HEADER TRANSPORT PROTEIN 20-OCT-16 5TP9
TITLE STRUCTURE OF THE HUMAN GLUN1/GLUN2A LBD IN COMPLEX WITH COMPOUND 2
TITLE 2 (GNE9178)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMATE RECEPTOR IONOTROPIC, NMDA 2A;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: LIGAND BINDING DOMAIN (UNP RESIDUES 401-539, GT LINKER, UNP
COMPND 5 RESIDUES 661-802);
COMPND 6 SYNONYM: GLUN2A, GLUTAMATE [NMDA] RECEPTOR SUBUNIT EPSILON-1, N-
COMPND 7 METHYL D-ASPARTATE RECEPTOR SUBTYPE 2A, HNR2A;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: GLUTAMATE RECEPTOR IONOTROPIC, NMDA 1;
COMPND 11 CHAIN: B;
COMPND 12 FRAGMENT: UNP RESIDUES 394-544, GT LINKER, UNP RESIDUES 663-800;
COMPND 13 SYNONYM: GLUN1, GLUTAMATE [NMDA] RECEPTOR SUBUNIT ZETA-1, N-METHYL-D-
COMPND 14 ASPARTATE RECEPTOR SUBUNIT NR1, NMD-R1;
COMPND 15 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: GRIN2A, NMDAR2A;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 GENE: GRIN1, NMDAR1;
SOURCE 14 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 15 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS NMDA RECEPTOR, GLUTAMATE, GLYCINE, CALCIUM CHANNEL, MEMBRANE,
KEYWDS 2 TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR H.J.A.WALLWEBER,P.J.LUPARDUS
REVDAT 3 08-FEB-17 5TP9 1 JRNL
REVDAT 2 28-DEC-16 5TP9 1 JRNL
REVDAT 1 30-NOV-16 5TP9 0
JRNL AUTH E.VILLEMURE,M.VOLGRAF,Y.JIANG,G.WU,C.Q.LY,P.W.YUEN,A.LU,
JRNL AUTH 2 X.LUO,M.LIU,S.ZHANG,P.J.LUPARDUS,H.J.WALLWEBER,B.M.LIEDERER,
JRNL AUTH 3 G.DESHMUKH,E.PLISE,S.TAY,T.M.WANG,J.E.HANSON,D.H.HACKOS,
JRNL AUTH 4 K.SCEARCE-LEVIE,J.B.SCHWARZ,B.D.SELLERS
JRNL TITL GLUN2A-SELECTIVE PYRIDOPYRIMIDINONE SERIES OF NMDAR POSITIVE
JRNL TITL 2 ALLOSTERIC MODULATORS WITH AN IMPROVED IN VIVO PROFILE.
JRNL REF ACS MED CHEM LETT V. 8 84 2017
JRNL REFN ISSN 1948-5875
JRNL PMID 28105280
JRNL DOI 10.1021/ACSMEDCHEMLETT.6B00388
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.6
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.67
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 24871
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) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 1251
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.000
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 12
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.39
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.50
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.81
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2914
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2320
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2794
REMARK 3 BIN R VALUE (WORKING SET) : 0.2280
REMARK 3 BIN FREE R VALUE : 0.3260
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.12
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 120
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4367
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 47
REMARK 3 SOLVENT ATOMS : 124
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 55.22
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.11
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.66840
REMARK 3 B22 (A**2) : 4.05420
REMARK 3 B33 (A**2) : -1.38580
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.290
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.392
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.241
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.377
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.242
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.930
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 4546 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 6161 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1579 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 107 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 686 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 4546 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 0 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 596 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 5142 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.08
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.11
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 18.28
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5TP9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-OCT-16.
REMARK 100 THE DEPOSITION ID IS D_1000224592.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JAN-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
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 : LIQUID NITROGEN-COOLED DUAL
REMARK 200 CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24941
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : 0.08100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.10
REMARK 200 R MERGE FOR SHELL (I) : 0.72200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, PH 7.0, 10-13% PEG8000, 2
REMARK 280 MM CALCIUM ACETATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 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 28.13000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 60.43000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.89000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 60.43000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.13000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.89000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 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 GLY A 1
REMARK 465 SER A 2
REMARK 465 PRO A 3
REMARK 465 ASP A 4
REMARK 465 ASP A 5
REMARK 465 PRO A 26
REMARK 465 LEU A 27
REMARK 465 THR A 28
REMARK 465 HIS A 284
REMARK 465 ASN A 285
REMARK 465 GLY B 1
REMARK 465 SER B 2
REMARK 465 ASN B 100
REMARK 465 ASN B 101
REMARK 465 SER B 102
REMARK 465 GLU B 290
REMARK 465 CYS B 291
REMARK 465 ASP B 292
REMARK 465 SER B 293
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 ASP A 25 CG OD1 OD2
REMARK 470 GLU A 29 CG CD OE1 OE2
REMARK 470 ARG A 33 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 144 CG CD OE1 NE2
REMARK 470 SER A 149 OG
REMARK 470 GLU A 226 CG CD OE1 OE2
REMARK 470 LYS A 229 CG CD CE NZ
REMARK 470 SER A 235 OG
REMARK 470 ASP B 50 CG OD1 OD2
REMARK 470 THR B 51 OG1 CG2
REMARK 470 ARG B 77 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 98 CG CD NE CZ NH1 NH2
REMARK 470 ASN B 103 CG OD1 ND2
REMARK 470 LYS B 104 CG CD CE NZ
REMARK 470 GLU B 106 CG CD OE1 OE2
REMARK 470 ASP B 170 CG OD1 OD2
REMARK 470 LYS B 171 CG CD CE NZ
REMARK 470 GLU B 244 CG CD OE1 OE2
REMARK 470 TYR B 288 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN B 289 CG CD OE1 NE2
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 GLU A 15 96.83 -173.31
REMARK 500 THR A 30 -166.46 -120.20
REMARK 500 ARG A 33 -134.32 55.14
REMARK 500 LYS A 74 72.07 63.21
REMARK 500 LYS A 86 -113.76 -119.46
REMARK 500 ASN A 96 -164.95 -112.28
REMARK 500 SER A 235 49.12 -98.78
REMARK 500 THR A 242 -157.93 -156.33
REMARK 500 SER B 4 123.02 172.96
REMARK 500 ASN B 80 69.95 63.63
REMARK 500 ASN B 108 -167.44 -101.51
REMARK 500 ASN B 217 5.91 56.70
REMARK 500 ASN B 217 6.36 56.40
REMARK 500 PHE B 247 67.99 18.90
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 ACT A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GLU A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7H0 A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GLY B 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5TPA RELATED DB: PDB
DBREF 5TP9 A 3 141 UNP Q12879 NMDE1_HUMAN 401 539
DBREF 5TP9 A 144 285 UNP Q12879 NMDE1_HUMAN 661 802
DBREF 5TP9 B 3 153 UNP Q05586 NMDZ1_HUMAN 415 565
DBREF 5TP9 B 156 293 UNP Q05586 NMDZ1_HUMAN 684 821
SEQADV 5TP9 GLY A 1 UNP Q12879 EXPRESSION TAG
SEQADV 5TP9 SER A 2 UNP Q12879 EXPRESSION TAG
SEQADV 5TP9 GLY A 142 UNP Q12879 LINKER
SEQADV 5TP9 THR A 143 UNP Q12879 LINKER
SEQADV 5TP9 GLY B 1 UNP Q05586 EXPRESSION TAG
SEQADV 5TP9 SER B 2 UNP Q05586 EXPRESSION TAG
SEQADV 5TP9 GLY B 154 UNP Q05586 LINKER
SEQADV 5TP9 THR B 155 UNP Q05586 LINKER
SEQRES 1 A 285 GLY SER PRO ASP ASP ASN HIS LEU SER ILE VAL THR LEU
SEQRES 2 A 285 GLU GLU ALA PRO PHE VAL ILE VAL GLU ASP ILE ASP PRO
SEQRES 3 A 285 LEU THR GLU THR CYS VAL ARG ASN THR VAL PRO CYS ARG
SEQRES 4 A 285 LYS PHE VAL LYS ILE ASN ASN SER THR ASN GLU GLY MET
SEQRES 5 A 285 ASN VAL LYS LYS CYS CYS LYS GLY PHE CYS ILE ASP ILE
SEQRES 6 A 285 LEU LYS LYS LEU SER ARG THR VAL LYS PHE THR TYR ASP
SEQRES 7 A 285 LEU TYR LEU VAL THR ASN GLY LYS HIS GLY LYS LYS VAL
SEQRES 8 A 285 ASN ASN VAL TRP ASN GLY MET ILE GLY GLU VAL VAL TYR
SEQRES 9 A 285 GLN ARG ALA VAL MET ALA VAL GLY SER LEU THR ILE ASN
SEQRES 10 A 285 GLU GLU ARG SER GLU VAL VAL ASP PHE SER VAL PRO PHE
SEQRES 11 A 285 VAL GLU THR GLY ILE SER VAL MET VAL SER ARG GLY THR
SEQRES 12 A 285 GLN VAL THR GLY LEU SER ASP LYS LYS PHE GLN ARG PRO
SEQRES 13 A 285 HIS ASP TYR SER PRO PRO PHE ARG PHE GLY THR VAL PRO
SEQRES 14 A 285 ASN GLY SER THR GLU ARG ASN ILE ARG ASN ASN TYR PRO
SEQRES 15 A 285 TYR MET HIS GLN TYR MET THR LYS PHE ASN GLN LYS GLY
SEQRES 16 A 285 VAL GLU ASP ALA LEU VAL SER LEU LYS THR GLY LYS LEU
SEQRES 17 A 285 ASP ALA PHE ILE TYR ASP ALA ALA VAL LEU ASN TYR LYS
SEQRES 18 A 285 ALA GLY ARG ASP GLU GLY CYS LYS LEU VAL THR ILE GLY
SEQRES 19 A 285 SER GLY TYR ILE PHE ALA THR THR GLY TYR GLY ILE ALA
SEQRES 20 A 285 LEU GLN LYS GLY SER PRO TRP LYS ARG GLN ILE ASP LEU
SEQRES 21 A 285 ALA LEU LEU GLN PHE VAL GLY ASP GLY GLU MET GLU GLU
SEQRES 22 A 285 LEU GLU THR LEU TRP LEU THR GLY ILE CYS HIS ASN
SEQRES 1 B 293 GLY SER MET SER THR ARG LEU LYS ILE VAL THR ILE HIS
SEQRES 2 B 293 GLN GLU PRO PHE VAL TYR VAL LYS PRO THR LEU SER ASP
SEQRES 3 B 293 GLY THR CYS LYS GLU GLU PHE THR VAL ASN GLY ASP PRO
SEQRES 4 B 293 VAL LYS LYS VAL ILE CYS THR GLY PRO ASN ASP THR SER
SEQRES 5 B 293 PRO GLY SER PRO ARG HIS THR VAL PRO GLN CYS CYS TYR
SEQRES 6 B 293 GLY PHE CYS ILE ASP LEU LEU ILE LYS LEU ALA ARG THR
SEQRES 7 B 293 MET ASN PHE THR TYR GLU VAL HIS LEU VAL ALA ASP GLY
SEQRES 8 B 293 LYS PHE GLY THR GLN GLU ARG VAL ASN ASN SER ASN LYS
SEQRES 9 B 293 LYS GLU TRP ASN GLY MET MET GLY GLU LEU LEU SER GLY
SEQRES 10 B 293 GLN ALA ASP MET ILE VAL ALA PRO LEU THR ILE ASN ASN
SEQRES 11 B 293 GLU ARG ALA GLN TYR ILE GLU PHE SER LYS PRO PHE LYS
SEQRES 12 B 293 TYR GLN GLY LEU THR ILE LEU VAL LYS LYS GLY THR ARG
SEQRES 13 B 293 ILE THR GLY ILE ASN ASP PRO ARG LEU ARG ASN PRO SER
SEQRES 14 B 293 ASP LYS PHE ILE TYR ALA THR VAL LYS GLN SER SER VAL
SEQRES 15 B 293 ASP ILE TYR PHE ARG ARG GLN VAL GLU LEU SER THR MET
SEQRES 16 B 293 TYR ARG HIS MET GLU LYS HIS ASN TYR GLU SER ALA ALA
SEQRES 17 B 293 GLU ALA ILE GLN ALA VAL ARG ASP ASN LYS LEU HIS ALA
SEQRES 18 B 293 PHE ILE TRP ASP SER ALA VAL LEU GLU PHE GLU ALA SER
SEQRES 19 B 293 GLN LYS CYS ASP LEU VAL THR THR GLY GLU LEU PHE PHE
SEQRES 20 B 293 ARG SER GLY PHE GLY ILE GLY MET ARG LYS ASP SER PRO
SEQRES 21 B 293 TRP LYS GLN ASN VAL SER LEU SER ILE LEU LYS SER HIS
SEQRES 22 B 293 GLU ASN GLY PHE MET GLU ASP LEU ASP LYS THR TRP VAL
SEQRES 23 B 293 ARG TYR GLN GLU CYS ASP SER
HET ACT A 301 4
HET GLU A 302 10
HET 7H0 A 303 27
HET CA B 301 1
HET GLY B 302 5
HETNAM ACT ACETATE ION
HETNAM GLU GLUTAMIC ACID
HETNAM 7H0 7-{[5-CHLORO-3-(TRIFLUOROMETHYL)-1H-PYRAZOL-1-
HETNAM 2 7H0 YL]METHYL}-N-ETHYL-2-METHYL-5-OXO-5H-[1,3]THIAZOLO[3,
HETNAM 3 7H0 2-A]PYRIMIDINE-3-CARBOXAMIDE
HETNAM CA CALCIUM ION
HETNAM GLY GLYCINE
FORMUL 3 ACT C2 H3 O2 1-
FORMUL 4 GLU C5 H9 N O4
FORMUL 5 7H0 C15 H13 CL F3 N5 O2 S
FORMUL 6 CA CA 2+
FORMUL 7 GLY C2 H5 N O2
FORMUL 8 HOH *124(H2 O)
HELIX 1 AA1 GLY A 60 VAL A 73 1 14
HELIX 2 AA2 ASN A 96 TYR A 104 1 9
HELIX 3 AA3 ASN A 117 GLU A 122 1 6
HELIX 4 AA4 ASP A 150 ARG A 155 1 6
HELIX 5 AA5 PRO A 156 TYR A 159 5 4
HELIX 6 AA6 GLY A 171 TYR A 181 1 11
HELIX 7 AA7 TYR A 181 THR A 189 1 9
HELIX 8 AA8 LYS A 190 ASN A 192 5 3
HELIX 9 AA9 GLY A 195 THR A 205 1 11
HELIX 10 AB1 ALA A 215 ASP A 225 1 11
HELIX 11 AB2 ILE A 233 TYR A 237 1 5
HELIX 12 AB3 TRP A 254 ASP A 268 1 15
HELIX 13 AB4 GLY A 269 LEU A 279 1 11
HELIX 14 AB5 GLY B 66 ASN B 80 1 15
HELIX 15 AB6 ASN B 108 SER B 116 1 9
HELIX 16 AB7 ASN B 129 GLN B 134 1 6
HELIX 17 AB8 ASP B 162 ASN B 167 1 6
HELIX 18 AB9 SER B 180 GLN B 189 1 10
HELIX 19 AC1 LEU B 192 GLU B 200 1 9
HELIX 20 AC2 SER B 206 ASP B 216 1 11
HELIX 21 AC3 SER B 226 LYS B 236 1 11
HELIX 22 AC4 TRP B 261 ASN B 275 1 15
HELIX 23 AC5 GLY B 276 VAL B 286 1 11
SHEET 1 AA1 5 THR A 76 LEU A 81 0
SHEET 2 AA1 5 HIS A 7 THR A 12 1 N LEU A 8 O THR A 76
SHEET 3 AA1 5 MET A 109 ALA A 110 1 O MET A 109 N VAL A 11
SHEET 4 AA1 5 ALA A 247 LEU A 248 -1 O ALA A 247 N ALA A 110
SHEET 5 AA1 5 ASP A 125 PHE A 126 -1 N ASP A 125 O LEU A 248
SHEET 1 AA2 3 ILE A 20 ASP A 23 0
SHEET 2 AA2 3 GLY A 51 LYS A 59 -1 O LYS A 59 N ILE A 20
SHEET 3 AA2 3 VAL A 36 LYS A 43 -1 N VAL A 42 O MET A 52
SHEET 1 AA3 2 LYS A 90 VAL A 91 0
SHEET 2 AA3 2 VAL A 94 TRP A 95 -1 O VAL A 94 N VAL A 91
SHEET 1 AA4 4 PHE A 165 GLY A 166 0
SHEET 2 AA4 4 ALA A 210 ASP A 214 1 O ILE A 212 N GLY A 166
SHEET 3 AA4 4 VAL A 131 SER A 140 -1 N MET A 138 O PHE A 211
SHEET 4 AA4 4 LEU A 230 THR A 232 -1 O VAL A 231 N VAL A 139
SHEET 1 AA5 4 PHE A 165 GLY A 166 0
SHEET 2 AA5 4 ALA A 210 ASP A 214 1 O ILE A 212 N GLY A 166
SHEET 3 AA5 4 VAL A 131 SER A 140 -1 N MET A 138 O PHE A 211
SHEET 4 AA5 4 PHE A 239 TYR A 244 -1 O THR A 242 N THR A 133
SHEET 1 AA6 6 TYR B 19 PRO B 22 0
SHEET 2 AA6 6 THR B 59 TYR B 65 -1 O CYS B 63 N LYS B 21
SHEET 3 AA6 6 VAL B 43 PRO B 48 -1 N VAL B 43 O CYS B 64
SHEET 4 AA6 6 TYR B 83 LEU B 87 1 O LEU B 87 N THR B 46
SHEET 5 AA6 6 LEU B 7 THR B 11 1 N ILE B 9 O GLU B 84
SHEET 6 AA6 6 MET B 121 ILE B 122 1 O MET B 121 N VAL B 10
SHEET 1 AA7 2 GLN B 96 ARG B 98 0
SHEET 2 AA7 2 LYS B 105 TRP B 107 -1 O GLU B 106 N GLU B 97
SHEET 1 AA8 2 ILE B 136 PHE B 138 0
SHEET 2 AA8 2 GLY B 254 ARG B 256 -1 O MET B 255 N GLU B 137
SHEET 1 AA9 4 TYR B 174 ALA B 175 0
SHEET 2 AA9 4 ALA B 221 ASP B 225 1 O ILE B 223 N ALA B 175
SHEET 3 AA9 4 LYS B 143 LYS B 152 -1 N LEU B 150 O PHE B 222
SHEET 4 AA9 4 LEU B 239 PHE B 251 -1 O VAL B 240 N VAL B 151
SSBOND 1 CYS A 31 CYS A 57 1555 1555 2.05
SSBOND 2 CYS A 38 CYS A 58 1555 1555 2.08
SSBOND 3 CYS A 228 CYS A 283 1555 1555 2.05
SSBOND 4 CYS B 29 CYS B 63 1555 1555 2.05
SSBOND 5 CYS B 45 CYS B 64 1555 1555 2.04
CISPEP 1 ALA A 16 PRO A 17 0 -2.94
CISPEP 2 SER A 160 PRO A 161 0 -4.11
CISPEP 3 GLU B 15 PRO B 16 0 3.28
SITE 1 AC1 2 ARG A 39 ARG A 106
SITE 1 AC2 12 HIS A 87 SER A 113 THR A 115 ARG A 120
SITE 2 AC2 12 GLY A 171 SER A 172 THR A 173 TYR A 213
SITE 3 AC2 12 ASP A 214 HOH A 407 HOH A 411 HOH A 459
SITE 1 AC3 15 ILE A 116 VAL A 128 PRO A 129 PHE A 130
SITE 2 AC3 15 VAL A 131 GLU A 132 THR A 242 GLY A 243
SITE 3 AC3 15 LEU A 262 HOH A 404 LYS B 140 PRO B 141
SITE 4 AC3 15 TYR B 144 LEU B 270 HIS B 273
SITE 1 AC4 9 PHE B 93 PRO B 125 LEU B 126 THR B 127
SITE 2 AC4 9 ARG B 132 SER B 180 SER B 181 ASP B 225
SITE 3 AC4 9 PHE B 251
CRYST1 56.260 89.780 120.860 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 0.017775 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011138 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008274 0.00000
(ATOM LINES ARE NOT SHOWN.)
END