HEADER MEMBRANE PROTEIN 17-MAY-22 7ZW1 TITLE HUMAN PRPH2-ROM1 HETERO-DIMER COMPND MOL_ID: 1; COMPND 2 MOLECULE: PERIPHERIN-2; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: RETINAL DEGENERATION SLOW PROTEIN,TETRASPANIN-22,TSPAN-22; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES; COMPND 7 OTHER_DETAILS: HHHHHH = TAG OF PURIFICATION SEQUENCE OF THE PROTEIN COMPND 8 STARTS AT A-L-L (AMINOACIDS 2-3-4); COMPND 9 MOL_ID: 2; COMPND 10 MOLECULE: ROD OUTER SEGMENT MEMBRANE PROTEIN 1; COMPND 11 CHAIN: B; COMPND 12 SYNONYM: ROSP1,TETRASPANIN-23,TSPAN-23; COMPND 13 ENGINEERED: YES; COMPND 14 OTHER_DETAILS: THE PROTEIN SEQUENCE STARTS AT A-P-V-L, RESIDUES 2-3- COMPND 15 4-5; COMPND 16 MOL_ID: 3; COMPND 17 MOLECULE: NANOBODY; COMPND 18 CHAIN: C; COMPND 19 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: PRPH2, PRPH, RDS, TSPAN22; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_COMMON: HUMAN; SOURCE 12 ORGANISM_TAXID: 9606; SOURCE 13 GENE: ROM1, TSPAN23; SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 15 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 17 MOL_ID: 3; SOURCE 18 ORGANISM_SCIENTIFIC: LAMA; SOURCE 19 ORGANISM_TAXID: 9839; SOURCE 20 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS PRPH2, PERIPHERIN-2, ROM1, HETERO-COMPLEX, MEMBRANE PROTEIN, KEYWDS 2 TETRASPANIN EXPDTA ELECTRON MICROSCOPY AUTHOR D.EL MAZOUNI,P.GROS REVDAT 1 16-NOV-22 7ZW1 0 JRNL AUTH D.EL MAZOUNI,P.GROS JRNL TITL CRYO-EM STRUCTURES OF PERIPHERIN-2 AND ROM1 SUGGEST MULTIPLE JRNL TITL 2 ROLES IN PHOTORECEPTOR MEMBRANE MORPHOGENESIS. JRNL REF SCI ADV V. 8 D3677 2022 JRNL REFN ESSN 2375-2548 JRNL PMID 36351012 JRNL DOI 10.1126/SCIADV.ADD3677 REMARK 2 REMARK 2 RESOLUTION. 3.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC 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) : 3.700 REMARK 3 NUMBER OF PARTICLES : 93727 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 7ZW1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-MAY-22. REMARK 100 THE DEPOSITION ID IS D_1292123090. 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 : HUMAN PRPH2-ROM1 HETERO-DIMER; REMARK 245 HUMAN PRPH2-ROM1 HETERO-DIMER; REMARK 245 NANOBODY 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 : 7.60 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 BIOQUANTUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2300.00 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 : OTHER 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: TRIMERIC 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 HIS A -6 REMARK 465 HIS A -5 REMARK 465 HIS A -4 REMARK 465 HIS A -3 REMARK 465 HIS A -2 REMARK 465 HIS A -1 REMARK 465 GLY A 0 REMARK 465 SER A 1 REMARK 465 ALA A 2 REMARK 465 LEU A 3 REMARK 465 LEU A 4 REMARK 465 SER A 322 REMARK 465 VAL A 323 REMARK 465 LYS A 324 REMARK 465 LYS A 325 REMARK 465 LEU A 326 REMARK 465 GLY A 327 REMARK 465 LYS A 328 REMARK 465 GLY A 329 REMARK 465 ASN A 330 REMARK 465 GLN A 331 REMARK 465 VAL A 332 REMARK 465 GLU A 333 REMARK 465 ALA A 334 REMARK 465 GLU A 335 REMARK 465 GLY A 336 REMARK 465 ALA A 337 REMARK 465 GLY A 338 REMARK 465 ALA A 339 REMARK 465 GLY A 340 REMARK 465 GLN A 341 REMARK 465 ALA A 342 REMARK 465 PRO A 343 REMARK 465 GLU A 344 REMARK 465 ALA A 345 REMARK 465 GLY A 346 REMARK 465 GLY B 0 REMARK 465 SER B 1 REMARK 465 ALA B 2 REMARK 465 PRO B 3 REMARK 465 VAL B 4 REMARK 465 LEU B 5 REMARK 465 PRO B 6 REMARK 465 TRP B 323 REMARK 465 LEU B 324 REMARK 465 GLN B 325 REMARK 465 GLY B 326 REMARK 465 GLY B 327 REMARK 465 VAL B 328 REMARK 465 ALA B 329 REMARK 465 CYS B 330 REMARK 465 ARG B 331 REMARK 465 PRO B 332 REMARK 465 ALA B 333 REMARK 465 PRO B 334 REMARK 465 GLU B 335 REMARK 465 GLU B 336 REMARK 465 ALA B 337 REMARK 465 PRO B 338 REMARK 465 PRO B 339 REMARK 465 GLY B 340 REMARK 465 GLU B 341 REMARK 465 ALA B 342 REMARK 465 PRO B 343 REMARK 465 PRO B 344 REMARK 465 LYS B 345 REMARK 465 GLU B 346 REMARK 465 ASP B 347 REMARK 465 LEU B 348 REMARK 465 SER B 349 REMARK 465 GLU B 350 REMARK 465 ALA B 351 REMARK 465 ALA C 129 REMARK 465 ALA C 130 REMARK 465 PRO C 131 REMARK 465 LEU C 132 REMARK 465 GLU C 133 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 OG SER A 294 OE1 GLU A 298 2.02 REMARK 500 OG SER A 311 OE1 GLU A 314 2.13 REMARK 500 O HIS C 54 NH2 ARG C 74 2.17 REMARK 500 OE1 GLU A 56 OG1 THR A 129 2.19 REMARK 500 NH2 ARG B 171 O TYR C 106 2.19 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 GLU A 56 135.99 -171.24 REMARK 500 ARG A 203 157.72 63.42 REMARK 500 LEU A 308 119.85 -161.14 REMARK 500 GLU B 204 -2.24 71.94 REMARK 500 GLN B 243 109.51 -49.42 REMARK 500 GLN B 246 -165.69 -79.75 REMARK 500 ASN B 247 -121.03 45.03 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-14991 RELATED DB: EMDB REMARK 900 HUMAN PRPH2-ROM1 HETERO-DIMER DBREF 7ZW1 A 2 346 UNP P23942 PRPH2_HUMAN 2 346 DBREF 7ZW1 B 2 351 UNP Q03395 ROM1_HUMAN 2 351 DBREF 7ZW1 C 2 133 PDB 7ZW1 7ZW1 2 133 SEQADV 7ZW1 HIS A -6 UNP P23942 EXPRESSION TAG SEQADV 7ZW1 HIS A -5 UNP P23942 EXPRESSION TAG SEQADV 7ZW1 HIS A -4 UNP P23942 EXPRESSION TAG SEQADV 7ZW1 HIS A -3 UNP P23942 EXPRESSION TAG SEQADV 7ZW1 HIS A -2 UNP P23942 EXPRESSION TAG SEQADV 7ZW1 HIS A -1 UNP P23942 EXPRESSION TAG SEQADV 7ZW1 GLY A 0 UNP P23942 EXPRESSION TAG SEQADV 7ZW1 SER A 1 UNP P23942 EXPRESSION TAG SEQADV 7ZW1 SER A 150 UNP P23942 CYS 150 ENGINEERED MUTATION SEQADV 7ZW1 GLY B 0 UNP Q03395 EXPRESSION TAG SEQADV 7ZW1 SER B 1 UNP Q03395 EXPRESSION TAG SEQRES 1 A 353 HIS HIS HIS HIS HIS HIS GLY SER ALA LEU LEU LYS VAL SEQRES 2 A 353 LYS PHE ASP GLN LYS LYS ARG VAL LYS LEU ALA GLN GLY SEQRES 3 A 353 LEU TRP LEU MET ASN TRP PHE SER VAL LEU ALA GLY ILE SEQRES 4 A 353 ILE ILE PHE SER LEU GLY LEU PHE LEU LYS ILE GLU LEU SEQRES 5 A 353 ARG LYS ARG SER ASP VAL MET ASN ASN SER GLU SER HIS SEQRES 6 A 353 PHE VAL PRO ASN SER LEU ILE GLY MET GLY VAL LEU SER SEQRES 7 A 353 CYS VAL PHE ASN SER LEU ALA GLY LYS ILE CYS TYR ASP SEQRES 8 A 353 ALA LEU ASP PRO ALA LYS TYR ALA ARG TRP LYS PRO TRP SEQRES 9 A 353 LEU LYS PRO TYR LEU ALA ILE CYS VAL LEU PHE ASN ILE SEQRES 10 A 353 ILE LEU PHE LEU VAL ALA LEU CYS CYS PHE LEU LEU ARG SEQRES 11 A 353 GLY SER LEU GLU ASN THR LEU GLY GLN GLY LEU LYS ASN SEQRES 12 A 353 GLY MET LYS TYR TYR ARG ASP THR ASP THR PRO GLY ARG SEQRES 13 A 353 SER PHE MET LYS LYS THR ILE ASP MET LEU GLN ILE GLU SEQRES 14 A 353 PHE LYS CYS CYS GLY ASN ASN GLY PHE ARG ASP TRP PHE SEQRES 15 A 353 GLU ILE GLN TRP ILE SER ASN ARG TYR LEU ASP PHE SER SEQRES 16 A 353 SER LYS GLU VAL LYS ASP ARG ILE LYS SER ASN VAL ASP SEQRES 17 A 353 GLY ARG TYR LEU VAL ASP GLY VAL PRO PHE SER CYS CYS SEQRES 18 A 353 ASN PRO SER SER PRO ARG PRO CYS ILE GLN TYR GLN ILE SEQRES 19 A 353 THR ASN ASN SER ALA HIS TYR SER TYR ASP HIS GLN THR SEQRES 20 A 353 GLU GLU LEU ASN LEU TRP VAL ARG GLY CYS ARG ALA ALA SEQRES 21 A 353 LEU LEU SER TYR TYR SER SER LEU MET ASN SER MET GLY SEQRES 22 A 353 VAL VAL THR LEU LEU ILE TRP LEU PHE GLU VAL THR ILE SEQRES 23 A 353 THR ILE GLY LEU ARG TYR LEU GLN THR SER LEU ASP GLY SEQRES 24 A 353 VAL SER ASN PRO GLU GLU SER GLU SER GLU SER GLU GLY SEQRES 25 A 353 TRP LEU LEU GLU LYS SER VAL PRO GLU THR TRP LYS ALA SEQRES 26 A 353 PHE LEU GLU SER VAL LYS LYS LEU GLY LYS GLY ASN GLN SEQRES 27 A 353 VAL GLU ALA GLU GLY ALA GLY ALA GLY GLN ALA PRO GLU SEQRES 28 A 353 ALA GLY SEQRES 1 B 352 GLY SER ALA PRO VAL LEU PRO LEU VAL LEU PRO LEU GLN SEQRES 2 B 352 PRO ARG ILE ARG LEU ALA GLN GLY LEU TRP LEU LEU SER SEQRES 3 B 352 TRP LEU LEU ALA LEU ALA GLY GLY VAL ILE LEU LEU CYS SEQRES 4 B 352 SER GLY HIS LEU LEU VAL GLN LEU ARG HIS LEU GLY THR SEQRES 5 B 352 PHE LEU ALA PRO SER CYS GLN PHE PRO VAL LEU PRO GLN SEQRES 6 B 352 ALA ALA LEU ALA ALA GLY ALA VAL ALA LEU GLY THR GLY SEQRES 7 B 352 LEU VAL GLY VAL GLY ALA SER ARG ALA SER LEU ASN ALA SEQRES 8 B 352 ALA LEU TYR PRO PRO TRP ARG GLY VAL LEU GLY PRO LEU SEQRES 9 B 352 LEU VAL ALA GLY THR ALA GLY GLY GLY GLY LEU LEU VAL SEQRES 10 B 352 VAL GLY LEU GLY LEU ALA LEU ALA LEU PRO GLY SER LEU SEQRES 11 B 352 ASP GLU ALA LEU GLU GLU GLY LEU VAL THR ALA LEU ALA SEQRES 12 B 352 HIS TYR LYS ASP THR GLU VAL PRO GLY HIS CYS GLN ALA SEQRES 13 B 352 LYS ARG LEU VAL ASP GLU LEU GLN LEU ARG TYR HIS CYS SEQRES 14 B 352 CYS GLY ARG HIS GLY TYR LYS ASP TRP PHE GLY VAL GLN SEQRES 15 B 352 TRP VAL SER SER ARG TYR LEU ASP PRO GLY ASP ARG ASP SEQRES 16 B 352 VAL ALA ASP ARG ILE GLN SER ASN VAL GLU GLY LEU TYR SEQRES 17 B 352 LEU THR ASP GLY VAL PRO PHE SER CYS CYS ASN PRO HIS SEQRES 18 B 352 SER PRO ARG PRO CYS LEU GLN ASN ARG LEU SER ASP SER SEQRES 19 B 352 TYR ALA HIS PRO LEU PHE ASP PRO ARG GLN PRO ASN GLN SEQRES 20 B 352 ASN LEU TRP ALA GLN GLY CYS HIS GLU VAL LEU LEU GLU SEQRES 21 B 352 HIS LEU GLN ASP LEU ALA GLY THR LEU GLY SER MET LEU SEQRES 22 B 352 ALA VAL THR PHE LEU LEU GLN ALA LEU VAL LEU LEU GLY SEQRES 23 B 352 LEU ARG TYR LEU GLN THR ALA LEU GLU GLY LEU GLY GLY SEQRES 24 B 352 VAL ILE ASP ALA GLY GLY GLU THR GLN GLY TYR LEU PHE SEQRES 25 B 352 PRO SER GLY LEU LYS ASP MET LEU LYS THR ALA TRP LEU SEQRES 26 B 352 GLN GLY GLY VAL ALA CYS ARG PRO ALA PRO GLU GLU ALA SEQRES 27 B 352 PRO PRO GLY GLU ALA PRO PRO LYS GLU ASP LEU SER GLU SEQRES 28 B 352 ALA SEQRES 1 C 132 SER GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL SEQRES 2 C 132 GLN ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER SEQRES 3 C 132 THR ARG THR THR SER ARG TYR THR VAL GLY TRP PHE CYS SEQRES 4 C 132 GLN ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA VAL SEQRES 5 C 132 HIS TRP SER GLY GLY SER THR TRP TYR ALA ASP SER VAL SEQRES 6 C 132 LYS GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SEQRES 7 C 132 THR VAL TYR LEU GLN MET ASN SER LEU LYS GLN GLU ASP SEQRES 8 C 132 THR ALA VAL TYR TYR CYS ALA ALA ALA GLU PRO ARG ARG SEQRES 9 C 132 TYR SER TYR TYR MET ARG PRO ASP GLU TYR ASN TYR TRP SEQRES 10 C 132 GLY GLN GLY THR GLN VAL THR VAL SER SER ALA ALA PRO SEQRES 11 C 132 LEU GLU HELIX 1 AA1 ASP A 9 ARG A 48 1 40 HELIX 2 AA2 PHE A 59 ASP A 87 1 29 HELIX 3 AA3 ASP A 87 ARG A 93 1 7 HELIX 4 AA4 TRP A 94 PRO A 96 5 3 HELIX 5 AA5 TRP A 97 LEU A 122 1 26 HELIX 6 AA6 LEU A 122 TYR A 140 1 19 HELIX 7 AA7 ARG A 149 LYS A 164 1 16 HELIX 8 AA8 PHE A 171 ILE A 177 1 7 HELIX 9 AA9 SER A 189 ASN A 199 1 11 HELIX 10 AB1 PRO A 210 CYS A 214 5 5 HELIX 11 AB2 ASN A 229 HIS A 233 5 5 HELIX 12 AB3 GLY A 249 VAL A 293 1 45 HELIX 13 AB4 SER A 311 GLU A 321 1 11 HELIX 14 AB5 PRO B 10 HIS B 48 1 39 HELIX 15 AB6 LEU B 49 LEU B 53 5 5 HELIX 16 AB7 PRO B 60 ASN B 89 1 30 HELIX 17 AB8 ALA B 90 ARG B 97 5 8 HELIX 18 AB9 VAL B 99 HIS B 143 1 45 HELIX 19 AC1 CYS B 153 HIS B 167 1 15 HELIX 20 AC2 TYR B 174 VAL B 180 5 7 HELIX 21 AC3 SER B 184 LEU B 188 5 5 HELIX 22 AC4 ASP B 192 ASN B 202 1 11 HELIX 23 AC5 VAL B 203 LEU B 206 5 4 HELIX 24 AC6 PRO B 213 CYS B 217 5 5 HELIX 25 AC7 GLY B 252 GLY B 297 1 46 HELIX 26 AC8 GLY B 314 ALA B 322 1 9 HELIX 27 AC9 THR C 30 TYR C 34 5 5 HELIX 28 AD1 ASP C 64 LYS C 67 5 4 HELIX 29 AD2 LYS C 89 THR C 93 5 5 SHEET 1 AA1 2 VAL A 6 PHE A 8 0 SHEET 2 AA1 2 SER A 303 GLY A 305 -1 O GLY A 305 N VAL A 6 SHEET 1 AA2 4 GLN C 7 SER C 9 0 SHEET 2 AA2 4 LEU C 20 ALA C 25 -1 O ALA C 25 N GLN C 7 SHEET 3 AA2 4 THR C 80 MET C 85 -1 O VAL C 81 N CYS C 24 SHEET 4 AA2 4 PHE C 70 ASP C 75 -1 N ASP C 75 O THR C 80 SHEET 1 AA3 6 LEU C 13 GLN C 15 0 SHEET 2 AA3 6 THR C 122 SER C 127 1 O SER C 127 N VAL C 14 SHEET 3 AA3 6 ALA C 94 ALA C 101 -1 N TYR C 96 O THR C 122 SHEET 4 AA3 6 THR C 35 GLN C 41 -1 N GLN C 41 O VAL C 95 SHEET 5 AA3 6 GLU C 48 VAL C 53 -1 O VAL C 53 N VAL C 36 SHEET 6 AA3 6 THR C 60 TYR C 62 -1 O TRP C 61 N ALA C 52 SHEET 1 AA4 4 LEU C 13 GLN C 15 0 SHEET 2 AA4 4 THR C 122 SER C 127 1 O SER C 127 N VAL C 14 SHEET 3 AA4 4 ALA C 94 ALA C 101 -1 N TYR C 96 O THR C 122 SHEET 4 AA4 4 TYR C 117 TRP C 118 -1 O TYR C 117 N ALA C 100 SSBOND 1 CYS A 165 CYS A 250 1555 1555 2.03 SSBOND 2 CYS A 166 CYS A 213 1555 1555 2.03 SSBOND 3 CYS A 214 CYS A 222 1555 1555 2.03 SSBOND 4 CYS B 168 CYS B 253 1555 1555 2.03 SSBOND 5 CYS B 169 CYS B 216 1555 1555 2.03 SSBOND 6 CYS B 217 CYS B 225 1555 1555 2.03 SSBOND 7 CYS C 24 CYS C 98 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