HEADER TRANSPORT PROTEIN, MEMBRANE PROTEIN 15-JUL-14 4U1O
TITLE GLUA2FLIP SLBD COMPLEXED WITH KAINATE AND (R,R)-2B CRYSTAL FORM C
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMATE RECEPTOR 2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GLUR-2, AMPA-SELECTIVE GLUTAMATE RECEPTOR 2, GLUR-B, GLUR-
COMPND 5 K2, GLUTAMATE RECEPTOR IONOTROPIC, AMPA 2, GLUA2;
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: GRIA2, GLUR2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS AMPA RECEPTOR, TRANSPORT PROTEIN, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR L.CHEN,E.GOUAUX
REVDAT 3 27-DEC-23 4U1O 1 SOURCE REMARK
REVDAT 2 01-OCT-14 4U1O 1 JRNL
REVDAT 1 20-AUG-14 4U1O 0
JRNL AUTH K.L.DURR,L.CHEN,R.A.STEIN,R.DE ZORZI,I.M.FOLEA,T.WALZ,
JRNL AUTH 2 H.S.MCHAOURAB,E.GOUAUX
JRNL TITL STRUCTURE AND DYNAMICS OF AMPA RECEPTOR GLUA2 IN RESTING,
JRNL TITL 2 PRE-OPEN, AND DESENSITIZED STATES.
JRNL REF CELL V. 158 778 2014
JRNL REFN ISSN 1097-4172
JRNL PMID 25109876
JRNL DOI 10.1016/J.CELL.2014.07.023
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309)
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) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.77
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 21861
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.209
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.150
REMARK 3 FREE R VALUE TEST SET COUNT : 1126
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 42.7811 - 3.6995 0.99 2785 136 0.1474 0.1590
REMARK 3 2 3.6995 - 2.9366 1.00 2647 129 0.1526 0.1974
REMARK 3 3 2.9366 - 2.5655 1.00 2575 164 0.1640 0.2528
REMARK 3 4 2.5655 - 2.3309 1.00 2579 163 0.1638 0.1908
REMARK 3 5 2.3309 - 2.1639 1.00 2585 124 0.1757 0.2281
REMARK 3 6 2.1639 - 2.0363 1.00 2553 148 0.1831 0.2096
REMARK 3 7 2.0363 - 1.9343 1.00 2605 131 0.2025 0.2796
REMARK 3 8 1.9343 - 1.8501 0.94 2406 131 0.2675 0.3366
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 : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.390
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.68
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.84
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 : 0.007 2120
REMARK 3 ANGLE : 1.206 2857
REMARK 3 CHIRALITY : 0.078 319
REMARK 3 PLANARITY : 0.004 354
REMARK 3 DIHEDRAL : 12.359 798
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 2:109)
REMARK 3 ORIGIN FOR THE GROUP (A): 16.2769 6.0679 72.9607
REMARK 3 T TENSOR
REMARK 3 T11: 0.0347 T22: 0.0909
REMARK 3 T33: 0.0595 T12: -0.0068
REMARK 3 T13: 0.0046 T23: -0.0119
REMARK 3 L TENSOR
REMARK 3 L11: 1.3811 L22: 1.3417
REMARK 3 L33: 1.6543 L12: 0.0421
REMARK 3 L13: 0.5546 L23: 0.2043
REMARK 3 S TENSOR
REMARK 3 S11: -0.0574 S12: -0.0838 S13: 0.0824
REMARK 3 S21: -0.0102 S22: 0.0303 S23: -0.0791
REMARK 3 S31: -0.0875 S32: 0.1990 S33: 0.0142
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 110:212)
REMARK 3 ORIGIN FOR THE GROUP (A): 17.1194 -9.2453 52.3705
REMARK 3 T TENSOR
REMARK 3 T11: 0.0815 T22: 0.0671
REMARK 3 T33: 0.0604 T12: 0.0030
REMARK 3 T13: 0.0036 T23: -0.0022
REMARK 3 L TENSOR
REMARK 3 L11: 1.5128 L22: 2.0488
REMARK 3 L33: 2.7383 L12: -0.3795
REMARK 3 L13: -0.7214 L23: 0.0777
REMARK 3 S TENSOR
REMARK 3 S11: -0.0748 S12: -0.0105 S13: -0.1478
REMARK 3 S21: -0.0765 S22: -0.0562 S23: 0.0088
REMARK 3 S31: 0.2972 S32: 0.1150 S33: 0.0854
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 213:263)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.2222 8.0384 64.6897
REMARK 3 T TENSOR
REMARK 3 T11: 0.0495 T22: 0.0496
REMARK 3 T33: 0.0940 T12: 0.0120
REMARK 3 T13: -0.0186 T23: -0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 1.0453 L22: 1.1860
REMARK 3 L33: 0.7474 L12: 0.2376
REMARK 3 L13: -0.4303 L23: 0.5381
REMARK 3 S TENSOR
REMARK 3 S11: 0.0057 S12: -0.0040 S13: 0.0806
REMARK 3 S21: -0.1132 S22: 0.0631 S23: 0.1379
REMARK 3 S31: -0.0648 S32: -0.0655 S33: -0.0389
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 4U1O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUL-14.
REMARK 100 THE DEPOSITION ID IS D_1000202657.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-JAN-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21890
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 42.770
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.4000
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: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M NA CACODYLATE, PH 6.5, 1.26 M
REMARK 280 AMMONIUM SULFATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 28.65500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.84000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.65500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.84000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13190 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 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 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 470 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 516 LIES ON A SPECIAL POSITION.
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 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 ARG A 172 CG CD NE CZ NH1 NH2
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 688 DISTANCE = 5.82 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KAI A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FWF A 302
DBREF 4U1O A 3 117 UNP P19491 GRIA2_RAT 413 527
DBREF 4U1O A 120 263 UNP P19491 GRIA2_RAT 653 796
SEQADV 4U1O GLY A 1 UNP P19491 EXPRESSION TAG
SEQADV 4U1O ALA A 2 UNP P19491 EXPRESSION TAG
SEQADV 4U1O GLY A 118 UNP P19491 LINKER
SEQADV 4U1O THR A 119 UNP P19491 LINKER
SEQADV 4U1O SER A 263 UNP P19491 ALA 796 ENGINEERED MUTATION
SEQRES 1 A 263 GLY ALA ASN LYS THR VAL VAL VAL THR THR ILE LEU GLU
SEQRES 2 A 263 SER PRO TYR VAL MET MET LYS LYS ASN HIS GLU MET LEU
SEQRES 3 A 263 GLU GLY ASN GLU ARG TYR GLU GLY TYR CYS VAL ASP LEU
SEQRES 4 A 263 ALA ALA GLU ILE ALA LYS HIS CYS GLY PHE LYS TYR LYS
SEQRES 5 A 263 LEU THR ILE VAL GLY ASP GLY LYS TYR GLY ALA ARG ASP
SEQRES 6 A 263 ALA ASP THR LYS ILE TRP ASN GLY MET VAL GLY GLU LEU
SEQRES 7 A 263 VAL TYR GLY LYS ALA ASP ILE ALA ILE ALA PRO LEU THR
SEQRES 8 A 263 ILE THR LEU VAL ARG GLU GLU VAL ILE ASP PHE SER LYS
SEQRES 9 A 263 PRO PHE MET SER LEU GLY ILE SER ILE MET ILE LYS LYS
SEQRES 10 A 263 GLY THR PRO ILE GLU SER ALA GLU ASP LEU SER LYS GLN
SEQRES 11 A 263 THR GLU ILE ALA TYR GLY THR LEU ASP SER GLY SER THR
SEQRES 12 A 263 LYS GLU PHE PHE ARG ARG SER LYS ILE ALA VAL PHE ASP
SEQRES 13 A 263 LYS MET TRP THR TYR MET ARG SER ALA GLU PRO SER VAL
SEQRES 14 A 263 PHE VAL ARG THR THR ALA GLU GLY VAL ALA ARG VAL ARG
SEQRES 15 A 263 LYS SER LYS GLY LYS TYR ALA TYR LEU LEU GLU SER THR
SEQRES 16 A 263 MET ASN GLU TYR ILE GLU GLN ARG LYS PRO CYS ASP THR
SEQRES 17 A 263 MET LYS VAL GLY GLY ASN LEU ASP SER LYS GLY TYR GLY
SEQRES 18 A 263 ILE ALA THR PRO LYS GLY SER SER LEU GLY THR PRO VAL
SEQRES 19 A 263 ASN LEU ALA VAL LEU LYS LEU SER GLU GLN GLY VAL LEU
SEQRES 20 A 263 ASP LYS LEU LYS ASN LYS TRP TRP TYR ASP LYS GLY GLU
SEQRES 21 A 263 CYS GLY SER
HET KAI A 301 15
HET FWF A 302 32
HETNAM KAI 3-(CARBOXYMETHYL)-4-ISOPROPENYLPROLINE
HETNAM FWF N,N'-[BIPHENYL-4,4'-DIYLDI(2R)PROPANE-2,1-
HETNAM 2 FWF DIYL]DIPROPANE-2-SULFONAMIDE
HETSYN KAI KAINATE
FORMUL 2 KAI C10 H15 N O4
FORMUL 3 FWF C24 H36 N2 O4 S2
FORMUL 4 HOH *319(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 SER A 184 1 12
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 TYR A 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 8 O THR A 54
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 GLY A 136 0
SHEET 2 AA5 4 TYR A 188 GLU A 193 1 O LEU A 191 N GLY A 136
SHEET 3 AA5 4 ILE A 111 LYS A 116 -1 N MET A 114 O TYR A 190
SHEET 4 AA5 4 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 2.03
CISPEP 1 SER A 14 PRO A 15 0 -4.47
CISPEP 2 GLU A 166 PRO A 167 0 -4.02
CISPEP 3 LYS A 204 PRO A 205 0 4.98
SITE 1 AC1 12 TYR A 61 PRO A 89 THR A 91 ARG A 96
SITE 2 AC1 12 LEU A 138 GLY A 141 SER A 142 THR A 143
SITE 3 AC1 12 GLU A 193 HOH A 552 HOH A 553 HOH A 554
SITE 1 AC2 8 ILE A 92 LYS A 104 PRO A 105 SER A 217
SITE 2 AC2 8 LYS A 218 GLY A 219 LEU A 239 SER A 242
CRYST1 57.310 89.680 48.660 90.00 90.00 90.00 P 21 21 2 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 0.017449 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011151 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020551 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
