HEADER MEMBRANE PROTEIN/IMMUNE SYSTEM 31-JAN-24 8Y4X TITLE APO FORM OF TRIPARTITE ATP-INDEPENDENT PERIPLASMIC (TRAP) TRANSPORTER TITLE 2 FROM FUSOBACTERIUM NUCLEATUM. COMPND MOL_ID: 1; COMPND 2 MOLECULE: N-ACETYLNEURAMINATE TRANSPORTER SMALL SUBUNIT; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: NANOBODY AGAINST FNTRAP; COMPND 7 CHAIN: B; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: FUSOBACTERIUM NUCLEATUM; SOURCE 3 ORGANISM_TAXID: 851; SOURCE 4 GENE: FN1473; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: VICUGNA PACOS; SOURCE 9 ORGANISM_TAXID: 30538; SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS SIALIC ACID TRANSPORTER, TRAP TRANSPORTER, MEMBRANE PROTEIN, MEMBRANE KEYWDS 2 PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR P.GOYAL,S.RAMASWAMY,K.R.VINOTHKUMAR REVDAT 1 11-DEC-24 8Y4X 0 JRNL AUTH P.GOYAL,S.RAMASWAMY,K.R.VINOTHKUMAR JRNL TITL APO FORM OF TRIPARTITE ATP-INDEPENDENT PERIPLASMIC (TRAP) JRNL TITL 2 TRANSPORTER FROM FUSOBACTERIUM NUCLEATUM. JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : PHENIX REMARK 3 RECONSTRUCTION SCHEMA : BACK PROJECTION REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : REAL REMARK 3 REFINEMENT PROTOCOL : OTHER REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : 42.520 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) : 3.200 REMARK 3 NUMBER OF PARTICLES : 141272 REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE REMARK 3 CORRECTION REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 8Y4X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-FEB-24. REMARK 100 THE DEPOSITION ID IS D_1300044572. 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 : APO FORM OF TRAP TRANSPORTER IN REMARK 245 1:1 COMPLEX WITH ITS NANOBODY. REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 2.90 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 8.00 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 960 REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : FEI FALCON III (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 3000.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : 2.70 REMARK 245 IMAGING MODE : OTHER REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 2770.00 REMARK 245 ILLUMINATION MODE : OTHER REMARK 245 NOMINAL MAGNIFICATION : 75000 REMARK 245 CALIBRATED MAGNIFICATION : 130841 REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 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: DIMERIC 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 MET A -46 REMARK 465 GLY A -45 REMARK 465 GLY A -44 REMARK 465 SER A -43 REMARK 465 HIS A -42 REMARK 465 HIS A -41 REMARK 465 HIS A -40 REMARK 465 HIS A -39 REMARK 465 HIS A -38 REMARK 465 HIS A -37 REMARK 465 GLY A -36 REMARK 465 SER A -35 REMARK 465 TRP A -34 REMARK 465 SER A -33 REMARK 465 HIS A -32 REMARK 465 PRO A -31 REMARK 465 GLN A -30 REMARK 465 PHE A -29 REMARK 465 GLU A -28 REMARK 465 LYS A -27 REMARK 465 ALA A -26 REMARK 465 SER A -25 REMARK 465 MET A -24 REMARK 465 THR A -23 REMARK 465 GLY A -22 REMARK 465 GLY A -21 REMARK 465 GLN A -20 REMARK 465 GLN A -19 REMARK 465 MET A -18 REMARK 465 GLY A -17 REMARK 465 ARG A -16 REMARK 465 ASP A -15 REMARK 465 LEU A -14 REMARK 465 TYR A -13 REMARK 465 ASP A -12 REMARK 465 ASP A -11 REMARK 465 ASP A -10 REMARK 465 ASP A -9 REMARK 465 LYS A -8 REMARK 465 ASP A -7 REMARK 465 ARG A -6 REMARK 465 TRP A -5 REMARK 465 GLY A -4 REMARK 465 SER A -3 REMARK 465 GLU A -2 REMARK 465 LEU A -1 REMARK 465 GLU A 0 REMARK 465 LEU A 613 REMARK 465 ILE A 614 REMARK 465 VAL A 615 REMARK 465 GLY A 616 REMARK 465 GLY A 617 REMARK 465 GLN B 1 REMARK 465 SER B 122 REMARK 465 HIS B 123 REMARK 465 HIS B 124 REMARK 465 HIS B 125 REMARK 465 HIS B 126 REMARK 465 HIS B 127 REMARK 465 HIS B 128 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 O LEU A 128 OG1 THR A 132 2.12 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 PRO A 156 42.23 -80.60 REMARK 500 ILE A 172 -61.19 -122.89 REMARK 500 MET A 191 52.44 -96.06 REMARK 500 THR A 225 -66.13 -97.37 REMARK 500 ARG A 226 116.46 -161.61 REMARK 500 SER A 406 58.03 -97.38 REMARK 500 PRO A 562 44.78 -94.13 REMARK 500 PRO B 41 76.49 -69.16 REMARK 500 HIS B 52 -2.36 69.73 REMARK 500 ASP B 66 -7.82 69.27 REMARK 500 PRO B 88 2.22 -66.22 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 PRO A 562 PRO A 563 146.99 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA A 701 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 SER A 295 O REMARK 620 2 SER A 298 O 78.3 REMARK 620 3 GLY A 337 O 124.9 132.4 REMARK 620 4 VAL A 340 O 86.7 141.5 85.0 REMARK 620 5 PRO A 342 O 111.8 82.5 116.2 70.6 REMARK 620 N 1 2 3 4 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-38925 RELATED DB: EMDB REMARK 900 SIALIC ACID BOUND TRANSPORTER REMARK 900 RELATED ID: EMD-38926 RELATED DB: EMDB REMARK 900 APO FORM OF TRIPARTITE ATP-INDEPENDENT PERIPLASMIC (TRAP) REMARK 900 TRANSPORTER FROM FUSOBACTERIUM NUCLEATUM. DBREF 8Y4X A 1 617 UNP Q8RDN8 Q8RDN8_FUSNN 1 617 DBREF 8Y4X B 1 128 PDB 8Y4X 8Y4X 1 128 SEQADV 8Y4X MET A -46 UNP Q8RDN8 INITIATING METHIONINE SEQADV 8Y4X GLY A -45 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X GLY A -44 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X SER A -43 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X HIS A -42 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X HIS A -41 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X HIS A -40 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X HIS A -39 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X HIS A -38 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X HIS A -37 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X GLY A -36 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X SER A -35 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X TRP A -34 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X SER A -33 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X HIS A -32 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X PRO A -31 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X GLN A -30 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X PHE A -29 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X GLU A -28 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X LYS A -27 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X ALA A -26 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X SER A -25 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X MET A -24 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X THR A -23 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X GLY A -22 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X GLY A -21 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X GLN A -20 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X GLN A -19 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X MET A -18 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X GLY A -17 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X ARG A -16 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X ASP A -15 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X LEU A -14 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X TYR A -13 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X ASP A -12 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X ASP A -11 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X ASP A -10 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X ASP A -9 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X LYS A -8 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X ASP A -7 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X ARG A -6 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X TRP A -5 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X GLY A -4 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X SER A -3 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X GLU A -2 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X LEU A -1 UNP Q8RDN8 EXPRESSION TAG SEQADV 8Y4X GLU A 0 UNP Q8RDN8 EXPRESSION TAG SEQRES 1 A 664 MET GLY GLY SER HIS HIS HIS HIS HIS HIS GLY SER TRP SEQRES 2 A 664 SER HIS PRO GLN PHE GLU LYS ALA SER MET THR GLY GLY SEQRES 3 A 664 GLN GLN MET GLY ARG ASP LEU TYR ASP ASP ASP ASP LYS SEQRES 4 A 664 ASP ARG TRP GLY SER GLU LEU GLU MET LYS VAL PHE ASN SEQRES 5 A 664 LYS LEU GLU GLU TRP LEU GLY GLY SER LEU PHE ILE GLY SEQRES 6 A 664 MET PHE VAL ILE LEU VAL MET GLN ILE PHE SER ARG GLN SEQRES 7 A 664 ILE PHE ASN SER PRO LEU ILE TRP SER GLU GLU LEU SER SEQRES 8 A 664 ARG LEU ILE PHE VAL TYR VAL GLY LEU LEU GLY VAL SER SEQRES 9 A 664 MET GLY ILE ARG SER GLN GLN HIS ILE MET ILE ASP PHE SEQRES 10 A 664 LEU TYR ALA LYS PHE PRO LYS SER MET GLN LYS ILE ILE SEQRES 11 A 664 PHE THR ILE ILE GLN ILE LEU ILE LEU ALA CYS LEU ILE SEQRES 12 A 664 PHE PHE LEU TYR PHE GLY TYR ASP LEU PHE ILE LYS LYS SEQRES 13 A 664 GLU GLU ILE GLU ILE VAL SER LEU GLY ILE SER MET LYS SEQRES 14 A 664 TRP MET TYR LEU ALA LEU PRO LEU ILE THR LEU LEU MET SEQRES 15 A 664 LEU VAL ARG PHE TYR GLN ALA TYR SER GLU ASN TYR ALA SEQRES 16 A 664 GLN ASN LYS VAL TYR ILE LYS PRO ILE PHE ILE LEU ALA SEQRES 17 A 664 LEU MET ILE ILE LEU VAL LEU ILE ALA PHE ILE LYS PRO SEQRES 18 A 664 GLU LEU PHE LYS ILE LEU LYS LEU SER ASN TYR PHE ASP SEQRES 19 A 664 LEU GLY GLU MET THR ILE TYR TYR VAL LEU ILE ALA TRP SEQRES 20 A 664 LEU VAL MET ILE PHE PHE GLY VAL PRO VAL GLY TRP SER SEQRES 21 A 664 LEU LEU VAL ALA CYS ILE LEU TYR PHE ALA LEU THR ARG SEQRES 22 A 664 TRP LYS VAL VAL TYR PHE ALA ALA ASP LYS LEU VAL TYR SEQRES 23 A 664 SER LEU ASP SER PHE SER LEU LEU SER VAL PRO PHE PHE SEQRES 24 A 664 ILE LEU THR GLY ILE LEU MET ASN GLY ALA GLY ILE THR SEQRES 25 A 664 GLU ARG ILE PHE ASN PHE ALA LYS ALA MET LEU GLY HIS SEQRES 26 A 664 TYR THR GLY GLY MET GLY HIS VAL ASN VAL ALA ALA SER SEQRES 27 A 664 LEU ILE PHE SER GLY MET SER GLY SER ALA ILE ALA ASP SEQRES 28 A 664 ALA GLY GLY LEU GLY GLN LEU GLU ILE LYS ALA MET ARG SEQRES 29 A 664 ASP GLU GLY TYR ASP ASP ASP ILE CYS GLY GLY LEU THR SEQRES 30 A 664 ALA ALA SER CYS ILE ILE GLY PRO LEU VAL PRO PRO SER SEQRES 31 A 664 ILE SER MET ILE ILE TYR GLY VAL ILE ALA ASN GLN SER SEQRES 32 A 664 ILE ALA LYS LEU PHE LEU ALA GLY PHE VAL PRO GLY PHE SEQRES 33 A 664 LEU THR THR ILE ALA LEU MET ILE MET ASN TYR PHE VAL SEQRES 34 A 664 CYS LYS LYS ARG GLY TYR LYS LYS THR ALA LYS ALA SER SEQRES 35 A 664 PRO LYS GLU ARG TRP ILE ALA PHE LYS LYS SER PHE TRP SEQRES 36 A 664 ALA LEU LEU THR PRO ILE LEU ILE ILE GLY GLY ILE PHE SEQRES 37 A 664 SER GLY ILE PHE THR PRO THR GLU ALA ALA VAL ILE ALA SEQRES 38 A 664 THR PHE TYR SER ILE ILE LEU GLY GLY PHE ILE TYR LYS SEQRES 39 A 664 GLU LEU THR VAL LYS SER PHE PHE LYS HIS CYS VAL GLU SEQRES 40 A 664 ALA VAL ALA ILE SER GLY VAL THR VAL LEU MET ILE MET SEQRES 41 A 664 THR VAL THR PHE PHE GLY ASP ILE ILE ALA ARG GLU GLN SEQRES 42 A 664 VAL ALA MET ARG VAL ALA GLU ILE PHE ILE LYS TYR ALA SEQRES 43 A 664 THR SER PRO MET MET VAL LEU VAL MET ILE ASN LEU LEU SEQRES 44 A 664 LEU LEU PHE LEU GLY MET PHE ILE ASP ALA LEU ALA LEU SEQRES 45 A 664 GLN PHE LEU VAL LEU PRO MET LEU ILE PRO ILE ALA GLU SEQRES 46 A 664 GLN VAL GLY ILE ASP LEU VAL PHE PHE GLY VAL MET THR SEQRES 47 A 664 THR LEU ASN MET MET ILE GLY ILE LEU THR PRO PRO MET SEQRES 48 A 664 GLY MET ALA LEU PHE VAL VAL ALA GLN VAL GLY LYS MET SEQRES 49 A 664 SER VAL SER THR VAL ALA LYS GLY VAL LEU PRO PHE LEU SEQRES 50 A 664 LEU PRO ILE PHE ILE THR LEU VAL ILE ILE THR ILE PHE SEQRES 51 A 664 PRO GLN ILE ILE LEU PHE LEU PRO ASN LEU ILE VAL GLY SEQRES 52 A 664 GLY SEQRES 1 B 128 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 B 128 ALA GLY GLY SER LEU ARG LEU SER CYS THR THR SER GLY SEQRES 3 B 128 PHE ASN PHE ASP ASP TYR ALA ILE GLY TRP PHE ARG GLN SEQRES 4 B 128 ALA PRO GLY LYS GLU ARG GLU GLY VAL SER CYS ILE HIS SEQRES 5 B 128 CYS THR ALA TYR THR PRO TYR TYR ALA ARG SER VAL ARG SEQRES 6 B 128 ASP ARG PHE THR ILE SER SER ASP ASN ALA THR ASN THR SEQRES 7 B 128 VAL PHE LEU GLN MET ASN ASN LEU ARG PRO GLU ASP THR SEQRES 8 B 128 ALA VAL TYR TYR CYS VAL ALA ASP ALA THR ARG TYR PRO SEQRES 9 B 128 TYR PRO GLU PHE TYR ASP TYR VAL GLY GLN GLY THR GLN SEQRES 10 B 128 VAL THR VAL SER SER HIS HIS HIS HIS HIS HIS HET NA A 701 1 HET NA A 702 1 HET PTY A 703 50 HETNAM NA SODIUM ION HETNAM PTY PHOSPHATIDYLETHANOLAMINE FORMUL 3 NA 2(NA 1+) FORMUL 5 PTY C40 H80 N O8 P HELIX 1 AA1 LEU A 7 ILE A 32 1 26 HELIX 2 AA2 TRP A 39 GLN A 63 1 25 HELIX 3 AA3 LEU A 71 PHE A 75 5 5 HELIX 4 AA4 PRO A 76 LYS A 109 1 34 HELIX 5 AA5 MET A 121 LEU A 126 1 6 HELIX 6 AA6 LEU A 126 GLN A 149 1 24 HELIX 7 AA7 ILE A 157 LYS A 173 1 17 HELIX 8 AA8 PRO A 174 LEU A 180 5 7 HELIX 9 AA9 LYS A 181 TYR A 185 5 5 HELIX 10 AB1 THR A 192 PHE A 206 1 15 HELIX 11 AB2 PRO A 209 THR A 225 1 17 HELIX 12 AB3 ARG A 226 LYS A 228 5 3 HELIX 13 AB4 VAL A 229 ALA A 234 1 6 HELIX 14 AB5 ASP A 235 SER A 240 1 6 HELIX 15 AB6 LEU A 247 THR A 255 1 9 HELIX 16 AB7 ILE A 264 LEU A 276 1 13 HELIX 17 AB8 GLY A 281 SER A 295 1 15 HELIX 18 AB9 SER A 300 GLU A 319 1 20 HELIX 19 AC1 ASP A 322 SER A 333 1 12 HELIX 20 AC2 CYS A 334 GLY A 337 5 4 HELIX 21 AC3 SER A 343 ASN A 354 1 12 HELIX 22 AC4 SER A 356 GLY A 387 1 32 HELIX 23 AC5 LYS A 397 SER A 406 1 10 HELIX 24 AC6 LEU A 410 SER A 422 1 13 HELIX 25 AC7 THR A 426 ILE A 445 1 20 HELIX 26 AC8 VAL A 451 GLU A 485 1 35 HELIX 27 AC9 GLN A 486 ALA A 499 1 14 HELIX 28 AD1 SER A 501 ILE A 520 1 20 HELIX 29 AD2 ASP A 521 VAL A 529 1 9 HELIX 30 AD3 VAL A 529 VAL A 540 1 12 HELIX 31 AD4 ASP A 543 ILE A 559 1 17 HELIX 32 AD5 GLY A 565 LYS A 576 1 12 HELIX 33 AD6 SER A 578 VAL A 586 1 9 HELIX 34 AD7 PHE A 589 ILE A 602 1 14 HELIX 35 AD8 ARG B 62 ARG B 65 5 4 HELIX 36 AD9 ARG B 87 THR B 91 5 5 HELIX 37 AE1 TYR B 105 TYR B 109 5 5 SHEET 1 AA1 4 GLN B 3 GLY B 8 0 SHEET 2 AA1 4 ARG B 19 SER B 25 -1 O THR B 23 N GLN B 5 SHEET 3 AA1 4 THR B 78 MET B 83 -1 O LEU B 81 N LEU B 20 SHEET 4 AA1 4 PHE B 68 ASP B 73 -1 N SER B 71 O PHE B 80 SHEET 1 AA2 6 GLY B 10 VAL B 12 0 SHEET 2 AA2 6 THR B 116 VAL B 120 1 O GLN B 117 N GLY B 10 SHEET 3 AA2 6 ALA B 92 ASP B 99 -1 N ALA B 92 O VAL B 118 SHEET 4 AA2 6 ALA B 33 GLN B 39 -1 N GLY B 35 O VAL B 97 SHEET 5 AA2 6 ARG B 45 ILE B 51 -1 O GLU B 46 N ARG B 38 SHEET 6 AA2 6 TYR B 59 TYR B 60 -1 O TYR B 59 N CYS B 50 SHEET 1 AA3 4 GLY B 10 VAL B 12 0 SHEET 2 AA3 4 THR B 116 VAL B 120 1 O GLN B 117 N GLY B 10 SHEET 3 AA3 4 ALA B 92 ASP B 99 -1 N ALA B 92 O VAL B 118 SHEET 4 AA3 4 TYR B 111 VAL B 112 -1 O TYR B 111 N ALA B 98 SSBOND 1 CYS B 22 CYS B 96 1555 1555 2.03 SSBOND 2 CYS B 50 CYS B 53 1555 1555 2.03 LINK O SER A 295 NA NA A 701 1555 1555 2.36 LINK O SER A 298 NA NA A 701 1555 1555 2.46 LINK OE1 GLU A 312 NA NA A 702 1555 1555 2.83 LINK O GLY A 337 NA NA A 701 1555 1555 2.20 LINK O VAL A 340 NA NA A 701 1555 1555 2.73 LINK O PRO A 342 NA NA A 701 1555 1555 2.30 CISPEP 1 PRO A 341 PRO A 342 0 -1.94 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