HEADER MEMBRANE PROTEIN 12-SEP-00 1FTL
TITLE CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J) IN COMPLEX
TITLE 2 WITH THE ANTAGONIST DNQX AT 1.8 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMATE RECEPTOR SUBUNIT 2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: LIGAND BINDING CORE (S1S2J);
COMPND 5 SYNONYM: GLUR-2;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 ORGAN: BRAIN;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET30B
KEYWDS GLUTAMATE RECEPTOR, S1S2, LIGAND BINDING CORE, ANTAGONIST, DNQX,
KEYWDS 2 MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR N.ARMSTRONG,E.GOUAUX
REVDAT 3 02-AUG-17 1FTL 1 SOURCE REMARK
REVDAT 2 24-FEB-09 1FTL 1 VERSN
REVDAT 1 01-NOV-00 1FTL 0
JRNL AUTH N.ARMSTRONG,E.GOUAUX
JRNL TITL MECHANISMS FOR ACTIVATION AND ANTAGONISM OF AN
JRNL TITL 2 AMPA-SENSITIVE GLUTAMATE RECEPTOR: CRYSTAL STRUCTURES OF THE
JRNL TITL 3 GLUR2 LIGAND BINDING CORE.
JRNL REF NEURON V. 28 165 2000
JRNL REFN ISSN 0896-6273
JRNL PMID 11086992
JRNL DOI 10.1016/S0896-6273(00)00094-5
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.Q.CHEN,Y.SUN,R.JIN,E.GOUAUX
REMARK 1 TITL PROBING THE LIGAND BINDING DOMAIN OF THE GLUR2 RECEPTOR BY
REMARK 1 TITL 2 PROTEOLYSIS AND DELETION MUTATGENESIS DEFINES DOMAIN
REMARK 1 TITL 3 BOUNDARIES AND YIELDS A CRYSTALLIZABLE CONSTRUCT
REMARK 1 REF PROTEIN SCI. V. 7 2623 1998
REMARK 1 REFN ISSN 0961-8368
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
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 : 50699
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.219
REMARK 3 FREE R VALUE : 0.272
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 5149
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 : 3847
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 41
REMARK 3 SOLVENT ATOMS : 363
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.96
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) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.421
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: NULL
REMARK 4
REMARK 4 1FTL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-OCT-00.
REMARK 100 THE DEPOSITION ID IS D_1000011889.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-OCT-99
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50796
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 200 DATA REDUNDANCY : 5.880
REMARK 200 R MERGE (I) : 0.05300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 40.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : 0.08400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 19% PEG 4000 0.3 M AMMONIUM SULFATE
REMARK 280 0.1 M SODIUM ACETATE, PH 5.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
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 31.07650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 48.68450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.85150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 48.68450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.07650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.85150
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: DIMERIC
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 GLY A 1
REMARK 465 ALA A 2
REMARK 465 ASN A 3
REMARK 465 LYS A 4
REMARK 465 GLY A 262
REMARK 465 SER A 263
REMARK 465 GLY B 1
REMARK 465 ALA B 2
REMARK 465 ASN B 3
REMARK 465 LYS B 4
REMARK 465 GLY B 262
REMARK 465 SER B 263
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 LYS A 21 CB CG CD CE NZ
REMARK 470 MET A 25 CG SD CE
REMARK 470 GLU A 27 CB CG CD OE1 OE2
REMARK 470 GLU A 30 CG CD OE1 OE2
REMARK 470 LYS A 52 CB CG CD CE NZ
REMARK 470 ASP A 65 CG OD1 OD2
REMARK 470 THR A 68 CB OG1 CG2
REMARK 470 LYS A 69 CB CG CD CE NZ
REMARK 470 GLU A 122 CG CD OE1 OE2
REMARK 470 LYS A 129 CG CD CE NZ
REMARK 470 GLU A 132 CG CD OE1 OE2
REMARK 470 SER A 140 CB OG
REMARK 470 GLU A 145 CG CD OE1 OE2
REMARK 470 ARG A 149 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 151 CG CD CE NZ
REMARK 470 ARG A 163 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 172 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 204 CB CG CD CE NZ
REMARK 470 LYS A 226 CG CD CE NZ
REMARK 470 LEU A 246 CG CD1 CD2
REMARK 470 CYS A 261 O
REMARK 470 LYS B 21 CG CD CE NZ
REMARK 470 GLU B 30 CG CD OE1 OE2
REMARK 470 LYS B 50 CG CD CE NZ
REMARK 470 LYS B 52 CG CD CE NZ
REMARK 470 ASP B 65 CG OD1 OD2
REMARK 470 ASP B 67 CB CG OD1 OD2
REMARK 470 THR B 68 CB OG1 CG2
REMARK 470 LYS B 69 CB CG CD CE NZ
REMARK 470 LYS B 82 CG CD CE NZ
REMARK 470 GLU B 125 CG CD OE1 OE2
REMARK 470 GLU B 132 CG CD OE1 OE2
REMARK 470 SER B 140 CB OG
REMARK 470 SER B 142 OG
REMARK 470 ARG B 148 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 149 CB CG CD NE CZ NH1 NH2
REMARK 470 LYS B 151 CB CG CD CE NZ
REMARK 470 ARG B 172 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 185 CG CD CE NZ
REMARK 470 LYS B 204 CG CD CE NZ
REMARK 470 SER B 229 CB OG
REMARK 470 ASN B 232 CB CG OD1 ND2
REMARK 470 CYS B 261 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 LYS A 69 -1.53 76.43
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 366
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DNQ B 364
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DNQ A 365
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1GR2 RELATED DB: PDB
REMARK 900 GLUR2 S1S2I IN COMPLEX WITH THE PARTIAL AGONIST KAINATE
REMARK 900 RELATED ID: 1FTJ RELATED DB: PDB
REMARK 900 GLUR2 S1S2J IN COMPLEX WITH FULL AGONIST GLUTAMATE
REMARK 900 RELATED ID: 1FTK RELATED DB: PDB
REMARK 900 GLUR2 S1S2J IN COMPLEX WITH THE PARTIAL AGONIST KAINATE
REMARK 900 RELATED ID: 1FTM RELATED DB: PDB
REMARK 900 GLUR2 LIGAND BINDING CORE (S1S2J) IN COMPLEX WITH AMPA
REMARK 900 RELATED ID: 1FTO RELATED DB: PDB
REMARK 900 GLUR2 LIGAND BINDING CORE (S1S2J) IN THE APO STATE
REMARK 900 RELATED ID: 1FW0 RELATED DB: PDB
REMARK 900 GLUR2 LIGAND BINDING CORE (S1S2J) IN COMPLEX WITH KAINATE
DBREF 1FTL A 3 117 UNP P19491 GRIA2_RAT 413 527
DBREF 1FTL A 120 263 UNP P19491 GRIA2_RAT 653 796
DBREF 1FTL B 3 117 UNP P19491 GRIA2_RAT 413 527
DBREF 1FTL B 120 263 UNP P19491 GRIA2_RAT 653 796
SEQADV 1FTL GLY A 1 UNP P19491 CLONING ARTIFACT
SEQADV 1FTL ALA A 2 UNP P19491 CLONING ARTIFACT
SEQADV 1FTL GLY B 1 UNP P19491 CLONING ARTIFACT
SEQADV 1FTL ALA B 2 UNP P19491 CLONING ARTIFACT
SEQADV 1FTL GLY A 118 UNP P19491 LINKER
SEQADV 1FTL THR A 119 UNP P19491 LINKER
SEQADV 1FTL GLY B 118 UNP P19491 LINKER
SEQADV 1FTL THR B 119 UNP P19491 LINKER
SEQRES 1 A 263 GLY ALA ASN LYS THR VAL VAL VAL THR THR ILE LEU GLU
SEQRES 2 A 263 SER PRO TYR VAL MET MET LYS LYS ASN HIS GLU MET LEU
SEQRES 3 A 263 GLU GLY ASN GLU ARG TYR GLU GLY TYR CYS VAL ASP LEU
SEQRES 4 A 263 ALA ALA GLU ILE ALA LYS HIS CYS GLY PHE LYS TYR LYS
SEQRES 5 A 263 LEU THR ILE VAL GLY ASP GLY LYS TYR GLY ALA ARG ASP
SEQRES 6 A 263 ALA ASP THR LYS ILE TRP ASN GLY MET VAL GLY GLU LEU
SEQRES 7 A 263 VAL TYR GLY LYS ALA ASP ILE ALA ILE ALA PRO LEU THR
SEQRES 8 A 263 ILE THR LEU VAL ARG GLU GLU VAL ILE ASP PHE SER LYS
SEQRES 9 A 263 PRO PHE MET SER LEU GLY ILE SER ILE MET ILE LYS LYS
SEQRES 10 A 263 GLY THR PRO ILE GLU SER ALA GLU ASP LEU SER LYS GLN
SEQRES 11 A 263 THR GLU ILE ALA TYR GLY THR LEU ASP SER GLY SER THR
SEQRES 12 A 263 LYS GLU PHE PHE ARG ARG SER LYS ILE ALA VAL PHE ASP
SEQRES 13 A 263 LYS MET TRP THR TYR MET ARG SER ALA GLU PRO SER VAL
SEQRES 14 A 263 PHE VAL ARG THR THR ALA GLU GLY VAL ALA ARG VAL ARG
SEQRES 15 A 263 LYS SER LYS GLY LYS TYR ALA TYR LEU LEU GLU SER THR
SEQRES 16 A 263 MET ASN GLU TYR ILE GLU GLN ARG LYS PRO CYS ASP THR
SEQRES 17 A 263 MET LYS VAL GLY GLY ASN LEU ASP SER LYS GLY TYR GLY
SEQRES 18 A 263 ILE ALA THR PRO LYS GLY SER SER LEU GLY ASN ALA VAL
SEQRES 19 A 263 ASN LEU ALA VAL LEU LYS LEU ASN GLU GLN GLY LEU LEU
SEQRES 20 A 263 ASP LYS LEU LYS ASN LYS TRP TRP TYR ASP LYS GLY GLU
SEQRES 21 A 263 CYS GLY SER
SEQRES 1 B 263 GLY ALA ASN LYS THR VAL VAL VAL THR THR ILE LEU GLU
SEQRES 2 B 263 SER PRO TYR VAL MET MET LYS LYS ASN HIS GLU MET LEU
SEQRES 3 B 263 GLU GLY ASN GLU ARG TYR GLU GLY TYR CYS VAL ASP LEU
SEQRES 4 B 263 ALA ALA GLU ILE ALA LYS HIS CYS GLY PHE LYS TYR LYS
SEQRES 5 B 263 LEU THR ILE VAL GLY ASP GLY LYS TYR GLY ALA ARG ASP
SEQRES 6 B 263 ALA ASP THR LYS ILE TRP ASN GLY MET VAL GLY GLU LEU
SEQRES 7 B 263 VAL TYR GLY LYS ALA ASP ILE ALA ILE ALA PRO LEU THR
SEQRES 8 B 263 ILE THR LEU VAL ARG GLU GLU VAL ILE ASP PHE SER LYS
SEQRES 9 B 263 PRO PHE MET SER LEU GLY ILE SER ILE MET ILE LYS LYS
SEQRES 10 B 263 GLY THR PRO ILE GLU SER ALA GLU ASP LEU SER LYS GLN
SEQRES 11 B 263 THR GLU ILE ALA TYR GLY THR LEU ASP SER GLY SER THR
SEQRES 12 B 263 LYS GLU PHE PHE ARG ARG SER LYS ILE ALA VAL PHE ASP
SEQRES 13 B 263 LYS MET TRP THR TYR MET ARG SER ALA GLU PRO SER VAL
SEQRES 14 B 263 PHE VAL ARG THR THR ALA GLU GLY VAL ALA ARG VAL ARG
SEQRES 15 B 263 LYS SER LYS GLY LYS TYR ALA TYR LEU LEU GLU SER THR
SEQRES 16 B 263 MET ASN GLU TYR ILE GLU GLN ARG LYS PRO CYS ASP THR
SEQRES 17 B 263 MET LYS VAL GLY GLY ASN LEU ASP SER LYS GLY TYR GLY
SEQRES 18 B 263 ILE ALA THR PRO LYS GLY SER SER LEU GLY ASN ALA VAL
SEQRES 19 B 263 ASN LEU ALA VAL LEU LYS LEU ASN GLU GLN GLY LEU LEU
SEQRES 20 B 263 ASP LYS LEU LYS ASN LYS TRP TRP TYR ASP LYS GLY GLU
SEQRES 21 B 263 CYS GLY SER
HET DNQ A 365 18
HET SO4 B 366 5
HET DNQ B 364 18
HETNAM DNQ 6,7-DINITROQUINOXALINE-2,3-DIONE
HETNAM SO4 SULFATE ION
HETSYN DNQ DNQX
FORMUL 3 DNQ 2(C8 H2 N4 O6)
FORMUL 4 SO4 O4 S 2-
FORMUL 6 HOH *363(H2 O)
HELIX 1 1 ASN A 22 LEU A 26 5 5
HELIX 2 2 GLU A 27 GLU A 30 5 4
HELIX 3 3 GLY A 34 GLY A 48 1 15
HELIX 4 4 ASN A 72 TYR A 80 1 9
HELIX 5 5 THR A 93 GLU A 98 1 6
HELIX 6 6 SER A 123 LYS A 129 1 7
HELIX 7 7 GLY A 141 SER A 150 1 10
HELIX 8 8 ILE A 152 ALA A 165 1 14
HELIX 9 9 THR A 173 SER A 184 1 12
HELIX 10 10 SER A 194 GLN A 202 1 9
HELIX 11 11 LEU A 230 GLN A 244 1 15
HELIX 12 12 GLY A 245 TYR A 256 1 12
HELIX 13 13 ASN B 22 LEU B 26 5 5
HELIX 14 14 GLU B 27 GLU B 30 5 4
HELIX 15 15 GLY B 34 GLY B 48 1 15
HELIX 16 16 ASN B 72 TYR B 80 1 9
HELIX 17 17 THR B 93 GLU B 98 1 6
HELIX 18 18 SER B 123 LYS B 129 1 7
HELIX 19 19 GLY B 141 SER B 150 1 10
HELIX 20 20 ILE B 152 ALA B 165 1 14
HELIX 21 21 THR B 173 SER B 184 1 12
HELIX 22 22 SER B 194 GLU B 201 1 8
HELIX 23 23 LEU B 230 GLN B 244 1 15
HELIX 24 24 GLY B 245 TYR B 256 1 12
SHEET 1 A 3 TYR A 51 ILE A 55 0
SHEET 2 A 3 VAL A 6 THR A 10 1 O VAL A 6 N LYS A 52
SHEET 3 A 3 ILE A 85 ALA A 86 1 O ILE A 85 N THR A 9
SHEET 1 B 2 MET A 18 MET A 19 0
SHEET 2 B 2 TYR A 32 GLU A 33 -1 O GLU A 33 N MET A 18
SHEET 1 C 2 ILE A 100 PHE A 102 0
SHEET 2 C 2 ALA A 223 PRO A 225 -1 O THR A 224 N ASP A 101
SHEET 1 D 2 MET A 107 LEU A 109 0
SHEET 2 D 2 LYS A 218 TYR A 220 -1 N LYS A 218 O LEU A 109
SHEET 1 E 4 ALA A 134 GLY A 136 0
SHEET 2 E 4 TYR A 188 GLU A 193 1 N ALA A 189 O ALA A 134
SHEET 3 E 4 ILE A 111 LYS A 116 -1 N SER A 112 O LEU A 192
SHEET 4 E 4 THR A 208 VAL A 211 -1 O MET A 209 N ILE A 115
SHEET 1 F 5 TYR B 51 ILE B 55 0
SHEET 2 F 5 VAL B 6 THR B 10 1 O VAL B 6 N LYS B 52
SHEET 3 F 5 ILE B 85 THR B 91 1 O ILE B 85 N THR B 9
SHEET 4 F 5 LYS B 218 PRO B 225 -1 N GLY B 221 O LEU B 90
SHEET 5 F 5 ILE B 100 PHE B 102 -1 N ASP B 101 O THR B 224
SHEET 1 G 5 TYR B 51 ILE B 55 0
SHEET 2 G 5 VAL B 6 THR B 10 1 O VAL B 6 N LYS B 52
SHEET 3 G 5 ILE B 85 THR B 91 1 O ILE B 85 N THR B 9
SHEET 4 G 5 LYS B 218 PRO B 225 -1 N GLY B 221 O LEU B 90
SHEET 5 G 5 MET B 107 LEU B 109 -1 O MET B 107 N TYR B 220
SHEET 1 H 2 MET B 18 MET B 19 0
SHEET 2 H 2 TYR B 32 GLU B 33 -1 O GLU B 33 N MET B 18
SHEET 1 I 4 ALA B 134 GLY B 136 0
SHEET 2 I 4 TYR B 188 GLU B 193 1 N ALA B 189 O ALA B 134
SHEET 3 I 4 ILE B 111 LYS B 116 -1 N SER B 112 O LEU B 192
SHEET 4 I 4 THR B 208 VAL B 211 -1 N MET B 209 O ILE B 115
SSBOND 1 CYS A 206 CYS A 261 1555 1555 2.04
SSBOND 2 CYS B 206 CYS B 261 1555 1555 2.26
CISPEP 1 SER A 14 PRO A 15 0 0.11
CISPEP 2 GLU A 166 PRO A 167 0 -0.06
CISPEP 3 LYS A 204 PRO A 205 0 0.79
CISPEP 4 SER B 14 PRO B 15 0 -0.60
CISPEP 5 GLU B 166 PRO B 167 0 -0.42
CISPEP 6 LYS B 204 PRO B 205 0 0.50
SITE 1 AC1 7 GLY B 141 SER B 142 THR B 143 GLU B 193
SITE 2 AC1 7 DNQ B 364 HOH B 476 HOH B 493
SITE 1 AC2 14 GLU B 13 TYR B 16 TYR B 61 PRO B 89
SITE 2 AC2 14 LEU B 90 THR B 91 ARG B 96 THR B 174
SITE 3 AC2 14 GLU B 193 MET B 196 TYR B 220 SO4 B 366
SITE 4 AC2 14 HOH B 484 HOH B 493
SITE 1 AC3 12 GLU A 13 TYR A 61 PRO A 89 LEU A 90
SITE 2 AC3 12 THR A 91 ARG A 96 THR A 174 GLU A 193
SITE 3 AC3 12 THR A 195 MET A 196 TYR A 220 HOH A 488
CRYST1 62.153 93.703 97.369 90.00 90.00 90.00 P 21 21 21 8
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 0.016089 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010672 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010270 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
