HEADER LIGAND BINDING PROTEIN 14-MAY-03 1PB7
TITLE CRYSTAL STRUCTURE OF THE NR1 LIGAND BINDING CORE IN COMPLEX WITH
TITLE 2 GLYCINE AT 1.35 ANGSTROMS RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: N-METHYL-D-ASPARTATE RECEPTOR SUBUNIT 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: LIGAND BINDING CORE;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 ORGAN: FOREBRAIN;
SOURCE 6 GENE: NMDAR1;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: ORIGAMIB (DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET22B(+)
KEYWDS LIGAND BINDING RECEPTOR; RAT; NR1, LIGAND BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR H.FURUKAWA,E.GOUAUX
REVDAT 4 26-JUL-17 1PB7 1 SOURCE REMARK
REVDAT 3 24-FEB-09 1PB7 1 VERSN
REVDAT 2 22-JUL-03 1PB7 1 DBREF SEQADV REMARK
REVDAT 1 24-JUN-03 1PB7 0
JRNL AUTH H.FURUKAWA,E.GOUAUX
JRNL TITL MECHANISMS OF ACTIVATION, INHIBITION AND SPECIFICITY:
JRNL TITL 2 CRYSTAL STRUCTURES OF THE NMDA RECEPTOR NR1 LIGAND-BINDING
JRNL TITL 3 CORE
JRNL REF EMBO J. V. 22 2873 2003
JRNL REFN ISSN 0261-4189
JRNL PMID 12805203
JRNL DOI 10.1093/EMBOJ/CDG303
REMARK 2
REMARK 2 RESOLUTION. 1.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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) : 1.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 9.96
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 86.1
REMARK 3 NUMBER OF REFLECTIONS : 56472
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) : 0.194
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.200
REMARK 3 FREE R VALUE TEST SET COUNT : 5745
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
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) : 1.35
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.43
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 44.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4302
REMARK 3 BIN R VALUE (WORKING SET) : 0.2440
REMARK 3 BIN FREE R VALUE : 0.2540
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 476
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.012
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2151
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 331
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.40
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.17
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.10
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.880
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) : 1.640 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.330 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.080 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.070 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.49
REMARK 3 BSOL : 66.40
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 : GLY.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 : GLY.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 1PB7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-MAY-03.
REMARK 100 THE DEPOSITION ID IS D_1000019213.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-APR-02
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 6.0
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) : 0.9202
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57637
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.350
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 14.150
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87.7
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) : 1.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 41.1
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: MAD
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 (%): 44.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 1000, SODIUM CACODYLATE, LITHIUM
REMARK 280 SULFATE, PH 6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 20.83000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 48.42500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.51000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 48.42500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.83000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.51000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 1
REMARK 465 MET A 2
REMARK 465 SER A 3
REMARK 465 ASP A 49
REMARK 465 THR A 50
REMARK 465 SER A 51
REMARK 465 PRO A 52
REMARK 465 GLY A 53
REMARK 465 SER A 54
REMARK 465 PRO A 55
REMARK 465 ARG A 56
REMARK 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 THR A 4 OG1 CG2
REMARK 470 LYS A 7 CG CD CE NZ
REMARK 470 LYS A 29 CG CD CE NZ
REMARK 470 ASN A 48 CG OD1 ND2
REMARK 470 ARG A 76 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 83 CG CD OE1 OE2
REMARK 470 LYS A 103 CG CD CE NZ
REMARK 470 GLU A 136 CG CD OE1 OE2
REMARK 470 LYS A 151 CG CD CE NZ
REMARK 470 ARG A 155 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 169 CG OD1 OD2
REMARK 470 LYS A 170 CG CD CE NZ
REMARK 470 ARG A 186 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 187 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 189 CG1 CG2
REMARK 470 GLU A 190 CG CD OE1 OE2
REMARK 470 ARG A 196 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 199 CG CD OE1 OE2
REMARK 470 LYS A 200 CG CD CE NZ
REMARK 470 GLN A 234 CG CD OE1 NE2
REMARK 470 GLU A 243 CG CD OE1 OE2
REMARK 470 ARG A 247 CG CD NE CZ NH1 NH2
REMARK 470 PRO A 259 CG CD
REMARK 470 LYS A 261 CG CD CE NZ
REMARK 470 GLN A 262 CG CD OE1 NE2
REMARK 470 LYS A 270 CG CD CE NZ
REMARK 470 GLU A 278 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 105 CD GLU A 105 OE2 0.078
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLN A 13 89.85 -168.98
REMARK 500 GLN A 144 -146.22 -150.75
REMARK 500 TYR A 287 -11.27 -153.29
REMARK 500 ASP A 291 5.32 -160.64
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLY A 901
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PB8 RELATED DB: PDB
REMARK 900 RELATED ID: 1PB9 RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE FIRST RESIDUE IN SEQUENCE, GLY, IS A CLONING ARTIFACT.
REMARK 999 RESIDUES 153 AND 154, GLY AND THR, ARE INSERTED AS A LINK
REMARK 999 REPLACING RESIDUES 545 -- 662 OF THE PROTEIN FROM THE GB
REMARK 999 SEQUENCE ENTRY AAB50932 475566.
DBREF 1PB7 A 2 152 UNP P35439 NMDZ1_RAT 394 544
DBREF 1PB7 A 155 292 UNP P35439 NMDZ1_RAT 663 800
SEQRES 1 A 292 GLY MET SER THR ARG LEU LYS ILE VAL THR ILE HIS GLN
SEQRES 2 A 292 GLU PRO PHE VAL TYR VAL LYS PRO THR MET SER ASP GLY
SEQRES 3 A 292 THR CYS LYS GLU GLU PHE THR VAL ASN GLY ASP PRO VAL
SEQRES 4 A 292 LYS LYS VAL ILE CYS THR GLY PRO ASN ASP THR SER PRO
SEQRES 5 A 292 GLY SER PRO ARG HIS THR VAL PRO GLN CYS CYS TYR GLY
SEQRES 6 A 292 PHE CYS ILE ASP LEU LEU ILE LYS LEU ALA ARG THR MET
SEQRES 7 A 292 ASN PHE THR TYR GLU VAL HIS LEU VAL ALA ASP GLY LYS
SEQRES 8 A 292 PHE GLY THR GLN GLU ARG VAL ASN ASN SER ASN LYS LYS
SEQRES 9 A 292 GLU TRP ASN GLY MET MET GLY GLU LEU LEU SER GLY GLN
SEQRES 10 A 292 ALA ASP MET ILE VAL ALA PRO LEU THR ILE ASN ASN GLU
SEQRES 11 A 292 ARG ALA GLN TYR ILE GLU PHE SER LYS PRO PHE LYS TYR
SEQRES 12 A 292 GLN GLY LEU THR ILE LEU VAL LYS LYS GLY THR ARG ILE
SEQRES 13 A 292 THR GLY ILE ASN ASP PRO ARG LEU ARG ASN PRO SER ASP
SEQRES 14 A 292 LYS PHE ILE TYR ALA THR VAL LYS GLN SER SER VAL ASP
SEQRES 15 A 292 ILE TYR PHE ARG ARG GLN VAL GLU LEU SER THR MET TYR
SEQRES 16 A 292 ARG HIS MET GLU LYS HIS ASN TYR GLU SER ALA ALA GLU
SEQRES 17 A 292 ALA ILE GLN ALA VAL ARG ASP ASN LYS LEU HIS ALA PHE
SEQRES 18 A 292 ILE TRP ASP SER ALA VAL LEU GLU PHE GLU ALA SER GLN
SEQRES 19 A 292 LYS CYS ASP LEU VAL THR THR GLY GLU LEU PHE PHE ARG
SEQRES 20 A 292 SER GLY PHE GLY ILE GLY MET ARG LYS ASP SER PRO TRP
SEQRES 21 A 292 LYS GLN ASN VAL SER LEU SER ILE LEU LYS SER HIS GLU
SEQRES 22 A 292 ASN GLY PHE MET GLU ASP LEU ASP LYS THR TRP VAL ARG
SEQRES 23 A 292 TYR GLN GLU CYS ASP SER
HET GLY A 901 5
HETNAM GLY GLYCINE
FORMUL 2 GLY C2 H5 N O2
FORMUL 3 HOH *331(H2 O)
HELIX 1 1 GLY A 65 ASN A 79 1 15
HELIX 2 2 ASN A 107 SER A 115 1 9
HELIX 3 3 ASN A 128 GLN A 133 1 6
HELIX 4 4 ASP A 161 ASN A 166 1 6
HELIX 5 5 SER A 179 ARG A 187 1 9
HELIX 6 6 GLN A 188 GLU A 190 5 3
HELIX 7 7 LEU A 191 GLU A 199 1 9
HELIX 8 8 SER A 205 ASP A 215 1 11
HELIX 9 9 SER A 225 LYS A 235 1 11
HELIX 10 10 TRP A 260 ASN A 274 1 15
HELIX 11 11 GLY A 275 VAL A 285 1 11
SHEET 1 A 8 TYR A 18 PRO A 21 0
SHEET 2 A 8 VAL A 59 TYR A 64 -1 O TYR A 64 N TYR A 18
SHEET 3 A 8 VAL A 42 GLY A 46 -1 N VAL A 42 O CYS A 63
SHEET 4 A 8 TYR A 82 LEU A 86 1 O LEU A 86 N THR A 45
SHEET 5 A 8 LEU A 6 THR A 10 1 N ILE A 8 O GLU A 83
SHEET 6 A 8 MET A 120 ILE A 121 1 O MET A 120 N VAL A 9
SHEET 7 A 8 GLY A 253 ARG A 255 -1 O GLY A 253 N ILE A 121
SHEET 8 A 8 ILE A 135 PHE A 137 -1 N GLU A 136 O MET A 254
SHEET 1 B 2 GLN A 95 ARG A 97 0
SHEET 2 B 2 LYS A 104 TRP A 106 -1 O GLU A 105 N GLU A 96
SHEET 1 C 4 PHE A 246 PHE A 250 0
SHEET 2 C 4 LYS A 142 LYS A 151 -1 N GLN A 144 O SER A 248
SHEET 3 C 4 ALA A 220 ASP A 224 -1 O PHE A 221 N LEU A 149
SHEET 4 C 4 TYR A 173 ALA A 174 1 N ALA A 174 O ILE A 222
SHEET 1 D 3 PHE A 246 PHE A 250 0
SHEET 2 D 3 LYS A 142 LYS A 151 -1 N GLN A 144 O SER A 248
SHEET 3 D 3 LEU A 238 THR A 240 -1 O VAL A 239 N VAL A 150
SSBOND 1 CYS A 28 CYS A 62 1555 1555 2.05
SSBOND 2 CYS A 44 CYS A 63 1555 1555 2.04
SSBOND 3 CYS A 236 CYS A 290 1555 1555 2.03
CISPEP 1 GLU A 14 PRO A 15 0 0.55
SITE 1 AC1 8 PHE A 92 PRO A 124 LEU A 125 THR A 126
SITE 2 AC1 8 ARG A 131 SER A 179 SER A 180 ASP A 224
CRYST1 41.660 73.020 96.850 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.024004 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013695 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010325 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
