HEADER MEMBRANE PROTEIN 15-JAN-09 3FVG
TITLE CRYSTAL STRUCTURE OF THE HUMAN GLUTAMATE RECEPTOR, GLUR5, LIGAND-
TITLE 2 BINDING CORE IN COMPLEX WITH MSVIII-19 IN SPACE GROUP P1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMATE RECEPTOR, IONOTROPIC KAINATE 1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: LIGAND-BINDING DOMAIN, UNP RESIDUES 445-559, 682-820;
COMPND 5 SYNONYM: GLUTAMATE RECEPTOR 5, GLUR-5, GLUR5, EXCITATORY AMINO ACID
COMPND 6 RECEPTOR 3, EAA3;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PCOLD-1
KEYWDS GLUTAMATE RECEPTOR, DYSIHERBAINE ANALOGUE, LIGAND-BINDING DOMAIN,
KEYWDS 2 MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.UNNO,M.SASAKI,M.IKEDA-SAITO
REVDAT 4 01-NOV-23 3FVG 1 REMARK SEQADV
REVDAT 3 16-AUG-17 3FVG 1 SOURCE REMARK
REVDAT 2 26-OCT-11 3FVG 1 JRNL VERSN
REVDAT 1 19-JAN-10 3FVG 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. 1.50 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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.24
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 75825
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) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.192
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4002
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) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5408
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.49
REMARK 3 BIN R VALUE (WORKING SET) : 0.1980
REMARK 3 BIN FREE R VALUE SET COUNT : 303
REMARK 3 BIN FREE R VALUE : 0.2390
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4028
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 104
REMARK 3 SOLVENT ATOMS : 371
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.63
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.05000
REMARK 3 B22 (A**2) : -0.31000
REMARK 3 B33 (A**2) : 0.28000
REMARK 3 B12 (A**2) : -0.02000
REMARK 3 B13 (A**2) : 0.10000
REMARK 3 B23 (A**2) : -0.07000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.073
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.073
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.042
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.160
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.951
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4293 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5829 ; 1.266 ; 1.998
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 541 ; 5.562 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 177 ;30.093 ;24.350
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 767 ;12.372 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 23 ;11.931 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 655 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3141 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1980 ; 0.197 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3037 ; 0.308 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 368 ; 0.104 ; 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): 60 ; 0.173 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 12 ; 0.123 ; 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): 2675 ; 0.765 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4207 ; 1.117 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1861 ; 1.793 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1606 ; 2.702 ; 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 : 8
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 415 A 517
REMARK 3 RESIDUE RANGE : A 750 A 790
REMARK 3 ORIGIN FOR THE GROUP (A): 0.7660 4.7730 18.2270
REMARK 3 T TENSOR
REMARK 3 T11: -0.0329 T22: -0.0280
REMARK 3 T33: -0.0148 T12: 0.0232
REMARK 3 T13: -0.0013 T23: -0.0018
REMARK 3 L TENSOR
REMARK 3 L11: 0.5660 L22: 0.8750
REMARK 3 L33: 0.7033 L12: 0.0983
REMARK 3 L13: 0.0444 L23: 0.0924
REMARK 3 S TENSOR
REMARK 3 S11: -0.0551 S12: -0.0548 S13: 0.0196
REMARK 3 S21: 0.0124 S22: 0.0276 S23: -0.0327
REMARK 3 S31: 0.0286 S32: 0.0467 S33: 0.0275
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 415 B 517
REMARK 3 RESIDUE RANGE : B 750 B 790
REMARK 3 ORIGIN FOR THE GROUP (A): 0.7590 13.8130 -10.7740
REMARK 3 T TENSOR
REMARK 3 T11: -0.0303 T22: -0.0258
REMARK 3 T33: -0.0101 T12: -0.0182
REMARK 3 T13: -0.0024 T23: 0.0077
REMARK 3 L TENSOR
REMARK 3 L11: 0.5766 L22: 0.8758
REMARK 3 L33: 0.6889 L12: 0.1191
REMARK 3 L13: 0.0252 L23: 0.2537
REMARK 3 S TENSOR
REMARK 3 S11: -0.0685 S12: 0.0718 S13: 0.0049
REMARK 3 S21: -0.0329 S22: 0.0368 S23: 0.0193
REMARK 3 S31: -0.0536 S32: 0.0698 S33: 0.0317
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 522 A 746
REMARK 3 ORIGIN FOR THE GROUP (A): -16.3740 21.7830 21.0990
REMARK 3 T TENSOR
REMARK 3 T11: -0.0276 T22: -0.0243
REMARK 3 T33: -0.0215 T12: 0.0453
REMARK 3 T13: -0.0077 T23: -0.0046
REMARK 3 L TENSOR
REMARK 3 L11: 1.5411 L22: 1.6474
REMARK 3 L33: 0.5489 L12: -0.0997
REMARK 3 L13: -0.1737 L23: -0.0792
REMARK 3 S TENSOR
REMARK 3 S11: -0.0222 S12: -0.1065 S13: 0.0533
REMARK 3 S21: 0.0720 S22: 0.0564 S23: 0.0510
REMARK 3 S31: -0.0855 S32: -0.0843 S33: -0.0342
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 522 B 746
REMARK 3 ORIGIN FOR THE GROUP (A): -16.2710 -3.1900 -13.8880
REMARK 3 T TENSOR
REMARK 3 T11: -0.0212 T22: -0.0150
REMARK 3 T33: -0.0169 T12: -0.0327
REMARK 3 T13: 0.0086 T23: -0.0034
REMARK 3 L TENSOR
REMARK 3 L11: 0.9129 L22: 1.2968
REMARK 3 L33: 0.5913 L12: -0.0381
REMARK 3 L13: 0.0411 L23: -0.0549
REMARK 3 S TENSOR
REMARK 3 S11: 0.0123 S12: 0.0278 S13: -0.0037
REMARK 3 S21: -0.0518 S22: 0.0050 S23: 0.0696
REMARK 3 S31: 0.0931 S32: -0.1075 S33: -0.0173
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 518 A 521
REMARK 3 RESIDUE RANGE : A 747 A 749
REMARK 3 ORIGIN FOR THE GROUP (A): -7.5690 9.5880 11.0390
REMARK 3 T TENSOR
REMARK 3 T11: -0.0135 T22: -0.0088
REMARK 3 T33: 0.0040 T12: 0.0213
REMARK 3 T13: 0.0002 T23: -0.0022
REMARK 3 L TENSOR
REMARK 3 L11: 0.2510 L22: 3.8937
REMARK 3 L33: 0.9240 L12: -0.2613
REMARK 3 L13: 0.1613 L23: 1.5558
REMARK 3 S TENSOR
REMARK 3 S11: -0.0766 S12: -0.1313 S13: -0.0236
REMARK 3 S21: 0.2272 S22: 0.0216 S23: 0.1971
REMARK 3 S31: -0.0393 S32: -0.1349 S33: 0.0549
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 518 B 521
REMARK 3 RESIDUE RANGE : B 747 B 749
REMARK 3 ORIGIN FOR THE GROUP (A): -7.6000 9.1220 -3.6520
REMARK 3 T TENSOR
REMARK 3 T11: -0.0186 T22: -0.0129
REMARK 3 T33: 0.0083 T12: -0.0107
REMARK 3 T13: 0.0023 T23: -0.0043
REMARK 3 L TENSOR
REMARK 3 L11: 0.4129 L22: 1.9234
REMARK 3 L33: 1.2046 L12: 0.6632
REMARK 3 L13: 0.3580 L23: 1.4510
REMARK 3 S TENSOR
REMARK 3 S11: -0.1167 S12: 0.1615 S13: -0.0049
REMARK 3 S21: -0.2047 S22: 0.0647 S23: 0.1661
REMARK 3 S31: 0.0438 S32: -0.0944 S33: 0.0521
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 901 A 901
REMARK 3 ORIGIN FOR THE GROUP (A): -7.3130 14.7533 19.7361
REMARK 3 T TENSOR
REMARK 3 T11: -0.0209 T22: -0.0146
REMARK 3 T33: 0.0047 T12: 0.0218
REMARK 3 T13: -0.0227 T23: -0.0013
REMARK 3 L TENSOR
REMARK 3 L11: 21.2008 L22: 5.8428
REMARK 3 L33: 5.7868 L12: 2.8554
REMARK 3 L13: -6.9265 L23: 3.4527
REMARK 3 S TENSOR
REMARK 3 S11: -0.0622 S12: -0.0509 S13: -0.1659
REMARK 3 S21: -0.0593 S22: -0.0458 S23: 0.0949
REMARK 3 S31: 0.0529 S32: 0.0243 S33: 0.1079
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 902 B 902
REMARK 3 ORIGIN FOR THE GROUP (A): -7.3243 3.9600 -12.3182
REMARK 3 T TENSOR
REMARK 3 T11: -0.0149 T22: -0.0204
REMARK 3 T33: 0.0134 T12: -0.0110
REMARK 3 T13: 0.0197 T23: -0.0033
REMARK 3 L TENSOR
REMARK 3 L11: 13.6462 L22: 3.4775
REMARK 3 L33: 6.5452 L12: -4.7551
REMARK 3 L13: 6.9649 L23: -0.0937
REMARK 3 S TENSOR
REMARK 3 S11: 0.0262 S12: 0.0216 S13: -0.0092
REMARK 3 S21: 0.0643 S22: -0.0887 S23: 0.0716
REMARK 3 S31: -0.1138 S32: -0.0057 S33: 0.0625
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 3FVG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-JAN-09.
REMARK 100 THE DEPOSITION ID IS D_1000051091.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-NOV-08
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL26B2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 79952
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
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 (%) : 96.9
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 32.0000
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 (%) : 93.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.26500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.540
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 3FVN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 35% PEG3350, 0.3M LISO4, 5MM MSVIII
REMARK 280 -19, PH5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 303K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -58.8 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 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 LYS A 434 CG CD CE NZ
REMARK 470 LYS A 480 CG CD CE NZ
REMARK 470 LYS A 664 CG CD CE NZ
REMARK 470 ARG A 704 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 785 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 787 CG OD1 ND2
REMARK 470 LYS B 434 CG CD CE NZ
REMARK 470 ASP B 436 CG OD1 OD2
REMARK 470 LYS B 437 CG CD CE NZ
REMARK 470 ASP B 479 CG OD1 OD2
REMARK 470 LYS B 480 CG CD CE NZ
REMARK 470 ARG B 785 CG CD NE CZ NH1 NH2
REMARK 470 ASN B 787 CG OD1 ND2
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 426 105.12 -164.25
REMARK 500 GLU B 426 103.86 -164.79
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 GOL A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MS8 A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 808
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MS8 B 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 5
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2ZNS RELATED DB: PDB
REMARK 900 SAME PROTEIN IN DIFFERENT SPACE GROUP
REMARK 900 RELATED ID: 2ZNT RELATED DB: PDB
REMARK 900 SAME PROTEIN IN DIFFERENT SPACE GROUP
REMARK 900 RELATED ID: 2ZNU RELATED DB: PDB
REMARK 900 SAME PROTEIN IN DIFFERENT SPACE GROUP
REMARK 900 RELATED ID: 3FUZ RELATED DB: PDB
REMARK 900 SAME PROTEIN WITH DIFFERENT LIGAND
REMARK 900 RELATED ID: 3FV1 RELATED DB: PDB
REMARK 900 SAME PROTEIN WITH DIFFERENT LIGAND
REMARK 900 RELATED ID: 3FV2 RELATED DB: PDB
REMARK 900 SAME PROTEIN WITH DIFFERENT LIGAND
REMARK 900 RELATED ID: 3FVK RELATED DB: PDB
REMARK 900 SAME PROTEIN WITH DIFFERENT LIGAND
REMARK 900 RELATED ID: 3FVN RELATED DB: PDB
REMARK 900 SAME PROTEIN WITH DIFFERENT LIGAND
REMARK 900 RELATED ID: 3FVO RELATED DB: PDB
REMARK 900 SAME PROTEIN WITH DIFFERENT LIGAND
DBREF 3FVG A 415 529 UNP P39086 GRIK1_HUMAN 445 559
DBREF 3FVG A 652 790 UNP P39086 GRIK1_HUMAN 682 820
DBREF 3FVG B 415 529 UNP P39086 GRIK1_HUMAN 445 559
DBREF 3FVG B 652 790 UNP P39086 GRIK1_HUMAN 682 820
SEQADV 3FVG GLY A 600 UNP P39086 LINKER
SEQADV 3FVG THR A 601 UNP P39086 LINKER
SEQADV 3FVG GLY B 600 UNP P39086 LINKER
SEQADV 3FVG THR B 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
SEQRES 1 B 256 ALA ASN ARG THR LEU ILE VAL THR THR ILE LEU GLU GLU
SEQRES 2 B 256 PRO TYR VAL MET TYR ARG LYS SER ASP LYS PRO LEU TYR
SEQRES 3 B 256 GLY ASN ASP ARG PHE GLU GLY TYR CYS LEU ASP LEU LEU
SEQRES 4 B 256 LYS GLU LEU SER ASN ILE LEU GLY PHE ILE TYR ASP VAL
SEQRES 5 B 256 LYS LEU VAL PRO ASP GLY LYS TYR GLY ALA GLN ASN ASP
SEQRES 6 B 256 LYS GLY GLU TRP ASN GLY MET VAL LYS GLU LEU ILE ASP
SEQRES 7 B 256 HIS ARG ALA ASP LEU ALA VAL ALA PRO LEU THR ILE THR
SEQRES 8 B 256 TYR VAL ARG GLU LYS VAL ILE ASP PHE SER LYS PRO PHE
SEQRES 9 B 256 MET THR LEU GLY ILE SER ILE LEU TYR ARG LYS GLY THR
SEQRES 10 B 256 PRO ILE ASP SER ALA ASP ASP LEU ALA LYS GLN THR LYS
SEQRES 11 B 256 ILE GLU TYR GLY ALA VAL ARG ASP GLY SER THR MET THR
SEQRES 12 B 256 PHE PHE LYS LYS SER LYS ILE SER THR TYR GLU LYS MET
SEQRES 13 B 256 TRP ALA PHE MET SER SER ARG GLN GLN THR ALA LEU VAL
SEQRES 14 B 256 ARG ASN SER ASP GLU GLY ILE GLN ARG VAL LEU THR THR
SEQRES 15 B 256 ASP TYR ALA LEU LEU MET GLU SER THR SER ILE GLU TYR
SEQRES 16 B 256 VAL THR GLN ARG ASN CYS ASN LEU THR GLN ILE GLY GLY
SEQRES 17 B 256 LEU ILE ASP SER LYS GLY TYR GLY VAL GLY THR PRO ILE
SEQRES 18 B 256 GLY SER PRO TYR ARG ASP LYS ILE THR ILE ALA ILE LEU
SEQRES 19 B 256 GLN LEU GLN GLU GLU GLY LYS LEU HIS MET MET LYS GLU
SEQRES 20 B 256 LYS TRP TRP ARG GLY ASN GLY CYS PRO
HET GOL A 801 6
HET GOL A 804 6
HET GOL A 806 6
HET MS8 A 901 18
HET SO4 A 1 5
HET SO4 A 2 5
HET GOL B 802 6
HET GOL B 803 6
HET GOL B 805 6
HET GOL B 807 6
HET GOL B 808 6
HET MS8 B 902 18
HET SO4 B 4 5
HET SO4 B 5 5
HETNAM GOL GLYCEROL
HETNAM MS8 (2R,3AR,7AR)-2-[(2S)-2-AMINO-3-HYDROXY-3-OXO-PROPYL]-3,
HETNAM 2 MS8 3A,5,6,7,7A-HEXAHYDROFURO[4,5-B]PYRAN-2-CARBOXYLIC
HETNAM 3 MS8 ACID
HETNAM SO4 SULFATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL 8(C3 H8 O3)
FORMUL 6 MS8 2(C11 H17 N O6)
FORMUL 7 SO4 4(O4 S 2-)
FORMUL 17 HOH *371(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 GLN A 662 1 8
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 GLN A 732 1 9
HELIX 11 11 TYR A 759 GLU A 773 1 15
HELIX 12 12 GLY A 774 ARG A 785 1 12
HELIX 13 13 TYR B 440 ASP B 443 5 4
HELIX 14 14 GLY B 447 GLY B 461 1 15
HELIX 15 15 ASN B 484 ASP B 492 1 9
HELIX 16 16 THR B 505 LYS B 510 1 6
HELIX 17 17 SER B 655 GLN B 662 1 8
HELIX 18 18 GLY B 673 SER B 682 1 10
HELIX 19 19 ILE B 684 ARG B 697 1 14
HELIX 20 20 ARG B 697 ALA B 701 1 5
HELIX 21 21 ASN B 705 THR B 716 1 12
HELIX 22 22 SER B 724 GLN B 732 1 9
HELIX 23 23 PRO B 758 GLU B 773 1 16
HELIX 24 24 GLY B 774 ARG B 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
SHEET 1 F 3 TYR B 464 LEU B 468 0
SHEET 2 F 3 LEU B 419 THR B 423 1 N VAL B 421 O LYS B 467
SHEET 3 F 3 LEU B 497 ALA B 498 1 O LEU B 497 N THR B 422
SHEET 1 G 2 MET B 431 TYR B 432 0
SHEET 2 G 2 PHE B 445 GLU B 446 -1 O GLU B 446 N MET B 431
SHEET 1 H 2 ILE B 512 PHE B 514 0
SHEET 2 H 2 GLY B 752 PRO B 754 -1 O THR B 753 N ASP B 513
SHEET 1 I 2 MET B 519 LEU B 521 0
SHEET 2 I 2 LYS B 747 TYR B 749 -1 O LYS B 747 N LEU B 521
SHEET 1 J 5 LEU B 702 VAL B 703 0
SHEET 2 J 5 GLU B 666 VAL B 670 1 N ALA B 669 O VAL B 703
SHEET 3 J 5 TYR B 718 GLU B 723 1 O LEU B 721 N GLY B 668
SHEET 4 J 5 ILE B 523 ARG B 528 -1 N LEU B 526 O LEU B 720
SHEET 5 J 5 LEU B 737 ILE B 740 -1 O THR B 738 N TYR B 527
SSBOND 1 CYS A 735 CYS A 789 1555 1555 2.04
SSBOND 2 CYS B 735 CYS B 789 1555 1555 2.04
CISPEP 1 GLU A 427 PRO A 428 0 -2.87
CISPEP 2 GLU A 427 PRO A 428 0 -2.07
CISPEP 3 ARG A 785 GLY A 786 0 -10.60
CISPEP 4 GLU B 427 PRO B 428 0 -2.87
CISPEP 5 ARG B 785 GLY B 786 0 -11.87
SITE 1 AC1 9 HOH A 4 HOH A 23 HOH A 226 THR A 505
SITE 2 AC1 9 THR A 677 PHE A 678 LYS A 747 HOH B 42
SITE 3 AC1 9 HOH B 55
SITE 1 AC2 9 HOH A 211 HOH A 212 HOH A 252 HOH A 399
SITE 2 AC2 9 PRO A 517 SER A 746 GLY A 748 THR B 520
SITE 3 AC2 9 GLN B 771
SITE 1 AC3 2 HOH A 295 ASN A 734
SITE 1 AC4 14 HOH A 41 HOH A 243 GLU A 426 TYR A 474
SITE 2 AC4 14 PRO A 501 LEU A 502 THR A 503 ARG A 508
SITE 3 AC4 14 GLY A 673 SER A 674 THR A 675 SER A 706
SITE 4 AC4 14 GLU A 723 SER A 726
SITE 1 AC5 6 HOH A 69 HOH A 120 HOH A 277 ARG A 444
SITE 2 AC5 6 LEU A 468 ARG B 704
SITE 1 AC6 3 ARG A 417 TYR A 759 ASN A 787
SITE 1 AC7 8 HOH A 212 THR A 520 GLN A 771 HOH B 210
SITE 2 AC7 8 HOH B 369 PRO B 517 SER B 746 GLY B 748
SITE 1 AC8 9 HOH A 13 HOH A 40 HOH B 3 HOH B 17
SITE 2 AC8 9 HOH B 280 THR B 505 THR B 677 PHE B 678
SITE 3 AC8 9 LYS B 747
SITE 1 AC9 9 HOH B 154 HOH B 266 HOH B 282 LYS B 454
SITE 2 AC9 9 TYR B 464 ALA B 660 LYS B 661 THR B 663
SITE 3 AC9 9 LYS B 689
SITE 1 BC1 10 HOH B 397 HOH B 398 ILE B 420 THR B 422
SITE 2 BC1 10 LYS B 467 LEU B 468 VAL B 469 GLU B 489
SITE 3 BC1 10 ARG B 494 ALA B 495
SITE 1 BC2 11 HOH A 120 TYR A 432 HOH B 278 HOH B 388
SITE 2 BC2 11 GLN B 699 THR B 700 LEU B 702 VAL B 703
SITE 3 BC2 11 ARG B 704 GLU B 708 ARG B 712
SITE 1 BC3 14 HOH B 14 HOH B 241 GLU B 426 TYR B 474
SITE 2 BC3 14 PRO B 501 LEU B 502 THR B 503 ARG B 508
SITE 3 BC3 14 GLY B 673 SER B 674 THR B 675 SER B 706
SITE 4 BC3 14 GLU B 723 SER B 726
SITE 1 BC4 5 HOH B 233 ARG B 444 VAL B 466 LYS B 467
SITE 2 BC4 5 LEU B 468
SITE 1 BC5 3 ARG B 417 TYR B 759 ASN B 787
CRYST1 47.627 50.860 62.931 80.41 84.16 62.06 P 1 2
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 0.020996 -0.011135 -0.000648 0.00000
SCALE2 0.000000 0.022256 -0.003039 0.00000
SCALE3 0.000000 0.000000 0.016122 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
