HEADER PROTEIN TRANSPORT/IMMUNE SYSTEM 12-FEB-25 9LVB TITLE IAA-FREE AUX1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: AUXIN TRANSPORTER PROTEIN 1,SOLUBLE CYTOCHROME B562; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: HEAVY CHAIN; COMPND 7 CHAIN: H; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: LIGHT CHAIN; COMPND 11 CHAIN: L; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: NANOBODY; COMPND 15 CHAIN: N; COMPND 16 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA, ESCHERICHIA COLI; SOURCE 3 ORGANISM_COMMON: THALE CRESS; SOURCE 4 ORGANISM_TAXID: 3702, 562; SOURCE 5 GENE: AUX1, CYBC; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_TAXID: 9606; SOURCE 11 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 18 MOL_ID: 4; SOURCE 19 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 20 ORGANISM_TAXID: 9844; SOURCE 21 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 22 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS LEUT-FOLD, TRANSPORT, PROTEIN TRANSPORT/IMMUNE SYSTEM, PROTEIN KEYWDS 2 TRANSPORT-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR D.JING,F.KONG,C.C.WANG,Y.G.SHI,G.X.Y.HUANG REVDAT 1 23-JUL-25 9LVB 0 JRNL AUTH D.JING,F.KONG JRNL TITL STRUCTURAL BASIS OF AUXIN BINDING AND TRANSPORT BY JRNL TITL 2 ARABIDOPSIS THALIANA AUX1 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.97 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : PHENIX 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) : 3.970 REMARK 3 NUMBER OF PARTICLES : 175799 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 9LVB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 14-FEB-25. REMARK 100 THE DEPOSITION ID IS D_1300056530. 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 : AUX1 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 : 7.40 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 : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1200.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1600.00 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) : 5000.00 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, L, N 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 -24 REMARK 465 HIS A -23 REMARK 465 HIS A -22 REMARK 465 HIS A -21 REMARK 465 HIS A -20 REMARK 465 HIS A -19 REMARK 465 HIS A -18 REMARK 465 HIS A -17 REMARK 465 HIS A -16 REMARK 465 HIS A -15 REMARK 465 HIS A -14 REMARK 465 GLY A -13 REMARK 465 SER A -12 REMARK 465 VAL A -11 REMARK 465 GLU A -10 REMARK 465 ASP A -9 REMARK 465 TYR A -8 REMARK 465 LYS A -7 REMARK 465 ASP A -6 REMARK 465 ASP A -5 REMARK 465 ASP A -4 REMARK 465 ASP A -3 REMARK 465 LYS A -2 REMARK 465 GLY A -1 REMARK 465 SER A 0 REMARK 465 MET A 1 REMARK 465 SER A 2 REMARK 465 GLU A 3 REMARK 465 GLY A 4 REMARK 465 VAL A 5 REMARK 465 GLU A 6 REMARK 465 ALA A 7 REMARK 465 ILE A 8 REMARK 465 VAL A 9 REMARK 465 ALA A 10 REMARK 465 ASN A 11 REMARK 465 ASP A 12 REMARK 465 ASN A 13 REMARK 465 GLY A 14 REMARK 465 THR A 15 REMARK 465 ASP A 16 REMARK 465 GLN A 17 REMARK 465 VAL A 18 REMARK 465 ASN A 19 REMARK 465 GLY A 20 REMARK 465 ASN A 21 REMARK 465 ARG A 22 REMARK 465 THR A 23 REMARK 465 GLY A 24 REMARK 465 LYS A 25 REMARK 465 ASP A 26 REMARK 465 ASN A 27 REMARK 465 GLU A 28 REMARK 465 GLU A 29 REMARK 465 HIS A 30 REMARK 465 ASP A 31 REMARK 465 GLY A 32 REMARK 465 SER A 33 REMARK 465 THR A 34 REMARK 465 GLY A 35 REMARK 465 SER A 36 REMARK 465 ASN A 37 REMARK 465 LEU A 38 REMARK 465 SER A 39 REMARK 465 ASN A 40 REMARK 465 PHE A 41 REMARK 465 LEU A 42 REMARK 465 TRP A 43 REMARK 465 HIS A 44 REMARK 465 ILE A 361 REMARK 465 MET A 362 REMARK 465 HIS A 363 REMARK 465 ALA A 364 REMARK 465 MET A 365 REMARK 465 TRP A 366 REMARK 465 LYS A 367 REMARK 465 PRO A 368 REMARK 465 GLN A 369 REMARK 465 LYS A 370 REMARK 465 PHE A 371 REMARK 465 LYS A 372 REMARK 465 TYR A 373 REMARK 465 ILE A 374 REMARK 465 TYR A 375 REMARK 465 MET A 449 REMARK 465 HIS A 450 REMARK 465 ASP A 451 REMARK 465 THR A 452 REMARK 465 LYS A 453 REMARK 465 SER A 454 REMARK 465 ILE A 455 REMARK 465 CYS A 456 REMARK 465 LEU A 457 REMARK 465 LYS A 574 REMARK 465 PRO A 575 REMARK 465 ALA A 576 REMARK 465 ALA A 577 REMARK 465 ALA A 578 REMARK 465 ALA A 579 REMARK 465 ALA A 580 REMARK 465 HIS A 581 REMARK 465 ALA A 582 REMARK 465 PRO A 583 REMARK 465 VAL A 584 REMARK 465 SER A 585 REMARK 465 ALA A 586 REMARK 465 LEU A 587 REMARK 465 HIS A 588 REMARK 465 HIS A 589 REMARK 465 ARG A 590 REMARK 465 LEU A 591 REMARK 465 MET H -18 REMARK 465 GLY H -17 REMARK 465 TRP H -16 REMARK 465 SER H -15 REMARK 465 LEU H -14 REMARK 465 ILE H -13 REMARK 465 LEU H -12 REMARK 465 LEU H -11 REMARK 465 PHE H -10 REMARK 465 LEU H -9 REMARK 465 VAL H -8 REMARK 465 ALA H -7 REMARK 465 VAL H -6 REMARK 465 ALA H -5 REMARK 465 THR H -4 REMARK 465 ARG H -3 REMARK 465 VAL H -2 REMARK 465 LEU H -1 REMARK 465 SER H 0 REMARK 465 GLU H 1 REMARK 465 ILE H 2 REMARK 465 SER H 3 REMARK 465 SER H 229 REMARK 465 CYS H 230 REMARK 465 ASP H 231 REMARK 465 LYS H 232 REMARK 465 HIS H 233 REMARK 465 HIS H 234 REMARK 465 HIS H 235 REMARK 465 HIS H 236 REMARK 465 HIS H 237 REMARK 465 HIS H 238 REMARK 465 MET L -18 REMARK 465 GLY L -17 REMARK 465 TRP L -16 REMARK 465 SER L -15 REMARK 465 CYS L -14 REMARK 465 ILE L -13 REMARK 465 ILE L -12 REMARK 465 LEU L -11 REMARK 465 PHE L -10 REMARK 465 LEU L -9 REMARK 465 VAL L -8 REMARK 465 ALA L -7 REMARK 465 THR L -6 REMARK 465 ALA L -5 REMARK 465 THR L -4 REMARK 465 GLY L -3 REMARK 465 VAL L -2 REMARK 465 HIS L -1 REMARK 465 SER L 0 REMARK 465 SER L 1 REMARK 465 GLY L 214 REMARK 465 GLU L 215 REMARK 465 CYS L 216 REMARK 465 MET N -33 REMARK 465 ASP N -32 REMARK 465 MET N -31 REMARK 465 ARG N -30 REMARK 465 VAL N -29 REMARK 465 PRO N -28 REMARK 465 ALA N -27 REMARK 465 GLN N -26 REMARK 465 LEU N -25 REMARK 465 LEU N -24 REMARK 465 GLY N -23 REMARK 465 LEU N -22 REMARK 465 LEU N -21 REMARK 465 LEU N -20 REMARK 465 LEU N -19 REMARK 465 TRP N -18 REMARK 465 LEU N -17 REMARK 465 SER N -16 REMARK 465 GLY N -15 REMARK 465 ALA N -14 REMARK 465 ARG N -13 REMARK 465 CYS N -12 REMARK 465 MET N -11 REMARK 465 ASP N -10 REMARK 465 TYR N -9 REMARK 465 LYS N -8 REMARK 465 ASP N -7 REMARK 465 ASP N -6 REMARK 465 ASP N -5 REMARK 465 ASP N -4 REMARK 465 LYS N -3 REMARK 465 GLY N -2 REMARK 465 GLY N -1 REMARK 465 SER N 0 REMARK 465 VAL N 119 REMARK 465 SER N 120 REMARK 465 SER N 121 REMARK 465 LEU N 122 REMARK 465 GLU N 123 REMARK 465 HIS N 124 REMARK 465 HIS N 125 REMARK 465 HIS N 126 REMARK 465 HIS N 127 REMARK 465 HIS N 128 REMARK 465 HIS N 129 REMARK 465 GLY N 130 REMARK 465 SER N 131 REMARK 465 ASP N 132 REMARK 465 TYR N 133 REMARK 465 LYS N 134 REMARK 465 ASP N 135 REMARK 465 ASP N 136 REMARK 465 ASP N 137 REMARK 465 ASP N 138 REMARK 465 LYS N 139 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 ARG N 52 CG CD NE CZ NH1 NH2 REMARK 470 ARG N 67 CG CD NE CZ NH1 NH2 REMARK 470 ARG N 72 CG CD NE CZ NH1 NH2 REMARK 470 TYR N 104 CG CD1 CD2 CE1 CE2 CZ OH 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 L 78 OE1 GLN L 80 2.06 REMARK 500 O LYS A 276 OG1 THR A 280 2.13 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 116 10.79 81.82 REMARK 500 LEU A 236 -60.71 -91.90 REMARK 500 ASN A 266 -60.10 -93.45 REMARK 500 LEU A 460 0.24 -69.82 REMARK 500 LEU A 490 -60.34 -90.91 REMARK 500 SER H 60 43.57 -145.61 REMARK 500 THR H 94 109.95 -56.61 REMARK 500 SER L 32 -125.40 47.44 REMARK 500 ALA L 52 -12.85 75.33 REMARK 500 LEU L 97 17.80 -140.05 REMARK 500 SER L 176 116.13 -160.52 REMARK 500 ALA N 92 -176.07 -172.27 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-63418 RELATED DB: EMDB REMARK 900 IAA-FREE AUX1 DBREF 9LVB A 1 116 UNP Q96247 AUX1_ARATH 1 116 DBREF 9LVB A 117 221 UNP P0ABE7 C562_ECOLX 23 127 DBREF 9LVB A 223 591 UNP Q96247 AUX1_ARATH 117 485 DBREF 9LVB H -18 238 PDB 9LVB 9LVB -18 238 DBREF 9LVB L -18 216 PDB 9LVB 9LVB -18 216 DBREF 9LVB N -33 139 PDB 9LVB 9LVB -33 139 SEQADV 9LVB MET A -24 UNP Q96247 INITIATING METHIONINE SEQADV 9LVB HIS A -23 UNP Q96247 EXPRESSION TAG SEQADV 9LVB HIS A -22 UNP Q96247 EXPRESSION TAG SEQADV 9LVB HIS A -21 UNP Q96247 EXPRESSION TAG SEQADV 9LVB HIS A -20 UNP Q96247 EXPRESSION TAG SEQADV 9LVB HIS A -19 UNP Q96247 EXPRESSION TAG SEQADV 9LVB HIS A -18 UNP Q96247 EXPRESSION TAG SEQADV 9LVB HIS A -17 UNP Q96247 EXPRESSION TAG SEQADV 9LVB HIS A -16 UNP Q96247 EXPRESSION TAG SEQADV 9LVB HIS A -15 UNP Q96247 EXPRESSION TAG SEQADV 9LVB HIS A -14 UNP Q96247 EXPRESSION TAG SEQADV 9LVB GLY A -13 UNP Q96247 EXPRESSION TAG SEQADV 9LVB SER A -12 UNP Q96247 EXPRESSION TAG SEQADV 9LVB VAL A -11 UNP Q96247 EXPRESSION TAG SEQADV 9LVB GLU A -10 UNP Q96247 EXPRESSION TAG SEQADV 9LVB ASP A -9 UNP Q96247 EXPRESSION TAG SEQADV 9LVB TYR A -8 UNP Q96247 EXPRESSION TAG SEQADV 9LVB LYS A -7 UNP Q96247 EXPRESSION TAG SEQADV 9LVB ASP A -6 UNP Q96247 EXPRESSION TAG SEQADV 9LVB ASP A -5 UNP Q96247 EXPRESSION TAG SEQADV 9LVB ASP A -4 UNP Q96247 EXPRESSION TAG SEQADV 9LVB ASP A -3 UNP Q96247 EXPRESSION TAG SEQADV 9LVB LYS A -2 UNP Q96247 EXPRESSION TAG SEQADV 9LVB GLY A -1 UNP Q96247 EXPRESSION TAG SEQADV 9LVB SER A 0 UNP Q96247 EXPRESSION TAG SEQADV 9LVB TRP A 123 UNP P0ABE7 MET 29 CONFLICT SEQADV 9LVB ILE A 218 UNP P0ABE7 HIS 124 CONFLICT SEQADV 9LVB LEU A 222 UNP P0ABE7 LINKER SEQRES 1 A 616 MET HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS GLY SER SEQRES 2 A 616 VAL GLU ASP TYR LYS ASP ASP ASP ASP LYS GLY SER MET SEQRES 3 A 616 SER GLU GLY VAL GLU ALA ILE VAL ALA ASN ASP ASN GLY SEQRES 4 A 616 THR ASP GLN VAL ASN GLY ASN ARG THR GLY LYS ASP ASN SEQRES 5 A 616 GLU GLU HIS ASP GLY SER THR GLY SER ASN LEU SER ASN SEQRES 6 A 616 PHE LEU TRP HIS GLY GLY SER VAL TRP ASP ALA TRP PHE SEQRES 7 A 616 SER CYS ALA SER ASN GLN VAL ALA GLN VAL LEU LEU THR SEQRES 8 A 616 LEU PRO TYR SER PHE SER GLN LEU GLY MET LEU SER GLY SEQRES 9 A 616 ILE VAL LEU GLN ILE PHE TYR GLY LEU LEU GLY SER TRP SEQRES 10 A 616 THR ALA TYR LEU ILE SER VAL LEU TYR VAL GLU TYR ARG SEQRES 11 A 616 ALA ARG LYS GLU LYS GLU GLY LYS SER PHE LYS ALA ASP SEQRES 12 A 616 LEU GLU ASP ASN TRP GLU THR LEU ASN ASP ASN LEU LYS SEQRES 13 A 616 VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS ASP SEQRES 14 A 616 ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP ALA GLN SEQRES 15 A 616 LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER PRO ASP SEQRES 16 A 616 SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE ASP ILE SEQRES 17 A 616 LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN SEQRES 18 A 616 GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN SEQRES 19 A 616 LEU LYS THR THR ARG ASN ALA TYR ILE GLN LYS TYR LEU SEQRES 20 A 616 ASN HIS VAL ILE GLN TRP PHE GLU VAL LEU ASP GLY LEU SEQRES 21 A 616 LEU GLY SER TYR TRP LYS ALA LEU GLY LEU ALA PHE ASN SEQRES 22 A 616 CYS THR PHE LEU LEU PHE GLY SER VAL ILE GLN LEU ILE SEQRES 23 A 616 ALA CYS ALA SER ASN ILE TYR TYR ILE ASN ASP HIS LEU SEQRES 24 A 616 ASP LYS ARG THR TRP THR TYR ILE PHE GLY ALA CYS CYS SEQRES 25 A 616 ALA THR THR VAL PHE ILE PRO SER PHE HIS ASN TYR ARG SEQRES 26 A 616 ILE TRP SER PHE LEU GLY LEU GLY MET THR THR TYR THR SEQRES 27 A 616 ALA TRP TYR LEU ALA ILE ALA SER ILE ILE HIS GLY GLN SEQRES 28 A 616 ALA GLU GLY VAL LYS HIS SER GLY PRO THR LYS LEU VAL SEQRES 29 A 616 LEU TYR PHE THR GLY ALA THR ASN ILE LEU TYR THR PHE SEQRES 30 A 616 GLY GLY HIS ALA VAL THR VAL GLU ILE MET HIS ALA MET SEQRES 31 A 616 TRP LYS PRO GLN LYS PHE LYS TYR ILE TYR LEU MET ALA SEQRES 32 A 616 THR LEU TYR VAL PHE THR LEU THR ILE PRO SER ALA ALA SEQRES 33 A 616 ALA VAL TYR TRP ALA PHE GLY ASP ALA LEU LEU ASP HIS SEQRES 34 A 616 SER ASN ALA PHE SER LEU MET PRO LYS ASN ALA TRP ARG SEQRES 35 A 616 ASP ALA ALA VAL ILE LEU MET LEU ILE HIS GLN PHE ILE SEQRES 36 A 616 THR PHE GLY PHE ALA CYS THR PRO LEU TYR PHE VAL TRP SEQRES 37 A 616 GLU LYS VAL ILE GLY MET HIS ASP THR LYS SER ILE CYS SEQRES 38 A 616 LEU ARG ALA LEU ALA ARG LEU PRO VAL VAL ILE PRO ILE SEQRES 39 A 616 TRP PHE LEU ALA ILE ILE PHE PRO PHE PHE GLY PRO ILE SEQRES 40 A 616 ASN SER ALA VAL GLY ALA LEU LEU VAL SER PHE THR VAL SEQRES 41 A 616 TYR ILE ILE PRO SER LEU ALA HIS MET LEU THR TYR ARG SEQRES 42 A 616 SER ALA SER ALA ARG GLN ASN ALA ALA GLU LYS PRO PRO SEQRES 43 A 616 PHE PHE MET PRO SER TRP THR ALA MET TYR VAL LEU ASN SEQRES 44 A 616 ALA PHE VAL VAL VAL TRP VAL LEU ILE VAL GLY PHE GLY SEQRES 45 A 616 PHE GLY GLY TRP ALA SER VAL THR ASN PHE VAL ARG GLN SEQRES 46 A 616 VAL ASP THR PHE GLY LEU PHE ALA LYS CYS TYR GLN CYS SEQRES 47 A 616 LYS PRO ALA ALA ALA ALA ALA HIS ALA PRO VAL SER ALA SEQRES 48 A 616 LEU HIS HIS ARG LEU SEQRES 1 H 257 MET GLY TRP SER LEU ILE LEU LEU PHE LEU VAL ALA VAL SEQRES 2 H 257 ALA THR ARG VAL LEU SER GLU ILE SER GLU VAL GLN LEU SEQRES 3 H 257 VAL GLU SER GLY GLY GLY LEU VAL GLN PRO GLY GLY SER SEQRES 4 H 257 LEU ARG LEU SER CYS ALA ALA SER GLY PHE ASN VAL VAL SEQRES 5 H 257 ASP PHE SER LEU HIS TRP VAL ARG GLN ALA PRO GLY LYS SEQRES 6 H 257 GLY LEU GLU TRP VAL ALA TYR ILE SER SER SER SER GLY SEQRES 7 H 257 SER THR SER TYR ALA ASP SER VAL LYS GLY ARG PHE THR SEQRES 8 H 257 ILE SER ALA ASP THR SER LYS ASN THR ALA TYR LEU GLN SEQRES 9 H 257 MET ASN SER LEU ARG ALA GLU ASP THR ALA VAL TYR TYR SEQRES 10 H 257 CYS ALA ARG TRP GLY TYR TRP PRO GLY GLU PRO TRP TRP SEQRES 11 H 257 LYS ALA PHE ASP TYR TRP GLY GLN GLY THR LEU VAL THR SEQRES 12 H 257 VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO SEQRES 13 H 257 LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA SEQRES 14 H 257 ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO SEQRES 15 H 257 VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY SEQRES 16 H 257 VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU SEQRES 17 H 257 TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER SEQRES 18 H 257 LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS SEQRES 19 H 257 PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SEQRES 20 H 257 SER CYS ASP LYS HIS HIS HIS HIS HIS HIS SEQRES 1 L 235 MET GLY TRP SER CYS ILE ILE LEU PHE LEU VAL ALA THR SEQRES 2 L 235 ALA THR GLY VAL HIS SER SER ASP ILE GLN MET THR GLN SEQRES 3 L 235 SER PRO SER SER LEU SER ALA SER VAL GLY ASP ARG VAL SEQRES 4 L 235 THR ILE THR CYS ARG ALA SER GLN SER VAL SER SER ALA SEQRES 5 L 235 VAL ALA TRP TYR GLN GLN LYS PRO GLY LYS ALA PRO LYS SEQRES 6 L 235 LEU LEU ILE TYR SER ALA SER SER LEU TYR SER GLY VAL SEQRES 7 L 235 PRO SER ARG PHE SER GLY SER ARG SER GLY THR ASP PHE SEQRES 8 L 235 THR LEU THR ILE SER SER LEU GLN PRO GLU ASP PHE ALA SEQRES 9 L 235 THR TYR TYR CYS GLN GLN TYR LEU TYR TYR SER LEU VAL SEQRES 10 L 235 THR PHE GLY GLN GLY THR LYS VAL GLU ILE LYS ARG THR SEQRES 11 L 235 VAL ALA ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP SEQRES 12 L 235 SER GLN LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU SEQRES 13 L 235 LEU ASN ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP SEQRES 14 L 235 LYS VAL ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SEQRES 15 L 235 SER VAL THR GLU GLN ASP SER LYS ASP SER THR TYR SER SEQRES 16 L 235 LEU SER SER THR LEU THR LEU SER LYS ALA ASP TYR GLU SEQRES 17 L 235 LYS HIS LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY SEQRES 18 L 235 LEU SER SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU SEQRES 19 L 235 CYS SEQRES 1 N 173 MET ASP MET ARG VAL PRO ALA GLN LEU LEU GLY LEU LEU SEQRES 2 N 173 LEU LEU TRP LEU SER GLY ALA ARG CYS MET ASP TYR LYS SEQRES 3 N 173 ASP ASP ASP ASP LYS GLY GLY SER GLN VAL GLN LEU GLN SEQRES 4 N 173 GLU SER GLY GLY GLY LEU VAL GLN PRO GLY GLY SER LEU SEQRES 5 N 173 ARG LEU SER CYS ALA ALA SER GLY ARG THR ILE SER ARG SEQRES 6 N 173 TYR ALA MET SER TRP PHE ARG GLN ALA PRO GLY LYS GLU SEQRES 7 N 173 ARG GLU PHE VAL ALA VAL ALA ARG ARG SER GLY ASP GLY SEQRES 8 N 173 ALA PHE TYR ALA ASP SER VAL GLN GLY ARG PHE THR VAL SEQRES 9 N 173 SER ARG ASP ASP ALA LYS ASN THR VAL TYR LEU GLN MET SEQRES 10 N 173 ASN SER LEU LYS PRO GLU ASP THR ALA VAL TYR TYR CYS SEQRES 11 N 173 ALA ILE ASP SER ASP THR PHE TYR SER GLY SER TYR ASP SEQRES 12 N 173 TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER LEU SEQRES 13 N 173 GLU HIS HIS HIS HIS HIS HIS GLY SER ASP TYR LYS ASP SEQRES 14 N 173 ASP ASP ASP LYS HELIX 1 AA1 VAL A 48 GLY A 75 1 28 HELIX 2 AA2 GLY A 75 GLY A 112 1 38 HELIX 3 AA3 LYS A 116 ALA A 136 1 21 HELIX 4 AA4 ASN A 138 LYS A 158 1 21 HELIX 5 AA5 SER A 171 GLU A 197 1 27 HELIX 6 AA6 LYS A 199 LEU A 222 1 24 HELIX 7 AA7 GLN A 227 GLY A 234 1 8 HELIX 8 AA8 GLY A 237 TYR A 268 1 32 HELIX 9 AA9 ASP A 275 THR A 290 1 16 HELIX 10 AB1 TYR A 299 ILE A 323 1 25 HELIX 11 AB2 VAL A 339 TYR A 350 1 12 HELIX 12 AB3 GLY A 353 THR A 358 1 6 HELIX 13 AB4 MET A 377 GLY A 398 1 22 HELIX 14 AB5 ASP A 399 LEU A 402 5 4 HELIX 15 AB6 ALA A 407 MET A 411 5 5 HELIX 16 AB7 ASN A 414 GLY A 448 1 35 HELIX 17 AB8 ARG A 462 PRO A 464 5 3 HELIX 18 AB9 VAL A 465 ILE A 474 1 10 HELIX 19 AC1 GLY A 480 LEU A 490 1 11 HELIX 20 AC2 LEU A 490 VAL A 495 1 6 HELIX 21 AC3 TYR A 496 TYR A 507 1 12 HELIX 22 AC4 ARG A 508 SER A 509 5 2 HELIX 23 AC5 ALA A 510 ASN A 515 5 6 HELIX 24 AC6 ALA A 529 GLY A 565 1 37 HELIX 25 AC7 ASP H 65 LYS H 68 5 4 HELIX 26 AC8 ARG H 90 THR H 94 5 5 HELIX 27 AC9 GLY H 107 LYS H 112 1 6 HELIX 28 AD1 PRO H 199 LEU H 203 5 5 HELIX 29 AD2 GLN L 80 PHE L 84 5 5 HELIX 30 AD3 SER L 123 GLY L 130 1 8 HELIX 31 AD4 ALA L 186 LYS L 190 5 5 HELIX 32 AD5 LYS N 87 THR N 91 5 5 SHEET 1 AA1 3 VAL H 8 SER H 10 0 SHEET 2 AA1 3 SER H 24 ALA H 26 -1 O ALA H 26 N VAL H 8 SHEET 3 AA1 3 THR H 81 ALA H 82 -1 O ALA H 82 N CYS H 25 SHEET 1 AA2 2 LEU H 14 VAL H 15 0 SHEET 2 AA2 2 THR H 124 VAL H 125 1 O THR H 124 N VAL H 15 SHEET 1 AA3 2 SER H 20 ARG H 22 0 SHEET 2 AA3 2 GLN H 85 ASN H 87 -1 O MET H 86 N LEU H 21 SHEET 1 AA4 4 SER H 62 TYR H 63 0 SHEET 2 AA4 4 LEU H 48 SER H 55 -1 N TYR H 53 O SER H 62 SHEET 3 AA4 4 SER H 36 GLN H 42 -1 N ARG H 41 O GLU H 49 SHEET 4 AA4 4 VAL H 96 ALA H 100 -1 O TYR H 98 N VAL H 40 SHEET 1 AA5 4 SER H 134 LEU H 138 0 SHEET 2 AA5 4 ALA H 150 TYR H 159 -1 O LEU H 155 N PHE H 136 SHEET 3 AA5 4 TYR H 190 VAL H 198 -1 O LEU H 192 N VAL H 156 SHEET 4 AA5 4 HIS H 178 THR H 179 -1 N HIS H 178 O VAL H 195 SHEET 1 AA6 4 SER H 134 LEU H 138 0 SHEET 2 AA6 4 ALA H 150 TYR H 159 -1 O LEU H 155 N PHE H 136 SHEET 3 AA6 4 TYR H 190 VAL H 198 -1 O LEU H 192 N VAL H 156 SHEET 4 AA6 4 VAL H 183 LEU H 184 -1 N VAL H 183 O SER H 191 SHEET 1 AA7 3 VAL H 164 TRP H 168 0 SHEET 2 AA7 3 TYR H 208 HIS H 214 -1 O ASN H 213 N THR H 165 SHEET 3 AA7 3 VAL H 221 VAL H 225 -1 O LYS H 223 N CYS H 210 SHEET 1 AA8 4 MET L 5 THR L 6 0 SHEET 2 AA8 4 VAL L 20 ALA L 26 -1 O ARG L 25 N THR L 6 SHEET 3 AA8 4 ASP L 71 ILE L 76 -1 O PHE L 72 N CYS L 24 SHEET 4 AA8 4 PHE L 63 SER L 68 -1 N SER L 68 O ASP L 71 SHEET 1 AA9 4 LEU L 47 TYR L 50 0 SHEET 2 AA9 4 VAL L 34 GLN L 39 -1 N TRP L 36 O LEU L 48 SHEET 3 AA9 4 THR L 86 GLN L 91 -1 O GLN L 90 N ALA L 35 SHEET 4 AA9 4 THR L 99 PHE L 100 -1 O THR L 99 N GLN L 91 SHEET 1 AB1 4 SER L 116 PHE L 120 0 SHEET 2 AB1 4 THR L 131 PHE L 141 -1 O LEU L 137 N PHE L 118 SHEET 3 AB1 4 TYR L 175 SER L 184 -1 O LEU L 177 N LEU L 138 SHEET 4 AB1 4 SER L 161 GLN L 162 -1 N GLN L 162 O THR L 180 SHEET 1 AB2 2 ALA L 146 VAL L 148 0 SHEET 2 AB2 2 VAL L 198 HIS L 200 -1 O THR L 199 N LYS L 147 SHEET 1 AB3 2 LYS L 151 VAL L 152 0 SHEET 2 AB3 2 TYR L 194 ALA L 195 -1 O ALA L 195 N LYS L 151 SHEET 1 AB4 4 GLN N 5 SER N 7 0 SHEET 2 AB4 4 SER N 21 ALA N 23 -1 O ALA N 23 N GLN N 5 SHEET 3 AB4 4 THR N 78 GLN N 82 -1 O VAL N 79 N CYS N 22 SHEET 4 AB4 4 THR N 69 SER N 71 -1 N SER N 71 O TYR N 80 SHEET 1 AB5 4 GLU N 46 ALA N 51 0 SHEET 2 AB5 4 MET N 34 GLN N 39 -1 N ARG N 38 O GLU N 46 SHEET 3 AB5 4 ALA N 92 ASP N 99 -1 O ALA N 97 N SER N 35 SHEET 4 AB5 4 TYR N 108 TRP N 111 -1 O TYR N 110 N ILE N 98 SHEET 1 AB6 4 GLU N 46 ALA N 51 0 SHEET 2 AB6 4 MET N 34 GLN N 39 -1 N ARG N 38 O GLU N 46 SHEET 3 AB6 4 ALA N 92 ASP N 99 -1 O ALA N 97 N SER N 35 SHEET 4 AB6 4 GLN N 116 VAL N 117 -1 O VAL N 117 N ALA N 92 SSBOND 1 CYS A 570 CYS A 573 1555 1555 2.03 SSBOND 2 CYS H 25 CYS H 99 1555 1555 2.03 SSBOND 3 CYS H 154 CYS H 210 1555 1555 2.03 SSBOND 4 CYS L 24 CYS L 89 1555 1555 2.03 SSBOND 5 CYS L 136 CYS L 196 1555 1555 2.04 SSBOND 6 CYS N 22 CYS N 96 1555 1555 2.03 CISPEP 1 GLY A 334 PRO A 335 0 9.24 CISPEP 2 TRP H 105 PRO H 106 0 -28.88 CISPEP 3 PHE H 160 PRO H 161 0 -4.18 CISPEP 4 TYR L 142 PRO L 143 0 -4.25 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