HEADER SIGNALING PROTEIN 05-JUN-16 5KC8
TITLE CRYSTAL STRUCTURE OF THE AMINO-TERMINAL DOMAIN (ATD) OF IGLUR DELTA-2
TITLE 2 (GLUD2)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMATE RECEPTOR IONOTROPIC, DELTA-2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GLUR DELTA-2 SUBUNIT;
COMPND 5 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: GRID2, GLURD2;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HEK293S;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PHLSEC
KEYWDS IONOTROPIC GLUTAMATE RECEPTOR (IGLUR), NEUROTRANSMISSION, SIGNALING
KEYWDS 2 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.ELEGHEERT,J.E.CLAY,C.SIEBOLD,A.R.ARICESCU
REVDAT 3 10-JAN-24 5KC8 1 LINK
REVDAT 2 03-AUG-16 5KC8 1 TITLE
REVDAT 1 27-JUL-16 5KC8 0
JRNL AUTH J.ELEGHEERT,W.KAKEGAWA,J.E.CLAY,N.F.SHANKS,E.BEHIELS,
JRNL AUTH 2 K.MATSUDA,K.KOHDA,E.MIURA,M.ROSSMANN,N.MITAKIDIS,
JRNL AUTH 3 J.MOTOHASHI,V.T.CHANG,C.SIEBOLD,I.H.GREGER,T.NAKAGAWA,
JRNL AUTH 4 M.YUZAKI,A.R.ARICESCU
JRNL TITL STRUCTURAL BASIS FOR INTEGRATION OF GLUD RECEPTORS WITHIN
JRNL TITL 2 SYNAPTIC ORGANIZER COMPLEXES.
JRNL REF SCIENCE V. 353 295 2016
JRNL REFN ESSN 1095-9203
JRNL PMID 27418511
JRNL DOI 10.1126/SCIENCE.AAE0104
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_1772
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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.87
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 44931
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 2242
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 41.8830 - 4.4108 1.00 2880 143 0.1573 0.1719
REMARK 3 2 4.4108 - 3.5015 1.00 2735 147 0.1594 0.1859
REMARK 3 3 3.5015 - 3.0591 1.00 2733 126 0.1888 0.2339
REMARK 3 4 3.0591 - 2.7794 1.00 2706 146 0.1940 0.1960
REMARK 3 5 2.7794 - 2.5803 1.00 2697 131 0.1893 0.2273
REMARK 3 6 2.5803 - 2.4281 1.00 2666 135 0.1942 0.2320
REMARK 3 7 2.4281 - 2.3066 1.00 2650 144 0.1950 0.2131
REMARK 3 8 2.3066 - 2.2062 1.00 2675 143 0.1951 0.2269
REMARK 3 9 2.2062 - 2.1212 1.00 2605 162 0.2105 0.2493
REMARK 3 10 2.1212 - 2.0480 1.00 2643 138 0.2257 0.2653
REMARK 3 11 2.0480 - 1.9840 0.99 2630 150 0.2245 0.3093
REMARK 3 12 1.9840 - 1.9273 1.00 2636 145 0.2376 0.2733
REMARK 3 13 1.9273 - 1.8765 0.99 2589 137 0.2419 0.2786
REMARK 3 14 1.8765 - 1.8308 0.99 2656 132 0.2697 0.3165
REMARK 3 15 1.8308 - 1.7891 0.99 2593 139 0.2750 0.3185
REMARK 3 16 1.7891 - 1.7511 0.98 2595 124 0.3046 0.3420
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 1.00
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.440
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.80
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 3222
REMARK 3 ANGLE : 0.917 4335
REMARK 3 CHIRALITY : 0.037 492
REMARK 3 PLANARITY : 0.005 564
REMARK 3 DIHEDRAL : 12.476 1190
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 5KC8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-JUN-16.
REMARK 100 THE DEPOSITION ID IS D_1000221702.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-JUN-10
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 : DIAMOND
REMARK 200 BEAMLINE : I04
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 : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44958
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 57.030
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 15.30
REMARK 200 R MERGE (I) : 0.07800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : 9.50
REMARK 200 R MERGE FOR SHELL (I) : 1.31400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
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: 2WJW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% (W/V) POLYETHYLENE GLYCOL 1000,
REMARK 280 0.2 M CALCIUM ACETATE, 0.1 M IMIDAZOLE PH 8.0 AND 0.4 M NDSB-221
REMARK 280 (NON-DETERGENT SULFOBETAINE 221), VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 22.55000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.58000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 123.34500
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 22.55000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.58000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 123.34500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 22.55000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 39.58000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 123.34500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 22.55000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 39.58000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 123.34500
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 THE ASSEMBLY REPRESENTED IN THIS ENTRY HAS REGULAR
REMARK 300 CYCLIC POINT SYMMETRY (SCHOENFLIES SYMBOL = C2).
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: 4880 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 45.10000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 GLU A 21
REMARK 465 THR A 22
REMARK 465 GLY A 23
REMARK 465 ASN A 404
REMARK 465 TYR A 405
REMARK 465 GLY A 406
REMARK 465 GLU A 407
REMARK 465 GLU A 408
REMARK 465 LEU A 409
REMARK 465 GLY A 410
REMARK 465 ARG A 411
REMARK 465 THR A 430
REMARK 465 ASP A 431
REMARK 465 LYS A 432
REMARK 465 LYS A 433
REMARK 465 LEU A 434
REMARK 465 GLU A 435
REMARK 465 ASN A 436
REMARK 465 ASN A 437
REMARK 465 MET A 438
REMARK 465 ARG A 439
REMARK 465 GLY A 440
REMARK 465 GLY A 441
REMARK 465 THR A 442
REMARK 465 LYS A 443
REMARK 465 HIS A 444
REMARK 465 HIS A 445
REMARK 465 HIS A 446
REMARK 465 HIS A 447
REMARK 465 HIS A 448
REMARK 465 HIS A 449
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 GLN A 292 CG CD OE1 NE2
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 OD1 ASP A 186 O HOH A 601 2.17
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 THR A 134 44.62 37.59
REMARK 500 ASN A 262 133.76 -170.19
REMARK 500 PRO A 291 156.19 -49.69
REMARK 500 VAL A 422 -66.38 -93.08
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 CA A 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 81 OE1
REMARK 620 2 GLU A 81 OE2 51.8
REMARK 620 3 GLU A 84 OE1 82.3 119.1
REMARK 620 4 GLU A 84 OE2 92.8 89.1 51.1
REMARK 620 5 HOH A 622 O 132.8 175.4 64.0 90.6
REMARK 620 6 HOH A 677 O 66.6 107.2 82.1 131.8 76.4
REMARK 620 7 HOH A 777 O 133.9 82.8 119.9 76.9 92.6 148.4
REMARK 620 8 HOH A 805 O 105.5 86.4 150.2 152.5 91.7 75.2 75.6
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 502 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 639 O
REMARK 620 2 HOH A 669 O 85.5
REMARK 620 3 HOH A 686 O 76.4 108.3
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 505
DBREF 5KC8 A 24 440 UNP O43424 GRID2_HUMAN 24 440
SEQADV 5KC8 GLU A 21 UNP O43424 EXPRESSION TAG
SEQADV 5KC8 THR A 22 UNP O43424 EXPRESSION TAG
SEQADV 5KC8 GLY A 23 UNP O43424 EXPRESSION TAG
SEQADV 5KC8 GLY A 441 UNP O43424 EXPRESSION TAG
SEQADV 5KC8 THR A 442 UNP O43424 EXPRESSION TAG
SEQADV 5KC8 LYS A 443 UNP O43424 EXPRESSION TAG
SEQADV 5KC8 HIS A 444 UNP O43424 EXPRESSION TAG
SEQADV 5KC8 HIS A 445 UNP O43424 EXPRESSION TAG
SEQADV 5KC8 HIS A 446 UNP O43424 EXPRESSION TAG
SEQADV 5KC8 HIS A 447 UNP O43424 EXPRESSION TAG
SEQADV 5KC8 HIS A 448 UNP O43424 EXPRESSION TAG
SEQADV 5KC8 HIS A 449 UNP O43424 EXPRESSION TAG
SEQRES 1 A 429 GLU THR GLY ASP SER ILE ILE HIS ILE GLY ALA ILE PHE
SEQRES 2 A 429 ASP GLU SER ALA LYS LYS ASP ASP GLU VAL PHE ARG THR
SEQRES 3 A 429 ALA VAL GLY ASP LEU ASN GLN ASN GLU GLU ILE LEU GLN
SEQRES 4 A 429 THR GLU LYS ILE THR PHE SER VAL THR PHE VAL ASP GLY
SEQRES 5 A 429 ASN ASN PRO PHE GLN ALA VAL GLN GLU ALA CYS GLU LEU
SEQRES 6 A 429 MET ASN GLN GLY ILE LEU ALA LEU VAL SER SER ILE GLY
SEQRES 7 A 429 CYS THR SER ALA GLY SER LEU GLN SER LEU ALA ASP ALA
SEQRES 8 A 429 MET HIS ILE PRO HIS LEU PHE ILE GLN ARG SER THR ALA
SEQRES 9 A 429 GLY THR PRO ARG SER GLY CYS GLY LEU THR ARG SER ASN
SEQRES 10 A 429 ARG ASN ASP ASP TYR THR LEU SER VAL ARG PRO PRO VAL
SEQRES 11 A 429 TYR LEU HIS ASP VAL ILE LEU ARG VAL VAL THR GLU TYR
SEQRES 12 A 429 ALA TRP GLN LYS PHE ILE ILE PHE TYR ASP SER GLU TYR
SEQRES 13 A 429 ASP ILE ARG GLY ILE GLN GLU PHE LEU ASP LYS VAL SER
SEQRES 14 A 429 GLN GLN GLY MET ASP VAL ALA LEU GLN LYS VAL GLU ASN
SEQRES 15 A 429 ASN ILE ASN LYS MET ILE THR THR LEU PHE ASP THR MET
SEQRES 16 A 429 ARG ILE GLU GLU LEU ASN ARG TYR ARG ASP THR LEU ARG
SEQRES 17 A 429 ARG ALA ILE LEU VAL MET ASN PRO ALA THR ALA LYS SER
SEQRES 18 A 429 PHE ILE THR GLU VAL VAL GLU THR ASN LEU VAL ALA PHE
SEQRES 19 A 429 ASP CYS HIS TRP ILE ILE ILE ASN GLU GLU ILE ASN ASP
SEQRES 20 A 429 VAL ASP VAL GLN GLU LEU VAL ARG ARG SER ILE GLY ARG
SEQRES 21 A 429 LEU THR ILE ILE ARG GLN THR PHE PRO VAL PRO GLN ASN
SEQRES 22 A 429 ILE SER GLN ARG CYS PHE ARG GLY ASN HIS ARG ILE SER
SEQRES 23 A 429 SER THR LEU CYS ASP PRO LYS ASP PRO PHE ALA GLN ASN
SEQRES 24 A 429 MET GLU ILE SER ASN LEU TYR ILE TYR ASP THR VAL LEU
SEQRES 25 A 429 LEU LEU ALA ASN ALA PHE HIS LYS LYS LEU GLU ASP ARG
SEQRES 26 A 429 LYS TRP HIS SER MET ALA SER LEU SER CYS ILE ARG LYS
SEQRES 27 A 429 ASN SER LYS PRO TRP GLN GLY GLY ARG SER MET LEU GLU
SEQRES 28 A 429 THR ILE LYS LYS GLY GLY VAL SER GLY LEU THR GLY GLU
SEQRES 29 A 429 LEU GLU PHE GLY GLU ASN GLY GLY ASN PRO ASN VAL HIS
SEQRES 30 A 429 PHE GLU ILE LEU GLY THR ASN TYR GLY GLU GLU LEU GLY
SEQRES 31 A 429 ARG GLY VAL ARG LYS LEU GLY CYS TRP ASN PRO VAL THR
SEQRES 32 A 429 GLY LEU ASN GLY SER LEU THR ASP LYS LYS LEU GLU ASN
SEQRES 33 A 429 ASN MET ARG GLY GLY THR LYS HIS HIS HIS HIS HIS HIS
HET CA A 501 1
HET CA A 502 1
HET EDO A 503 4
HET EDO A 504 4
HET EDO A 505 4
HETNAM CA CALCIUM ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 CA 2(CA 2+)
FORMUL 4 EDO 3(C2 H6 O2)
FORMUL 7 HOH *237(H2 O)
HELIX 1 AA1 ALA A 37 ASN A 54 1 18
HELIX 2 AA2 ASN A 74 GLY A 89 1 16
HELIX 3 AA3 GLY A 98 HIS A 113 1 16
HELIX 4 AA4 TYR A 151 TYR A 163 1 13
HELIX 5 AA5 ASP A 177 GLY A 180 5 4
HELIX 6 AA6 ILE A 181 GLN A 191 1 11
HELIX 7 AA7 ASN A 203 MET A 215 1 13
HELIX 8 AA8 ARG A 216 LEU A 227 1 12
HELIX 9 AA9 ASN A 235 THR A 249 1 15
HELIX 10 AB1 ASN A 266 SER A 277 1 12
HELIX 11 AB2 ASN A 293 CYS A 298 1 6
HELIX 12 AB3 SER A 306 ASP A 311 1 6
HELIX 13 AB4 ASP A 314 ASN A 319 1 6
HELIX 14 AB5 GLU A 321 ASP A 344 1 24
HELIX 15 AB6 GLY A 365 LYS A 375 1 11
SHEET 1 AA1 5 ILE A 63 VAL A 70 0
SHEET 2 AA1 5 ILE A 27 ASP A 34 1 N PHE A 33 O VAL A 70
SHEET 3 AA1 5 LEU A 93 ILE A 97 1 O VAL A 94 N GLY A 30
SHEET 4 AA1 5 HIS A 116 GLN A 120 1 O LEU A 117 N LEU A 93
SHEET 5 AA1 5 THR A 143 SER A 145 1 O LEU A 144 N HIS A 116
SHEET 1 AA2 8 ASP A 194 LYS A 199 0
SHEET 2 AA2 8 LYS A 167 TYR A 172 1 N ILE A 170 O ALA A 196
SHEET 3 AA2 8 ARG A 229 VAL A 233 1 O VAL A 233 N PHE A 171
SHEET 4 AA2 8 HIS A 257 ILE A 261 1 O ILE A 259 N LEU A 232
SHEET 5 AA2 8 ARG A 280 THR A 287 1 O THR A 282 N ILE A 260
SHEET 6 AA2 8 HIS A 397 GLY A 402 -1 O LEU A 401 N ILE A 283
SHEET 7 AA2 8 ARG A 414 ASN A 420 -1 O TRP A 419 N PHE A 398
SHEET 8 AA2 8 GLY A 424 ASN A 426 -1 O ASN A 426 N CYS A 418
SHEET 1 AA3 2 PHE A 299 ARG A 300 0
SHEET 2 AA3 2 HIS A 303 ARG A 304 -1 O HIS A 303 N ARG A 300
SHEET 1 AA4 2 GLY A 377 GLY A 380 0
SHEET 2 AA4 2 GLY A 383 GLU A 386 -1 O GLY A 383 N GLY A 380
SSBOND 1 CYS A 83 CYS A 355 1555 1555 2.05
SSBOND 2 CYS A 99 CYS A 131 1555 1555 2.04
SSBOND 3 CYS A 298 CYS A 310 1555 1555 2.03
LINK OE1 GLU A 81 CA CA A 501 1555 1555 2.59
LINK OE2 GLU A 81 CA CA A 501 1555 1555 2.39
LINK OE1 GLU A 84 CA CA A 501 1555 1555 2.50
LINK OE2 GLU A 84 CA CA A 501 1555 1555 2.54
LINK CA CA A 501 O HOH A 622 1555 1555 2.30
LINK CA CA A 501 O HOH A 677 1555 1555 2.36
LINK CA CA A 501 O HOH A 777 1555 1555 2.34
LINK CA CA A 501 O HOH A 805 1555 1555 2.46
LINK CA CA A 502 O HOH A 639 1555 1555 2.43
LINK CA CA A 502 O HOH A 669 1555 1555 2.39
LINK CA CA A 502 O HOH A 686 1555 1555 2.41
SITE 1 AC1 6 GLU A 81 GLU A 84 HOH A 622 HOH A 677
SITE 2 AC1 6 HOH A 777 HOH A 805
SITE 1 AC2 3 HOH A 639 HOH A 669 HOH A 686
SITE 1 AC3 6 CYS A 83 ASN A 87 SER A 354 CYS A 355
SITE 2 AC3 6 ILE A 356 HOH A 634
SITE 1 AC4 4 GLN A 80 ALA A 111 HOH A 707 HOH A 797
SITE 1 AC5 6 SER A 122 ARG A 147 GLU A 264 ILE A 322
SITE 2 AC5 6 SER A 323 HOH A 642
CRYST1 45.100 79.160 246.690 90.00 90.00 90.00 I 2 2 2 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 0.022173 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012633 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004054 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
