HEADER TRANSPORT PROTEIN/AGONIST 07-MAY-12 4F29
TITLE QUISQUALATE BOUND TO THE LIGAND BINDING DOMAIN OF GLUA3I
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMATE RECEPTOR 3;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GLUR-3, AMPA-SELECTIVE GLUTAMATE RECEPTOR 3, GLUR-C, GLUR-
COMPND 5 K3, GLUTAMATE RECEPTOR IONOTROPIC, AMPA 3, GLUA3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: GLUR3, GRIA3, GRIA3; GLUA3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ORIGAMI B (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-22B(+)
KEYWDS GLUTAMATE RECEPTOR, GLUA3, GLUR3, AMPA RECEPTOR, S1S2, LBD,
KEYWDS 2 NEUROTRANSMITTER RECEPTOR, QUISQUALATE, TRANSPORT PROTEIN, TRANSPORT
KEYWDS 3 PROTEIN-AGONIST COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.H.AHMED,R.E.OSWALD
REVDAT 4 13-SEP-23 4F29 1 REMARK SEQADV
REVDAT 3 16-AUG-17 4F29 1 SOURCE REMARK
REVDAT 2 23-MAY-12 4F29 1 JRNL
REVDAT 1 16-MAY-12 4F29 0
JRNL AUTH S.M.HOLLEY,A.H.AHMED,J.SRINIVASAN,S.E.MURTHY,G.A.WEILAND,
JRNL AUTH 2 R.E.OSWALD,L.M.NOWAK
JRNL TITL THE LOSS OF AN ELECTROSTATIC CONTACT UNIQUE TO AMPA RECEPTOR
JRNL TITL 2 LIGAND BINDING DOMAIN 2 SLOWS CHANNEL ACTIVATION.
JRNL REF BIOCHEMISTRY V. 51 4015 2012
JRNL REFN ISSN 0006-2960
JRNL PMID 22512472
JRNL DOI 10.1021/BI3001837
REMARK 2
REMARK 2 RESOLUTION. 1.75 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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.83
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.100
REMARK 3 COMPLETENESS FOR RANGE (%) : 82.3
REMARK 3 NUMBER OF REFLECTIONS : 26559
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.180
REMARK 3 FREE R VALUE TEST SET COUNT : 1908
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 44.8393 - 4.2152 0.75 1748 134 0.2056 0.2484
REMARK 3 2 4.2152 - 3.3460 0.81 1764 139 0.1712 0.2090
REMARK 3 3 3.3460 - 2.9232 0.89 1920 146 0.1793 0.2445
REMARK 3 4 2.9232 - 2.6559 0.90 1925 146 0.1801 0.2308
REMARK 3 5 2.6559 - 2.4656 0.90 1910 151 0.1805 0.2286
REMARK 3 6 2.4656 - 2.3202 0.90 1911 146 0.1862 0.2430
REMARK 3 7 2.3202 - 2.2040 0.86 1837 140 0.1788 0.2364
REMARK 3 8 2.2040 - 2.1081 0.89 1875 145 0.1710 0.1964
REMARK 3 9 2.1081 - 2.0269 0.88 1864 147 0.1785 0.2546
REMARK 3 10 2.0269 - 1.9570 0.85 1790 142 0.1888 0.2512
REMARK 3 11 1.9570 - 1.8958 0.75 1545 118 0.2527 0.3324
REMARK 3 12 1.8958 - 1.8416 0.80 1706 134 0.2114 0.2712
REMARK 3 13 1.8416 - 1.7931 0.76 1601 122 0.2003 0.2630
REMARK 3 14 1.7931 - 1.7494 0.60 1255 98 0.1893 0.2474
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 : 0.39
REMARK 3 B_SOL : 49.52
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.640
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.13470
REMARK 3 B22 (A**2) : -4.01250
REMARK 3 B33 (A**2) : 4.14720
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 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 : 0.023 2085
REMARK 3 ANGLE : 1.991 2807
REMARK 3 CHIRALITY : 0.135 308
REMARK 3 PLANARITY : 0.010 350
REMARK 3 DIHEDRAL : 17.173 786
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 4F29 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-MAY-12.
REMARK 100 THE DEPOSITION ID IS D_1000072363.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-SEP-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.977
REMARK 200 MONOCHROMATOR : RH COATED SI
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.749
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87.6
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.06900
REMARK 200 R SYM (I) : 0.06900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.9440
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.88
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.26000
REMARK 200 R SYM FOR SHELL (I) : 0.26000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.050
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 3DLN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 14-15% PEG 8K, 0.1 M SODIUM
REMARK 280 CACODYLATE, 0.1-0.15 M ZINC ACETATE, 0.25 M AMMONIUM SULFATE, PH
REMARK 280 6.5, VAPOR DIFFUSION, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 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 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 68.79750
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 68.79750
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
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 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 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 68.79750
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 528 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 647 LIES ON A SPECIAL POSITION.
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 ARG A 48 60.51 60.45
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 QUS A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4F1Y RELATED DB: PDB
REMARK 900 RELATED ID: 4F22 RELATED DB: PDB
REMARK 900 RELATED ID: 4F2O RELATED DB: PDB
REMARK 900 RELATED ID: 4F2Q RELATED DB: PDB
REMARK 900 RELATED ID: 4F31 RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUES 232,233, 242, AND 246 CORRESPOND TO AN ALTERNATIVELY
REMARK 999 SPLICED VERSION OF THE PROTEIN, UNP P19492
DBREF 4F29 A 4 117 UNP P19492 GRIA3_RAT 417 530
DBREF 4F29 A 120 261 UNP P19492 GRIA3_RAT 658 799
SEQADV 4F29 GLY A 118 UNP P19492 LINKER
SEQADV 4F29 THR A 119 UNP P19492 LINKER
SEQADV 4F29 THR A 232 UNP P19492 ASN 770 SEE REMARK 999
SEQADV 4F29 PRO A 233 UNP P19492 ALA 771 SEE REMARK 999
SEQADV 4F29 SER A 242 UNP P19492 ASN 780 SEE REMARK 999
SEQADV 4F29 ILE A 246 UNP P19492 LEU 784 SEE REMARK 999
SEQRES 1 A 258 ARG THR ILE VAL VAL THR THR ILE LEU GLU SER PRO TYR
SEQRES 2 A 258 VAL MET TYR LYS LYS ASN HIS GLU GLN LEU GLU GLY ASN
SEQRES 3 A 258 GLU ARG TYR GLU GLY TYR CYS VAL ASP LEU ALA TYR GLU
SEQRES 4 A 258 ILE ALA LYS HIS VAL ARG ILE LYS TYR LYS LEU SER ILE
SEQRES 5 A 258 VAL GLY ASP GLY LYS TYR GLY ALA ARG ASP PRO GLU THR
SEQRES 6 A 258 LYS ILE TRP ASN GLY MET VAL GLY GLU LEU VAL TYR GLY
SEQRES 7 A 258 ARG ALA ASP ILE ALA VAL ALA PRO LEU THR ILE THR LEU
SEQRES 8 A 258 VAL ARG GLU GLU VAL ILE ASP PHE SER LYS PRO PHE MET
SEQRES 9 A 258 SER LEU GLY ILE SER ILE MET ILE LYS LYS GLY THR PRO
SEQRES 10 A 258 ILE GLU SER ALA GLU ASP LEU ALA LYS GLN THR GLU ILE
SEQRES 11 A 258 ALA TYR GLY THR LEU ASP SER GLY SER THR LYS GLU PHE
SEQRES 12 A 258 PHE ARG ARG SER LYS ILE ALA VAL TYR GLU LYS MET TRP
SEQRES 13 A 258 SER TYR MET LYS SER ALA GLU PRO SER VAL PHE THR LYS
SEQRES 14 A 258 THR THR ALA ASP GLY VAL ALA ARG VAL ARG LYS SER LYS
SEQRES 15 A 258 GLY LYS PHE ALA PHE LEU LEU GLU SER THR MET ASN GLU
SEQRES 16 A 258 TYR ILE GLU GLN ARG LYS PRO CYS ASP THR MET LYS VAL
SEQRES 17 A 258 GLY GLY ASN LEU ASP SER LYS GLY TYR GLY VAL ALA THR
SEQRES 18 A 258 PRO LYS GLY SER ALA LEU GLY THR PRO VAL ASN LEU ALA
SEQRES 19 A 258 VAL LEU LYS LEU SER GLU GLN GLY ILE LEU ASP LYS LEU
SEQRES 20 A 258 LYS ASN LYS TRP TRP TYR ASP LYS GLY GLU CYS
HET QUS A 301 13
HET ZN A 302 1
HETNAM QUS (S)-2-AMINO-3-(3,5-DIOXO-[1,2,4]OXADIAZOLIDIN-2-YL)-
HETNAM 2 QUS PROPIONIC ACID
HETNAM ZN ZINC ION
HETSYN QUS QUISQUALATE
FORMUL 2 QUS C5 H7 N3 O5
FORMUL 3 ZN ZN 2+
FORMUL 4 HOH *263(H2 O)
HELIX 1 1 ASN A 22 LEU A 26 5 5
HELIX 2 2 GLU A 27 GLU A 30 5 4
HELIX 3 3 GLY A 34 ARG A 48 1 15
HELIX 4 4 ASN A 72 TYR A 80 1 9
HELIX 5 5 THR A 93 GLU A 98 1 6
HELIX 6 6 SER A 123 LYS A 129 1 7
HELIX 7 7 GLY A 141 SER A 150 1 10
HELIX 8 8 ILE A 152 ALA A 165 1 14
HELIX 9 9 THR A 173 SER A 184 1 12
HELIX 10 10 SER A 194 GLN A 202 1 9
HELIX 11 11 LEU A 230 GLN A 244 1 15
HELIX 12 12 GLY A 245 TYR A 256 1 12
SHEET 1 A 3 LYS A 50 ILE A 55 0
SHEET 2 A 3 THR A 5 THR A 10 1 N ILE A 6 O LYS A 50
SHEET 3 A 3 ILE A 85 ALA A 86 1 O ILE A 85 N THR A 9
SHEET 1 B 2 MET A 18 TYR A 19 0
SHEET 2 B 2 TYR A 32 GLU A 33 -1 O GLU A 33 N MET A 18
SHEET 1 C 2 ILE A 100 PHE A 102 0
SHEET 2 C 2 ALA A 223 PRO A 225 -1 O THR A 224 N ASP A 101
SHEET 1 D 2 MET A 107 LEU A 109 0
SHEET 2 D 2 LYS A 218 TYR A 220 -1 O LYS A 218 N LEU A 109
SHEET 1 E 5 PHE A 170 THR A 171 0
SHEET 2 E 5 ALA A 134 LEU A 138 1 N THR A 137 O THR A 171
SHEET 3 E 5 PHE A 188 GLU A 193 1 O LEU A 191 N GLY A 136
SHEET 4 E 5 ILE A 111 LYS A 116 -1 N MET A 114 O PHE A 190
SHEET 5 E 5 THR A 208 VAL A 211 -1 O MET A 209 N ILE A 115
SSBOND 1 CYS A 206 CYS A 261 1555 1555 2.33
LINK NE2 HIS A 23 ZN ZN A 302 1555 1555 2.54
CISPEP 1 SER A 14 PRO A 15 0 -0.52
CISPEP 2 GLU A 166 PRO A 167 0 -5.85
CISPEP 3 LYS A 204 PRO A 205 0 4.83
SITE 1 AC1 13 TYR A 61 PRO A 89 LEU A 90 THR A 91
SITE 2 AC1 13 ARG A 96 LEU A 138 GLY A 141 SER A 142
SITE 3 AC1 13 THR A 143 LEU A 192 GLU A 193 HOH A 402
SITE 4 AC1 13 HOH A 657
SITE 1 AC2 2 HIS A 23 GLU A 24
CRYST1 47.411 47.516 137.595 90.00 90.00 90.00 P 2 2 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 0.021092 0.000000 0.000000 0.00000
SCALE2 0.000000 0.021046 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007268 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
