HEADER TRANSPORT PROTEIN/IMMUNE SYSTEM 19-MAR-24 9B3K TITLE NORA IN COMPLEX WITH FAB36 (NORA-BRIL FUSION) COMPND MOL_ID: 1; COMPND 2 MOLECULE: NORA-BRIL(3A) FUSION; COMPND 3 CHAIN: Z; COMPND 4 FRAGMENT: NORA DOMAIN (1-380) + 3A LINKER (381-383) + BRIL DOMAIN COMPND 5 (384-490); COMPND 6 ENGINEERED: YES; COMPND 7 OTHER_DETAILS: NORA-BRIL(3A) FUSION DETAILS: M1 TO R380 IS NORA COMPND 8 DOMAIN; A381 TO A383 IS THE 3A LINKER; A384 TO L490 IS BRIL DOMAIN COMPND 9 (MOST RESIDUES FOR BRIL DOMAIN WERE NOT BUILT SINCE A MASK WAS ADDED COMPND 10 ONLY AROUND NORA DOMAIN DURING DATA PROCESSING); COMPND 11 MOL_ID: 2; COMPND 12 MOLECULE: FAB36 HEAVY CHAIN; COMPND 13 CHAIN: H; COMPND 14 ENGINEERED: YES; COMPND 15 MOL_ID: 3; COMPND 16 MOLECULE: FAB36 LIGHT CHAIN; COMPND 17 CHAIN: L; COMPND 18 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS; SOURCE 3 ORGANISM_TAXID: 1280; SOURCE 4 GENE: NORA; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_COMMON: HUMAN; SOURCE 10 ORGANISM_TAXID: 9606; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_COMMON: HUMAN; SOURCE 16 ORGANISM_TAXID: 9606; SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 18 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS MEMBRANE PROTEIN, STAPHYLOCOCCUS AUREUS, ANTIBIOTIC RESISTANCE, KEYWDS 2 EFFLUX PUMP, TRANSPORT PROTEIN, TRANSPORT PROTEIN-IMMUNE SYSTEM KEYWDS 3 COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR P.XIE,Y.LI,H.KUANG,D.N.WANG,N.J.TRAASETH REVDAT 1 11-DEC-24 9B3K 0 JRNL AUTH P.XIE,Y.LI,H.KUANG,D.N.WANG,N.J.TRAASETH JRNL TITL A SHARED HELIX APPROACH TO SOLVE SMALL MEMBRANE TRANSPORTER JRNL TITL 2 STRUCTURES USING CRYO-EM JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.56 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, CRYOSPARC, PHENIX, PHENIX, REMARK 3 CRYOSPARC, CRYOSPARC, CRYOSPARC, REMARK 3 CRYOSPARC REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : 7LO8 REMARK 3 REFINEMENT SPACE : REAL REMARK 3 REFINEMENT PROTOCOL : RIGID BODY FIT 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) : 2.560 REMARK 3 NUMBER OF PARTICLES : 298088 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 9B3K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-MAR-24. REMARK 100 THE DEPOSITION ID IS D_1000278169. 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 : NORA-BRIL(3A)-FAB36-FABBRIL REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : HOLD FOR 10 SEC BEFORE 25SEC REMARK 245 GLOW DISCHARGING REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.50 REMARK 245 SAMPLE DETAILS : FABBRIL WAS ADDED BUT NOT BUILT REMARK 245 IN MODEL DUE TO MASKING. HERE IS ITS SEQUENCE: HEAVY CHAIN: REMARK 245 SEVQLVESGGGLVQPGGSLRLSCAASGFNVVDFSLHWVRQAPGKGLEWVAYISSSSGSTSYADSV REMARK 245 KGRFTISADTSKNTAYLQMNSLRAEDTAVYYCARWGYWPGEPWWKAFDYWGQGTLVTVSSASTKG REMARK 245 PSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVT REMARK 245 REMARK 245 VPSSSLGTQTYICNVNHKPSNTKVDKKVEPKS LIGHT CHAIN: DIQMTQSPSSLSASVGDRVTI 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) : 1000.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1800.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : 2.70 REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5554.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : 105000 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: Z, H, L 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 THR Z 184 REMARK 465 THR Z 185 REMARK 465 SER Z 186 REMARK 465 GLY Z 187 REMARK 465 PHE Z 188 REMARK 465 GLN Z 189 REMARK 465 LYS Z 190 REMARK 465 LEU Z 191 REMARK 465 GLU Z 192 REMARK 465 PRO Z 193 REMARK 465 GLN Z 194 REMARK 465 LEU Z 195 REMARK 465 LEU Z 196 REMARK 465 THR Z 197 REMARK 465 ASP Z 385 REMARK 465 LEU Z 386 REMARK 465 GLU Z 387 REMARK 465 ASP Z 388 REMARK 465 ASN Z 389 REMARK 465 TRP Z 390 REMARK 465 GLU Z 391 REMARK 465 THR Z 392 REMARK 465 LEU Z 393 REMARK 465 ASN Z 394 REMARK 465 ASP Z 395 REMARK 465 ASN Z 396 REMARK 465 LEU Z 397 REMARK 465 LYS Z 398 REMARK 465 VAL Z 399 REMARK 465 ILE Z 400 REMARK 465 GLU Z 401 REMARK 465 LYS Z 402 REMARK 465 ALA Z 403 REMARK 465 ASP Z 404 REMARK 465 ASN Z 405 REMARK 465 ALA Z 406 REMARK 465 ALA Z 407 REMARK 465 GLN Z 408 REMARK 465 VAL Z 409 REMARK 465 LYS Z 410 REMARK 465 ASP Z 411 REMARK 465 ALA Z 412 REMARK 465 LEU Z 413 REMARK 465 THR Z 414 REMARK 465 LYS Z 415 REMARK 465 MET Z 416 REMARK 465 ARG Z 417 REMARK 465 ALA Z 418 REMARK 465 ALA Z 419 REMARK 465 ALA Z 420 REMARK 465 LEU Z 421 REMARK 465 ASP Z 422 REMARK 465 ALA Z 423 REMARK 465 GLN Z 424 REMARK 465 LYS Z 425 REMARK 465 ALA Z 426 REMARK 465 THR Z 427 REMARK 465 PRO Z 428 REMARK 465 PRO Z 429 REMARK 465 LYS Z 430 REMARK 465 LEU Z 431 REMARK 465 GLU Z 432 REMARK 465 ASP Z 433 REMARK 465 LYS Z 434 REMARK 465 SER Z 435 REMARK 465 PRO Z 436 REMARK 465 ASP Z 437 REMARK 465 SER Z 438 REMARK 465 PRO Z 439 REMARK 465 GLU Z 440 REMARK 465 MET Z 441 REMARK 465 LYS Z 442 REMARK 465 ASP Z 443 REMARK 465 PHE Z 444 REMARK 465 ARG Z 445 REMARK 465 HIS Z 446 REMARK 465 GLY Z 447 REMARK 465 PHE Z 448 REMARK 465 ASP Z 449 REMARK 465 ILE Z 450 REMARK 465 LEU Z 451 REMARK 465 VAL Z 452 REMARK 465 GLY Z 453 REMARK 465 GLN Z 454 REMARK 465 ILE Z 455 REMARK 465 ASP Z 456 REMARK 465 ASP Z 457 REMARK 465 ALA Z 458 REMARK 465 LEU Z 459 REMARK 465 LYS Z 460 REMARK 465 LEU Z 461 REMARK 465 ALA Z 462 REMARK 465 ASN Z 463 REMARK 465 GLU Z 464 REMARK 465 GLY Z 465 REMARK 465 LYS Z 466 REMARK 465 VAL Z 467 REMARK 465 LYS Z 468 REMARK 465 GLU Z 469 REMARK 465 ALA Z 470 REMARK 465 GLN Z 471 REMARK 465 ALA Z 472 REMARK 465 ALA Z 473 REMARK 465 ALA Z 474 REMARK 465 GLU Z 475 REMARK 465 GLN Z 476 REMARK 465 LEU Z 477 REMARK 465 LYS Z 478 REMARK 465 THR Z 479 REMARK 465 THR Z 480 REMARK 465 ARG Z 481 REMARK 465 ASN Z 482 REMARK 465 ALA Z 483 REMARK 465 TYR Z 484 REMARK 465 ILE Z 485 REMARK 465 GLN Z 486 REMARK 465 LYS Z 487 REMARK 465 TYR Z 488 REMARK 465 LEU Z 489 REMARK 465 MET H 1 REMARK 465 LYS H 2 REMARK 465 LYS H 3 REMARK 465 ASN H 4 REMARK 465 ILE H 5 REMARK 465 ALA H 6 REMARK 465 PHE H 7 REMARK 465 LEU H 8 REMARK 465 LEU H 9 REMARK 465 ALA H 10 REMARK 465 SER H 11 REMARK 465 MET H 12 REMARK 465 PHE H 13 REMARK 465 VAL H 14 REMARK 465 PHE H 15 REMARK 465 SER H 16 REMARK 465 ILE H 17 REMARK 465 ALA H 18 REMARK 465 THR H 19 REMARK 465 ASN H 20 REMARK 465 ALA H 21 REMARK 465 TYR H 22 REMARK 465 ALA H 23 REMARK 465 GLU H 24 REMARK 465 ILE H 25 REMARK 465 SER H 26 REMARK 465 SER H 169 REMARK 465 LYS H 170 REMARK 465 SER H 171 REMARK 465 THR H 172 REMARK 465 SER H 173 REMARK 465 SER H 256 REMARK 465 CYS H 257 REMARK 465 ASP H 258 REMARK 465 LYS H 259 REMARK 465 THR H 260 REMARK 465 HIS H 261 REMARK 465 THR H 262 REMARK 465 MET L 1 REMARK 465 LYS L 2 REMARK 465 LYS L 3 REMARK 465 ASN L 4 REMARK 465 ILE L 5 REMARK 465 ALA L 6 REMARK 465 PHE L 7 REMARK 465 LEU L 8 REMARK 465 LEU L 9 REMARK 465 ALA L 10 REMARK 465 SER L 11 REMARK 465 MET L 12 REMARK 465 PHE L 13 REMARK 465 VAL L 14 REMARK 465 PHE L 15 REMARK 465 SER L 16 REMARK 465 ILE L 17 REMARK 465 ALA L 18 REMARK 465 THR L 19 REMARK 465 ASN L 20 REMARK 465 ALA L 21 REMARK 465 TYR L 22 REMARK 465 ALA L 23 REMARK 465 SER L 24 REMARK 465 ASP L 25 REMARK 465 ILE L 26 REMARK 465 VAL L 170 REMARK 465 ALA L 177 REMARK 465 HIS L 213 REMARK 465 LYS L 214 REMARK 465 GLN L 223 REMARK 465 ARG L 235 REMARK 465 GLY L 236 REMARK 465 GLU L 237 REMARK 465 CYS L 238 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 SER Z 154 143.37 -172.27 REMARK 500 TRP Z 201 51.34 -91.70 REMARK 500 PRO H 40 79.38 -69.18 REMARK 500 ALA H 132 87.27 -151.52 REMARK 500 TRP H 133 -135.36 54.23 REMARK 500 GLN H 156 39.20 -97.86 REMARK 500 PRO H 188 -157.97 -73.52 REMARK 500 SER L 80 115.68 -162.62 REMARK 500 SER L 116 -157.96 -149.41 REMARK 500 ASN L 182 57.93 -98.83 REMARK 500 SER L 195 42.02 70.53 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-44143 RELATED DB: EMDB REMARK 900 NORA IN COMPLEX WITH FAB36 (NORA-BRIL FUSION) DBREF 9B3K Z 1 381 UNP Q53459 Q53459_STAAU 1 381 DBREF 9B3K Z 382 489 PDB 9B3K 9B3K 382 489 DBREF 9B3K H 1 262 PDB 9B3K 9B3K 1 262 DBREF 9B3K L 1 238 PDB 9B3K 9B3K 1 238 SEQRES 1 Z 489 MET ASN LYS GLN ILE PHE VAL LEU TYR PHE ASN ILE PHE SEQRES 2 Z 489 LEU ILE PHE LEU GLY ILE GLY LEU VAL ILE PRO VAL LEU SEQRES 3 Z 489 PRO VAL TYR LEU LYS ASP LEU GLY LEU THR GLY SER ASP SEQRES 4 Z 489 LEU GLY LEU LEU VAL ALA ALA PHE ALA LEU SER GLN MET SEQRES 5 Z 489 ILE ILE SER PRO PHE GLY GLY THR LEU ALA ASP LYS LEU SEQRES 6 Z 489 GLY LYS LYS LEU ILE ILE CYS ILE GLY LEU ILE LEU PHE SEQRES 7 Z 489 SER VAL SER GLU PHE MET PHE ALA VAL GLY HIS ASN PHE SEQRES 8 Z 489 SER VAL LEU MET LEU SER ARG VAL ILE GLY GLY MET SER SEQRES 9 Z 489 ALA GLY MET VAL MET PRO GLY VAL THR GLY LEU ILE ALA SEQRES 10 Z 489 ASP ILE SER PRO SER HIS GLN LYS ALA LYS ASN PHE GLY SEQRES 11 Z 489 TYR MET SER ALA ILE ILE ASN SER GLY PHE ILE LEU GLY SEQRES 12 Z 489 PRO GLY ILE GLY GLY PHE MET ALA GLU VAL SER HIS ARG SEQRES 13 Z 489 MET PRO PHE TYR PHE ALA GLY ALA LEU GLY ILE LEU ALA SEQRES 14 Z 489 PHE ILE MET SER ILE VAL LEU ILE HIS ASP PRO LYS LYS SEQRES 15 Z 489 SER THR THR SER GLY PHE GLN LYS LEU GLU PRO GLN LEU SEQRES 16 Z 489 LEU THR LYS ILE ASN TRP LYS VAL PHE ILE THR PRO VAL SEQRES 17 Z 489 ILE LEU THR LEU VAL LEU SER PHE GLY LEU SER ALA PHE SEQRES 18 Z 489 GLU THR LEU TYR SER LEU TYR THR ALA ASP LYS VAL ASN SEQRES 19 Z 489 TYR SER PRO LYS ASP ILE SER ILE ALA ILE THR GLY GLY SEQRES 20 Z 489 GLY ILE PHE GLY ALA LEU PHE GLN ILE TYR PHE PHE ASP SEQRES 21 Z 489 LYS PHE MET LYS TYR PHE SER GLU LEU THR PHE ILE ALA SEQRES 22 Z 489 TRP SER LEU LEU TYR SER VAL VAL VAL LEU ILE LEU LEU SEQRES 23 Z 489 VAL PHE ALA ASN ASP TYR TRP SER ILE MET LEU ILE SER SEQRES 24 Z 489 PHE VAL VAL PHE ILE GLY PHE ASP MET ILE ARG PRO ALA SEQRES 25 Z 489 ILE THR ASN TYR PHE SER ASN ILE ALA GLY GLU ARG GLN SEQRES 26 Z 489 GLY PHE ALA GLY GLY LEU ASN SER THR PHE THR SER MET SEQRES 27 Z 489 GLY ASN PHE ILE GLY PRO LEU ILE ALA GLY ALA LEU PHE SEQRES 28 Z 489 ASP VAL HIS ILE GLU ALA PRO ILE TYR MET ALA ILE GLY SEQRES 29 Z 489 VAL SER LEU ALA GLY VAL VAL ILE VAL LEU ILE GLU LYS SEQRES 30 Z 489 GLN HIS ARG ALA ALA ALA ALA ASP LEU GLU ASP ASN TRP SEQRES 31 Z 489 GLU THR LEU ASN ASP ASN LEU LYS VAL ILE GLU LYS ALA SEQRES 32 Z 489 ASP ASN ALA ALA GLN VAL LYS ASP ALA LEU THR LYS MET SEQRES 33 Z 489 ARG ALA ALA ALA LEU ASP ALA GLN LYS ALA THR PRO PRO SEQRES 34 Z 489 LYS LEU GLU ASP LYS SER PRO ASP SER PRO GLU MET LYS SEQRES 35 Z 489 ASP PHE ARG HIS GLY PHE ASP ILE LEU VAL GLY GLN ILE SEQRES 36 Z 489 ASP ASP ALA LEU LYS LEU ALA ASN GLU GLY LYS VAL LYS SEQRES 37 Z 489 GLU ALA GLN ALA ALA ALA GLU GLN LEU LYS THR THR ARG SEQRES 38 Z 489 ASN ALA TYR ILE GLN LYS TYR LEU SEQRES 1 H 262 MET LYS LYS ASN ILE ALA PHE LEU LEU ALA SER MET PHE SEQRES 2 H 262 VAL PHE SER ILE ALA THR ASN ALA TYR ALA GLU ILE SER SEQRES 3 H 262 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 4 H 262 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 5 H 262 PHE THR PHE SER SER SER SER ILE HIS TRP VAL ARG GLN SEQRES 6 H 262 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA SER ILE SER SEQRES 7 H 262 SER SER SER GLY SER THR SER TYR ALA ASP SER VAL LYS SEQRES 8 H 262 GLY ARG PHE THR ILE SER ALA ASP THR SER LYS ASN THR SEQRES 9 H 262 ALA TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 10 H 262 ALA VAL TYR TYR CYS ALA ARG TYR SER ARG TYR TYR TYR SEQRES 11 H 262 TYR ALA TRP ARG VAL GLY GLY TYR TRP GLY GLY LEU ASP SEQRES 12 H 262 TYR TRP GLY GLN GLY THR LEU VAL THR VAL PHE ASN GLN SEQRES 13 H 262 ILE LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER SEQRES 14 H 262 LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU SEQRES 15 H 262 VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP SEQRES 16 H 262 ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO SEQRES 17 H 262 ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER SEQRES 18 H 262 VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR SEQRES 19 H 262 TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS SEQRES 20 H 262 VAL ASP LYS LYS VAL GLU PRO LYS SER CYS ASP LYS THR SEQRES 21 H 262 HIS THR SEQRES 1 L 238 MET LYS LYS ASN ILE ALA PHE LEU LEU ALA SER MET PHE SEQRES 2 L 238 VAL PHE SER ILE ALA THR ASN ALA TYR ALA SER ASP ILE SEQRES 3 L 238 GLN MET THR GLN SER PRO SER SER LEU SER ALA SER VAL SEQRES 4 L 238 GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER GLN SER SEQRES 5 L 238 VAL SER SER ALA VAL ALA TRP TYR GLN GLN LYS PRO GLY SEQRES 6 L 238 LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SER SER LEU SEQRES 7 L 238 TYR SER GLY VAL PRO SER ARG PHE SER GLY SER ARG SER SEQRES 8 L 238 GLY THR ASP PHE THR LEU THR ILE SER SER LEU GLN PRO SEQRES 9 L 238 GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER SER SER SEQRES 10 L 238 SER LEU ILE THR PHE GLY GLN GLY THR LYS VAL GLU ILE SEQRES 11 L 238 LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE PRO SEQRES 12 L 238 PRO SER ASP SER GLN LEU LYS SER GLY THR ALA SER VAL SEQRES 13 L 238 VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA LYS SEQRES 14 L 238 VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY ASN SEQRES 15 L 238 SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SER SEQRES 16 L 238 THR TYR SER LEU SER SER THR LEU THR LEU SER LYS ALA SEQRES 17 L 238 ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL THR SEQRES 18 L 238 HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE ASN SEQRES 19 L 238 ARG GLY GLU CYS HELIX 1 AA1 LYS Z 3 LEU Z 21 1 19 HELIX 2 AA2 VAL Z 22 PRO Z 24 5 3 HELIX 3 AA3 VAL Z 25 GLY Z 34 1 10 HELIX 4 AA4 THR Z 36 GLY Z 66 1 31 HELIX 5 AA5 GLY Z 66 GLY Z 88 1 23 HELIX 6 AA6 ASN Z 90 ILE Z 119 1 30 HELIX 7 AA7 GLN Z 124 MET Z 150 1 27 HELIX 8 AA8 ARG Z 156 ILE Z 177 1 22 HELIX 9 AA9 PHE Z 204 LEU Z 224 1 21 HELIX 10 AB1 LEU Z 224 ASN Z 234 1 11 HELIX 11 AB2 SER Z 236 PHE Z 258 1 23 HELIX 12 AB3 PHE Z 258 PHE Z 266 1 9 HELIX 13 AB4 SER Z 267 PHE Z 288 1 22 HELIX 14 AB5 ASP Z 291 VAL Z 302 1 12 HELIX 15 AB6 PHE Z 303 ALA Z 321 1 19 HELIX 16 AB7 ARG Z 324 ASP Z 352 1 29 HELIX 17 AB8 GLU Z 356 ALA Z 384 1 29 HELIX 18 AB9 ARG H 113 THR H 117 5 5 HELIX 19 AC1 SER H 228 LEU H 230 5 3 HELIX 20 AC2 GLN L 103 PHE L 107 5 5 HELIX 21 AC3 SER L 145 GLY L 152 1 8 HELIX 22 AC4 LYS L 207 LYS L 212 1 6 SHEET 1 AA1 4 GLN H 29 SER H 33 0 SHEET 2 AA1 4 LEU H 44 SER H 51 -1 O SER H 47 N SER H 33 SHEET 3 AA1 4 THR H 104 MET H 109 -1 O MET H 109 N LEU H 44 SHEET 4 AA1 4 PHE H 94 ASP H 99 -1 N THR H 95 O GLN H 108 SHEET 1 AA2 5 THR H 84 TYR H 86 0 SHEET 2 AA2 5 LEU H 71 SER H 78 -1 N SER H 76 O SER H 85 SHEET 3 AA2 5 SER H 57 GLN H 65 -1 N ARG H 64 O GLU H 72 SHEET 4 AA2 5 ALA H 118 ALA H 132 -1 O TYR H 121 N VAL H 63 SHEET 5 AA2 5 THR H 149 VAL H 151 -1 O THR H 149 N TYR H 120 SHEET 1 AA3 6 THR H 84 TYR H 86 0 SHEET 2 AA3 6 LEU H 71 SER H 78 -1 N SER H 76 O SER H 85 SHEET 3 AA3 6 SER H 57 GLN H 65 -1 N ARG H 64 O GLU H 72 SHEET 4 AA3 6 ALA H 118 ALA H 132 -1 O TYR H 121 N VAL H 63 SHEET 5 AA3 6 VAL H 135 TRP H 145 -1 O GLY H 141 N SER H 126 SHEET 6 AA3 6 SER L 74 ALA L 75 -1 O SER L 74 N GLY H 140 SHEET 1 AA4 4 SER H 161 LEU H 165 0 SHEET 2 AA4 4 THR H 176 TYR H 186 -1 O LYS H 184 N SER H 161 SHEET 3 AA4 4 TYR H 217 PRO H 226 -1 O VAL H 223 N LEU H 179 SHEET 4 AA4 4 VAL H 204 THR H 206 -1 N HIS H 205 O VAL H 222 SHEET 1 AA5 4 SER H 161 LEU H 165 0 SHEET 2 AA5 4 THR H 176 TYR H 186 -1 O LYS H 184 N SER H 161 SHEET 3 AA5 4 TYR H 217 PRO H 226 -1 O VAL H 223 N LEU H 179 SHEET 4 AA5 4 VAL H 210 LEU H 211 -1 N VAL H 210 O SER H 218 SHEET 1 AA6 3 VAL H 191 TRP H 195 0 SHEET 2 AA6 3 TYR H 235 HIS H 241 -1 O ASN H 240 N THR H 192 SHEET 3 AA6 3 THR H 246 VAL H 252 -1 O VAL H 248 N VAL H 239 SHEET 1 AA7 4 GLN L 30 SER L 31 0 SHEET 2 AA7 4 VAL L 43 ARG L 48 -1 O THR L 46 N SER L 31 SHEET 3 AA7 4 ASP L 94 ILE L 99 -1 O PHE L 95 N CYS L 47 SHEET 4 AA7 4 PHE L 86 SER L 91 -1 N SER L 87 O THR L 98 SHEET 1 AA8 5 SER L 34 ALA L 37 0 SHEET 2 AA8 5 THR L 126 ILE L 130 1 O LYS L 127 N LEU L 35 SHEET 3 AA8 5 THR L 109 SER L 115 -1 N TYR L 110 O THR L 126 SHEET 4 AA8 5 ALA L 58 GLN L 62 -1 N GLN L 62 O THR L 109 SHEET 5 AA8 5 LYS L 69 ILE L 72 -1 O LYS L 69 N GLN L 61 SHEET 1 AA9 4 SER L 34 ALA L 37 0 SHEET 2 AA9 4 THR L 126 ILE L 130 1 O LYS L 127 N LEU L 35 SHEET 3 AA9 4 THR L 109 SER L 115 -1 N TYR L 110 O THR L 126 SHEET 4 AA9 4 ILE L 120 PHE L 122 -1 O THR L 121 N GLN L 114 SHEET 1 AB1 4 PHE L 140 PHE L 142 0 SHEET 2 AB1 4 THR L 153 PHE L 163 -1 O LEU L 159 N PHE L 140 SHEET 3 AB1 4 TYR L 197 SER L 206 -1 O LEU L 203 N VAL L 156 SHEET 4 AB1 4 SER L 183 VAL L 187 -1 N GLN L 184 O THR L 202 SHEET 1 AB2 3 LYS L 169 LYS L 169 0 SHEET 2 AB2 3 TYR L 216 THR L 221 -1 O THR L 221 N LYS L 169 SHEET 3 AB2 3 TRP L 172 VAL L 174 -1 N LYS L 173 O ALA L 217 SHEET 1 AB3 3 LYS L 169 LYS L 169 0 SHEET 2 AB3 3 TYR L 216 THR L 221 -1 O THR L 221 N LYS L 169 SHEET 3 AB3 3 VAL L 229 PHE L 233 -1 O PHE L 233 N TYR L 216 SSBOND 1 CYS H 48 CYS H 122 1555 1555 2.03 SSBOND 2 CYS H 181 CYS H 237 1555 1555 2.03 SSBOND 3 CYS L 47 CYS L 112 1555 1555 2.03 SSBOND 4 CYS L 158 CYS L 218 1555 1555 2.03 CISPEP 1 PHE H 187 PRO H 188 0 -2.11 CISPEP 2 SER L 31 PRO L 32 0 -1.23 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