 162 SER GLU ASN HIS LEU ARG HIS CYS LEU SER CYS SER LYS
SEQRES 6 B 162 CYS ARG LYS GLU MET GLY GLN VAL GLU ILE SER SER CYS
SEQRES 7 B 162 THR VAL ASP ARG ASP THR VAL CYS GLY CYS ARG LYS ASN
SEQRES 8 B 162 GLN TYR ARG HIS TYR TRP SER GLU ASN LEU PHE GLN CYS
SEQRES 9 B 162 PHE ASN CYS SER LEU CYS LEU ASN GLY THR VAL HIS LEU
SEQRES 10 B 162 SER CYS GLN GLU LYS GLN ASN THR VAL CYS THR CYS HIS
SEQRES 11 B 162 ALA GLY PHE PHE LEU ARG GLU ASN GLU CYS VAL SER CYS
SEQRES 12 B 162 SER ASN CYS LYS LYS SER LEU GLU CYS THR LYS LEU CYS
SEQRES 13 B 162 LEU PRO GLN ILE GLU ASN
FORMUL 3 HOH *260(H2 O)
HELIX 1 1 ARG A 77 GLY A 81 5 5
HELIX 2 2 ARG B 77 GLY B 81 5 5
SHEET 1 A 2 LYS A 19 HIS A 22 0
SHEET 2 A 2 ASN A 25 THR A 31 -1 N ASN A 25 O HIS A 22
SHEET 1 B 2 THR A 37 ASN A 41 0
SHEET 2 B 2 ASP A 51 GLU A 54 -1 N ASP A 51 O ASN A 41
SHEET 1 C 2 SER A 59 PHE A 60 0
SHEET 2 C 2 LEU A 71 SER A 72 -1 N LEU A 71 O PHE A 60
SHEET 1 D 2 VAL A 83 SER A 86 0
SHEET 2 D 2 VAL A 95 GLY A 97 -1 N VAL A 95 O SER A 86
SHEET 1 E 2 GLN A 102 TYR A 106 0
SHEET 2 E 2 PHE A 112 ASN A 116 -1 O GLN A 113 N HIS A 105
SHEET 1 F 2 GLY A 123 LEU A 127 0
SHEET 2 F 2 VAL A 136 CYS A 139 -1 O VAL A 136 N HIS A 126
SHEET 1 G 2 LYS B 19 ILE B 21 0
SHEET 2 G 2 CYS B 29 THR B 31 -1 N CYS B 30 O TYR B 20
SHEET 1 H 2 THR B 37 ASN B 41 0
SHEET 2 H 2 ASP B 51 GLU B 54 -1 N ASP B 51 O ASN B 41
SHEET 1 I 2 SER B 59 PHE B 60 0
SHEET 2 I 2 LEU B 71 SER B 72 -1 N LEU B 71 O PHE B 60
SHEET 1 J 2 VAL B 83 SER B 86 0
SHEET 2 J 2 VAL B 95 GLY B 97 -1 N VAL B 95 O SER B 86
SHEET 1 K 2 GLN B 102 TYR B 106 0
SHEET 2 K 2 PHE B 112 ASN B 116 -1 O GLN B 113 N HIS B 105
SHEET 1 L 2 VAL B 125 LEU B 127 0
SHEET 2 L 2 VAL B 136 CYS B 137 -1 N VAL B 136 O LEU B 127
SHEET 1 M 2 PHE B 143 ARG B 146 0
SHEET 2 M 2 GLU B 149 SER B 152 -1 O GLU B 149 N ARG B 146
SSBOND 1 CYS A 15 CYS A 29 1555 1555 2.02
SSBOND 2 CYS A 30 CYS A 43 1555 1555 2.03
SSBOND 3 CYS A 33 CYS A 52 1555 1555 2.03
SSBOND 4 CYS A 55 CYS A 70 1555 1555 2.04
SSBOND 5 CYS A 73 CYS A 88 1555 1555 2.00
SSBOND 6 CYS A 76 CYS A 96 1555 1555 2.03
SSBOND 7 CYS A 98 CYS A 114 1555 1555 2.02
SSBOND 8 CYS A 117 CYS A 129 1555 1555 2.03
SSBOND 9 CYS A 120 CYS A 137 1555 1555 2.03
SSBOND 10 CYS A 139 CYS A 150 1555 1555 2.04
SSBOND 11 CYS B 15 CYS B 29 1555 1555 2.03
SSBOND 12 CYS B 30 CYS B 43 1555 1555 2.03
SSBOND 13 CYS B 33 CYS B 52 1555 1555 2.01
SSBOND 14 CYS B 55 CYS B 70 1555 1555 2.03
SSBOND 15 CYS B 73 CYS B 88 1555 1555 2.03
SSBOND 16 CYS B 76 CYS B 96 1555 1555 2.01
SSBOND 17 CYS B 98 CYS B 114 1555 1555 2.02
SSBOND 18 CYS B 117 CYS B 129 1555 1555 2.02
SSBOND 19 CYS B 120 CYS B 137 1555 1555 2.02
SSBOND 20 CYS B 139 CYS B 150 1555 1555 2.03
CRYST1 69.000 69.000 185.200 90.00 90.00 90.00 P 41 21 2 16
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 0.014493 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014493 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005400 0.00000
MTRIX1 1 -0.745000 0.008000 0.667000 14.56700 1
MTRIX2 1 0.020000 -0.999000 0.035000 27.10700 1
MTRIX3 1 0.667000 0.040000 0.744000 -6.04300 1
MTRIX1 2 -0.746000 -0.029000 0.665000 14.68300 1
MTRIX2 2 0.045000 -0.999000 0.007000 27.24500 1
MTRIX3 2 0.664000 0.035000 0.747000 -5.93200 1
MTRIX1 3 -0.814000 -0.073000 0.576000 19.59000 1
MTRIX2 3 0.147000 -0.986000 0.083000 22.20100 1
MTRIX3 3 0.562000 0.153000 0.813000 -7.71900 1
MTRIX1 4 -0.862000 0.043000 0.505000 23.91900 1
MTRIX2 4 0.102000 -0.961000 0.255000 11.13100 1
MTRIX3 4 0.496000 0.272000 0.825000 -7.60600 1
(ATOM LINES ARE NOT SHOWN.)
END
