HEADER TRANSPORT PROTEIN 03-APR-23 8ONT TITLE STRUCTURE OF SETARIA ITALICA NRAT IN COMPLEX WITH A NANOBODY COMPND MOL_ID: 1; COMPND 2 MOLECULE: NRAMP RELATED ALUMINIUM TRANSPORTER; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: NANOBODY1; COMPND 7 CHAIN: B; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SETARIA ITALICA; SOURCE 3 ORGANISM_COMMON: FOXTAIL MILLET; SOURCE 4 ORGANISM_TAXID: 4555; SOURCE 5 GENE: 101781512, SETIT_1G098100V2; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 11 ORGANISM_TAXID: 9844; SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 14 EXPRESSION_SYSTEM_CELL: MC1061 KEYWDS NRAT, NRAMP, SLC11, METAL UPTAKE, ALUMINIUM TRANSPORTER, TRANSPORT KEYWDS 2 PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR K.RAMANADANE,M.LIZICZAI,D.MARKOVIC,M.S.STRAUB,G.T.ROSALEN,A.UDOVCIC, AUTHOR 2 R.DUTZLER,C.MANATSCHAL REVDAT 1 12-APR-23 8ONT 0 JRNL AUTH K.RAMANADANE,M.LIZICZAI,D.MARKOVIC,M.S.STRAUB,G.T.ROSALEN, JRNL AUTH 2 A.UDOVCIC,R.DUTZLER,C.MANATSCHAL JRNL TITL STRUCTURE OF SETARIA ITALICA NRAT IN COMPLEX WITH A NANOBODY JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.66 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) : 3.660 REMARK 3 NUMBER OF PARTICLES : 300000 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 8ONT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-APR-23. REMARK 100 THE DEPOSITION ID IS D_1292129633. 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 : COMPLEX BETWEEN SINRAT AND A REMARK 245 NANOBODY USED AS A FIDUCIAL REMARK 245 MARKER FOR STRUCTURE REMARK 245 DETERMINATION REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 2.70 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 BIOQUANTUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1000.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2400.00 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) : 6968.00 REMARK 245 ILLUMINATION MODE : SPOT SCAN 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: 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 0 REMARK 465 SER A 1 REMARK 465 GLU A 2 REMARK 465 ARG A 3 REMARK 465 ALA A 4 REMARK 465 ARG A 5 REMARK 465 GLU A 6 REMARK 465 VAL A 7 REMARK 465 GLY A 8 REMARK 465 GLU A 9 REMARK 465 THR A 10 REMARK 465 GLY A 11 REMARK 465 ARG A 12 REMARK 465 GLU A 13 REMARK 465 ALA A 14 REMARK 465 ARG A 15 REMARK 465 HIS A 16 REMARK 465 GLY A 17 REMARK 465 VAL A 18 REMARK 465 LEU A 19 REMARK 465 GLN A 20 REMARK 465 SER A 21 REMARK 465 GLY A 22 REMARK 465 SER A 23 REMARK 465 ASP A 24 REMARK 465 THR A 25 REMARK 465 GLY A 26 REMARK 465 ASP A 27 REMARK 465 HIS A 28 REMARK 465 LYS A 29 REMARK 465 ASP A 30 REMARK 465 LYS A 31 REMARK 465 THR A 32 REMARK 465 VAL A 33 REMARK 465 GLU A 34 REMARK 465 LEU A 35 REMARK 465 GLU A 36 REMARK 465 LYS A 37 REMARK 465 ASP A 38 REMARK 465 GLU A 39 REMARK 465 GLN A 40 REMARK 465 PHE A 41 REMARK 465 GLN A 42 REMARK 465 GLY A 43 REMARK 465 GLN A 44 REMARK 465 PRO A 45 REMARK 465 LYS A 46 REMARK 465 TRP A 47 REMARK 465 ARG A 48 REMARK 465 LYS A 49 REMARK 465 PHE A 50 REMARK 465 LEU A 51 REMARK 465 ALA A 52 REMARK 465 HIS A 53 REMARK 465 LYS A 257 REMARK 465 THR A 258 REMARK 465 PRO A 259 REMARK 465 ARG A 260 REMARK 465 SER A 261 REMARK 465 VAL A 262 REMARK 465 LYS A 263 REMARK 465 SER A 264 REMARK 465 ILE A 265 REMARK 465 ARG A 266 REMARK 465 ALA A 267 REMARK 465 ALA A 268 REMARK 465 VAL A 505 REMARK 465 PRO A 506 REMARK 465 VAL A 507 REMARK 465 SER A 508 REMARK 465 GLU A 509 REMARK 465 ARG A 510 REMARK 465 ALA A 511 REMARK 465 GLN A 512 REMARK 465 GLY A 513 REMARK 465 GLN A 514 REMARK 465 VAL A 515 REMARK 465 GLU A 516 REMARK 465 ALA A 517 REMARK 465 GLY A 518 REMARK 465 GLY A 519 REMARK 465 ALA A 520 REMARK 465 GLN A 521 REMARK 465 ALA A 522 REMARK 465 VAL A 523 REMARK 465 ALA A 524 REMARK 465 SER A 525 REMARK 465 ALA A 526 REMARK 465 ALA A 527 REMARK 465 ASP A 528 REMARK 465 ALA A 529 REMARK 465 ASP A 530 REMARK 465 GLN A 531 REMARK 465 PRO A 532 REMARK 465 ALA A 533 REMARK 465 PRO A 534 REMARK 465 PHE A 535 REMARK 465 ARG A 536 REMARK 465 LYS A 537 REMARK 465 ASP A 538 REMARK 465 LEU A 539 REMARK 465 ALA A 540 REMARK 465 ASP A 541 REMARK 465 ALA A 542 REMARK 465 SER A 543 REMARK 465 MET A 544 REMARK 465 ALA A 545 REMARK 465 LEU A 546 REMARK 465 GLU A 547 REMARK 465 VAL A 548 REMARK 465 LEU A 549 REMARK 465 PHE A 550 REMARK 465 GLN A 551 REMARK 465 GLY A 552 REMARK 465 SER B 121 REMARK 465 SER B 122 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 A 82 OG1 THR A 296 1.91 REMARK 500 O SER A 139 OG SER A 402 2.03 REMARK 500 O VAL A 491 OG1 THR A 495 2.07 REMARK 500 OD1 ASP A 66 OG1 THR A 346 2.08 REMARK 500 OG1 THR A 351 ND2 ASN A 372 2.08 REMARK 500 OD2 ASP A 66 O HOH A 701 2.09 REMARK 500 OD2 ASP A 73 ND2 ASN A 287 2.09 REMARK 500 ND2 ASN A 153 OE1 GLN A 317 2.16 REMARK 500 O GLY A 295 ND2 ASN A 299 2.17 REMARK 500 NZ LYS A 108 OE1 GLU A 432 2.18 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 LYS A 81 -131.12 49.82 REMARK 500 TYR A 82 55.94 -95.59 REMARK 500 PRO A 122 -176.32 -69.89 REMARK 500 ARG A 208 71.11 60.51 REMARK 500 SER A 222 116.03 -162.96 REMARK 500 THR A 241 74.78 46.01 REMARK 500 ALA A 300 -138.69 47.41 REMARK 500 ARG A 329 5.83 57.55 REMARK 500 THR A 495 -63.14 -92.57 REMARK 500 ARG A 497 139.94 -171.90 REMARK 500 GLN B 13 -65.48 -104.39 REMARK 500 ASN B 77 65.67 60.69 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG B 19 0.08 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-17000 RELATED DB: EMDB REMARK 900 APO-STRUCTURE OF SETARIA ITALICA NRAT IN COMPLEX WITH A NANOBODY DBREF 8ONT A 2 544 UNP K3YRE7 K3YRE7_SETIT 2 543 DBREF 8ONT B 1 122 PDB 8ONT 8ONT 1 122 SEQADV 8ONT MET A 0 UNP K3YRE7 INITIATING METHIONINE SEQADV 8ONT SER A 1 UNP K3YRE7 EXPRESSION TAG SEQADV 8ONT ALA A 545 UNP K3YRE7 EXPRESSION TAG SEQADV 8ONT LEU A 546 UNP K3YRE7 EXPRESSION TAG SEQADV 8ONT GLU A 547 UNP K3YRE7 EXPRESSION TAG SEQADV 8ONT VAL A 548 UNP K3YRE7 EXPRESSION TAG SEQADV 8ONT LEU A 549 UNP K3YRE7 EXPRESSION TAG SEQADV 8ONT PHE A 550 UNP K3YRE7 EXPRESSION TAG SEQADV 8ONT GLN A 551 UNP K3YRE7 EXPRESSION TAG SEQADV 8ONT GLY A 552 UNP K3YRE7 EXPRESSION TAG SEQRES 1 A 552 MET SER GLU ARG ALA ARG GLU VAL GLY GLU THR GLY ARG SEQRES 2 A 552 GLU ALA ARG HIS GLY VAL LEU GLN SER GLY SER ASP THR SEQRES 3 A 552 GLY ASP HIS LYS ASP LYS THR VAL GLU LEU GLU LYS ASP SEQRES 4 A 552 GLU GLN PHE GLN GLY GLN PRO LYS TRP ARG LYS PHE LEU SEQRES 5 A 552 ALA HIS VAL GLY PRO GLY ALA LEU VAL ALA ILE GLY PHE SEQRES 6 A 552 LEU ASP PRO SER ASN LEU GLU THR ASP MET GLN ALA GLY SEQRES 7 A 552 ALA ASP PHE LYS TYR GLU LEU LEU TRP VAL VAL LEU VAL SEQRES 8 A 552 GLY MET ILE PHE ALA LEU LEU ILE GLN THR LEU ALA ALA SEQRES 9 A 552 ASN LEU GLY VAL LYS THR GLY ARG HIS LEU ALA GLU LEU SEQRES 10 A 552 CYS ARG GLU GLU TYR PRO ARG TYR VAL ASN ILE CYS LEU SEQRES 11 A 552 TRP ILE ILE ALA GLU LEU ALA VAL ILE SER ASP ASP ILE SEQRES 12 A 552 PRO GLU VAL LEU GLY THR ALA PHE ALA PHE ASN ILE LEU SEQRES 13 A 552 LEU LYS ILE PRO VAL TRP ALA GLY VAL ILE LEU THR VAL SEQRES 14 A 552 PHE SER THR LEU LEU LEU LEU GLY VAL GLN ARG PHE GLY SEQRES 15 A 552 ALA ARG LYS LEU GLU PHE ILE ILE ALA ALA PHE MET PHE SEQRES 16 A 552 THR MET ALA ALA CYS PHE PHE GLY GLU LEU SER TYR LEU SEQRES 17 A 552 ARG PRO SER ALA LYS GLU VAL VAL LYS GLY MET PHE VAL SEQRES 18 A 552 PRO SER LEU GLN GLY LYS GLY ALA ALA ALA ASN ALA ILE SEQRES 19 A 552 ALA LEU PHE GLY ALA ILE ILE THR PRO TYR ASN LEU PHE SEQRES 20 A 552 LEU HIS SER ALA LEU VAL LEU SER ARG LYS THR PRO ARG SEQRES 21 A 552 SER VAL LYS SER ILE ARG ALA ALA CYS ARG TYR PHE LEU SEQRES 22 A 552 ILE GLU CYS SER LEU ALA PHE ILE VAL ALA PHE LEU ILE SEQRES 23 A 552 ASN VAL SER VAL VAL VAL VAL ALA GLY THR ILE CYS ASN SEQRES 24 A 552 ALA ASP ASN LEU SER PRO THR ASP SER ASN THR CYS SER SEQRES 25 A 552 ASP LEU THR LEU GLN SER ALA PRO MET LEU LEU ARG ASN SEQRES 26 A 552 VAL LEU GLY ARG SER SER SER VAL VAL TYR ALA VAL ALA SEQRES 27 A 552 LEU LEU ALA SER GLY GLN SER THR THR ILE SER CYS THR SEQRES 28 A 552 PHE ALA GLY GLN VAL ILE MET GLN GLY PHE LEU ASP MET SEQRES 29 A 552 LYS MET LYS ASN TRP VAL ARG ASN LEU ILE THR ARG VAL SEQRES 30 A 552 ILE ALA ILE ALA PRO SER LEU ILE VAL SER ILE VAL SER SEQRES 31 A 552 GLY PRO SER GLY ALA GLY LYS LEU ILE ILE PHE SER SER SEQRES 32 A 552 MET VAL LEU SER PHE GLU MET PRO PHE ALA LEU ILE PRO SEQRES 33 A 552 LEU LEU LYS PHE CYS ASN SER SER LYS LYS VAL GLY PRO SEQRES 34 A 552 LEU LYS GLU SER ILE TYR THR VAL VAL ILE ALA TRP ILE SEQRES 35 A 552 LEU SER PHE ALA LEU ILE VAL VAL ASN THR TYR PHE LEU SEQRES 36 A 552 VAL TRP THR TYR VAL ASP TRP LEU VAL HIS ASN HIS LEU SEQRES 37 A 552 PRO LYS TYR ALA ASN ALA LEU VAL SER ILE VAL VAL PHE SEQRES 38 A 552 ALA LEU MET ALA ALA TYR LEU VAL PHE VAL VAL TYR LEU SEQRES 39 A 552 THR PHE ARG ARG ASP THR VAL SER THR TYR VAL PRO VAL SEQRES 40 A 552 SER GLU ARG ALA GLN GLY GLN VAL GLU ALA GLY GLY ALA SEQRES 41 A 552 GLN ALA VAL ALA SER ALA ALA ASP ALA ASP GLN PRO ALA SEQRES 42 A 552 PRO PHE ARG LYS ASP LEU ALA ASP ALA SER MET ALA LEU SEQRES 43 A 552 GLU VAL LEU PHE GLN GLY SEQRES 1 B 122 GLN TRP GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 B 122 ALA GLY GLY SER LEU ARG LEU SER CYS VAL GLY SER GLY SEQRES 3 B 122 ARG ALA PHE SER SER GLY ALA MET GLY TRP PHE ARG GLN SEQRES 4 B 122 THR PRO GLY GLN GLU ARG GLU PHE VAL ALA ALA ILE SER SEQRES 5 B 122 TRP SER GLY GLY SER THR VAL TYR ALA GLU SER VAL LYS SEQRES 6 B 122 GLY ARG PHE THR ILE SER MET ASP ASN ALA LYS ASN THR SEQRES 7 B 122 VAL TYR LEU ARG MET ASN SER LEU GLN PRO GLU ASP THR SEQRES 8 B 122 ALA VAL TYR TYR CYS ALA ALA GLY THR SER THR PHE ALA SEQRES 9 B 122 LEU ARG ARG SER PRO GLU TYR TRP GLY LYS GLY THR PRO SEQRES 10 B 122 VAL THR VAL SER SER HET PLC A 601 106 HETNAM PLC DIUNDECYL PHOSPHATIDYL CHOLINE FORMUL 3 PLC C32 H65 N O8 P 1+ FORMUL 4 HOH *(H2 O) HELIX 1 AA1 LEU A 59 LEU A 65 1 7 HELIX 2 AA2 ASP A 66 LYS A 81 1 16 HELIX 3 AA3 LEU A 84 GLY A 110 1 27 HELIX 4 AA4 HIS A 112 TYR A 121 1 10 HELIX 5 AA5 PRO A 122 LYS A 157 1 36 HELIX 6 AA6 PRO A 159 GLY A 181 1 23 HELIX 7 AA7 ALA A 182 ARG A 208 1 27 HELIX 8 AA8 SER A 210 PHE A 219 1 10 HELIX 9 AA9 GLY A 225 THR A 241 1 17 HELIX 10 AB1 PRO A 242 LEU A 253 1 12 HELIX 11 AB2 ARG A 270 ALA A 300 1 31 HELIX 12 AB3 SER A 304 LEU A 314 1 11 HELIX 13 AB4 ALA A 319 GLY A 328 1 10 HELIX 14 AB5 SER A 330 LEU A 362 1 33 HELIX 15 AB6 LYS A 367 SER A 390 1 24 HELIX 16 AB7 GLY A 391 SER A 423 1 33 HELIX 17 AB8 SER A 423 GLY A 428 1 6 HELIX 18 AB9 SER A 433 ASN A 466 1 34 HELIX 19 AC1 ALA A 472 PHE A 496 1 25 HELIX 20 AC2 GLN B 87 THR B 91 5 5 HELIX 21 AC3 PHE B 103 SER B 108 1 6 SHEET 1 AA1 4 GLN B 3 SER B 7 0 SHEET 2 AA1 4 ARG B 19 SER B 25 -1 O SER B 21 N SER B 7 SHEET 3 AA1 4 THR B 78 MET B 83 -1 O VAL B 79 N CYS B 22 SHEET 4 AA1 4 PHE B 68 ASP B 73 -1 N SER B 71 O TYR B 80 SHEET 1 AA2 4 GLU B 46 ALA B 49 0 SHEET 2 AA2 4 ALA B 33 GLN B 39 -1 N ARG B 38 O GLU B 46 SHEET 3 AA2 4 ALA B 92 GLY B 99 -1 O VAL B 93 N GLN B 39 SHEET 4 AA2 4 THR B 116 VAL B 118 -1 O THR B 116 N TYR B 94 SSBOND 1 CYS A 298 CYS A 311 1555 1555 2.03 SSBOND 2 CYS B 22 CYS B 96 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