HEADER MEMBRANE PROTEIN 01-MAY-08 2ZNU
TITLE CRYSTAL STRUCTURE OF THE LIGAND-BINDING CORE OF THE HUMAN IONOTROPIC
TITLE 2 GLUTAMATE RECEPTOR, GLUR5, IN COMPLEX WITH A NOVEL SELECTIVE AGONIST,
TITLE 3 NEODYSIHERBAINE A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMATE RECEPTOR, IONOTROPIC KAINATE 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: LIGAND-BINDING DOMAIN, UNP RESIDUES 445-559, UNP RESIDUES
COMPND 5 682-820;
COMPND 6 SYNONYM: GLUTAMATE RECEPTOR 5, GLUR-5, GLUR5, EXCITATORY AMINO ACID
COMPND 7 RECEPTOR 3, EAA3, GLUR5 LIGAND-BINDING CORE;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: GRIK1, GLUR5;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPCOLD-I DNA
KEYWDS GLUR5, LIGAND-BINDING CORE, NEODYSIHERBAINE A, AGONIST, ALTERNATIVE
KEYWDS 2 SPLICING, CELL JUNCTION, GLYCOPROTEIN, ION TRANSPORT, IONIC CHANNEL,
KEYWDS 3 MEMBRANE, PHOSPHOPROTEIN, POLYMORPHISM, POSTSYNAPTIC CELL MEMBRANE,
KEYWDS 4 RNA EDITING, SYNAPSE, TRANSMEMBRANE, TRANSPORT, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.UNNO,M.SASAKI,M.IKEDA-SAITO
REVDAT 4 01-NOV-23 2ZNU 1 REMARK SEQADV
REVDAT 3 16-AUG-17 2ZNU 1 SOURCE
REVDAT 2 26-OCT-11 2ZNU 1 JRNL VERSN
REVDAT 1 05-MAY-09 2ZNU 0
JRNL AUTH M.UNNO,M.SHINOHARA,K.TAKAYAMA,H.TANAKA,K.TERUYA,K.DOH-URA,
JRNL AUTH 2 R.SAKAI,M.SASAKI,M.IKEDA-SAITO
JRNL TITL BINDING AND SELECTIVITY OF THE MARINE TOXIN NEODYSIHERBAINE
JRNL TITL 2 A AND ITS SYNTHETIC ANALOGUES TO GLUK1 AND GLUK2 KAINATE
JRNL TITL 3 RECEPTORS.
JRNL REF J.MOL.BIOL. V. 413 667 2011
JRNL REFN ISSN 0022-2836
JRNL PMID 21893069
JRNL DOI 10.1016/J.JMB.2011.08.043
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 32025
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) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1674
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2232
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.82
REMARK 3 BIN R VALUE (WORKING SET) : 0.2750
REMARK 3 BIN FREE R VALUE SET COUNT : 129
REMARK 3 BIN FREE R VALUE : 0.2920
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2033
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 36
REMARK 3 SOLVENT ATOMS : 209
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.82
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.31000
REMARK 3 B22 (A**2) : 1.12000
REMARK 3 B33 (A**2) : -1.67000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.40000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.112
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.117
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.071
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.315
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2140 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2884 ; 1.372 ; 1.990
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 254 ; 5.906 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 93 ;32.910 ;23.763
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 402 ;13.430 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 15 ;13.865 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 325 ; 0.104 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1556 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1016 ; 0.207 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1504 ; 0.305 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 180 ; 0.147 ; 0.200
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): 20 ; 0.183 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 10 ; 0.119 ; 0.200
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): 1319 ; 0.921 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2067 ; 1.406 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 954 ; 2.034 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 817 ; 3.131 ; 4.500
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 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 415 A 789
REMARK 3 ORIGIN FOR THE GROUP (A): 19.3570 -0.7450 13.1710
REMARK 3 T TENSOR
REMARK 3 T11: -0.0660 T22: -0.0523
REMARK 3 T33: -0.1019 T12: 0.0016
REMARK 3 T13: -0.0218 T23: -0.0076
REMARK 3 L TENSOR
REMARK 3 L11: 1.5187 L22: 1.3603
REMARK 3 L33: 0.8321 L12: 0.6221
REMARK 3 L13: -0.5510 L23: -0.2867
REMARK 3 S TENSOR
REMARK 3 S11: 0.0018 S12: -0.0688 S13: -0.0195
REMARK 3 S21: 0.0044 S22: -0.0116 S23: -0.0167
REMARK 3 S31: -0.0184 S32: 0.0918 S33: 0.0098
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 1
REMARK 3 ORIGIN FOR THE GROUP (A): 23.1810 -1.0560 12.7820
REMARK 3 T TENSOR
REMARK 3 T11: 0.0243 T22: -0.0168
REMARK 3 T33: -0.0503 T12: -0.1064
REMARK 3 T13: -0.0079 T23: 0.0033
REMARK 3 L TENSOR
REMARK 3 L11: 10.8071 L22: 3.4776
REMARK 3 L33: 6.8217 L12: 1.1096
REMARK 3 L13: 4.4766 L23: -3.6280
REMARK 3 S TENSOR
REMARK 3 S11: 0.3137 S12: -0.1049 S13: -0.3202
REMARK 3 S21: 0.6933 S22: -0.3477 S23: -0.3989
REMARK 3 S31: 0.4374 S32: -0.1391 S33: 0.0340
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 2ZNU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-MAY-08.
REMARK 100 THE DEPOSITION ID IS D_1000028202.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-OCT-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-17A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33702
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 27.6000
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 (%) : 96.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.29400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.870
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 2ZNS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, NACL, EDTA, PH4.8, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 279K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 59.44300
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.49500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 59.44300
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 32.49500
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 981 LIES ON A SPECIAL POSITION.
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 PRO A 790
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 416 -50.30 -132.41
REMARK 500 GLU A 426 115.74 -164.29
REMARK 500 ASN A 484 -160.35 -129.78
REMARK 500 ARG A 785 -75.41 -91.31
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 NDZ A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 791
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 4
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2ZNS RELATED DB: PDB
REMARK 900 SAME PROTEIN BUT DIFFERENT LIGAND
REMARK 900 RELATED ID: 2ZNT RELATED DB: PDB
REMARK 900 SAME PROTEIN BUT DIFFERENT LIGAND
DBREF 2ZNU A 415 529 UNP P39086 GRIK1_HUMAN 445 559
DBREF 2ZNU A 652 790 UNP P39086 GRIK1_HUMAN 682 820
SEQADV 2ZNU GLY A 600 UNP P39086 LINKER
SEQADV 2ZNU THR A 601 UNP P39086 LINKER
SEQRES 1 A 256 ALA ASN ARG THR LEU ILE VAL THR THR ILE LEU GLU GLU
SEQRES 2 A 256 PRO TYR VAL MET TYR ARG LYS SER ASP LYS PRO LEU TYR
SEQRES 3 A 256 GLY ASN ASP ARG PHE GLU GLY TYR CYS LEU ASP LEU LEU
SEQRES 4 A 256 LYS GLU LEU SER ASN ILE LEU GLY PHE ILE TYR ASP VAL
SEQRES 5 A 256 LYS LEU VAL PRO ASP GLY LYS TYR GLY ALA GLN ASN ASP
SEQRES 6 A 256 LYS GLY GLU TRP ASN GLY MET VAL LYS GLU LEU ILE ASP
SEQRES 7 A 256 HIS ARG ALA ASP LEU ALA VAL ALA PRO LEU THR ILE THR
SEQRES 8 A 256 TYR VAL ARG GLU LYS VAL ILE ASP PHE SER LYS PRO PHE
SEQRES 9 A 256 MET THR LEU GLY ILE SER ILE LEU TYR ARG LYS GLY THR
SEQRES 10 A 256 PRO ILE ASP SER ALA ASP ASP LEU ALA LYS GLN THR LYS
SEQRES 11 A 256 ILE GLU TYR GLY ALA VAL ARG ASP GLY SER THR MET THR
SEQRES 12 A 256 PHE PHE LYS LYS SER LYS ILE SER THR TYR GLU LYS MET
SEQRES 13 A 256 TRP ALA PHE MET SER SER ARG GLN GLN THR ALA LEU VAL
SEQRES 14 A 256 ARG ASN SER ASP GLU GLY ILE GLN ARG VAL LEU THR THR
SEQRES 15 A 256 ASP TYR ALA LEU LEU MET GLU SER THR SER ILE GLU TYR
SEQRES 16 A 256 VAL THR GLN ARG ASN CYS ASN LEU THR GLN ILE GLY GLY
SEQRES 17 A 256 LEU ILE ASP SER LYS GLY TYR GLY VAL GLY THR PRO ILE
SEQRES 18 A 256 GLY SER PRO TYR ARG ASP LYS ILE THR ILE ALA ILE LEU
SEQRES 19 A 256 GLN LEU GLN GLU GLU GLY LYS LEU HIS MET MET LYS GLU
SEQRES 20 A 256 LYS TRP TRP ARG GLY ASN GLY CYS PRO
HET NDZ A 1 20
HET BME A 791 4
HET BME A 2 4
HET BME A 3 4
HET BME A 4 4
HETNAM NDZ (2R,3AR,6R,7R,7AR)-2-[(2S)-2-AMINO-2-CARBOXYETHYL]-6,7-
HETNAM 2 NDZ DIHYDROXYHEXAHYDRO-2H-FURO[3,2-B]PYRAN-2-CARBOXYLIC
HETNAM 3 NDZ ACID
HETNAM BME BETA-MERCAPTOETHANOL
FORMUL 2 NDZ C11 H17 N O8
FORMUL 3 BME 4(C2 H6 O S)
FORMUL 7 HOH *209(H2 O)
HELIX 1 1 TYR A 440 ASP A 443 5 4
HELIX 2 2 GLY A 447 GLY A 461 1 15
HELIX 3 3 ASN A 484 ASP A 492 1 9
HELIX 4 4 THR A 505 LYS A 510 1 6
HELIX 5 5 SER A 655 LYS A 661 1 7
HELIX 6 6 GLY A 673 SER A 682 1 10
HELIX 7 7 ILE A 684 ARG A 697 1 14
HELIX 8 8 ARG A 697 LEU A 702 1 6
HELIX 9 9 ASN A 705 THR A 716 1 12
HELIX 10 10 SER A 724 ASN A 734 1 11
HELIX 11 11 PRO A 758 GLU A 773 1 16
HELIX 12 12 GLY A 774 ARG A 785 1 12
SHEET 1 A 3 TYR A 464 LEU A 468 0
SHEET 2 A 3 LEU A 419 THR A 423 1 N VAL A 421 O LYS A 467
SHEET 3 A 3 LEU A 497 ALA A 498 1 O LEU A 497 N THR A 422
SHEET 1 B 2 MET A 431 TYR A 432 0
SHEET 2 B 2 PHE A 445 GLU A 446 -1 O GLU A 446 N MET A 431
SHEET 1 C 2 ILE A 512 PHE A 514 0
SHEET 2 C 2 GLY A 752 PRO A 754 -1 O THR A 753 N ASP A 513
SHEET 1 D 2 MET A 519 LEU A 521 0
SHEET 2 D 2 LYS A 747 TYR A 749 -1 O LYS A 747 N LEU A 521
SHEET 1 E 4 GLU A 666 GLY A 668 0
SHEET 2 E 4 TYR A 718 GLU A 723 1 O LEU A 721 N GLY A 668
SHEET 3 E 4 ILE A 523 ARG A 528 -1 N LEU A 526 O LEU A 720
SHEET 4 E 4 LEU A 737 ILE A 740 -1 O THR A 738 N TYR A 527
CISPEP 1 GLU A 427 PRO A 428 0 -6.02
CISPEP 2 ASN A 787 GLY A 788 0 1.57
CISPEP 3 GLY A 788 CYS A 789 0 6.82
SITE 1 AC1 14 GLU A 426 TYR A 474 PRO A 501 THR A 503
SITE 2 AC1 14 ARG A 508 GLY A 673 SER A 674 THR A 675
SITE 3 AC1 14 SER A 706 MET A 722 GLU A 723 SER A 726
SITE 4 AC1 14 TYR A 749 HOH A 797
SITE 1 AC2 9 GLU A 427 ASP A 707 ILE A 710 MET A 722
SITE 2 AC2 9 SER A 726 TYR A 729 HOH A 829 HOH A 838
SITE 3 AC2 9 HOH A 988
SITE 1 AC3 4 PRO A 517 GLN A 771 LEU A 776 HOH A 868
SITE 1 AC4 2 ASN A 442 TYR A 464
SITE 1 AC5 5 ILE A 504 TYR A 506 GLU A 509 HOH A 973
SITE 2 AC5 5 HOH A 974
CRYST1 118.886 64.990 50.232 90.00 107.29 90.00 C 1 2 1 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 0.008411 0.000000 0.002618 0.00000
SCALE2 0.000000 0.015387 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020850 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
