HEADER MEMBRANE PROTEIN 14-FEB-18 6FQG
TITLE GLUA2(FLOP) G724C LIGAND BINDING CORE DIMER BOUND TO L-GLUTAMATE (FORM
TITLE 2 A) AT 2.34 ANGSTROM RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMATE RECEPTOR 2;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: GLUR-2,AMPA-SELECTIVE GLUTAMATE RECEPTOR 2,GLUR-B,GLUR-K2,
COMPND 5 GLUTAMATE RECEPTOR IONOTROPIC,AMPA 2,GLUA2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: GRIA2, GLUR2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: ORIGAMI B;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS AMPAR RECEPTOR, LIGAND BINDING DOMAIN, COMPETITIVE ANTAGONIST, CROSS-
KEYWDS 2 LINKED DIMER, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR I.D.COOMBS,D.SOTO,M.G.GOLD,M.F.FARRANT,S.G.CULL-CANDY
REVDAT 3 07-FEB-24 6FQG 1 REMARK
REVDAT 2 15-MAR-23 6FQG 1 COMPND SOURCE REMARK HET
REVDAT 2 2 1 HETNAM HETSYN FORMUL ATOM
REVDAT 1 13-MAR-19 6FQG 0
JRNL AUTH I.D.COOMBS,D.SOTO,M.G.GOLD,M.F.FARRANT,S.G.CULL-CANDY
JRNL TITL X-RAY STRUCTURE OF GLUA2 FLOP G724C LIGAND BINDING CORE
JRNL TITL 2 DIMER BOUND TO GLUTAMATE AT 2.32 ANGSTROMS RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.34 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.11.1_2575
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.34
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 51.73
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.351
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.7
REMARK 3 NUMBER OF REFLECTIONS : 43789
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.926
REMARK 3 FREE R VALUE TEST SET COUNT : 2157
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 51.7385 - 5.7719 0.96 2779 191 0.1614 0.2213
REMARK 3 2 5.7719 - 4.5822 0.93 2694 164 0.1468 0.1704
REMARK 3 3 4.5822 - 4.0032 0.97 2870 132 0.1267 0.1787
REMARK 3 4 4.0032 - 3.6373 0.98 2894 116 0.1467 0.2237
REMARK 3 5 3.6373 - 3.3767 0.92 2664 144 0.1646 0.2394
REMARK 3 6 3.3767 - 3.1776 0.97 2819 180 0.1721 0.2269
REMARK 3 7 3.1776 - 3.0185 0.97 2899 104 0.2046 0.2546
REMARK 3 8 3.0185 - 2.8871 0.96 2854 134 0.2092 0.2120
REMARK 3 9 2.8871 - 2.7760 0.96 2762 161 0.2144 0.2657
REMARK 3 10 2.7760 - 2.6802 0.90 2692 111 0.2420 0.2908
REMARK 3 11 2.6802 - 2.5964 0.94 2772 155 0.2442 0.3636
REMARK 3 12 2.5964 - 2.5222 0.95 2727 162 0.2523 0.3052
REMARK 3 13 2.5222 - 2.4558 0.96 2865 142 0.2619 0.2711
REMARK 3 14 2.4558 - 2.3959 0.96 2773 155 0.2699 0.3650
REMARK 3 15 2.3959 - 2.3414 0.86 2568 106 0.3098 0.3478
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.300
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.697
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.91
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 : 0.013 4135
REMARK 3 ANGLE : 1.262 5560
REMARK 3 CHIRALITY : 0.063 616
REMARK 3 PLANARITY : 0.008 694
REMARK 3 DIHEDRAL : 14.500 2514
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 : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'A'
REMARK 3 SELECTION : (CHAIN 'B' AND RESID 4 THROUGH 261)
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6FQG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-FEB-18.
REMARK 100 THE DEPOSITION ID IS D_1200008363.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-DEC-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.0
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) : 0.97623
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.27
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45174
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.980
REMARK 200 RESOLUTION RANGE LOW (A) : 92.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.98
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 1.26700
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3KGC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM CHLORIDE, 20% PEG 3350,
REMARK 280 10UM ZK200775, PH 4.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 287K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 43.82750
REMARK 290 SMTRY3 2 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: 900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 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 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 ALA A 2
REMARK 465 ASN A 3
REMARK 465 GLY A 262
REMARK 465 SER A 263
REMARK 465 GLY A 264
REMARK 465 GLY B 1
REMARK 465 ALA B 2
REMARK 465 ASN B 3
REMARK 465 SER B 263
REMARK 465 GLY B 264
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 CYS A 261 O
REMARK 470 CYS B 261 O
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 HH22 ARG B 148 O HOH B 401 1.29
REMARK 500 HZ2 LYS A 69 O HOH A 401 1.34
REMARK 500 HE ARG A 148 O HOH A 404 1.55
REMARK 500 NH2 ARG B 148 O HOH B 401 2.02
REMARK 500 NZ LYS A 69 O HOH A 401 2.05
REMARK 500 O SER A 140 O HOH A 402 2.07
REMARK 500 OG1 THR B 224 O HOH B 402 2.07
REMARK 500 O HOH B 404 O HOH B 451 2.07
REMARK 500 OH TYR A 51 O HOH A 403 2.14
REMARK 500 O HOH B 456 O HOH B 457 2.16
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 ASN A 22 43.59 -101.44
REMARK 500 PRO A 89 69.19 -69.81
REMARK 500 SER A 140 60.15 -155.03
REMARK 500 TRP A 255 -65.57 -91.78
REMARK 500 ASN B 22 40.37 -101.80
REMARK 500 LYS B 69 19.74 54.08
REMARK 500 SER B 140 57.68 -158.07
REMARK 500 GLN B 202 30.57 -99.00
REMARK 500 TRP B 255 -65.90 -96.09
REMARK 500 GLU B 260 20.94 -141.53
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 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GLU B 301
DBREF 6FQG A 3 117 UNP P19491 GRIA2_RAT 413 527
DBREF 6FQG A 120 264 UNP P19491 GRIA2_RAT 653 797
DBREF 6FQG B 3 117 UNP P19491 GRIA2_RAT 413 527
DBREF 6FQG B 120 264 UNP P19491 GRIA2_RAT 653 797
SEQADV 6FQG GLY A 1 UNP P19491 EXPRESSION TAG
SEQADV 6FQG ALA A 2 UNP P19491 EXPRESSION TAG
SEQADV 6FQG GLY A 118 UNP P19491 LINKER
SEQADV 6FQG THR A 119 UNP P19491 LINKER
SEQADV 6FQG CYS A 212 UNP P19491 GLY 745 CONFLICT
SEQADV 6FQG GLY B 1 UNP P19491 EXPRESSION TAG
SEQADV 6FQG ALA B 2 UNP P19491 EXPRESSION TAG
SEQADV 6FQG GLY B 118 UNP P19491 LINKER
SEQADV 6FQG THR B 119 UNP P19491 LINKER
SEQADV 6FQG CYS B 212 UNP P19491 GLY 745 CONFLICT
SEQRES 1 A 264 GLY ALA ASN LYS THR VAL VAL VAL THR THR ILE LEU GLU
SEQRES 2 A 264 SER PRO TYR VAL MET MET LYS LYS ASN HIS GLU MET LEU
SEQRES 3 A 264 GLU GLY ASN GLU ARG TYR GLU GLY TYR CYS VAL ASP LEU
SEQRES 4 A 264 ALA ALA GLU ILE ALA LYS HIS CYS GLY PHE LYS TYR LYS
SEQRES 5 A 264 LEU THR ILE VAL GLY ASP GLY LYS TYR GLY ALA ARG ASP
SEQRES 6 A 264 ALA ASP THR LYS ILE TRP ASN GLY MET VAL GLY GLU LEU
SEQRES 7 A 264 VAL TYR GLY LYS ALA ASP ILE ALA ILE ALA PRO LEU THR
SEQRES 8 A 264 ILE THR LEU VAL ARG GLU GLU VAL ILE ASP PHE SER LYS
SEQRES 9 A 264 PRO PHE MET SER LEU GLY ILE SER ILE MET ILE LYS LYS
SEQRES 10 A 264 GLY THR PRO ILE GLU SER ALA GLU ASP LEU SER LYS GLN
SEQRES 11 A 264 THR GLU ILE ALA TYR GLY THR LEU ASP SER GLY SER THR
SEQRES 12 A 264 LYS GLU PHE PHE ARG ARG SER LYS ILE ALA VAL PHE ASP
SEQRES 13 A 264 LYS MET TRP THR TYR MET ARG SER ALA GLU PRO SER VAL
SEQRES 14 A 264 PHE VAL ARG THR THR ALA GLU GLY VAL ALA ARG VAL ARG
SEQRES 15 A 264 LYS SER LYS GLY LYS TYR ALA TYR LEU LEU GLU SER THR
SEQRES 16 A 264 MET ASN GLU TYR ILE GLU GLN ARG LYS PRO CYS ASP THR
SEQRES 17 A 264 MET LYS VAL CYS GLY ASN LEU ASP SER LYS GLY TYR GLY
SEQRES 18 A 264 ILE ALA THR PRO LYS GLY SER SER LEU GLY ASN ALA VAL
SEQRES 19 A 264 ASN LEU ALA VAL LEU LYS LEU ASN GLU GLN GLY LEU LEU
SEQRES 20 A 264 ASP LYS LEU LYS ASN LYS TRP TRP TYR ASP LYS GLY GLU
SEQRES 21 A 264 CYS GLY SER GLY
SEQRES 1 B 264 GLY ALA ASN LYS THR VAL VAL VAL THR THR ILE LEU GLU
SEQRES 2 B 264 SER PRO TYR VAL MET MET LYS LYS ASN HIS GLU MET LEU
SEQRES 3 B 264 GLU GLY ASN GLU ARG TYR GLU GLY TYR CYS VAL ASP LEU
SEQRES 4 B 264 ALA ALA GLU ILE ALA LYS HIS CYS GLY PHE LYS TYR LYS
SEQRES 5 B 264 LEU THR ILE VAL GLY ASP GLY LYS TYR GLY ALA ARG ASP
SEQRES 6 B 264 ALA ASP THR LYS ILE TRP ASN GLY MET VAL GLY GLU LEU
SEQRES 7 B 264 VAL TYR GLY LYS ALA ASP ILE ALA ILE ALA PRO LEU THR
SEQRES 8 B 264 ILE THR LEU VAL ARG GLU GLU VAL ILE ASP PHE SER LYS
SEQRES 9 B 264 PRO PHE MET SER LEU GLY ILE SER ILE MET ILE LYS LYS
SEQRES 10 B 264 GLY THR PRO ILE GLU SER ALA GLU ASP LEU SER LYS GLN
SEQRES 11 B 264 THR GLU ILE ALA TYR GLY THR LEU ASP SER GLY SER THR
SEQRES 12 B 264 LYS GLU PHE PHE ARG ARG SER LYS ILE ALA VAL PHE ASP
SEQRES 13 B 264 LYS MET TRP THR TYR MET ARG SER ALA GLU PRO SER VAL
SEQRES 14 B 264 PHE VAL ARG THR THR ALA GLU GLY VAL ALA ARG VAL ARG
SEQRES 15 B 264 LYS SER LYS GLY LYS TYR ALA TYR LEU LEU GLU SER THR
SEQRES 16 B 264 MET ASN GLU TYR ILE GLU GLN ARG LYS PRO CYS ASP THR
SEQRES 17 B 264 MET LYS VAL CYS GLY ASN LEU ASP SER LYS GLY TYR GLY
SEQRES 18 B 264 ILE ALA THR PRO LYS GLY SER SER LEU GLY ASN ALA VAL
SEQRES 19 B 264 ASN LEU ALA VAL LEU LYS LEU ASN GLU GLN GLY LEU LEU
SEQRES 20 B 264 ASP LYS LEU LYS ASN LYS TRP TRP TYR ASP LYS GLY GLU
SEQRES 21 B 264 CYS GLY SER GLY
HET GLU A 301 17
HET GLU B 301 17
HETNAM GLU GLUTAMIC ACID
FORMUL 3 GLU 2(C5 H9 N O4)
FORMUL 5 HOH *104(H2 O)
HELIX 1 AA1 ASN A 22 LEU A 26 5 5
HELIX 2 AA2 GLU A 27 GLU A 30 5 4
HELIX 3 AA3 GLY A 34 GLY A 48 1 15
HELIX 4 AA4 ASN A 72 TYR A 80 1 9
HELIX 5 AA5 THR A 93 GLU A 98 1 6
HELIX 6 AA6 SER A 123 LYS A 129 1 7
HELIX 7 AA7 GLY A 141 SER A 150 1 10
HELIX 8 AA8 ILE A 152 ALA A 165 1 14
HELIX 9 AA9 THR A 173 LYS A 183 1 11
HELIX 10 AB1 SER A 194 GLN A 202 1 9
HELIX 11 AB2 LEU A 230 GLN A 244 1 15
HELIX 12 AB3 GLY A 245 TRP A 255 1 11
HELIX 13 AB4 ASN B 22 LEU B 26 5 5
HELIX 14 AB5 GLU B 27 GLU B 30 5 4
HELIX 15 AB6 GLY B 34 CYS B 47 1 14
HELIX 16 AB7 ASN B 72 TYR B 80 1 9
HELIX 17 AB8 THR B 93 GLU B 98 1 6
HELIX 18 AB9 SER B 123 LYS B 129 1 7
HELIX 19 AC1 GLY B 141 SER B 150 1 10
HELIX 20 AC2 ILE B 152 ALA B 165 1 14
HELIX 21 AC3 THR B 173 LYS B 183 1 11
HELIX 22 AC4 SER B 194 GLN B 202 1 9
HELIX 23 AC5 SER B 229 GLN B 244 1 16
HELIX 24 AC6 GLY B 245 TYR B 256 1 12
SHEET 1 AA1 3 TYR A 51 ILE A 55 0
SHEET 2 AA1 3 VAL A 6 THR A 10 1 N VAL A 6 O LYS A 52
SHEET 3 AA1 3 ILE A 85 ALA A 86 1 O ILE A 85 N THR A 9
SHEET 1 AA2 2 MET A 18 MET A 19 0
SHEET 2 AA2 2 TYR A 32 GLU A 33 -1 O GLU A 33 N MET A 18
SHEET 1 AA3 2 ILE A 100 PHE A 102 0
SHEET 2 AA3 2 ALA A 223 PRO A 225 -1 O THR A 224 N ASP A 101
SHEET 1 AA4 2 MET A 107 LEU A 109 0
SHEET 2 AA4 2 LYS A 218 TYR A 220 -1 O LYS A 218 N LEU A 109
SHEET 1 AA5 4 ALA A 134 THR A 137 0
SHEET 2 AA5 4 TYR A 188 GLU A 193 1 O ALA A 189 N ALA A 134
SHEET 3 AA5 4 ILE A 111 LYS A 116 -1 N SER A 112 O LEU A 192
SHEET 4 AA5 4 THR A 208 LYS A 210 -1 O MET A 209 N ILE A 115
SHEET 1 AA6 3 TYR B 51 ILE B 55 0
SHEET 2 AA6 3 VAL B 6 THR B 10 1 N VAL B 8 O LYS B 52
SHEET 3 AA6 3 ILE B 85 ALA B 86 1 O ILE B 85 N THR B 9
SHEET 1 AA7 2 MET B 18 MET B 19 0
SHEET 2 AA7 2 TYR B 32 GLU B 33 -1 O GLU B 33 N MET B 18
SHEET 1 AA8 2 ILE B 100 PHE B 102 0
SHEET 2 AA8 2 ALA B 223 PRO B 225 -1 O THR B 224 N ASP B 101
SHEET 1 AA9 2 MET B 107 LEU B 109 0
SHEET 2 AA9 2 LYS B 218 TYR B 220 -1 O LYS B 218 N LEU B 109
SHEET 1 AB1 4 ALA B 134 GLY B 136 0
SHEET 2 AB1 4 TYR B 188 GLU B 193 1 O ALA B 189 N ALA B 134
SHEET 3 AB1 4 ILE B 111 LYS B 116 -1 N SER B 112 O LEU B 192
SHEET 4 AB1 4 THR B 208 LYS B 210 -1 O MET B 209 N ILE B 115
SSBOND 1 CYS A 206 CYS A 261 1555 1555 2.02
SSBOND 2 CYS A 212 CYS B 212 1555 1555 2.08
SSBOND 3 CYS B 206 CYS B 261 1555 1555 2.03
CISPEP 1 SER A 14 PRO A 15 0 2.57
CISPEP 2 GLU A 166 PRO A 167 0 3.18
CISPEP 3 LYS A 204 PRO A 205 0 1.76
CISPEP 4 SER B 14 PRO B 15 0 3.30
CISPEP 5 GLU B 166 PRO B 167 0 4.44
CISPEP 6 LYS B 204 PRO B 205 0 2.96
SITE 1 AC1 12 TYR A 61 PRO A 89 LEU A 90 THR A 91
SITE 2 AC1 12 ARG A 96 GLY A 141 SER A 142 THR A 143
SITE 3 AC1 12 GLU A 193 HOH A 412 HOH A 416 HOH A 431
SITE 1 AC2 11 TYR B 61 PRO B 89 THR B 91 ARG B 96
SITE 2 AC2 11 GLY B 141 SER B 142 THR B 143 GLU B 193
SITE 3 AC2 11 HOH B 412 HOH B 428 HOH B 430
CRYST1 50.465 87.655 68.280 90.00 110.22 90.00 P 1 21 1 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 0.019816 0.000000 0.007300 0.00000
SCALE2 0.000000 0.011408 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015608 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
