HEADER METAL TRANSPORT,MEMBRANE PROTEIN 30-JUN-05 2A5S
TITLE CRYSTAL STRUCTURE OF THE NR2A LIGAND BINDING CORE IN COMPLEX WITH
TITLE 2 GLUTAMATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: N-METHYL-D-ASPARTATE RECEPTOR NMDAR2A SUBUNIT;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: S1S2 LIGAND-BINDING CORE;
COMPND 5 SYNONYM: NMDA RECEPTOR NR2A SUBUNIT; NMDA RECEPTOR NMDAR2A SUBUNIT;
COMPND 6 GLUTAMATE RECEPTOR, IONOTROPIC, N-METHYL D-ASPARTATE 2A;
COMPND 7 ENGINEERED: YES;
COMPND 8 OTHER_DETAILS: CONSTRUCT OF RESIDUES 401-539 AND 661-802 OF GB
COMPND 9 AAB58801
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
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
KEYWDS PROTEIN-LIGAND COMPLEX, METAL TRANSPORT, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR H.FURUKAWA,S.K.SINGH,R.MANCUSSO,E.GOUAUX
REVDAT 3 26-JUL-17 2A5S 1 SOURCE REMARK
REVDAT 2 24-FEB-09 2A5S 1 VERSN
REVDAT 1 15-NOV-05 2A5S 0
JRNL AUTH H.FURUKAWA,S.K.SINGH,R.MANCUSSO,E.GOUAUX
JRNL TITL SUBUNIT ARRANGEMENT AND FUNCTION IN NMDA RECEPTORS
JRNL REF NATURE V. 438 185 2005
JRNL REFN ISSN 0028-0836
JRNL PMID 16281028
JRNL DOI 10.1038/NATURE04089
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.19
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1859072.890
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 30942
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 SET) : 0.196
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3074
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.81
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4249
REMARK 3 BIN R VALUE (WORKING SET) : 0.2150
REMARK 3 BIN FREE R VALUE : 0.2440
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 458
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.011
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2175
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 316
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.90000
REMARK 3 B22 (A**2) : 0.90000
REMARK 3 B33 (A**2) : -1.80000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.19
REMARK 3 ESD FROM SIGMAA (A) : 0.08
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.21
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.11
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.740
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.220 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.840 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.190 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.270 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.41
REMARK 3 BSOL : 52.04
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : GLUT.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : GLUT.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2A5S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JUL-05.
REMARK 100 THE DEPOSITION ID IS D_1000033522.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-OCT-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30725
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: COMBINATION OF MR AND SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, HEPES, CALCIUM ACETATE, PH
REMARK 280 7, EVAPORATION, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 99.33750
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 26.05300
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 26.05300
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 49.66875
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 26.05300
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 26.05300
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 149.00625
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 26.05300
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 26.05300
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 49.66875
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 26.05300
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 26.05300
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 149.00625
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 99.33750
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2790 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 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 0.000000 -1.000000 0.000000 52.10600
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 52.10600
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 99.33750
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 3
REMARK 465 PRO A 4
REMARK 465 ASP A 5
REMARK 465 ASP A 6
REMARK 465 THR A 29
REMARK 465 ASN A 286
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 LEU A 28 CG CD1 CD2
REMARK 470 GLU A 30 CG CD OE1 OE2
REMARK 470 ARG A 195 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 230 CG CD CE NZ
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 16 97.39 -169.00
REMARK 500 VAL A 33 -164.80 -123.79
REMARK 500 ARG A 34 -127.73 54.07
REMARK 500 LYS A 87 -109.85 -122.37
REMARK 500 THR A 243 -145.27 -160.38
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 GLU A 1001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PB7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE NR1 LIGAND BINDING CORE IN COMPLEX WITH
REMARK 900 GLYCINE AT 1.35 ANGSTROMS RESOLUTION
REMARK 900 RELATED ID: 2A5T RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE NMDA RECEPTOR NR1 SUBUNIT AND NR2A SUBUNITS
DBREF 2A5S A 4 142 UNP Q00959 NMDE1_RAT 401 539
DBREF 2A5S A 145 286 GB 2155310 AAB58801 661 802
SEQADV 2A5S GLY A 3 UNP Q00959 SEE REMARK 999
SEQADV 2A5S GLY A 143 UNP Q00959 SEE REMARK 999
SEQADV 2A5S THR A 144 UNP Q00959 SEE REMARK 999
SEQRES 1 A 284 GLY PRO ASP ASP ASN HIS LEU SER ILE VAL THR LEU GLU
SEQRES 2 A 284 GLU ALA PRO PHE VAL ILE VAL GLU ASP ILE ASP PRO LEU
SEQRES 3 A 284 THR GLU THR CYS VAL ARG ASN THR VAL PRO CYS ARG LYS
SEQRES 4 A 284 PHE VAL LYS ILE ASN ASN SER THR ASN GLU GLY MET ASN
SEQRES 5 A 284 VAL LYS LYS CYS CYS LYS GLY PHE CYS ILE ASP ILE LEU
SEQRES 6 A 284 LYS LYS LEU SER ARG THR VAL LYS PHE THR TYR ASP LEU
SEQRES 7 A 284 TYR LEU VAL THR ASN GLY LYS HIS GLY LYS LYS VAL ASN
SEQRES 8 A 284 ASN VAL TRP ASN GLY MET ILE GLY GLU VAL VAL TYR GLN
SEQRES 9 A 284 ARG ALA VAL MET ALA VAL GLY SER LEU THR ILE ASN GLU
SEQRES 10 A 284 GLU ARG SER GLU VAL VAL ASP PHE SER VAL PRO PHE VAL
SEQRES 11 A 284 GLU THR GLY ILE SER VAL MET VAL SER ARG GLY THR GLN
SEQRES 12 A 284 VAL THR GLY LEU SER ASP LYS LYS PHE GLN ARG PRO HIS
SEQRES 13 A 284 ASP TYR SER PRO PRO PHE ARG PHE GLY THR VAL PRO ASN
SEQRES 14 A 284 GLY SER THR GLU ARG ASN ILE ARG ASN ASN TYR PRO TYR
SEQRES 15 A 284 MET HIS GLN TYR MET THR ARG PHE ASN GLN ARG GLY VAL
SEQRES 16 A 284 GLU ASP ALA LEU VAL SER LEU LYS THR GLY LYS LEU ASP
SEQRES 17 A 284 ALA PHE ILE TYR ASP ALA ALA VAL LEU ASN TYR LYS ALA
SEQRES 18 A 284 GLY ARG ASP GLU GLY CYS LYS LEU VAL THR ILE GLY SER
SEQRES 19 A 284 GLY TYR ILE PHE ALA THR THR GLY TYR GLY ILE ALA LEU
SEQRES 20 A 284 GLN LYS GLY SER PRO TRP LYS ARG GLN ILE ASP LEU ALA
SEQRES 21 A 284 LEU LEU GLN PHE VAL GLY ASP GLY GLU MET GLU GLU LEU
SEQRES 22 A 284 GLU THR LEU TRP LEU THR GLY ILE CYS HIS ASN
HET GLU A1001 10
HETNAM GLU GLUTAMIC ACID
FORMUL 2 GLU C5 H9 N O4
FORMUL 3 HOH *316(H2 O)
HELIX 1 1 GLY A 61 LYS A 75 1 15
HELIX 2 2 ASN A 97 TYR A 105 1 9
HELIX 3 3 ASN A 118 GLU A 123 1 6
HELIX 4 4 ASP A 151 ARG A 156 1 6
HELIX 5 5 PRO A 157 TYR A 160 5 4
HELIX 6 6 GLY A 172 ASN A 180 1 9
HELIX 7 7 TYR A 182 THR A 190 1 9
HELIX 8 8 ARG A 191 ASN A 193 5 3
HELIX 9 9 GLY A 196 THR A 206 1 11
HELIX 10 10 ALA A 216 ARG A 225 1 10
HELIX 11 11 TYR A 238 THR A 242 5 5
HELIX 12 12 TRP A 255 ASP A 269 1 15
HELIX 13 13 GLY A 270 LEU A 280 1 11
SHEET 1 A 5 TYR A 78 LEU A 82 0
SHEET 2 A 5 LEU A 9 THR A 13 1 N LEU A 9 O ASP A 79
SHEET 3 A 5 MET A 110 ALA A 111 1 O MET A 110 N VAL A 12
SHEET 4 A 5 ALA A 248 GLN A 250 -1 O ALA A 248 N ALA A 111
SHEET 5 A 5 VAL A 125 PHE A 127 -1 N ASP A 126 O LEU A 249
SHEET 1 B 3 ILE A 21 ASP A 24 0
SHEET 2 B 3 GLY A 52 LYS A 60 -1 O LYS A 60 N ILE A 21
SHEET 3 B 3 VAL A 37 LYS A 44 -1 N LYS A 41 O VAL A 55
SHEET 1 C 2 LYS A 91 VAL A 92 0
SHEET 2 C 2 VAL A 95 TRP A 96 -1 O VAL A 95 N VAL A 92
SHEET 1 D 2 VAL A 132 THR A 134 0
SHEET 2 D 2 THR A 243 TYR A 245 -1 O TYR A 245 N VAL A 132
SHEET 1 E 4 PHE A 166 GLY A 167 0
SHEET 2 E 4 ALA A 211 ASP A 215 1 O ILE A 213 N GLY A 167
SHEET 3 E 4 ILE A 136 SER A 141 -1 N MET A 139 O PHE A 212
SHEET 4 E 4 LEU A 231 GLY A 235 -1 O ILE A 234 N VAL A 138
SSBOND 1 CYS A 32 CYS A 58 1555 1555 2.04
SSBOND 2 CYS A 39 CYS A 59 1555 1555 2.04
SSBOND 3 CYS A 229 CYS A 284 1555 1555 2.03
CISPEP 1 ALA A 17 PRO A 18 0 0.22
CISPEP 2 SER A 161 PRO A 162 0 0.03
SITE 1 AC1 11 HIS A 88 SER A 114 THR A 116 ARG A 121
SITE 2 AC1 11 GLY A 172 SER A 173 THR A 174 TYR A 214
SITE 3 AC1 11 ASP A 215 HOH A1004 HOH A1007
CRYST1 52.106 52.106 198.675 90.00 90.00 90.00 P 41 21 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 0.019192 0.000000 0.000000 0.00000
SCALE2 0.000000 0.019192 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005033 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
