HEADER MEMBRANE PROTEIN 02-FEB-09 3G3H
TITLE CRYSTAL STRUCTURE OF THE GLUR6 LIGAND BINDING DOMAIN DIMER K665R I749L
TITLE 2 Q753K MUTANT WITH GLUTAMATE AND NACL AT 1.5 ANGSTROM RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMATE RECEPTOR, IONOTROPIC KAINATE 2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 429-544, 667-806;
COMPND 5 SYNONYM: GLUTAMATE RECEPTOR 6, GLUR-6, GLUR6;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_TAXID: 10116;
SOURCE 4 GENE: GRIK2;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: ORIGAMIB (DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET22B MODIFIED
KEYWDS MEMBRANE PROTEIN, CELL JUNCTION, CELL MEMBRANE, GLYCOPROTEIN, ION
KEYWDS 2 TRANSPORT, IONIC CHANNEL, MEMBRANE, POSTSYNAPTIC CELL MEMBRANE,
KEYWDS 3 RECEPTOR, RNA EDITING, SYNAPSE, TRANSMEMBRANE, TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR C.CHAUDHRY,M.L.MAYER
REVDAT 4 20-OCT-21 3G3H 1 REMARK SEQADV LINK
REVDAT 3 01-NOV-17 3G3H 1 REMARK
REVDAT 2 26-JUL-17 3G3H 1 SOURCE
REVDAT 1 02-JUN-09 3G3H 0
JRNL AUTH C.CHAUDHRY,M.C.WESTON,P.SCHUCK,C.ROSENMUND,M.L.MAYER
JRNL TITL STABILITY OF LIGAND-BINDING DOMAIN DIMER ASSEMBLY CONTROLS
JRNL TITL 2 KAINATE RECEPTOR DESENSITIZATION.
JRNL REF EMBO J. V. 28 1518 2009
JRNL REFN ISSN 0261-4189
JRNL PMID 19339989
JRNL DOI 10.1038/EMBOJ.2009.86
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.53
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 83975
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.149
REMARK 3 R VALUE (WORKING SET) : 0.147
REMARK 3 FREE R VALUE : 0.176
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4201
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 29.5311 - 4.6550 0.94 2620 119 0.1575 0.1631
REMARK 3 2 4.6550 - 3.6971 0.96 2605 148 0.1184 0.1380
REMARK 3 3 3.6971 - 3.2304 0.96 2637 153 0.1279 0.1532
REMARK 3 4 3.2304 - 2.9353 0.97 2641 143 0.1408 0.1780
REMARK 3 5 2.9353 - 2.7251 0.98 2644 151 0.1526 0.1923
REMARK 3 6 2.7251 - 2.5645 0.98 2671 141 0.1427 0.1864
REMARK 3 7 2.5645 - 2.4361 0.98 2656 140 0.1427 0.1654
REMARK 3 8 2.4361 - 2.3301 0.98 2654 165 0.1420 0.1800
REMARK 3 9 2.3301 - 2.2405 0.98 2672 137 0.1272 0.1485
REMARK 3 10 2.2405 - 2.1632 0.98 2689 138 0.1234 0.1413
REMARK 3 11 2.1632 - 2.0956 0.99 2662 147 0.1220 0.1617
REMARK 3 12 2.0956 - 2.0357 0.99 2692 133 0.1297 0.1554
REMARK 3 13 2.0357 - 1.9821 0.99 2651 150 0.1285 0.1741
REMARK 3 14 1.9821 - 1.9338 0.99 2723 120 0.1386 0.1641
REMARK 3 15 1.9338 - 1.8898 0.99 2692 160 0.1380 0.1752
REMARK 3 16 1.8898 - 1.8496 0.99 2672 151 0.1453 0.1897
REMARK 3 17 1.8496 - 1.8126 0.99 2692 150 0.1437 0.1671
REMARK 3 18 1.8126 - 1.7784 0.99 2678 143 0.1440 0.1814
REMARK 3 19 1.7784 - 1.7466 0.99 2704 142 0.1457 0.1726
REMARK 3 20 1.7466 - 1.7170 1.00 2699 152 0.1492 0.2134
REMARK 3 21 1.7170 - 1.6893 0.99 2698 117 0.1552 0.1840
REMARK 3 22 1.6893 - 1.6634 0.99 2690 150 0.1620 0.1783
REMARK 3 23 1.6634 - 1.6389 1.00 2699 135 0.1649 0.2233
REMARK 3 24 1.6389 - 1.6158 0.99 2754 133 0.1708 0.2081
REMARK 3 25 1.6158 - 1.5940 0.99 2681 137 0.1709 0.2248
REMARK 3 26 1.5940 - 1.5733 0.97 2629 136 0.1780 0.1904
REMARK 3 27 1.5733 - 1.5536 0.97 2619 132 0.1797 0.2173
REMARK 3 28 1.5536 - 1.5349 0.96 2609 125 0.1856 0.2119
REMARK 3 29 1.5349 - 1.5170 0.94 2583 124 0.1963 0.2407
REMARK 3 30 1.5170 - 1.5000 0.93 2458 129 0.2068 0.2801
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 : 0.41
REMARK 3 B_SOL : 41.75
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.50
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 : 0.010 8822
REMARK 3 ANGLE : 1.125 16050
REMARK 3 CHIRALITY : 0.093 665
REMARK 3 PLANARITY : 0.006 1333
REMARK 3 DIHEDRAL : 14.302 2284
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESID 3:108)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.0503 27.9619 -3.0498
REMARK 3 T TENSOR
REMARK 3 T11: 0.0978 T22: 0.0660
REMARK 3 T33: 0.0768 T12: -0.0006
REMARK 3 T13: 0.0073 T23: 0.0201
REMARK 3 L TENSOR
REMARK 3 L11: 0.5863 L22: 1.0006
REMARK 3 L33: 0.7176 L12: 0.2929
REMARK 3 L13: 0.0295 L23: -0.0365
REMARK 3 S TENSOR
REMARK 3 S11: -0.0429 S12: 0.0684 S13: 0.0821
REMARK 3 S21: -0.1634 S22: 0.0570 S23: 0.0485
REMARK 3 S31: -0.0765 S32: 0.0013 S33: -0.0181
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESID 109:216)
REMARK 3 ORIGIN FOR THE GROUP (A): 24.3975 33.8104 17.3512
REMARK 3 T TENSOR
REMARK 3 T11: 0.0676 T22: 0.0504
REMARK 3 T33: 0.0713 T12: -0.0005
REMARK 3 T13: 0.0079 T23: -0.0074
REMARK 3 L TENSOR
REMARK 3 L11: 0.7063 L22: 1.1252
REMARK 3 L33: 0.7520 L12: 0.2366
REMARK 3 L13: 0.0432 L23: 0.4205
REMARK 3 S TENSOR
REMARK 3 S11: 0.0227 S12: -0.0178 S13: 0.0669
REMARK 3 S21: 0.0620 S22: -0.0062 S23: -0.1023
REMARK 3 S31: -0.0104 S32: 0.0425 S33: -0.0223
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND (RESID 217:252)
REMARK 3 ORIGIN FOR THE GROUP (A): 16.4740 15.4205 -1.1179
REMARK 3 T TENSOR
REMARK 3 T11: 0.0882 T22: 0.0746
REMARK 3 T33: 0.0777 T12: -0.0038
REMARK 3 T13: 0.0118 T23: -0.0034
REMARK 3 L TENSOR
REMARK 3 L11: 0.1076 L22: 0.6786
REMARK 3 L33: 0.1469 L12: 0.2781
REMARK 3 L13: 0.0612 L23: -0.2225
REMARK 3 S TENSOR
REMARK 3 S11: -0.0349 S12: 0.1260 S13: 0.0016
REMARK 3 S21: -0.1513 S22: 0.0470 S23: -0.0545
REMARK 3 S31: 0.0371 S32: 0.0187 S33: 0.0028
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN B AND (RESID 2:108)
REMARK 3 ORIGIN FOR THE GROUP (A): 5.1805 0.6246 16.7495
REMARK 3 T TENSOR
REMARK 3 T11: 0.0390 T22: 0.0536
REMARK 3 T33: 0.0498 T12: -0.0016
REMARK 3 T13: -0.0100 T23: 0.0114
REMARK 3 L TENSOR
REMARK 3 L11: 1.0525 L22: 0.6432
REMARK 3 L33: 0.5234 L12: -0.0122
REMARK 3 L13: -0.1896 L23: 0.0739
REMARK 3 S TENSOR
REMARK 3 S11: 0.0097 S12: -0.0533 S13: -0.0673
REMARK 3 S21: 0.0145 S22: 0.0144 S23: 0.0593
REMARK 3 S31: 0.0192 S32: -0.0473 S33: -0.0198
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN B AND (RESID 109:216)
REMARK 3 ORIGIN FOR THE GROUP (A): 27.7589 -4.7161 11.3192
REMARK 3 T TENSOR
REMARK 3 T11: 0.0412 T22: 0.0533
REMARK 3 T33: 0.0536 T12: 0.0068
REMARK 3 T13: -0.0003 T23: 0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 1.1055 L22: 0.5799
REMARK 3 L33: 0.8010 L12: -0.2387
REMARK 3 L13: 0.0740 L23: -0.1066
REMARK 3 S TENSOR
REMARK 3 S11: 0.0279 S12: 0.0018 S13: -0.0708
REMARK 3 S21: -0.0067 S22: -0.0354 S23: -0.0528
REMARK 3 S31: 0.0645 S32: 0.0735 S33: 0.0062
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN B AND (RESID 217:252)
REMARK 3 ORIGIN FOR THE GROUP (A): 7.5992 13.4435 16.9761
REMARK 3 T TENSOR
REMARK 3 T11: 0.0540 T22: 0.0595
REMARK 3 T33: 0.0646 T12: 0.0044
REMARK 3 T13: 0.0051 T23: -0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 0.4911 L22: 0.6111
REMARK 3 L33: 0.5225 L12: 0.0651
REMARK 3 L13: 0.0231 L23: -0.2838
REMARK 3 S TENSOR
REMARK 3 S11: 0.0262 S12: -0.0477 S13: 0.0902
REMARK 3 S21: 0.0711 S22: 0.0172 S23: 0.0487
REMARK 3 S31: -0.0831 S32: -0.0063 S33: -0.0457
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT WAS STARTED WITH REFMAC_5.2.
REMARK 3 THE FINAL ROUNDS OF REFINEMENT WERE PERFORMED WITH PHENIX AND
REMARK 3 INCLUDED OCCUPANCY REFINEMENT FOR IONS, AND FOR RESIDUES WITH
REMARK 3 ALTERNATIVE CONFORMATIONS.
REMARK 4
REMARK 4 3G3H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-FEB-09.
REMARK 100 THE DEPOSITION ID IS D_1000051375.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-MAR-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00000
REMARK 200 MONOCHROMATOR : SI(220)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 86616
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
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 (%) : 97.9
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : 0.05300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.55
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.020
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: FOURIER DIFFERENCE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 4K, 13% ISOPROPANOL, 0.1 M
REMARK 280 NACITRATE, PH 5.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 56.74950
REMARK 290 SMTRY3 2 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 300 REMARK: THE NATIVE PROTEIN IS BELIEVED TO BE A DIMER OF DIMERS;
REMARK 300 ONLY 1 COPY OF THE DIMER FORMED BY CHAINS A AND B IS PRESENT IN
REMARK 300 THIS CRYSTAL FORM.
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: 2850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 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 ARG A 253
REMARK 465 GLY A 254
REMARK 465 ASN A 255
REMARK 465 GLY A 256
REMARK 465 GLU A 259
REMARK 465 ARG B 253
REMARK 465 GLY B 254
REMARK 465 ASN B 255
REMARK 465 GLY B 256
REMARK 465 PRO B 258
REMARK 465 GLU B 259
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 517 O HOH B 630 2655 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 MET B 162 CG - SD - CE ANGL. DEV. = -14.7 DEGREES
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 GLU A 13 109.55 -161.95
REMARK 500 GLU A 13 111.65 -163.24
REMARK 500 ASN A 72 -169.84 -129.21
REMARK 500 GLU B 13 108.04 -164.73
REMARK 500 GLU B 13 111.63 -166.98
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 263 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU A 12 O
REMARK 620 2 HOH A 483 O 102.8
REMARK 620 3 HOH A 705 O 156.3 80.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 262 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 97 O
REMARK 620 2 GLU A 97 OE2 100.3
REMARK 620 3 ILE A 100 O 82.6 84.9
REMARK 620 4 ASP A 101 OD1 158.3 100.5 93.2
REMARK 620 5 HOH A 345 O 87.3 113.0 160.9 90.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 262 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 97 O
REMARK 620 2 GLU B 97 OE2 99.0
REMARK 620 3 ILE B 100 O 82.6 88.2
REMARK 620 4 ASP B 101 OD1 157.9 102.9 95.2
REMARK 620 5 HOH B 510 O 83.0 106.8 160.6 93.3
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLU A 260
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 261
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 262
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 263
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLU B 260
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 261
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 262
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3G3F RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE GLUR6 WILD TYPE LIGAND BINDING DOMAIN DIMER
REMARK 900 RELATED ID: 3G3G RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE GLUR6 K665R MUTANT LIGAND BINDING DOMAIN
REMARK 900 DIMER
REMARK 900 RELATED ID: 3G3I RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE GLUR6 I442H K494E I749L Q753K MUTANT
REMARK 900 LIGAND BINDING DOMAIN DIMER
REMARK 900 RELATED ID: 3G3J RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE GLUR6 I442H K494E K665R I749L Q753K MUTANT
REMARK 900 LIGAND BINDING DOMAIN DIMER
REMARK 900 RELATED ID: 3G3K RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE GLUR6 I442H K494E K665R I749L Q753K E757Q
REMARK 900 MUTANT LIGAND BINDING DOMAIN DIMER
DBREF 3G3H A 2 117 UNP P42260 GRIK2_RAT 429 544
DBREF 3G3H A 120 259 UNP P42260 GRIK2_RAT 667 806
DBREF 3G3H B 2 117 UNP P42260 GRIK2_RAT 429 544
DBREF 3G3H B 120 259 UNP P42260 GRIK2_RAT 667 806
SEQADV 3G3H GLY A 1 UNP P42260 EXPRESSION TAG
SEQADV 3G3H GLY A 118 UNP P42260 LINKER
SEQADV 3G3H THR A 119 UNP P42260 LINKER
SEQADV 3G3H ARG A 149 UNP P42260 LYS 696 ENGINEERED MUTATION
SEQADV 3G3H LEU A 233 UNP P42260 ILE 780 ENGINEERED MUTATION
SEQADV 3G3H LYS A 237 UNP P42260 GLN 784 ENGINEERED MUTATION
SEQADV 3G3H GLY B 1 UNP P42260 EXPRESSION TAG
SEQADV 3G3H GLY B 118 UNP P42260 LINKER
SEQADV 3G3H THR B 119 UNP P42260 LINKER
SEQADV 3G3H ARG B 149 UNP P42260 LYS 696 ENGINEERED MUTATION
SEQADV 3G3H LEU B 233 UNP P42260 ILE 780 ENGINEERED MUTATION
SEQADV 3G3H LYS B 237 UNP P42260 GLN 784 ENGINEERED MUTATION
SEQRES 1 A 259 GLY SER ASN ARG SER LEU ILE VAL THR THR ILE LEU GLU
SEQRES 2 A 259 GLU PRO TYR VAL LEU PHE LYS LYS SER ASP LYS PRO LEU
SEQRES 3 A 259 TYR GLY ASN ASP ARG PHE GLU GLY TYR CYS ILE ASP LEU
SEQRES 4 A 259 LEU ARG GLU LEU SER THR ILE LEU GLY PHE THR TYR GLU
SEQRES 5 A 259 ILE ARG LEU VAL GLU ASP GLY LYS TYR GLY ALA GLN ASP
SEQRES 6 A 259 ASP VAL ASN GLY GLN TRP ASN GLY MET VAL ARG GLU LEU
SEQRES 7 A 259 ILE ASP HIS LYS ALA ASP LEU ALA VAL ALA PRO LEU ALA
SEQRES 8 A 259 ILE THR TYR VAL ARG GLU LYS VAL ILE ASP PHE SER LYS
SEQRES 9 A 259 PRO PHE MET THR LEU GLY ILE SER ILE LEU TYR ARG LYS
SEQRES 10 A 259 GLY THR PRO ILE ASP SER ALA ASP ASP LEU ALA LYS GLN
SEQRES 11 A 259 THR LYS ILE GLU TYR GLY ALA VAL GLU ASP GLY ALA THR
SEQRES 12 A 259 MET THR PHE PHE LYS ARG SER LYS ILE SER THR TYR ASP
SEQRES 13 A 259 LYS MET TRP ALA PHE MET SER SER ARG ARG GLN SER VAL
SEQRES 14 A 259 LEU VAL LYS SER ASN GLU GLU GLY ILE GLN ARG VAL LEU
SEQRES 15 A 259 THR SER ASP TYR ALA PHE LEU MET GLU SER THR THR ILE
SEQRES 16 A 259 GLU PHE VAL THR GLN ARG ASN CYS ASN LEU THR GLN ILE
SEQRES 17 A 259 GLY GLY LEU ILE ASP SER LYS GLY TYR GLY VAL GLY THR
SEQRES 18 A 259 PRO MET GLY SER PRO TYR ARG ASP LYS ILE THR LEU ALA
SEQRES 19 A 259 ILE LEU LYS LEU GLN GLU GLU GLY LYS LEU HIS MET MET
SEQRES 20 A 259 LYS GLU LYS TRP TRP ARG GLY ASN GLY CYS PRO GLU
SEQRES 1 B 259 GLY SER ASN ARG SER LEU ILE VAL THR THR ILE LEU GLU
SEQRES 2 B 259 GLU PRO TYR VAL LEU PHE LYS LYS SER ASP LYS PRO LEU
SEQRES 3 B 259 TYR GLY ASN ASP ARG PHE GLU GLY TYR CYS ILE ASP LEU
SEQRES 4 B 259 LEU ARG GLU LEU SER THR ILE LEU GLY PHE THR TYR GLU
SEQRES 5 B 259 ILE ARG LEU VAL GLU ASP GLY LYS TYR GLY ALA GLN ASP
SEQRES 6 B 259 ASP VAL ASN GLY GLN TRP ASN GLY MET VAL ARG GLU LEU
SEQRES 7 B 259 ILE ASP HIS LYS ALA ASP LEU ALA VAL ALA PRO LEU ALA
SEQRES 8 B 259 ILE THR TYR VAL ARG GLU LYS VAL ILE ASP PHE SER LYS
SEQRES 9 B 259 PRO PHE MET THR LEU GLY ILE SER ILE LEU TYR ARG LYS
SEQRES 10 B 259 GLY THR PRO ILE ASP SER ALA ASP ASP LEU ALA LYS GLN
SEQRES 11 B 259 THR LYS ILE GLU TYR GLY ALA VAL GLU ASP GLY ALA THR
SEQRES 12 B 259 MET THR PHE PHE LYS ARG SER LYS ILE SER THR TYR ASP
SEQRES 13 B 259 LYS MET TRP ALA PHE MET SER SER ARG ARG GLN SER VAL
SEQRES 14 B 259 LEU VAL LYS SER ASN GLU GLU GLY ILE GLN ARG VAL LEU
SEQRES 15 B 259 THR SER ASP TYR ALA PHE LEU MET GLU SER THR THR ILE
SEQRES 16 B 259 GLU PHE VAL THR GLN ARG ASN CYS ASN LEU THR GLN ILE
SEQRES 17 B 259 GLY GLY LEU ILE ASP SER LYS GLY TYR GLY VAL GLY THR
SEQRES 18 B 259 PRO MET GLY SER PRO TYR ARG ASP LYS ILE THR LEU ALA
SEQRES 19 B 259 ILE LEU LYS LEU GLN GLU GLU GLY LYS LEU HIS MET MET
SEQRES 20 B 259 LYS GLU LYS TRP TRP ARG GLY ASN GLY CYS PRO GLU
HET GLU A 260 18
HET CL A 261 1
HET NA A 262 1
HET NA A 263 1
HET GLU B 260 15
HET CL B 261 1
HET NA B 262 1
HETNAM GLU GLUTAMIC ACID
HETNAM CL CHLORIDE ION
HETNAM NA SODIUM ION
FORMUL 3 GLU 2(C5 H9 N O4)
FORMUL 4 CL 2(CL 1-)
FORMUL 5 NA 3(NA 1+)
FORMUL 10 HOH *710(H2 O)
HELIX 1 1 TYR A 27 ASP A 30 5 4
HELIX 2 2 GLY A 34 GLY A 48 1 15
HELIX 3 3 ASN A 72 ASP A 80 1 9
HELIX 4 4 THR A 93 LYS A 98 1 6
HELIX 5 5 SER A 123 LYS A 129 1 7
HELIX 6 6 GLY A 141 SER A 150 1 10
HELIX 7 7 ILE A 152 ARG A 165 1 14
HELIX 8 8 ARG A 165 VAL A 169 1 5
HELIX 9 9 SER A 173 SER A 184 1 12
HELIX 10 10 SER A 192 ASN A 202 1 11
HELIX 11 11 PRO A 226 GLU A 241 1 16
HELIX 12 12 GLY A 242 TRP A 252 1 11
HELIX 13 13 TYR B 27 ASP B 30 5 4
HELIX 14 14 GLY B 34 GLY B 48 1 15
HELIX 15 15 ASN B 72 ASP B 80 1 9
HELIX 16 16 THR B 93 LYS B 98 1 6
HELIX 17 17 SER B 123 LYS B 129 1 7
HELIX 18 18 GLY B 141 SER B 150 1 10
HELIX 19 19 ILE B 152 ARG B 165 1 14
HELIX 20 20 ARG B 165 LEU B 170 1 6
HELIX 21 21 SER B 173 SER B 184 1 12
HELIX 22 22 SER B 192 ASN B 202 1 11
HELIX 23 23 PRO B 226 GLU B 241 1 16
HELIX 24 24 GLY B 242 TRP B 252 1 11
SHEET 1 A 3 TYR A 51 LEU A 55 0
SHEET 2 A 3 LEU A 6 THR A 10 1 N VAL A 8 O ARG A 54
SHEET 3 A 3 LEU A 85 ALA A 86 1 O LEU A 85 N THR A 9
SHEET 1 B 2 LEU A 18 PHE A 19 0
SHEET 2 B 2 PHE A 32 GLU A 33 -1 O GLU A 33 N LEU A 18
SHEET 1 C 2 ILE A 100 PHE A 102 0
SHEET 2 C 2 GLY A 220 PRO A 222 -1 O THR A 221 N ASP A 101
SHEET 1 D 2 MET A 107 LEU A 109 0
SHEET 2 D 2 LYS A 215 TYR A 217 -1 O LYS A 215 N LEU A 109
SHEET 1 E 5 LEU A 170 VAL A 171 0
SHEET 2 E 5 GLU A 134 VAL A 138 1 N ALA A 137 O VAL A 171
SHEET 3 E 5 TYR A 186 GLU A 191 1 O LEU A 189 N GLY A 136
SHEET 4 E 5 ILE A 111 ARG A 116 -1 N LEU A 114 O PHE A 188
SHEET 5 E 5 LEU A 205 ILE A 208 -1 O THR A 206 N TYR A 115
SHEET 1 F 3 TYR B 51 LEU B 55 0
SHEET 2 F 3 LEU B 6 THR B 10 1 N VAL B 8 O ARG B 54
SHEET 3 F 3 LEU B 85 ALA B 86 1 O LEU B 85 N THR B 9
SHEET 1 G 2 LEU B 18 PHE B 19 0
SHEET 2 G 2 PHE B 32 GLU B 33 -1 O GLU B 33 N LEU B 18
SHEET 1 H 2 ILE B 100 PHE B 102 0
SHEET 2 H 2 GLY B 220 PRO B 222 -1 O THR B 221 N ASP B 101
SHEET 1 I 2 MET B 107 LEU B 109 0
SHEET 2 I 2 LYS B 215 TYR B 217 -1 O LYS B 215 N LEU B 109
SHEET 1 J 4 GLU B 134 GLY B 136 0
SHEET 2 J 4 TYR B 186 GLU B 191 1 O LEU B 189 N GLY B 136
SHEET 3 J 4 ILE B 111 ARG B 116 -1 N LEU B 114 O PHE B 188
SHEET 4 J 4 LEU B 205 ILE B 208 -1 O THR B 206 N TYR B 115
SSBOND 1 CYS A 203 CYS A 257 1555 1555 2.03
SSBOND 2 CYS B 203 CYS B 257 1555 1555 2.04
LINK O LEU A 12 NA NA A 263 1555 1555 2.80
LINK O GLU A 97 NA NA A 262 1555 1555 2.38
LINK OE2 GLU A 97 NA NA A 262 1555 1555 2.48
LINK O ILE A 100 NA NA A 262 1555 1555 2.43
LINK OD1 ASP A 101 NA NA A 262 1555 1555 2.41
LINK NA NA A 262 O HOH A 345 1555 1555 2.32
LINK NA NA A 263 O HOH A 483 1555 1555 2.99
LINK NA NA A 263 O HOH A 705 1555 1555 2.49
LINK O GLU B 97 NA NA B 262 1555 1555 2.41
LINK OE2 GLU B 97 NA NA B 262 1555 1555 2.55
LINK O ILE B 100 NA NA B 262 1555 1555 2.35
LINK OD1 ASP B 101 NA NA B 262 1555 1555 2.36
LINK NA NA B 262 O HOH B 510 1555 1555 2.40
CISPEP 1 GLU A 14 PRO A 15 0 2.59
CISPEP 2 GLU B 14 PRO B 15 0 -1.66
SITE 1 AC1 13 TYR A 61 PRO A 89 LEU A 90 ALA A 91
SITE 2 AC1 13 ARG A 96 GLY A 141 ALA A 142 THR A 143
SITE 3 AC1 13 GLU A 191 HOH A 270 HOH A 281 HOH A 282
SITE 4 AC1 13 HOH A 289
SITE 1 AC2 4 LYS A 104 ARG A 228 LYS B 104 ARG B 228
SITE 1 AC3 5 GLU A 97 ILE A 100 ASP A 101 MET A 223
SITE 2 AC3 5 HOH A 345
SITE 1 AC4 5 ILE A 11 LEU A 12 HOH A 445 HOH A 483
SITE 2 AC4 5 HOH A 705
SITE 1 AC5 13 TYR B 61 PRO B 89 LEU B 90 ALA B 91
SITE 2 AC5 13 ARG B 96 GLY B 141 ALA B 142 THR B 143
SITE 3 AC5 13 GLU B 191 HOH B 271 HOH B 272 HOH B 279
SITE 4 AC5 13 HOH B 284
SITE 1 AC6 2 SER B 5 GLY B 118
SITE 1 AC7 5 GLU B 97 ILE B 100 ASP B 101 MET B 223
SITE 2 AC7 5 HOH B 510
CRYST1 51.136 113.499 52.163 90.00 115.14 90.00 P 1 21 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 0.019556 0.000000 0.009178 0.00000
SCALE2 0.000000 0.008811 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021177 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
