HEADER PROTEIN TRANSPORT 07-FEB-24 8Y9Z TITLE STRUCTURE OF THE SECA-SECY COMPLEX WITH THE SUBSTRATE HMBRI-3TM COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN TRANSLOCASE SUBUNIT SECA; COMPND 3 CHAIN: A; COMPND 4 EC: 7.4.2.8; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: PROTEIN TRANSLOCASE SUBUNIT SECY; COMPND 8 CHAIN: Y; COMPND 9 ENGINEERED: YES; COMPND 10 MUTATION: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: PROTEIN TRANSLOCASE SUBUNIT SECE; COMPND 13 CHAIN: E; COMPND 14 ENGINEERED: YES; COMPND 15 MOL_ID: 4; COMPND 16 MOLECULE: NANOBODY; COMPND 17 CHAIN: V; COMPND 18 ENGINEERED: YES; COMPND 19 OTHER_DETAILS: THE NCBI ACCESSION FOR THE NANOBODY IS 6ITC_V.; COMPND 20 MOL_ID: 5; COMPND 21 MOLECULE: BACTERIORHODOPSIN-I; COMPND 22 CHAIN: B; COMPND 23 SYNONYM: HMBRI; COMPND 24 ENGINEERED: YES; COMPND 25 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS SUBSP. SUBTILIS STR. 168; SOURCE 3 ORGANISM_TAXID: 224308; SOURCE 4 GENE: SECA; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 83333; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: K-12; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: GEOBACILLUS THERMODENITRIFICANS NG80-2; SOURCE 10 ORGANISM_TAXID: 420246; SOURCE 11 GENE: SECY; SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 83333; SOURCE 14 EXPRESSION_SYSTEM_STRAIN: K-12; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: GEOBACILLUS THERMODENITRIFICANS NG80-2; SOURCE 17 ORGANISM_TAXID: 420246; SOURCE 18 GENE: SECE; SOURCE 19 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12; SOURCE 20 EXPRESSION_SYSTEM_TAXID: 83333; SOURCE 21 EXPRESSION_SYSTEM_STRAIN: K-12; SOURCE 22 MOL_ID: 4; SOURCE 23 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 24 ORGANISM_TAXID: 9844; SOURCE 25 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12; SOURCE 26 EXPRESSION_SYSTEM_TAXID: 83333; SOURCE 27 EXPRESSION_SYSTEM_STRAIN: K-12; SOURCE 28 MOL_ID: 5; SOURCE 29 ORGANISM_SCIENTIFIC: HALOARCULA MARISMORTUI ATCC 43049; SOURCE 30 ORGANISM_TAXID: 272569; SOURCE 31 STRAIN: ATCC 43049; SOURCE 32 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12; SOURCE 33 EXPRESSION_SYSTEM_TAXID: 83333; SOURCE 34 EXPRESSION_SYSTEM_STRAIN: K-12 KEYWDS PROTEIN TRANSLOCATION, MEMBRANE PROTEIN INSERTION, PROTEIN CHAPERONE, KEYWDS 2 PROTEIN TRANSPORT EXPDTA ELECTRON MICROSCOPY AUTHOR X.OU,C.MA,D.SUN,J.XU,X.WU,N.GAO,L.LI REVDAT 1 26-FEB-25 8Y9Z 0 JRNL AUTH X.OU,C.MA,D.SUN,J.XU,Y.WANG,X.WU,D.WANG,S.YANG,N.GAO,C.SONG, JRNL AUTH 2 L.LI JRNL TITL SECY TRANSLOCON CHAPERONES PROTEIN FOLDING DURING MEMBRANE JRNL TITL 2 PROTEIN INSERTION JRNL REF CELL 2025 REMARK 2 REMARK 2 RESOLUTION. 3.41 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) : 3.410 REMARK 3 NUMBER OF PARTICLES : 380199 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 8Y9Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-FEB-24. REMARK 100 THE DEPOSITION ID IS D_1300045131. 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 : SECA-SECY COMPLEX WITH THE REMARK 245 SUBSTRATE HMBRI-3TM 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 : 7.00 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 TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1500.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2500.00 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) : 6000.00 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) : 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: PENTAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, Y, E, V, 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 1 REMARK 465 LEU A 2 REMARK 465 GLY A 3 REMARK 465 ILE A 4 REMARK 465 LEU A 5 REMARK 465 ASN A 6 REMARK 465 LYS A 7 REMARK 465 MET A 8 REMARK 465 PHE A 9 REMARK 465 ASP A 10 REMARK 465 PRO A 11 REMARK 465 THR A 12 REMARK 465 LYS A 13 REMARK 465 MET Y 1 REMARK 465 ASP Y 48 REMARK 465 GLN Y 49 REMARK 465 LEU Y 50 REMARK 465 ASN Y 51 REMARK 465 ALA Y 52 REMARK 465 PHE Y 53 REMARK 465 GLY Y 54 REMARK 465 VAL Y 55 REMARK 465 LEU Y 56 REMARK 465 ASN Y 57 REMARK 465 ILE Y 58 REMARK 465 PHE Y 59 REMARK 465 CYS Y 60 REMARK 465 GLY Y 61 REMARK 465 GLY Y 62 REMARK 465 ALA Y 63 REMARK 465 LEU Y 64 REMARK 465 PHE Y 203 REMARK 465 GLU Y 204 REMARK 465 ASN Y 205 REMARK 465 VAL Y 206 REMARK 465 GLY Y 207 REMARK 465 GLU Y 208 REMARK 465 ASP Y 209 REMARK 465 LEU Y 210 REMARK 465 THR Y 211 REMARK 465 MET E 1 REMARK 465 GLU E 60 REMARK 465 GLY E 61 REMARK 465 GLY E 62 REMARK 465 HIS E 63 REMARK 465 HIS E 64 REMARK 465 HIS E 65 REMARK 465 HIS E 66 REMARK 465 HIS E 67 REMARK 465 HIS E 68 REMARK 465 HIS E 69 REMARK 465 HIS E 70 REMARK 465 SER V 117 REMARK 465 MET B 1 REMARK 465 PRO B 2 REMARK 465 ALA B 3 REMARK 465 PRO B 4 REMARK 465 GLY B 5 REMARK 465 SER B 6 REMARK 465 GLU B 7 REMARK 465 GLY B 8 REMARK 465 ILE B 9 REMARK 465 TRP B 10 REMARK 465 LEU B 11 REMARK 465 TRP B 12 REMARK 465 LEU B 13 REMARK 465 GLY B 14 REMARK 465 THR B 15 REMARK 465 ALA B 16 REMARK 465 GLY B 17 REMARK 465 MET B 18 REMARK 465 PHE B 19 REMARK 465 LEU B 20 REMARK 465 GLY B 21 REMARK 465 MET B 22 REMARK 465 LEU B 23 REMARK 465 TYR B 24 REMARK 465 PHE B 25 REMARK 465 ILE B 26 REMARK 465 ALA B 27 REMARK 465 ARG B 28 REMARK 465 GLY B 29 REMARK 465 TRP B 30 REMARK 465 GLY B 31 REMARK 465 GLU B 32 REMARK 465 THR B 33 REMARK 465 GLY B 61 REMARK 465 PHE B 62 REMARK 465 GLY B 63 REMARK 465 LEU B 64 REMARK 465 THR B 65 REMARK 465 PHE B 66 REMARK 465 ILE B 67 REMARK 465 GLU B 68 REMARK 465 PHE B 69 REMARK 465 GLY B 70 REMARK 465 GLY B 71 REMARK 465 LEU B 91 REMARK 465 LEU B 92 REMARK 465 TYR B 93 REMARK 465 ASP B 94 REMARK 465 LEU B 95 REMARK 465 GLY B 96 REMARK 465 LEU B 97 REMARK 465 LEU B 98 REMARK 465 ALA B 99 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 LYS V 86 CG CD CE NZ 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 VAL A 76 -61.49 -94.93 REMARK 500 ILE A 214 -59.13 -122.04 REMARK 500 LYS A 245 72.52 59.00 REMARK 500 MET A 350 111.20 -160.02 REMARK 500 GLU A 365 -12.24 72.11 REMARK 500 LYS A 366 116.48 -163.00 REMARK 500 ALA A 368 -169.29 -119.25 REMARK 500 VAL A 437 -54.15 -126.34 REMARK 500 GLN A 529 62.04 63.68 REMARK 500 ASP A 564 -54.08 -120.11 REMARK 500 ASP A 619 51.14 -92.41 REMARK 500 THR A 643 70.42 56.09 REMARK 500 GLU A 647 78.52 -107.08 REMARK 500 LEU A 666 51.72 -111.27 REMARK 500 ASP A 667 45.44 35.18 REMARK 500 GLU A 668 -5.53 66.97 REMARK 500 ARG Y 107 48.77 -89.01 REMARK 500 ASN Y 143 73.03 52.19 REMARK 500 ALA Y 246 56.93 -99.04 REMARK 500 ASN Y 253 74.06 57.86 REMARK 500 PRO Y 254 46.01 -85.23 REMARK 500 VAL Y 255 -61.73 -120.48 REMARK 500 ASN Y 332 74.72 57.66 REMARK 500 ILE V 28 -57.43 -125.08 REMARK 500 ARG V 38 -61.94 -100.32 REMARK 500 LYS V 43 -166.60 -75.41 REMARK 500 ARG V 44 70.37 57.53 REMARK 500 TRP B 84 40.81 -96.34 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-39086 RELATED DB: EMDB REMARK 900 STRUCTURE OF THE SECA-SECY COMPLEX WITH THE SUBSTRATE HMBRI-3TM DBREF 8Y9Z A 1 778 UNP P28366 SECA_BACSU 1 778 DBREF 8Y9Z Y 1 430 UNP A4IJK8 A4IJK8_GEOTN 1 430 DBREF 8Y9Z E 1 60 UNP A4IJH4 A4IJH4_GEOTN 1 60 DBREF 8Y9Z V 1 117 PDB 8Y9Z 8Y9Z 1 117 DBREF 8Y9Z B 1 99 UNP Q5UXY6 BACR1_HALMA 1 99 SEQADV 8Y9Z CYS Y 60 UNP A4IJK8 GLY 60 ENGINEERED MUTATION SEQADV 8Y9Z THR Y 202 UNP A4IJK8 GLN 202 ENGINEERED MUTATION SEQADV 8Y9Z THR Y 211 UNP A4IJK8 PHE 211 ENGINEERED MUTATION SEQADV 8Y9Z ASN Y 213 UNP A4IJK8 ARG 213 ENGINEERED MUTATION SEQADV 8Y9Z GLY E 61 UNP A4IJH4 EXPRESSION TAG SEQADV 8Y9Z GLY E 62 UNP A4IJH4 EXPRESSION TAG SEQADV 8Y9Z HIS E 63 UNP A4IJH4 EXPRESSION TAG SEQADV 8Y9Z HIS E 64 UNP A4IJH4 EXPRESSION TAG SEQADV 8Y9Z HIS E 65 UNP A4IJH4 EXPRESSION TAG SEQADV 8Y9Z HIS E 66 UNP A4IJH4 EXPRESSION TAG SEQADV 8Y9Z HIS E 67 UNP A4IJH4 EXPRESSION TAG SEQADV 8Y9Z HIS E 68 UNP A4IJH4 EXPRESSION TAG SEQADV 8Y9Z HIS E 69 UNP A4IJH4 EXPRESSION TAG SEQADV 8Y9Z HIS E 70 UNP A4IJH4 EXPRESSION TAG SEQADV 8Y9Z CYS B 75 UNP Q5UXY6 PRO 75 ENGINEERED MUTATION SEQRES 1 A 778 MET LEU GLY ILE LEU ASN LYS MET PHE ASP PRO THR LYS SEQRES 2 A 778 ARG THR LEU ASN ARG TYR GLU LYS ILE ALA ASN ASP ILE SEQRES 3 A 778 ASP ALA ILE ARG GLY ASP TYR GLU ASN LEU SER ASP ASP SEQRES 4 A 778 ALA LEU LYS HIS LYS THR ILE GLU PHE LYS GLU ARG LEU SEQRES 5 A 778 GLU LYS GLY ALA THR THR ASP ASP LEU LEU VAL GLU ALA SEQRES 6 A 778 PHE ALA VAL VAL ARG GLU ALA SER ARG ARG VAL THR GLY SEQRES 7 A 778 MET PHE PRO PHE LYS VAL GLN LEU MET GLY GLY VAL ALA SEQRES 8 A 778 LEU HIS ASP GLY ASN ILE ALA GLU MET LYS THR GLY GLU SEQRES 9 A 778 GLY LYS THR LEU THR SER THR LEU PRO VAL TYR LEU ASN SEQRES 10 A 778 ALA LEU THR GLY LYS GLY VAL HIS VAL VAL THR VAL ASN SEQRES 11 A 778 GLU TYR LEU ALA SER ARG ASP ALA GLU GLN MET GLY LYS SEQRES 12 A 778 ILE PHE GLU PHE LEU GLY LEU THR VAL GLY LEU ASN LEU SEQRES 13 A 778 ASN SER MET SER LYS ASP GLU LYS ARG GLU ALA TYR ALA SEQRES 14 A 778 ALA ASP ILE THR TYR SER THR ASN ASN GLU LEU GLY PHE SEQRES 15 A 778 ASP TYR LEU ARG ASP ASN MET VAL LEU TYR LYS GLU GLN SEQRES 16 A 778 MET VAL GLN ARG PRO LEU HIS PHE ALA VAL ILE ASP GLU SEQRES 17 A 778 VAL ASP SER ILE LEU ILE ASP GLU ALA ARG THR PRO LEU SEQRES 18 A 778 ILE ILE SER GLY GLN ALA ALA LYS SER THR LYS LEU TYR SEQRES 19 A 778 VAL GLN ALA ASN ALA PHE VAL ARG THR LEU LYS ALA GLU SEQRES 20 A 778 LYS ASP TYR THR TYR ASP ILE LYS THR LYS ALA VAL GLN SEQRES 21 A 778 LEU THR GLU GLU GLY MET THR LYS ALA GLU LYS ALA PHE SEQRES 22 A 778 GLY ILE ASP ASN LEU PHE ASP VAL LYS HIS VAL ALA LEU SEQRES 23 A 778 ASN HIS HIS ILE ASN GLN ALA LEU LYS ALA HIS VAL ALA SEQRES 24 A 778 MET GLN LYS ASP VAL ASP TYR VAL VAL GLU ASP GLY GLN SEQRES 25 A 778 VAL VAL ILE VAL ASP SER PHE THR GLY ARG LEU MET LYS SEQRES 26 A 778 GLY ARG ARG TYR SER GLU GLY LEU HIS GLN ALA ILE GLU SEQRES 27 A 778 ALA LYS GLU GLY LEU GLU ILE GLN ASN GLU SER MET THR SEQRES 28 A 778 LEU ALA THR ILE THR PHE GLN ASN TYR PHE ARG MET TYR SEQRES 29 A 778 GLU LYS LEU ALA GLY MET THR GLY THR ALA LYS THR GLU SEQRES 30 A 778 GLU GLU GLU PHE ARG ASN ILE TYR ASN MET GLN VAL VAL SEQRES 31 A 778 THR ILE PRO THR ASN ARG PRO VAL VAL ARG ASP ASP ARG SEQRES 32 A 778 PRO ASP LEU ILE TYR ARG THR MET GLU GLY LYS PHE LYS SEQRES 33 A 778 ALA VAL ALA GLU ASP VAL ALA GLN ARG TYR MET THR GLY SEQRES 34 A 778 GLN PRO VAL LEU VAL GLY THR VAL ALA VAL GLU THR SER SEQRES 35 A 778 GLU LEU ILE SER LYS LEU LEU LYS ASN LYS GLY ILE PRO SEQRES 36 A 778 HIS GLN VAL LEU ASN ALA LYS ASN HIS GLU ARG GLU ALA SEQRES 37 A 778 GLN ILE ILE GLU GLU ALA GLY GLN LYS GLY ALA VAL THR SEQRES 38 A 778 ILE ALA THR ASN MET ALA GLY ARG GLY THR ASP ILE LYS SEQRES 39 A 778 LEU GLY GLU GLY VAL LYS GLU LEU GLY GLY LEU ALA VAL SEQRES 40 A 778 VAL GLY THR GLU ARG HIS GLU SER ARG ARG ILE ASP ASN SEQRES 41 A 778 GLN LEU ARG GLY ARG SER GLY ARG GLN GLY ASP PRO GLY SEQRES 42 A 778 ILE THR GLN PHE TYR LEU SER MET GLU ASP GLU LEU MET SEQRES 43 A 778 ARG ARG PHE GLY ALA GLU ARG THR MET ALA MET LEU ASP SEQRES 44 A 778 ARG PHE GLY MET ASP ASP SER THR PRO ILE GLN SER LYS SEQRES 45 A 778 MET VAL SER ARG ALA VAL GLU SER SER GLN LYS ARG VAL SEQRES 46 A 778 GLU GLY ASN ASN PHE ASP SER ARG LYS GLN LEU LEU GLN SEQRES 47 A 778 TYR ASP ASP VAL LEU ARG GLN GLN ARG GLU VAL ILE TYR SEQRES 48 A 778 LYS GLN ARG PHE GLU VAL ILE ASP SER GLU ASN LEU ARG SEQRES 49 A 778 GLU ILE VAL GLU ASN MET ILE LYS SER SER LEU GLU ARG SEQRES 50 A 778 ALA ILE ALA ALA TYR THR PRO ARG GLU GLU LEU PRO GLU SEQRES 51 A 778 GLU TRP LYS LEU ASP GLY LEU VAL ASP LEU ILE ASN THR SEQRES 52 A 778 THR TYR LEU ASP GLU GLY ALA LEU GLU LYS SER ASP ILE SEQRES 53 A 778 PHE GLY LYS GLU PRO ASP GLU MET LEU GLU LEU ILE MET SEQRES 54 A 778 ASP ARG ILE ILE THR LYS TYR ASN GLU LYS GLU GLU GLN SEQRES 55 A 778 PHE GLY LYS GLU GLN MET ARG GLU PHE GLU LYS VAL ILE SEQRES 56 A 778 VAL LEU ARG ALA VAL ASP SER LYS TRP MET ASP HIS ILE SEQRES 57 A 778 ASP ALA MET ASP GLN LEU ARG GLN GLY ILE HIS LEU ARG SEQRES 58 A 778 ALA TYR ALA GLN THR ASN PRO LEU ARG GLU TYR GLN MET SEQRES 59 A 778 GLU GLY PHE ALA MET PHE GLU HIS MET ILE GLU SER ILE SEQRES 60 A 778 GLU ASP GLU VAL ALA LYS PHE VAL MET LYS ALA SEQRES 1 Y 430 MET PHE ARG THR ILE SER ASN PHE MET ARG VAL SER ASP SEQRES 2 Y 430 ILE ARG ASN LYS ILE ILE PHE THR LEU LEU MET LEU ILE SEQRES 3 Y 430 VAL PHE ARG ILE GLY THR PHE ILE PRO VAL PRO SER VAL SEQRES 4 Y 430 ASN THR ASP VAL LEU LYS LEU GLN ASP GLN LEU ASN ALA SEQRES 5 Y 430 PHE GLY VAL LEU ASN ILE PHE CYS GLY GLY ALA LEU GLN SEQRES 6 Y 430 ASN PHE SER ILE PHE ALA MET GLY VAL MET PRO TYR ILE SEQRES 7 Y 430 THR ALA SER ILE ILE VAL GLN LEU LEU GLN MET ASP VAL SEQRES 8 Y 430 VAL PRO LYS PHE ALA GLU TRP SER LYS GLN GLY GLU MET SEQRES 9 Y 430 GLY ARG ARG LYS LEU ALA GLN PHE THR ARG TYR PHE THR SEQRES 10 Y 430 ILE VAL LEU GLY PHE ILE GLN ALA LEU GLY MET SER TYR SEQRES 11 Y 430 GLY PHE ASN ASN LEU ALA GLY GLY MET LEU ILE GLN ASN SEQRES 12 Y 430 PRO GLY ILE GLY THR TYR LEU LEU ILE ALA VAL VAL LEU SEQRES 13 Y 430 THR ALA GLY THR ALA PHE LEU MET TRP LEU GLY GLU GLN SEQRES 14 Y 430 ILE THR ALA LYS GLY VAL GLY ASN GLY ILE SER ILE ILE SEQRES 15 Y 430 ILE PHE ALA GLY ILE VAL SER GLY ILE PRO THR ILE LEU SEQRES 16 Y 430 ASN GLN ILE TYR ALA GLN THR PHE GLU ASN VAL GLY GLU SEQRES 17 Y 430 ASP LEU THR LEU ASN ILE VAL ARG LEU LEU LEU VAL ALA SEQRES 18 Y 430 LEU ALA VAL VAL ALA VAL ILE VAL GLY VAL ILE TYR ILE SEQRES 19 Y 430 GLN GLN ALA PHE ARG LYS ILE PRO ILE GLN TYR ALA LYS SEQRES 20 Y 430 ARG LEU GLU GLY ARG ASN PRO VAL GLY GLY HIS SER THR SEQRES 21 Y 430 HIS LEU PRO LEU LYS VAL ASN PRO ALA GLY VAL ILE PRO SEQRES 22 Y 430 VAL ILE PHE ALA VAL SER PHE LEU ILE ALA PRO PRO THR SEQRES 23 Y 430 ILE ALA SER PHE PHE GLY THR ASN ASP VAL THR LEU TRP SEQRES 24 Y 430 ILE ARG ARG THR PHE ASP TYR THR HIS PRO VAL GLY MET SEQRES 25 Y 430 THR ILE TYR VAL VAL LEU ILE ILE ALA PHE THR TYR PHE SEQRES 26 Y 430 TYR ALA PHE VAL GLN VAL ASN PRO GLU GLN MET ALA ASP SEQRES 27 Y 430 ASN LEU LYS LYS GLN GLY GLY TYR ILE PRO GLY ILE ARG SEQRES 28 Y 430 PRO GLY LYS ASN THR GLN GLU TYR VAL THR ARG ILE LEU SEQRES 29 Y 430 TYR ARG LEU THR LEU VAL GLY SER LEU PHE LEU ALA PHE SEQRES 30 Y 430 ILE ALA VAL LEU PRO VAL PHE PHE VAL ASN PHE ALA ASN SEQRES 31 Y 430 LEU PRO PRO SER ALA GLN ILE GLY GLY THR SER LEU LEU SEQRES 32 Y 430 ILE VAL VAL GLY VAL ALA LEU GLU THR MET LYS GLN LEU SEQRES 33 Y 430 GLU SER GLN LEU VAL LYS ARG HIS TYR ARG GLY PHE ILE SEQRES 34 Y 430 LYS SEQRES 1 E 70 MET GLN ARG VAL THR ASN PHE PHE LYS GLU VAL VAL ARG SEQRES 2 E 70 GLU LEU LYS LYS VAL SER TRP PRO ASN ARG LYS GLU LEU SEQRES 3 E 70 VAL ASN TYR THR ALA VAL VAL LEU ALA THR VAL ALA PHE SEQRES 4 E 70 PHE THR VAL PHE PHE ALA VAL ILE ASP LEU GLY ILE SER SEQRES 5 E 70 GLN LEU ILE ARG LEU VAL PHE GLU GLY GLY HIS HIS HIS SEQRES 6 E 70 HIS HIS HIS HIS HIS SEQRES 1 V 117 GLN VAL GLN LEU VAL GLU THR GLY GLY GLY LEU VAL GLN SEQRES 2 V 117 PRO GLY GLY SER LEU ARG LEU SER CYS GLY ALA SER GLY SEQRES 3 V 117 SER ILE PHE ASN MET TYR ALA MET GLY TRP TYR ARG GLN SEQRES 4 V 117 ALA PRO GLY LYS ARG ARG GLU VAL VAL ALA ARG ILE ALA SEQRES 5 V 117 THR ASP ASP SER THR MET TYR PRO ASP SER VAL LYS GLY SEQRES 6 V 117 ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR VAL SEQRES 7 V 117 TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR ALA SEQRES 8 V 117 VAL TYR TYR CYS TYR TYR GLN ARG THR VAL MET SER GLN SEQRES 9 V 117 PRO TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER SEQRES 1 B 99 MET PRO ALA PRO GLY SER GLU GLY ILE TRP LEU TRP LEU SEQRES 2 B 99 GLY THR ALA GLY MET PHE LEU GLY MET LEU TYR PHE ILE SEQRES 3 B 99 ALA ARG GLY TRP GLY GLU THR ASP GLY ARG ARG GLN LYS SEQRES 4 B 99 PHE TYR ILE ALA THR ILE LEU ILE THR ALA ILE ALA PHE SEQRES 5 B 99 VAL ASN TYR LEU ALA MET ALA LEU GLY PHE GLY LEU THR SEQRES 6 B 99 PHE ILE GLU PHE GLY GLY GLU GLN HIS CYS ILE TYR TRP SEQRES 7 B 99 ALA ARG TYR THR ASP TRP LEU PHE THR THR PRO LEU LEU SEQRES 8 B 99 LEU TYR ASP LEU GLY LEU LEU ALA HET MG A1001 1 HET BEF A1002 4 HET ADP A1003 27 HETNAM MG MAGNESIUM ION HETNAM BEF BERYLLIUM TRIFLUORIDE ION HETNAM ADP ADENOSINE-5'-DIPHOSPHATE FORMUL 6 MG MG 2+ FORMUL 7 BEF BE F3 1- FORMUL 8 ADP C10 H15 N5 O10 P2 HELIX 1 AA1 ARG A 14 ALA A 28 1 15 HELIX 2 AA2 LYS A 42 GLY A 55 1 14 HELIX 3 AA3 THR A 57 ASP A 60 5 4 HELIX 4 AA4 LEU A 61 THR A 77 1 17 HELIX 5 AA5 PHE A 82 ASP A 94 1 13 HELIX 6 AA6 THR A 107 SER A 110 5 4 HELIX 7 AA7 THR A 111 ASN A 117 1 7 HELIX 8 AA8 ASN A 130 GLY A 149 1 20 HELIX 9 AA9 SER A 160 ALA A 169 1 10 HELIX 10 AB1 ASN A 177 ASN A 188 1 12 HELIX 11 AB2 TYR A 192 MET A 196 5 5 HELIX 12 AB3 GLU A 208 LEU A 213 1 6 HELIX 13 AB4 ASP A 215 THR A 219 5 5 HELIX 14 AB5 THR A 231 ARG A 242 1 12 HELIX 15 AB6 THR A 262 GLY A 274 1 13 HELIX 16 AB7 HIS A 283 ALA A 299 1 17 HELIX 17 AB8 GLN A 301 ASP A 305 1 5 HELIX 18 AB9 GLY A 332 GLU A 341 1 10 HELIX 19 AC1 THR A 356 PHE A 361 1 6 HELIX 20 AC2 GLU A 377 ILE A 384 1 8 HELIX 21 AC3 THR A 410 MET A 427 1 18 HELIX 22 AC4 VAL A 439 LEU A 449 1 11 HELIX 23 AC5 LYS A 450 ILE A 454 5 5 HELIX 24 AC6 ARG A 466 ALA A 474 1 9 HELIX 25 AC7 ASN A 485 GLY A 488 5 4 HELIX 26 AC8 SER A 515 GLY A 524 1 10 HELIX 27 AC9 ASP A 543 GLY A 550 1 8 HELIX 28 AD1 ALA A 556 GLY A 562 5 7 HELIX 29 AD2 VAL A 574 ASP A 619 1 46 HELIX 30 AD3 LEU A 623 TYR A 642 1 20 HELIX 31 AD4 ASP A 655 TYR A 665 1 11 HELIX 32 AD5 GLU A 672 ILE A 676 5 5 HELIX 33 AD6 GLU A 680 GLY A 704 1 25 HELIX 34 AD7 LYS A 705 ARG A 735 1 31 HELIX 35 AD8 GLN A 736 GLN A 745 5 10 HELIX 36 AD9 LEU A 749 LYS A 777 1 29 HELIX 37 AE1 ARG Y 3 MET Y 9 1 7 HELIX 38 AE2 VAL Y 11 GLY Y 31 1 21 HELIX 39 AE3 THR Y 32 ILE Y 34 5 3 HELIX 40 AE4 VAL Y 74 GLN Y 88 1 15 HELIX 41 AE5 VAL Y 92 GLU Y 97 1 6 HELIX 42 AE6 GLY Y 102 ARG Y 107 1 6 HELIX 43 AE7 LEU Y 109 GLY Y 137 1 29 HELIX 44 AE8 GLY Y 145 LYS Y 173 1 29 HELIX 45 AE9 ASN Y 177 SER Y 189 1 13 HELIX 46 AF1 GLY Y 190 THR Y 202 1 13 HELIX 47 AF2 ASN Y 213 GLN Y 236 1 24 HELIX 48 AF3 VAL Y 271 ALA Y 288 1 18 HELIX 49 AF4 ASN Y 294 PHE Y 304 1 11 HELIX 50 AF5 HIS Y 308 ASN Y 332 1 25 HELIX 51 AF6 ASN Y 332 GLY Y 344 1 13 HELIX 52 AF7 GLY Y 353 ASN Y 390 1 38 HELIX 53 AF8 GLY Y 399 GLN Y 419 1 21 HELIX 54 AF9 LEU Y 420 HIS Y 424 5 5 HELIX 55 AG1 ARG E 3 LEU E 15 1 13 HELIX 56 AG2 LYS E 16 VAL E 18 5 3 HELIX 57 AG3 ASN E 22 PHE E 59 1 38 HELIX 58 AG4 LYS V 86 THR V 90 5 5 HELIX 59 AG5 GLY B 35 LEU B 60 1 26 HELIX 60 AG6 GLN B 73 TRP B 84 1 12 SHEET 1 AA1 7 VAL A 152 LEU A 154 0 SHEET 2 AA1 7 ILE A 172 THR A 176 1 O ILE A 172 N GLY A 153 SHEET 3 AA1 7 VAL A 124 THR A 128 1 N VAL A 126 O THR A 173 SHEET 4 AA1 7 ALA A 204 ASP A 207 1 O ASP A 207 N VAL A 127 SHEET 5 AA1 7 LEU A 367 THR A 371 1 O ALA A 368 N ALA A 204 SHEET 6 AA1 7 ILE A 97 GLU A 99 1 N ALA A 98 O GLY A 369 SHEET 7 AA1 7 VAL A 389 THR A 391 1 O VAL A 390 N ILE A 97 SHEET 1 AA2 2 LEU A 221 SER A 224 0 SHEET 2 AA2 2 THR A 351 ILE A 355 -1 O ILE A 355 N LEU A 221 SHEET 1 AA3 2 TYR A 250 ASP A 253 0 SHEET 2 AA3 2 ALA A 258 LEU A 261 -1 O GLN A 260 N THR A 251 SHEET 1 AA4 3 TYR A 306 GLU A 309 0 SHEET 2 AA4 3 GLN A 312 VAL A 316 -1 O VAL A 314 N VAL A 307 SHEET 3 AA4 3 LEU A 323 MET A 324 -1 O MET A 324 N ILE A 315 SHEET 1 AA5 3 ARG A 400 ASP A 402 0 SHEET 2 AA5 3 GLY A 533 SER A 540 1 O GLY A 533 N ASP A 401 SHEET 3 AA5 3 LEU A 406 TYR A 408 1 N LEU A 406 O LEU A 539 SHEET 1 AA6 6 ARG A 400 ASP A 402 0 SHEET 2 AA6 6 GLY A 533 SER A 540 1 O GLY A 533 N ASP A 401 SHEET 3 AA6 6 ALA A 506 GLY A 509 1 N GLY A 509 O GLN A 536 SHEET 4 AA6 6 VAL A 432 GLY A 435 1 N LEU A 433 O VAL A 508 SHEET 5 AA6 6 VAL A 480 ALA A 483 1 O ALA A 483 N VAL A 434 SHEET 6 AA6 6 HIS A 456 LEU A 459 1 N GLN A 457 O ILE A 482 SHEET 1 AA7 2 PHE Y 238 PRO Y 242 0 SHEET 2 AA7 2 HIS Y 261 LYS Y 265 -1 O LEU Y 264 N ARG Y 239 SHEET 1 AA8 2 GLN Y 244 TYR Y 245 0 SHEET 2 AA8 2 GLY Y 345 TYR Y 346 -1 O TYR Y 346 N GLN Y 244 SHEET 1 AA9 4 VAL V 5 THR V 7 0 SHEET 2 AA9 4 SER V 17 GLY V 23 -1 O GLY V 23 N VAL V 5 SHEET 3 AA9 4 VAL V 78 ASN V 83 -1 O LEU V 80 N LEU V 20 SHEET 4 AA9 4 PHE V 67 ARG V 71 -1 N THR V 68 O GLN V 81 SHEET 1 AB1 2 LEU V 11 VAL V 12 0 SHEET 2 AB1 2 THR V 114 VAL V 115 1 O THR V 114 N VAL V 12 SHEET 1 AB2 3 VAL V 47 ILE V 51 0 SHEET 2 AB2 3 ALA V 33 TYR V 37 -1 N MET V 34 O ILE V 51 SHEET 3 AB2 3 TYR V 94 GLN V 98 -1 O TYR V 94 N TYR V 37 SSBOND 1 CYS V 22 CYS V 95 1555 1555 2.03 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