HEADER TRANSPORT PROTEIN, RECEPTOR 16-APR-17 5VII
TITLE CRYSTAL STRUCTURE OF GLUN1/GLUN2A NMDA RECEPTOR AGONIST BINDING
TITLE 2 DOMAINS WITH GLYCINE AND ANTAGONIST, 4-(3-FLUOROPROPYL)PHENYL-ACEPC
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMATE RECEPTOR IONOTROPIC, NMDA 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GLUN1,GLUTAMATE [NMDA] RECEPTOR SUBUNIT ZETA-1,N-METHYL-D-
COMPND 5 ASPARTATE RECEPTOR SUBUNIT NR1,NMD-R1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: GLUTAMATE RECEPTOR IONOTROPIC, NMDA 2A;
COMPND 9 CHAIN: B;
COMPND 10 SYNONYM: GLUN2A,GLUTAMATE [NMDA] RECEPTOR SUBUNIT EPSILON-1,N-METHYL
COMPND 11 D-ASPARTATE RECEPTOR SUBTYPE 2A,NR2A;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: GRIN1, NMDAR1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 10 ORGANISM_COMMON: RAT;
SOURCE 11 ORGANISM_TAXID: 10116;
SOURCE 12 GENE: GRIN2A;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS NMDA RECEPTOR, ANTAGONIST, TRANSPORT PROTEIN, RECEPTOR
EXPDTA X-RAY DIFFRACTION
AUTHOR T.-C.MOU,P.CONTI,A.PINTO,L.TAMBORINI,S.R.SPRANG,K.B.HANSEN
REVDAT 8 04-OCT-23 5VII 1 REMARK
REVDAT 7 01-JAN-20 5VII 1 REMARK
REVDAT 6 20-SEP-17 5VII 1 REMARK
REVDAT 5 23-AUG-17 5VII 1 JRNL
REVDAT 4 16-AUG-17 5VII 1 JRNL
REVDAT 3 02-AUG-17 5VII 1 JRNL
REVDAT 2 17-MAY-17 5VII 1 OBSLTE SPRSDE REMARK
REVDAT 1 26-APR-17 5VII 0
SPRSDE 17-MAY-17 5VII 5DDX
JRNL AUTH G.E.LIND,T.C.MOU,L.TAMBORINI,M.G.POMPER,C.DE MICHELI,
JRNL AUTH 2 P.CONTI,A.PINTO,K.B.HANSEN
JRNL TITL STRUCTURAL BASIS OF SUBUNIT SELECTIVITY FOR COMPETITIVE NMDA
JRNL TITL 2 RECEPTOR ANTAGONISTS WITH PREFERENCE FOR GLUN2A OVER GLUN2B
JRNL TITL 3 SUBUNITS.
JRNL REF PROC. NATL. ACAD. SCI. V. 114 E6942 2017
JRNL REF 2 U.S.A.
JRNL REFN ESSN 1091-6490
JRNL PMID 28760974
JRNL DOI 10.1073/PNAS.1707752114
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.01
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 42261
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.730
REMARK 3 FREE R VALUE TEST SET COUNT : 2000
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 20.0066 - 4.6839 1.00 3144 156 0.1706 0.2376
REMARK 3 2 4.6839 - 3.7256 1.00 2999 149 0.1483 0.1852
REMARK 3 3 3.7256 - 3.2570 1.00 2978 148 0.1701 0.2207
REMARK 3 4 3.2570 - 2.9602 1.00 2952 147 0.1933 0.2625
REMARK 3 5 2.9602 - 2.7486 0.99 2934 145 0.1946 0.2491
REMARK 3 6 2.7486 - 2.5869 0.99 2911 145 0.2020 0.2667
REMARK 3 7 2.5869 - 2.4576 0.99 2907 144 0.2136 0.3381
REMARK 3 8 2.4576 - 2.3508 0.99 2893 144 0.2134 0.3045
REMARK 3 9 2.3508 - 2.2604 0.99 2886 144 0.2287 0.3197
REMARK 3 10 2.2604 - 2.1825 0.98 2844 141 0.2530 0.3181
REMARK 3 11 2.1825 - 2.1144 0.97 2870 142 0.2633 0.3252
REMARK 3 12 2.1144 - 2.0540 0.95 2777 138 0.2879 0.3411
REMARK 3 13 2.0540 - 2.0000 0.94 2700 135 0.3171 0.3265
REMARK 3 14 2.0000 - 1.9512 0.85 2466 122 0.3530 0.3878
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.330
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.980
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.60
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 4481
REMARK 3 ANGLE : 0.894 6043
REMARK 3 CHIRALITY : 0.054 666
REMARK 3 PLANARITY : 0.006 769
REMARK 3 DIHEDRAL : 11.167 2673
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5VII COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-APR-17.
REMARK 100 THE DEPOSITION ID IS D_1000227479.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-JUN-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9794
REMARK 200 MONOCHROMATOR : SI (111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42271
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.951
REMARK 200 RESOLUTION RANGE LOW (A) : 20.010
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.5900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.47600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.920
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: 4NF8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIA ACETATE, PEG 4000, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 27.29100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.29800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.68100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.29800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.29100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.68100
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: 3070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 6.0 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 MET A 2
REMARK 465 SER A 3
REMARK 465 THR A 4
REMARK 465 ASN A 48
REMARK 465 ASP A 49
REMARK 465 THR A 50
REMARK 465 SER A 51
REMARK 465 PRO A 52
REMARK 465 GLY A 53
REMARK 465 SER A 54
REMARK 465 PRO A 55
REMARK 465 ARG A 56
REMARK 465 HIS A 57
REMARK 465 ASN A 99
REMARK 465 ASN A 100
REMARK 465 SER A 101
REMARK 465 TYR A 287
REMARK 465 GLN A 288
REMARK 465 GLU A 289
REMARK 465 CYS A 290
REMARK 465 ASP A 291
REMARK 465 SER A 292
REMARK 465 SER B 4
REMARK 465 ASP B 5
REMARK 465 PRO B 27
REMARK 465 LEU B 28
REMARK 465 HIS B 285
REMARK 465 ASN B 286
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O TYR B 188 O HOH B 401 1.95
REMARK 500 NH1 ARG B 142 O CYS B 229 2.01
REMARK 500 O HOH A 1232 O HOH A 1245 2.11
REMARK 500 OE1 GLU A 243 O HOH A 1101 2.14
REMARK 500 O HOH A 1222 O HOH B 529 2.15
REMARK 500 OD2 ASP B 6 O HOH B 402 2.16
REMARK 500 NH2 ARG B 72 O HOH B 403 2.17
REMARK 500 O HOH B 597 O HOH B 638 2.18
REMARK 500 O HOH B 630 O HOH B 632 2.18
REMARK 500 OG SER A 192 O HOH A 1102 2.19
REMARK 500 O HOH A 1140 O HOH B 499 2.19
REMARK 500 ND2 ASN A 102 O HOH A 1103 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 1122 O HOH B 534 3444 2.11
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 GLN A 13 84.16 -166.51
REMARK 500 ASN A 79 70.11 56.02
REMARK 500 PRO A 124 70.25 -69.64
REMARK 500 GLN A 144 -150.18 -156.30
REMARK 500 ASN A 166 65.72 -119.03
REMARK 500 THR A 175 -167.81 -128.60
REMARK 500 ASN A 216 -0.16 72.55
REMARK 500 ASP A 257 18.78 55.22
REMARK 500 GLU B 16 98.60 -163.69
REMARK 500 ILE B 25 -166.65 -78.02
REMARK 500 GLU B 30 60.55 -67.87
REMARK 500 ASN B 35 -31.82 84.16
REMARK 500 LYS B 75 80.67 64.79
REMARK 500 LYS B 87 -105.69 -124.90
REMARK 500 ASN B 97 -165.66 -107.38
REMARK 500 THR B 243 -147.71 -153.96
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 GLY A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5DY B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS B 303
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5VIJ RELATED DB: PDB
REMARK 900 RELATED ID: 5VIH RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THIS SAMPLE SEQUENCE MATCHES WITH NCBI REFERENCE SEQUENCE NP_
REMARK 999 036705.3 FOR GLUN2A
DBREF 5VII A 2 152 UNP P35439 NMDZ1_RAT 415 565
DBREF 5VII A 155 292 UNP P35439 NMDZ1_RAT 684 821
DBREF 5VII B 5 142 UNP Q00959 NMDE1_RAT 402 539
DBREF 5VII B 145 286 UNP G3V9C5 G3V9C5_RAT 504 645
SEQADV 5VII GLY A 1 UNP P35439 EXPRESSION TAG
SEQADV 5VII GLY A 153 UNP P35439 LINKER
SEQADV 5VII THR A 154 UNP P35439 LINKER
SEQADV 5VII SER B 4 UNP Q00959 EXPRESSION TAG
SEQADV 5VII GLY B 143 UNP Q00959 LINKER
SEQADV 5VII THR B 144 UNP Q00959 LINKER
SEQRES 1 A 292 GLY MET SER THR ARG LEU LYS ILE VAL THR ILE HIS GLN
SEQRES 2 A 292 GLU PRO PHE VAL TYR VAL LYS PRO THR MET SER ASP GLY
SEQRES 3 A 292 THR CYS LYS GLU GLU PHE THR VAL ASN GLY ASP PRO VAL
SEQRES 4 A 292 LYS LYS VAL ILE CYS THR GLY PRO ASN ASP THR SER PRO
SEQRES 5 A 292 GLY SER PRO ARG HIS THR VAL PRO GLN CYS CYS TYR GLY
SEQRES 6 A 292 PHE CYS ILE ASP LEU LEU ILE LYS LEU ALA ARG THR MET
SEQRES 7 A 292 ASN PHE THR TYR GLU VAL HIS LEU VAL ALA ASP GLY LYS
SEQRES 8 A 292 PHE GLY THR GLN GLU ARG VAL ASN ASN SER ASN LYS LYS
SEQRES 9 A 292 GLU TRP ASN GLY MET MET GLY GLU LEU LEU SER GLY GLN
SEQRES 10 A 292 ALA ASP MET ILE VAL ALA PRO LEU THR ILE ASN ASN GLU
SEQRES 11 A 292 ARG ALA GLN TYR ILE GLU PHE SER LYS PRO PHE LYS TYR
SEQRES 12 A 292 GLN GLY LEU THR ILE LEU VAL LYS LYS GLY THR ARG ILE
SEQRES 13 A 292 THR GLY ILE ASN ASP PRO ARG LEU ARG ASN PRO SER ASP
SEQRES 14 A 292 LYS PHE ILE TYR ALA THR VAL LYS GLN SER SER VAL ASP
SEQRES 15 A 292 ILE TYR PHE ARG ARG GLN VAL GLU LEU SER THR MET TYR
SEQRES 16 A 292 ARG HIS MET GLU LYS HIS ASN TYR GLU SER ALA ALA GLU
SEQRES 17 A 292 ALA ILE GLN ALA VAL ARG ASP ASN LYS LEU HIS ALA PHE
SEQRES 18 A 292 ILE TRP ASP SER ALA VAL LEU GLU PHE GLU ALA SER GLN
SEQRES 19 A 292 LYS CYS ASP LEU VAL THR THR GLY GLU LEU PHE PHE ARG
SEQRES 20 A 292 SER GLY PHE GLY ILE GLY MET ARG LYS ASP SER PRO TRP
SEQRES 21 A 292 LYS GLN ASN VAL SER LEU SER ILE LEU LYS SER HIS GLU
SEQRES 22 A 292 ASN GLY PHE MET GLU ASP LEU ASP LYS THR TRP VAL ARG
SEQRES 23 A 292 TYR GLN GLU CYS ASP SER
SEQRES 1 B 283 SER ASP ASP ASN HIS LEU SER ILE VAL THR LEU GLU GLU
SEQRES 2 B 283 ALA PRO PHE VAL ILE VAL GLU ASP ILE ASP PRO LEU THR
SEQRES 3 B 283 GLU THR CYS VAL ARG ASN THR VAL PRO CYS ARG LYS PHE
SEQRES 4 B 283 VAL LYS ILE ASN ASN SER THR ASN GLU GLY MET ASN VAL
SEQRES 5 B 283 LYS LYS CYS CYS LYS GLY PHE CYS ILE ASP ILE LEU LYS
SEQRES 6 B 283 LYS LEU SER ARG THR VAL LYS PHE THR TYR ASP LEU TYR
SEQRES 7 B 283 LEU VAL THR ASN GLY LYS HIS GLY LYS LYS VAL ASN ASN
SEQRES 8 B 283 VAL TRP ASN GLY MET ILE GLY GLU VAL VAL TYR GLN ARG
SEQRES 9 B 283 ALA VAL MET ALA VAL GLY SER LEU THR ILE ASN GLU GLU
SEQRES 10 B 283 ARG SER GLU VAL VAL ASP PHE SER VAL PRO PHE VAL GLU
SEQRES 11 B 283 THR GLY ILE SER VAL MET VAL SER ARG GLY THR GLN VAL
SEQRES 12 B 283 THR GLY LEU SER ASP LYS LYS PHE GLN ARG PRO HIS ASP
SEQRES 13 B 283 TYR SER PRO PRO PHE ARG PHE GLY THR VAL PRO ASN GLY
SEQRES 14 B 283 SER THR GLU ARG ASN ILE ARG ASN ASN TYR PRO TYR MET
SEQRES 15 B 283 HIS GLN TYR MET THR ARG PHE ASN GLN ARG GLY VAL GLU
SEQRES 16 B 283 ASP ALA LEU VAL SER LEU LYS THR GLY LYS LEU ASP ALA
SEQRES 17 B 283 PHE ILE TYR ASP ALA ALA VAL LEU ASN TYR LYS ALA GLY
SEQRES 18 B 283 ARG ASP GLU GLY CYS LYS LEU VAL THR ILE GLY SER GLY
SEQRES 19 B 283 TYR ILE PHE ALA THR THR GLY TYR GLY ILE ALA LEU GLN
SEQRES 20 B 283 LYS GLY SER PRO TRP LYS ARG GLN ILE ASP LEU ALA LEU
SEQRES 21 B 283 LEU GLN PHE VAL GLY ASP GLY GLU MET GLU GLU LEU GLU
SEQRES 22 B 283 THR LEU TRP LEU THR GLY ILE CYS HIS ASN
HET GLY A1001 5
HET 5DY B 301 24
HET PEG B 302 7
HET TRS B 303 8
HETNAM GLY GLYCINE
HETNAM 5DY 5-[(2R)-2-AMINO-2-CARBOXYETHYL]-1-[4-(3-FLUOROPROPYL)
HETNAM 2 5DY PHENYL]-1H-PYRAZOLE-3-CARBOXYLIC ACID
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETSYN TRS TRIS BUFFER
FORMUL 3 GLY C2 H5 N O2
FORMUL 4 5DY C16 H18 F N3 O4
FORMUL 5 PEG C4 H10 O3
FORMUL 6 TRS C4 H12 N O3 1+
FORMUL 7 HOH *422(H2 O)
HELIX 1 AA1 GLY A 65 ASN A 79 1 15
HELIX 2 AA2 ASN A 107 SER A 115 1 9
HELIX 3 AA3 ASN A 128 GLN A 133 1 6
HELIX 4 AA4 ASP A 161 ASN A 166 1 6
HELIX 5 AA5 SER A 179 ARG A 187 1 9
HELIX 6 AA6 GLN A 188 GLU A 190 5 3
HELIX 7 AA7 LEU A 191 LYS A 200 1 10
HELIX 8 AA8 SER A 205 ASP A 215 1 11
HELIX 9 AA9 SER A 225 LYS A 235 1 11
HELIX 10 AB1 TRP A 260 ASN A 274 1 15
HELIX 11 AB2 GLY A 275 VAL A 285 1 11
HELIX 12 AB3 GLY B 61 LYS B 75 1 15
HELIX 13 AB4 ASN B 97 TYR B 105 1 9
HELIX 14 AB5 ASN B 118 VAL B 125 1 8
HELIX 15 AB6 ASP B 151 ARG B 156 1 6
HELIX 16 AB7 PRO B 157 TYR B 160 5 4
HELIX 17 AB8 GLY B 172 TYR B 182 1 11
HELIX 18 AB9 TYR B 182 THR B 190 1 9
HELIX 19 AC1 ARG B 191 ASN B 193 5 3
HELIX 20 AC2 GLY B 196 THR B 206 1 11
HELIX 21 AC3 ALA B 216 ARG B 225 1 10
HELIX 22 AC4 ASP B 226 CYS B 229 5 4
HELIX 23 AC5 GLY B 235 ILE B 239 5 5
HELIX 24 AC6 TRP B 255 ASP B 269 1 15
HELIX 25 AC7 GLY B 270 LEU B 280 1 11
SHEET 1 AA1 8 TYR A 18 LYS A 20 0
SHEET 2 AA1 8 VAL A 59 TYR A 64 -1 O CYS A 62 N LYS A 20
SHEET 3 AA1 8 VAL A 42 GLY A 46 -1 N VAL A 42 O CYS A 63
SHEET 4 AA1 8 TYR A 82 LEU A 86 1 O LEU A 86 N THR A 45
SHEET 5 AA1 8 LEU A 6 THR A 10 1 N ILE A 8 O GLU A 83
SHEET 6 AA1 8 MET A 120 ILE A 121 1 O MET A 120 N VAL A 9
SHEET 7 AA1 8 GLY A 253 ARG A 255 -1 O GLY A 253 N ILE A 121
SHEET 8 AA1 8 ILE A 135 PHE A 137 -1 N GLU A 136 O MET A 254
SHEET 1 AA2 2 GLN A 95 ARG A 97 0
SHEET 2 AA2 2 LYS A 104 TRP A 106 -1 O GLU A 105 N GLU A 96
SHEET 1 AA3 4 TYR A 173 ALA A 174 0
SHEET 2 AA3 4 ALA A 220 ASP A 224 1 O ILE A 222 N ALA A 174
SHEET 3 AA3 4 LYS A 142 LYS A 151 -1 N LEU A 149 O PHE A 221
SHEET 4 AA3 4 LEU A 238 THR A 240 -1 O VAL A 239 N VAL A 150
SHEET 1 AA4 4 TYR A 173 ALA A 174 0
SHEET 2 AA4 4 ALA A 220 ASP A 224 1 O ILE A 222 N ALA A 174
SHEET 3 AA4 4 LYS A 142 LYS A 151 -1 N LEU A 149 O PHE A 221
SHEET 4 AA4 4 PHE A 246 PHE A 250 -1 O PHE A 246 N LEU A 146
SHEET 1 AA5 5 THR B 77 LEU B 82 0
SHEET 2 AA5 5 HIS B 8 THR B 13 1 N LEU B 9 O THR B 77
SHEET 3 AA5 5 MET B 110 ALA B 111 1 O MET B 110 N VAL B 12
SHEET 4 AA5 5 ALA B 248 LEU B 249 -1 O ALA B 248 N ALA B 111
SHEET 5 AA5 5 ASP B 126 PHE B 127 -1 N ASP B 126 O LEU B 249
SHEET 1 AA6 3 ILE B 21 GLU B 23 0
SHEET 2 AA6 3 GLY B 52 LYS B 60 -1 O CYS B 58 N GLU B 23
SHEET 3 AA6 3 VAL B 37 LYS B 44 -1 N LYS B 41 O VAL B 55
SHEET 1 AA7 2 LYS B 91 VAL B 92 0
SHEET 2 AA7 2 VAL B 95 TRP B 96 -1 O VAL B 95 N VAL B 92
SHEET 1 AA8 4 PHE B 166 GLY B 167 0
SHEET 2 AA8 4 ALA B 211 ASP B 215 1 O ILE B 213 N GLY B 167
SHEET 3 AA8 4 VAL B 132 SER B 141 -1 N SER B 137 O TYR B 214
SHEET 4 AA8 4 LEU B 231 THR B 233 -1 O VAL B 232 N VAL B 140
SHEET 1 AA9 4 PHE B 166 GLY B 167 0
SHEET 2 AA9 4 ALA B 211 ASP B 215 1 O ILE B 213 N GLY B 167
SHEET 3 AA9 4 VAL B 132 SER B 141 -1 N SER B 137 O TYR B 214
SHEET 4 AA9 4 PHE B 240 TYR B 245 -1 O PHE B 240 N ILE B 136
SSBOND 1 CYS A 28 CYS A 62 1555 1555 2.03
SSBOND 2 CYS A 44 CYS A 63 1555 1555 2.05
SSBOND 3 CYS B 32 CYS B 58 1555 1555 2.04
SSBOND 4 CYS B 39 CYS B 59 1555 1555 2.04
SSBOND 5 CYS B 229 CYS B 284 1555 1555 2.02
LINK ND1 HIS B 88 O1 TRS B 303 1555 1555 1.31
CISPEP 1 GLU A 14 PRO A 15 0 3.49
CISPEP 2 ALA B 17 PRO B 18 0 1.94
CISPEP 3 SER B 161 PRO B 162 0 -3.05
SITE 1 AC1 7 PHE A 92 PRO A 124 THR A 126 ARG A 131
SITE 2 AC1 7 SER A 179 SER A 180 ASP A 224
SITE 1 AC2 22 HIS B 88 SER B 114 THR B 116 ILE B 117
SITE 2 AC2 22 ASN B 118 ARG B 121 GLY B 135 ILE B 136
SITE 3 AC2 22 GLY B 172 SER B 173 THR B 174 TYR B 214
SITE 4 AC2 22 ASP B 215 ALA B 241 THR B 243 TYR B 245
SITE 5 AC2 22 TRS B 303 HOH B 432 HOH B 452 HOH B 469
SITE 6 AC2 22 HOH B 507 HOH B 518
SITE 1 AC3 6 GLU A 273 ARG B 176 ASN B 180 ASN B 181
SITE 2 AC3 6 HOH B 415 HOH B 493
SITE 1 AC4 8 LYS B 87 HIS B 88 GLY B 89 ASN B 97
SITE 2 AC4 8 ARG B 121 5DY B 301 HOH B 465 HOH B 518
CRYST1 54.582 87.362 122.596 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 0.018321 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011447 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008157 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
