HEADER TRANSPORT PROTEIN 24-JAN-20 6XWP
TITLE STRUCTURE OF GLUTAMATE TRANSPORTER HOMOLOGUE GLTTK IN UNSATURATED
TITLE 2 CONDITIONS - OUTWARD-OUTWARD-INWARD CONFIGURATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTON/GLUTAMATE SYMPORTER, SDF FAMILY;
COMPND 3 CHAIN: A, B, C;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOCOCCUS KODAKARENSIS (STRAIN ATCC BAA-918
SOURCE 3 / JCM 12380 / KOD1);
SOURCE 4 ORGANISM_TAXID: 69014;
SOURCE 5 GENE: TK0986;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS AMINO ACID TRANSPORTER, ASPARTATE TRANSPORT, GLUTAMATE TRANSPORTER
KEYWDS 2 HOMOLOGUE, TRANSPORT PROTEIN, MEMBRANE PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR V.ARKHIPOVA,D.J.SLOTBOOM,A.GUSKOV
REVDAT 1 04-MAR-20 6XWP 0
JRNL AUTH V.ARKHIPOVA,A.GUSKOV,D.J.SLOTBOOM
JRNL TITL STRUCTURAL ENSEMBLE OF A GLUTAMATE TRANSPORTER HOMOLOGUE IN
JRNL TITL 2 LIPID NANODISC ENVIRONMENT.
JRNL REF NAT COMMUN V. 11 998 2020
JRNL REFN ESSN 2041-1723
JRNL PMID 32081874
JRNL DOI 10.1038/S41467-020-14834-8
REMARK 2
REMARK 2 RESOLUTION. 3.38 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : NULL
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : NULL
REMARK 3 REFINEMENT SPACE : NULL
REMARK 3 REFINEMENT PROTOCOL : NULL
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : NULL
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.380
REMARK 3 NUMBER OF PARTICLES : 72313
REMARK 3 CTF CORRECTION METHOD : NONE
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 6XWP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-JAN-20.
REMARK 100 THE DEPOSITION ID IS D_1292105757.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE
REMARK 245 SPECIMEN TYPE : NULL
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : PARTICLE
REMARK 245 PARTICLE TYPE : POINT
REMARK 245 NAME OF SAMPLE : TRIMER OF GLTTK
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 7.40
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TECNAI ARCTICA
REMARK 245 DETECTOR TYPE : GATAN K2 QUANTUM (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : NULL
REMARK 245 MAXIMUM DEFOCUS (NM) : NULL
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : NULL
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 53.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : NULL
REMARK 245 CALIBRATED MAGNIFICATION : NULL
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 200
REMARK 245 IMAGING DETAILS : NULL
REMARK 247
REMARK 247 ELECTRON MICROSCOPY
REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON
REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE
REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES
REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION
REMARK 247 OF THE STRUCTURE FACTORS.
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 47880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -63.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 MET A 1
REMARK 465 GLY A 2
REMARK 465 LYS A 3
REMARK 465 SER A 4
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 LYS B 3
REMARK 465 SER B 4
REMARK 465 MET C 1
REMARK 465 GLY C 2
REMARK 465 LYS C 3
REMARK 465 SER C 4
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 OH TYR B 9 O GLN B 205 2.11
REMARK 500 OD1 ASP C 424 OG SER C 426 2.16
REMARK 500 NZ LYS B 17 OE1 GLN B 205 2.17
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 TYR A 37 15.14 -140.12
REMARK 500 ASN A 114 35.66 -99.66
REMARK 500 GLU A 126 -13.48 74.00
REMARK 500 ALA A 127 11.32 51.07
REMARK 500 GLN A 128 73.82 44.07
REMARK 500 ARG A 278 19.71 52.29
REMARK 500 VAL A 358 143.36 -170.02
REMARK 500 LYS A 421 65.71 60.47
REMARK 500 GLU B 126 33.39 -91.93
REMARK 500 MET B 171 3.79 -66.51
REMARK 500 VAL B 227 -50.63 -127.50
REMARK 500 LYS B 268 -9.81 -55.21
REMARK 500 PRO B 335 -176.72 -69.45
REMARK 500 PRO B 379 -5.04 -56.30
REMARK 500 LEU C 15 -8.94 73.45
REMARK 500 ILE C 75 -72.33 -87.08
REMARK 500 SER C 76 169.67 176.95
REMARK 500 ALA C 113 -60.37 -94.91
REMARK 500 MET C 171 4.17 -66.00
REMARK 500 PRO C 229 0.08 -63.46
REMARK 500 ARG C 278 17.01 56.46
REMARK 500 ASP C 424 99.96 -69.79
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 ASP B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ASP C 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-10634 RELATED DB: EMDB
REMARK 900 STRUCTURE OF GLUTAMATE TRANSPORTER HOMOLOGUE GLTTK IN UNSATURATED
REMARK 900 CONDITIONS - OUTWARD-OUTWARD-INWARD CONFIGURATION
REMARK 900 RELATED ID: 6XWO RELATED DB: PDB
REMARK 900 STRUCTURE OF GLUTAMATE TRANSPORTER HOMOLOGUE GLTTK IN THE
REMARK 900 UNSATURATED CONDITIONS - INWARD-INWARD-OUTWARD CONFIGURATION
REMARK 900 RELATED ID: 6XWQ RELATED DB: PDB
REMARK 900 STRUCTURE OF GLUTAMATE TRANSPORTER HOMOLOGUE GLTTK IN THE SATURATED
REMARK 900 CONDITIONS
REMARK 900 RELATED ID: 6XWR RELATED DB: PDB
REMARK 900 STRUCTURE OF GLUTAMATE TRANSPORTER HOMOLOGUE GLTTK IN SODIUM ONLY
REMARK 900 CONDITION
REMARK 900 RELATED ID: 6XWN RELATED DB: PDB
REMARK 900 STRUCTURE OF GLUTAMATE TRANSPORTER HOMOLOGUE GLTTK IN THE PRESENCE
REMARK 900 OF TBOA INHIBITOR
DBREF 6XWP A 1 430 UNP Q5JID0 Q5JID0_THEKO 1 430
DBREF 6XWP B 1 430 UNP Q5JID0 Q5JID0_THEKO 1 430
DBREF 6XWP C 1 430 UNP Q5JID0 Q5JID0_THEKO 1 430
SEQRES 1 A 430 MET GLY LYS SER LEU LEU ARG ARG TYR LEU ASP TYR PRO
SEQRES 2 A 430 VAL LEU TRP LYS ILE LEU TRP GLY LEU VAL LEU GLY ALA
SEQRES 3 A 430 VAL PHE GLY LEU ILE ALA GLY HIS PHE GLY TYR ALA GLY
SEQRES 4 A 430 ALA VAL LYS THR TYR ILE LYS PRO PHE GLY ASP LEU PHE
SEQRES 5 A 430 VAL ARG LEU LEU LYS MET LEU VAL MET PRO ILE VAL LEU
SEQRES 6 A 430 ALA SER LEU VAL VAL GLY ALA ALA SER ILE SER PRO ALA
SEQRES 7 A 430 ARG LEU GLY ARG VAL GLY VAL LYS ILE VAL VAL TYR TYR
SEQRES 8 A 430 LEU ALA THR SER ALA MET ALA VAL PHE PHE GLY LEU ILE
SEQRES 9 A 430 VAL GLY ARG LEU PHE ASN VAL GLY ALA ASN VAL ASN LEU
SEQRES 10 A 430 GLY SER GLY THR GLY LYS ALA ILE GLU ALA GLN PRO PRO
SEQRES 11 A 430 SER LEU VAL GLN THR LEU LEU ASN ILE VAL PRO THR ASN
SEQRES 12 A 430 PRO PHE ALA SER LEU ALA LYS GLY GLU VAL LEU PRO VAL
SEQRES 13 A 430 ILE PHE PHE ALA ILE ILE LEU GLY ILE ALA ILE THR TYR
SEQRES 14 A 430 LEU MET ASN ARG ASN GLU GLU ARG VAL ARG LYS SER ALA
SEQRES 15 A 430 GLU THR LEU LEU ARG VAL PHE ASP GLY LEU ALA GLU ALA
SEQRES 16 A 430 MET TYR LEU ILE VAL GLY GLY VAL MET GLN TYR ALA PRO
SEQRES 17 A 430 ILE GLY VAL PHE ALA LEU ILE ALA TYR VAL MET ALA GLU
SEQRES 18 A 430 GLN GLY VAL ARG VAL VAL GLY PRO LEU ALA LYS VAL VAL
SEQRES 19 A 430 GLY ALA VAL TYR THR GLY LEU PHE LEU GLN ILE VAL ILE
SEQRES 20 A 430 THR TYR PHE ILE LEU LEU LYS VAL PHE GLY ILE ASP PRO
SEQRES 21 A 430 ILE LYS PHE ILE ARG LYS ALA LYS ASP ALA MET ILE THR
SEQRES 22 A 430 ALA PHE VAL THR ARG SER SER SER GLY THR LEU PRO VAL
SEQRES 23 A 430 THR MET ARG VAL ALA GLU GLU GLU MET GLY VAL ASP LYS
SEQRES 24 A 430 GLY ILE PHE SER PHE THR LEU PRO LEU GLY ALA THR ILE
SEQRES 25 A 430 ASN MET ASP GLY THR ALA LEU TYR GLN GLY VAL THR VAL
SEQRES 26 A 430 LEU PHE VAL ALA ASN ALA ILE GLY HIS PRO LEU THR LEU
SEQRES 27 A 430 GLY GLN GLN LEU VAL VAL VAL LEU THR ALA VAL LEU ALA
SEQRES 28 A 430 SER ILE GLY THR ALA GLY VAL PRO GLY ALA GLY ALA ILE
SEQRES 29 A 430 MET LEU ALA MET VAL LEU GLN SER VAL GLY LEU ASP LEU
SEQRES 30 A 430 THR PRO GLY SER PRO VAL ALA LEU ALA TYR ALA MET ILE
SEQRES 31 A 430 LEU GLY ILE ASP ALA ILE LEU ASP MET GLY ARG THR MET
SEQRES 32 A 430 VAL ASN VAL THR GLY ASP LEU ALA GLY THR VAL ILE VAL
SEQRES 33 A 430 ALA LYS THR GLU LYS GLU LEU ASP GLU SER LYS TRP ILE
SEQRES 34 A 430 SER
SEQRES 1 B 430 MET GLY LYS SER LEU LEU ARG ARG TYR LEU ASP TYR PRO
SEQRES 2 B 430 VAL LEU TRP LYS ILE LEU TRP GLY LEU VAL LEU GLY ALA
SEQRES 3 B 430 VAL PHE GLY LEU ILE ALA GLY HIS PHE GLY TYR ALA GLY
SEQRES 4 B 430 ALA VAL LYS THR TYR ILE LYS PRO PHE GLY ASP LEU PHE
SEQRES 5 B 430 VAL ARG LEU LEU LYS MET LEU VAL MET PRO ILE VAL LEU
SEQRES 6 B 430 ALA SER LEU VAL VAL GLY ALA ALA SER ILE SER PRO ALA
SEQRES 7 B 430 ARG LEU GLY ARG VAL GLY VAL LYS ILE VAL VAL TYR TYR
SEQRES 8 B 430 LEU ALA THR SER ALA MET ALA VAL PHE PHE GLY LEU ILE
SEQRES 9 B 430 VAL GLY ARG LEU PHE ASN VAL GLY ALA ASN VAL ASN LEU
SEQRES 10 B 430 GLY SER GLY THR GLY LYS ALA ILE GLU ALA GLN PRO PRO
SEQRES 11 B 430 SER LEU VAL GLN THR LEU LEU ASN ILE VAL PRO THR ASN
SEQRES 12 B 430 PRO PHE ALA SER LEU ALA LYS GLY GLU VAL LEU PRO VAL
SEQRES 13 B 430 ILE PHE PHE ALA ILE ILE LEU GLY ILE ALA ILE THR TYR
SEQRES 14 B 430 LEU MET ASN ARG ASN GLU GLU ARG VAL ARG LYS SER ALA
SEQRES 15 B 430 GLU THR LEU LEU ARG VAL PHE ASP GLY LEU ALA GLU ALA
SEQRES 16 B 430 MET TYR LEU ILE VAL GLY GLY VAL MET GLN TYR ALA PRO
SEQRES 17 B 430 ILE GLY VAL PHE ALA LEU ILE ALA TYR VAL MET ALA GLU
SEQRES 18 B 430 GLN GLY VAL ARG VAL VAL GLY PRO LEU ALA LYS VAL VAL
SEQRES 19 B 430 GLY ALA VAL TYR THR GLY LEU PHE LEU GLN ILE VAL ILE
SEQRES 20 B 430 THR TYR PHE ILE LEU LEU LYS VAL PHE GLY ILE ASP PRO
SEQRES 21 B 430 ILE LYS PHE ILE ARG LYS ALA LYS ASP ALA MET ILE THR
SEQRES 22 B 430 ALA PHE VAL THR ARG SER SER SER GLY THR LEU PRO VAL
SEQRES 23 B 430 THR MET ARG VAL ALA GLU GLU GLU MET GLY VAL ASP LYS
SEQRES 24 B 430 GLY ILE PHE SER PHE THR LEU PRO LEU GLY ALA THR ILE
SEQRES 25 B 430 ASN MET ASP GLY THR ALA LEU TYR GLN GLY VAL THR VAL
SEQRES 26 B 430 LEU PHE VAL ALA ASN ALA ILE GLY HIS PRO LEU THR LEU
SEQRES 27 B 430 GLY GLN GLN LEU VAL VAL VAL LEU THR ALA VAL LEU ALA
SEQRES 28 B 430 SER ILE GLY THR ALA GLY VAL PRO GLY ALA GLY ALA ILE
SEQRES 29 B 430 MET LEU ALA MET VAL LEU GLN SER VAL GLY LEU ASP LEU
SEQRES 30 B 430 THR PRO GLY SER PRO VAL ALA LEU ALA TYR ALA MET ILE
SEQRES 31 B 430 LEU GLY ILE ASP ALA ILE LEU ASP MET GLY ARG THR MET
SEQRES 32 B 430 VAL ASN VAL THR GLY ASP LEU ALA GLY THR VAL ILE VAL
SEQRES 33 B 430 ALA LYS THR GLU LYS GLU LEU ASP GLU SER LYS TRP ILE
SEQRES 34 B 430 SER
SEQRES 1 C 430 MET GLY LYS SER LEU LEU ARG ARG TYR LEU ASP TYR PRO
SEQRES 2 C 430 VAL LEU TRP LYS ILE LEU TRP GLY LEU VAL LEU GLY ALA
SEQRES 3 C 430 VAL PHE GLY LEU ILE ALA GLY HIS PHE GLY TYR ALA GLY
SEQRES 4 C 430 ALA VAL LYS THR TYR ILE LYS PRO PHE GLY ASP LEU PHE
SEQRES 5 C 430 VAL ARG LEU LEU LYS MET LEU VAL MET PRO ILE VAL LEU
SEQRES 6 C 430 ALA SER LEU VAL VAL GLY ALA ALA SER ILE SER PRO ALA
SEQRES 7 C 430 ARG LEU GLY ARG VAL GLY VAL LYS ILE VAL VAL TYR TYR
SEQRES 8 C 430 LEU ALA THR SER ALA MET ALA VAL PHE PHE GLY LEU ILE
SEQRES 9 C 430 VAL GLY ARG LEU PHE ASN VAL GLY ALA ASN VAL ASN LEU
SEQRES 10 C 430 GLY SER GLY THR GLY LYS ALA ILE GLU ALA GLN PRO PRO
SEQRES 11 C 430 SER LEU VAL GLN THR LEU LEU ASN ILE VAL PRO THR ASN
SEQRES 12 C 430 PRO PHE ALA SER LEU ALA LYS GLY GLU VAL LEU PRO VAL
SEQRES 13 C 430 ILE PHE PHE ALA ILE ILE LEU GLY ILE ALA ILE THR TYR
SEQRES 14 C 430 LEU MET ASN ARG ASN GLU GLU ARG VAL ARG LYS SER ALA
SEQRES 15 C 430 GLU THR LEU LEU ARG VAL PHE ASP GLY LEU ALA GLU ALA
SEQRES 16 C 430 MET TYR LEU ILE VAL GLY GLY VAL MET GLN TYR ALA PRO
SEQRES 17 C 430 ILE GLY VAL PHE ALA LEU ILE ALA TYR VAL MET ALA GLU
SEQRES 18 C 430 GLN GLY VAL ARG VAL VAL GLY PRO LEU ALA LYS VAL VAL
SEQRES 19 C 430 GLY ALA VAL TYR THR GLY LEU PHE LEU GLN ILE VAL ILE
SEQRES 20 C 430 THR TYR PHE ILE LEU LEU LYS VAL PHE GLY ILE ASP PRO
SEQRES 21 C 430 ILE LYS PHE ILE ARG LYS ALA LYS ASP ALA MET ILE THR
SEQRES 22 C 430 ALA PHE VAL THR ARG SER SER SER GLY THR LEU PRO VAL
SEQRES 23 C 430 THR MET ARG VAL ALA GLU GLU GLU MET GLY VAL ASP LYS
SEQRES 24 C 430 GLY ILE PHE SER PHE THR LEU PRO LEU GLY ALA THR ILE
SEQRES 25 C 430 ASN MET ASP GLY THR ALA LEU TYR GLN GLY VAL THR VAL
SEQRES 26 C 430 LEU PHE VAL ALA ASN ALA ILE GLY HIS PRO LEU THR LEU
SEQRES 27 C 430 GLY GLN GLN LEU VAL VAL VAL LEU THR ALA VAL LEU ALA
SEQRES 28 C 430 SER ILE GLY THR ALA GLY VAL PRO GLY ALA GLY ALA ILE
SEQRES 29 C 430 MET LEU ALA MET VAL LEU GLN SER VAL GLY LEU ASP LEU
SEQRES 30 C 430 THR PRO GLY SER PRO VAL ALA LEU ALA TYR ALA MET ILE
SEQRES 31 C 430 LEU GLY ILE ASP ALA ILE LEU ASP MET GLY ARG THR MET
SEQRES 32 C 430 VAL ASN VAL THR GLY ASP LEU ALA GLY THR VAL ILE VAL
SEQRES 33 C 430 ALA LYS THR GLU LYS GLU LEU ASP GLU SER LYS TRP ILE
SEQRES 34 C 430 SER
HET ASP B 501 9
HET ASP C 501 9
HETNAM ASP ASPARTIC ACID
FORMUL 4 ASP 2(C4 H7 N O4)
HELIX 1 AA1 LEU A 5 TYR A 12 1 8
HELIX 2 AA2 PRO A 13 PHE A 35 1 23
HELIX 3 AA3 TYR A 37 TYR A 44 1 8
HELIX 4 AA4 LYS A 46 SER A 74 1 29
HELIX 5 AA5 GLY A 81 ASN A 110 1 30
HELIX 6 AA6 LEU A 132 LEU A 136 5 5
HELIX 7 AA7 ASN A 143 LYS A 150 1 8
HELIX 8 AA8 VAL A 153 MET A 171 1 19
HELIX 9 AA9 GLU A 176 GLN A 222 1 47
HELIX 10 AB1 VAL A 226 PHE A 256 1 31
HELIX 11 AB2 ASP A 259 ARG A 278 1 20
HELIX 12 AB3 THR A 283 GLU A 294 1 12
HELIX 13 AB4 ASP A 298 ASN A 313 1 16
HELIX 14 AB5 MET A 314 ILE A 332 1 19
HELIX 15 AB6 THR A 337 ILE A 353 1 17
HELIX 16 AB7 GLY A 360 VAL A 373 1 14
HELIX 17 AB8 SER A 381 THR A 419 1 39
HELIX 18 AB9 ASP A 424 TRP A 428 5 5
HELIX 19 AC1 ARG B 7 TYR B 12 1 6
HELIX 20 AC2 PRO B 13 PHE B 35 1 23
HELIX 21 AC3 TYR B 37 ILE B 45 1 9
HELIX 22 AC4 ILE B 45 LEU B 56 1 12
HELIX 23 AC5 VAL B 60 SER B 74 1 15
HELIX 24 AC6 SER B 76 PHE B 109 1 34
HELIX 25 AC7 LEU B 132 ILE B 139 1 8
HELIX 26 AC8 ASN B 143 GLY B 151 1 9
HELIX 27 AC9 GLU B 152 MET B 171 1 20
HELIX 28 AD1 GLU B 176 VAL B 211 1 36
HELIX 29 AD2 VAL B 211 GLY B 223 1 13
HELIX 30 AD3 GLY B 228 VAL B 255 1 28
HELIX 31 AD4 ASP B 259 ARG B 278 1 20
HELIX 32 AD5 THR B 283 ALA B 291 1 9
HELIX 33 AD6 ILE B 301 ASN B 313 1 13
HELIX 34 AD7 MET B 314 ALA B 331 1 18
HELIX 35 AD8 THR B 337 ILE B 353 1 17
HELIX 36 AD9 GLY B 360 VAL B 373 1 14
HELIX 37 AE1 SER B 381 MET B 389 1 9
HELIX 38 AE2 ILE B 393 GLU B 420 1 28
HELIX 39 AE3 ASP B 424 TRP B 428 5 5
HELIX 40 AE4 LEU C 6 LEU C 10 1 5
HELIX 41 AE5 LYS C 17 GLY C 36 1 20
HELIX 42 AE6 TYR C 37 ILE C 45 1 9
HELIX 43 AE7 ILE C 45 LEU C 59 1 15
HELIX 44 AE8 VAL C 60 ILE C 75 1 16
HELIX 45 AE9 PRO C 77 ASN C 110 1 34
HELIX 46 AF1 SER C 131 ILE C 139 1 9
HELIX 47 AF2 ASN C 143 LYS C 150 1 8
HELIX 48 AF3 GLU C 152 MET C 171 1 20
HELIX 49 AF4 GLU C 176 GLN C 222 1 47
HELIX 50 AF5 PRO C 229 THR C 248 1 20
HELIX 51 AF6 THR C 248 GLY C 257 1 10
HELIX 52 AF7 ASP C 259 ILE C 272 1 14
HELIX 53 AF8 SER C 279 GLY C 282 5 4
HELIX 54 AF9 THR C 283 ARG C 289 1 7
HELIX 55 AG1 ARG C 289 GLU C 294 1 6
HELIX 56 AG2 ASP C 298 GLY C 309 1 12
HELIX 57 AG3 MET C 314 GLY C 333 1 20
HELIX 58 AG4 THR C 337 GLY C 354 1 18
HELIX 59 AG5 MET C 365 VAL C 373 1 9
HELIX 60 AG6 SER C 381 GLU C 420 1 40
SITE 1 AC1 13 ARG B 278 SER B 279 SER B 280 MET B 314
SITE 2 AC1 13 THR B 317 GLY B 357 VAL B 358 ALA B 361
SITE 3 AC1 13 GLY B 362 ASP B 398 ARG B 401 THR B 402
SITE 4 AC1 13 ASN B 405
SITE 1 AC2 14 ARG C 278 SER C 280 MET C 314 THR C 317
SITE 2 AC2 14 THR C 355 ALA C 356 GLY C 357 VAL C 358
SITE 3 AC2 14 ALA C 361 GLY C 362 ASP C 398 ARG C 401
SITE 4 AC2 14 THR C 402 ASN C 405
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
