HEADER TRANSPORT PROTEIN 11-APR-25 9QUW TITLE CRYO-EM STRUCTURE OF THE HUMAN NHA2-FAB COMPLEX BOUND TO PHLORETIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB LIGHT CHAIN; COMPND 3 CHAIN: E, C; COMPND 4 MOL_ID: 2; COMPND 5 MOLECULE: FAB HEAVY CHAIN; COMPND 6 CHAIN: D, F; COMPND 7 MOL_ID: 3; COMPND 8 MOLECULE: SODIUM/HYDROGEN EXCHANGER 9B2; COMPND 9 CHAIN: A, B; COMPND 10 SYNONYM: NA(+)/H(+) EXCHANGER NHA2,NA(+)/H(+) EXCHANGER-LIKE DOMAIN- COMPND 11 CONTAINING PROTEIN 2,NHE DOMAIN-CONTAINING PROTEIN 2,SODIUM/HYDROGEN COMPND 12 EXCHANGER-LIKE DOMAIN-CONTAINING PROTEIN 2,SOLUTE CARRIER FAMILY 9 COMPND 13 SUBFAMILY B MEMBER 2; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 MOL_ID: 2; SOURCE 5 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 6 ORGANISM_TAXID: 10090; SOURCE 7 MOL_ID: 3; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_COMMON: HUMAN; SOURCE 10 ORGANISM_TAXID: 9606; SOURCE 11 GENE: SLC9B2, NHA2, NHEDC2; SOURCE 12 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 4932 KEYWDS NA+/H+ EXCHANGER, TRANSPORT PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR S.JUNG,D.DREW REVDAT 1 14-MAY-25 9QUW 0 JRNL AUTH S.JUNG,S.KOKANE,H.LI,S.IWATA,N.NOMURA,D.DREW JRNL TITL STRUCTURE AND INHIBITION OF THE HUMAN NA+/H+ EXCHANGER JRNL TITL 2 SLC9B2 JRNL REF INT J MOL SCI 2025 JRNL REFN ESSN 1422-0067 JRNL DOI 10.3390/IJMS26094221 REMARK 2 REMARK 2 RESOLUTION. 2.90 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) : 2.900 REMARK 3 NUMBER OF PARTICLES : 251355 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 9QUW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-APR-25. REMARK 100 THE DEPOSITION ID IS D_1292147069. 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 : PHLORETIN-BOUND COMPLEX OF REMARK 245 HUMAN NHA2 WITH FAB 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 : 7.50 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 BIOQUANTUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 400.00 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 : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 6570.00 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: HEXAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, D, F, 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 THR E 197 REMARK 465 HIS E 198 REMARK 465 LYS E 199 REMARK 465 THR E 200 REMARK 465 SER E 201 REMARK 465 THR E 202 REMARK 465 SER E 203 REMARK 465 PRO E 204 REMARK 465 ILE E 205 REMARK 465 VAL E 206 REMARK 465 LYS E 207 REMARK 465 SER E 208 REMARK 465 PHE E 209 REMARK 465 ASN E 210 REMARK 465 ARG E 211 REMARK 465 ASN E 212 REMARK 465 GLU E 213 REMARK 465 CYS E 214 REMARK 465 VAL D 135 REMARK 465 CYS D 136 REMARK 465 GLY D 137 REMARK 465 ASP D 138 REMARK 465 THR D 139 REMARK 465 SER D 140 REMARK 465 GLY D 141 REMARK 465 SER D 142 REMARK 465 SER D 143 REMARK 465 THR D 192 REMARK 465 SER D 193 REMARK 465 SER D 194 REMARK 465 THR D 195 REMARK 465 TRP D 196 REMARK 465 GLY D 222 REMARK 465 PRO D 223 REMARK 465 THR D 224 REMARK 465 ILE D 225 REMARK 465 LYS D 226 REMARK 465 PRO D 227 REMARK 465 CYS D 228 REMARK 465 PRO D 229 REMARK 465 PRO D 230 REMARK 465 CYS D 231 REMARK 465 LYS D 232 REMARK 465 CYS D 233 REMARK 465 PRO D 234 REMARK 465 ALA D 235 REMARK 465 PRO D 236 REMARK 465 ASN D 237 REMARK 465 LEU D 238 REMARK 465 LEU D 239 REMARK 465 GLY D 240 REMARK 465 GLY D 241 REMARK 465 PRO D 242 REMARK 465 SER D 243 REMARK 465 VAL D 244 REMARK 465 PHE D 245 REMARK 465 ILE D 246 REMARK 465 PHE D 247 REMARK 465 PRO D 248 REMARK 465 PRO D 249 REMARK 465 LYS D 250 REMARK 465 ILE D 251 REMARK 465 LYS D 252 REMARK 465 ASP D 253 REMARK 465 VAL D 254 REMARK 465 LEU D 255 REMARK 465 MET D 256 REMARK 465 VAL F 135 REMARK 465 CYS F 136 REMARK 465 GLY F 137 REMARK 465 ASP F 138 REMARK 465 THR F 139 REMARK 465 SER F 140 REMARK 465 GLY F 141 REMARK 465 SER F 142 REMARK 465 SER F 143 REMARK 465 THR F 192 REMARK 465 SER F 193 REMARK 465 SER F 194 REMARK 465 THR F 195 REMARK 465 TRP F 196 REMARK 465 GLY F 222 REMARK 465 PRO F 223 REMARK 465 THR F 224 REMARK 465 ILE F 225 REMARK 465 LYS F 226 REMARK 465 PRO F 227 REMARK 465 CYS F 228 REMARK 465 PRO F 229 REMARK 465 PRO F 230 REMARK 465 CYS F 231 REMARK 465 LYS F 232 REMARK 465 CYS F 233 REMARK 465 PRO F 234 REMARK 465 ALA F 235 REMARK 465 PRO F 236 REMARK 465 ASN F 237 REMARK 465 LEU F 238 REMARK 465 LEU F 239 REMARK 465 GLY F 240 REMARK 465 GLY F 241 REMARK 465 PRO F 242 REMARK 465 SER F 243 REMARK 465 VAL F 244 REMARK 465 PHE F 245 REMARK 465 ILE F 246 REMARK 465 PHE F 247 REMARK 465 PRO F 248 REMARK 465 PRO F 249 REMARK 465 LYS F 250 REMARK 465 ILE F 251 REMARK 465 LYS F 252 REMARK 465 ASP F 253 REMARK 465 VAL F 254 REMARK 465 LEU F 255 REMARK 465 MET F 256 REMARK 465 MET A 1 REMARK 465 GLY A 2 REMARK 465 ASP A 3 REMARK 465 GLU A 4 REMARK 465 ASP A 5 REMARK 465 LYS A 6 REMARK 465 ARG A 7 REMARK 465 ILE A 8 REMARK 465 THR A 9 REMARK 465 TYR A 10 REMARK 465 GLU A 11 REMARK 465 ASP A 12 REMARK 465 SER A 13 REMARK 465 GLU A 14 REMARK 465 PRO A 15 REMARK 465 SER A 16 REMARK 465 THR A 17 REMARK 465 GLY A 18 REMARK 465 MET A 19 REMARK 465 ASN A 20 REMARK 465 TYR A 21 REMARK 465 THR A 22 REMARK 465 PRO A 23 REMARK 465 SER A 24 REMARK 465 MET A 25 REMARK 465 HIS A 26 REMARK 465 GLN A 27 REMARK 465 GLU A 28 REMARK 465 ALA A 29 REMARK 465 GLN A 30 REMARK 465 GLU A 31 REMARK 465 GLU A 32 REMARK 465 THR A 33 REMARK 465 VAL A 34 REMARK 465 MET A 35 REMARK 465 LYS A 36 REMARK 465 LEU A 37 REMARK 465 LYS A 38 REMARK 465 GLY A 39 REMARK 465 ILE A 40 REMARK 465 ASP A 41 REMARK 465 ALA A 42 REMARK 465 ASN A 43 REMARK 465 GLU A 44 REMARK 465 PRO A 45 REMARK 465 THR A 46 REMARK 465 GLU A 47 REMARK 465 GLY A 48 REMARK 465 SER A 49 REMARK 465 ILE A 50 REMARK 465 LEU A 51 REMARK 465 LEU A 52 REMARK 465 LYS A 53 REMARK 465 SER A 54 REMARK 465 SER A 55 REMARK 465 GLU A 56 REMARK 465 LYS A 57 REMARK 465 LYS A 58 REMARK 465 LEU A 59 REMARK 465 GLN A 60 REMARK 465 GLU A 61 REMARK 465 THR A 62 REMARK 465 PRO A 63 REMARK 465 THR A 64 REMARK 465 GLU A 65 REMARK 465 ALA A 66 REMARK 465 ASN A 67 REMARK 465 HIS A 68 REMARK 465 VAL A 69 REMARK 465 GLN A 70 REMARK 465 ARG A 71 REMARK 465 LEU A 72 REMARK 465 ARG A 73 REMARK 465 GLN A 74 REMARK 465 MET A 75 REMARK 465 LEU A 76 REMARK 465 ALA A 77 REMARK 465 CYS A 78 REMARK 465 HIS A 522 REMARK 465 GLN A 523 REMARK 465 ASN A 524 REMARK 465 LYS A 525 REMARK 465 ASP A 526 REMARK 465 GLU A 527 REMARK 465 GLU A 528 REMARK 465 VAL A 529 REMARK 465 GLN A 530 REMARK 465 GLY A 531 REMARK 465 GLU A 532 REMARK 465 THR A 533 REMARK 465 SER A 534 REMARK 465 VAL A 535 REMARK 465 GLN A 536 REMARK 465 VAL A 537 REMARK 465 MET B 1 REMARK 465 GLY B 2 REMARK 465 ASP B 3 REMARK 465 GLU B 4 REMARK 465 ASP B 5 REMARK 465 LYS B 6 REMARK 465 ARG B 7 REMARK 465 ILE B 8 REMARK 465 THR B 9 REMARK 465 TYR B 10 REMARK 465 GLU B 11 REMARK 465 ASP B 12 REMARK 465 SER B 13 REMARK 465 GLU B 14 REMARK 465 PRO B 15 REMARK 465 SER B 16 REMARK 465 THR B 17 REMARK 465 GLY B 18 REMARK 465 MET B 19 REMARK 465 ASN B 20 REMARK 465 TYR B 21 REMARK 465 THR B 22 REMARK 465 PRO B 23 REMARK 465 SER B 24 REMARK 465 MET B 25 REMARK 465 HIS B 26 REMARK 465 GLN B 27 REMARK 465 GLU B 28 REMARK 465 ALA B 29 REMARK 465 GLN B 30 REMARK 465 GLU B 31 REMARK 465 GLU B 32 REMARK 465 THR B 33 REMARK 465 VAL B 34 REMARK 465 MET B 35 REMARK 465 LYS B 36 REMARK 465 LEU B 37 REMARK 465 LYS B 38 REMARK 465 GLY B 39 REMARK 465 ILE B 40 REMARK 465 ASP B 41 REMARK 465 ALA B 42 REMARK 465 ASN B 43 REMARK 465 GLU B 44 REMARK 465 PRO B 45 REMARK 465 THR B 46 REMARK 465 GLU B 47 REMARK 465 GLY B 48 REMARK 465 SER B 49 REMARK 465 ILE B 50 REMARK 465 LEU B 51 REMARK 465 LEU B 52 REMARK 465 LYS B 53 REMARK 465 SER B 54 REMARK 465 SER B 55 REMARK 465 GLU B 56 REMARK 465 LYS B 57 REMARK 465 LYS B 58 REMARK 465 LEU B 59 REMARK 465 GLN B 60 REMARK 465 GLU B 61 REMARK 465 THR B 62 REMARK 465 PRO B 63 REMARK 465 THR B 64 REMARK 465 GLU B 65 REMARK 465 ALA B 66 REMARK 465 ASN B 67 REMARK 465 HIS B 68 REMARK 465 VAL B 69 REMARK 465 GLN B 70 REMARK 465 ARG B 71 REMARK 465 LEU B 72 REMARK 465 ARG B 73 REMARK 465 GLN B 74 REMARK 465 MET B 75 REMARK 465 LEU B 76 REMARK 465 ALA B 77 REMARK 465 CYS B 78 REMARK 465 HIS B 522 REMARK 465 GLN B 523 REMARK 465 ASN B 524 REMARK 465 LYS B 525 REMARK 465 ASP B 526 REMARK 465 GLU B 527 REMARK 465 GLU B 528 REMARK 465 VAL B 529 REMARK 465 GLN B 530 REMARK 465 GLY B 531 REMARK 465 GLU B 532 REMARK 465 THR B 533 REMARK 465 SER B 534 REMARK 465 VAL B 535 REMARK 465 GLN B 536 REMARK 465 VAL B 537 REMARK 465 THR C 197 REMARK 465 HIS C 198 REMARK 465 LYS C 199 REMARK 465 THR C 200 REMARK 465 SER C 201 REMARK 465 THR C 202 REMARK 465 SER C 203 REMARK 465 PRO C 204 REMARK 465 ILE C 205 REMARK 465 VAL C 206 REMARK 465 LYS C 207 REMARK 465 SER C 208 REMARK 465 PHE C 209 REMARK 465 ASN C 210 REMARK 465 ARG C 211 REMARK 465 ASN C 212 REMARK 465 GLU C 213 REMARK 465 CYS C 214 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 GLN E 27 -162.91 -161.83 REMARK 500 ASN E 31 10.61 -145.24 REMARK 500 ASN E 34 153.85 -46.68 REMARK 500 THR E 51 -69.57 73.41 REMARK 500 SER E 65 -165.32 -74.78 REMARK 500 ALA E 84 -167.71 -161.76 REMARK 500 PRO E 141 -158.58 -79.60 REMARK 500 ILE D 48 -63.98 -102.04 REMARK 500 PRO D 53 38.96 -82.91 REMARK 500 ASP D 109 -6.12 67.62 REMARK 500 HIS D 207 107.83 -54.33 REMARK 500 ILE F 48 -62.71 -109.68 REMARK 500 PRO F 53 38.83 -82.69 REMARK 500 THR F 87 -169.69 -123.93 REMARK 500 ALA F 107 -155.79 -149.91 REMARK 500 ASP F 109 6.49 54.23 REMARK 500 LYS F 151 -159.35 -93.10 REMARK 500 LEU F 167 0.74 -67.17 REMARK 500 HIS F 207 107.60 -55.18 REMARK 500 CYS A 109 48.82 -93.98 REMARK 500 PRO A 230 -174.99 -68.26 REMARK 500 LEU A 241 48.79 -83.80 REMARK 500 THR A 379 -119.26 55.73 REMARK 500 LEU A 413 50.25 -94.30 REMARK 500 ALA A 461 170.51 179.81 REMARK 500 THR A 462 -4.89 61.16 REMARK 500 CYS B 109 48.87 -94.01 REMARK 500 PRO B 230 -174.99 -68.26 REMARK 500 LEU B 241 48.75 -83.80 REMARK 500 THR B 379 -119.20 55.73 REMARK 500 LEU B 413 50.22 -94.30 REMARK 500 ALA B 461 170.53 179.82 REMARK 500 THR B 462 -4.87 61.13 REMARK 500 GLN C 27 -162.85 -161.81 REMARK 500 ASN C 31 10.51 -145.22 REMARK 500 ASN C 34 153.81 -46.70 REMARK 500 THR C 51 -69.51 73.37 REMARK 500 SER C 65 -165.28 -74.71 REMARK 500 ALA C 84 -167.72 -161.73 REMARK 500 PRO C 141 -158.61 -79.67 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 E 24 0.29 SIDE CHAIN REMARK 500 ARG C 24 0.29 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 9QUB RELATED DB: PDB REMARK 900 HUMAN NHA2 WITH FAB REMARK 900 RELATED ID: EMD-53384 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF THE HUMAN NHA2-FAB COMPLEX BOUND TO PHLORETIN DBREF 9QUW E 1 214 PDB 9QUW 9QUW 1 214 DBREF 9QUW D 1 256 PDB 9QUW 9QUW 1 256 DBREF 9QUW F 1 256 PDB 9QUW 9QUW 1 256 DBREF 9QUW A 1 537 UNP Q86UD5 SL9B2_HUMAN 1 537 DBREF 9QUW B 1 537 UNP Q86UD5 SL9B2_HUMAN 1 537 DBREF 9QUW C 1 214 PDB 9QUW 9QUW 1 214 SEQRES 1 E 214 ASP ILE VAL MET THR GLN THR THR SER SER LEU SER ALA SEQRES 2 E 214 SER LEU GLY ASP ARG VAL THR ILE SER CYS ARG ALA SER SEQRES 3 E 214 GLN ASP ILE SER ASN TYR LEU ASN TRP PHE GLN GLN LYS SEQRES 4 E 214 PRO ASP GLY THR VAL LYS LEU LEU ILE CYS TYR THR SER SEQRES 5 E 214 ARG LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 E 214 GLY SER GLY THR ASP TYR SER LEU THR ILE SER ASN LEU SEQRES 7 E 214 GLU GLN GLU ASP ILE ALA THR TYR PHE CYS GLN GLN ASP SEQRES 8 E 214 SER LYS HIS PRO TRP THR PHE GLY GLY GLY THR LYS LEU SEQRES 9 E 214 GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE SEQRES 10 E 214 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SEQRES 11 E 214 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP SEQRES 12 E 214 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN SEQRES 13 E 214 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS SEQRES 14 E 214 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR SEQRES 15 E 214 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU SEQRES 16 E 214 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER SEQRES 17 E 214 PHE ASN ARG ASN GLU CYS SEQRES 1 D 256 GLU VAL GLN LEU GLN GLU SER GLY PRO GLU LEU VAL LYS SEQRES 2 D 256 PRO GLY ALA SER VAL LYS MET SER CYS LYS ALA SER GLY SEQRES 3 D 256 TYR THR PHE THR ASN TYR PHE ILE HIS TRP VAL LYS GLN SEQRES 4 D 256 LYS PRO GLY GLN GLY LEU GLU TRP ILE GLY TYR ILE ASN SEQRES 5 D 256 PRO TYR ASN ASP ILE THR LYS PHE ASN GLU LYS PHE LYS SEQRES 6 D 256 GLY LYS ALA THR LEU THR SER ASP LYS SER SER ARG THR SEQRES 7 D 256 ALA TYR MET GLU LEU SER SER LEU THR SER GLU ASP SER SEQRES 8 D 256 ALA VAL TYR TYR CYS ALA ARG CYS ASP GLY TYR TYR ARG SEQRES 9 D 256 TYR TYR ALA MET ASP TYR TRP GLY GLN GLY THR SER VAL SEQRES 10 D 256 THR VAL SER SER ALA LYS THR THR ALA PRO SER VAL TYR SEQRES 11 D 256 PRO LEU ALA PRO VAL CYS GLY ASP THR SER GLY SER SER SEQRES 12 D 256 VAL THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU SEQRES 13 D 256 PRO VAL THR LEU THR TRP ASN SER GLY SER LEU SER SER SEQRES 14 D 256 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU SEQRES 15 D 256 TYR THR LEU SER SER SER VAL THR VAL THR SER SER THR SEQRES 16 D 256 TRP PRO SER GLN SER ILE THR CYS ASN VAL ALA HIS PRO SEQRES 17 D 256 ALA SER SER THR LYS VAL ASP LYS LYS ILE GLU PRO ARG SEQRES 18 D 256 GLY PRO THR ILE LYS PRO CYS PRO PRO CYS LYS CYS PRO SEQRES 19 D 256 ALA PRO ASN LEU LEU GLY GLY PRO SER VAL PHE ILE PHE SEQRES 20 D 256 PRO PRO LYS ILE LYS ASP VAL LEU MET SEQRES 1 F 256 GLU VAL GLN LEU GLN GLU SER GLY PRO GLU LEU VAL LYS SEQRES 2 F 256 PRO GLY ALA SER VAL LYS MET SER CYS LYS ALA SER GLY SEQRES 3 F 256 TYR THR PHE THR ASN TYR PHE ILE HIS TRP VAL LYS GLN SEQRES 4 F 256 LYS PRO GLY GLN GLY LEU GLU TRP ILE GLY TYR ILE ASN SEQRES 5 F 256 PRO TYR ASN ASP ILE THR LYS PHE ASN GLU LYS PHE LYS SEQRES 6 F 256 GLY LYS ALA THR LEU THR SER ASP LYS SER SER ARG THR SEQRES 7 F 256 ALA TYR MET GLU LEU SER SER LEU THR SER GLU ASP SER SEQRES 8 F 256 ALA VAL TYR TYR CYS ALA ARG CYS ASP GLY TYR TYR ARG SEQRES 9 F 256 TYR TYR ALA MET ASP TYR TRP GLY GLN GLY THR SER VAL SEQRES 10 F 256 THR VAL SER SER ALA LYS THR THR ALA PRO SER VAL TYR SEQRES 11 F 256 PRO LEU ALA PRO VAL CYS GLY ASP THR SER GLY SER SER SEQRES 12 F 256 VAL THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU SEQRES 13 F 256 PRO VAL THR LEU THR TRP ASN SER GLY SER LEU SER SER SEQRES 14 F 256 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU SEQRES 15 F 256 TYR THR LEU SER SER SER VAL THR VAL THR SER SER THR SEQRES 16 F 256 TRP PRO SER GLN SER ILE THR CYS ASN VAL ALA HIS PRO SEQRES 17 F 256 ALA SER SER THR LYS VAL ASP LYS LYS ILE GLU PRO ARG SEQRES 18 F 256 GLY PRO THR ILE LYS PRO CYS PRO PRO CYS LYS CYS PRO SEQRES 19 F 256 ALA PRO ASN LEU LEU GLY GLY PRO SER VAL PHE ILE PHE SEQRES 20 F 256 PRO PRO LYS ILE LYS ASP VAL LEU MET SEQRES 1 A 537 MET GLY ASP GLU ASP LYS ARG ILE THR TYR GLU ASP SER SEQRES 2 A 537 GLU PRO SER THR GLY MET ASN TYR THR PRO SER MET HIS SEQRES 3 A 537 GLN GLU ALA GLN GLU GLU THR VAL MET LYS LEU LYS GLY SEQRES 4 A 537 ILE ASP ALA ASN GLU PRO THR GLU GLY SER ILE LEU LEU SEQRES 5 A 537 LYS SER SER GLU LYS LYS LEU GLN GLU THR PRO THR GLU SEQRES 6 A 537 ALA ASN HIS VAL GLN ARG LEU ARG GLN MET LEU ALA CYS SEQRES 7 A 537 PRO PRO HIS GLY LEU LEU ASP ARG VAL ILE THR ASN VAL SEQRES 8 A 537 THR ILE ILE VAL LEU LEU TRP ALA VAL VAL TRP SER ILE SEQRES 9 A 537 THR GLY SER GLU CYS LEU PRO GLY GLY ASN LEU PHE GLY SEQRES 10 A 537 ILE ILE ILE LEU PHE TYR CYS ALA ILE ILE GLY GLY LYS SEQRES 11 A 537 LEU LEU GLY LEU ILE LYS LEU PRO THR LEU PRO PRO LEU SEQRES 12 A 537 PRO SER LEU LEU GLY MET LEU LEU ALA GLY PHE LEU ILE SEQRES 13 A 537 ARG ASN ILE PRO VAL ILE ASN ASP ASN VAL GLN ILE LYS SEQRES 14 A 537 HIS LYS TRP SER SER SER LEU ARG SER ILE ALA LEU SER SEQRES 15 A 537 ILE ILE LEU VAL ARG ALA GLY LEU GLY LEU ASP SER LYS SEQRES 16 A 537 ALA LEU LYS LYS LEU LYS GLY VAL CYS VAL ARG LEU SER SEQRES 17 A 537 MET GLY PRO CYS ILE VAL GLU ALA CYS THR SER ALA LEU SEQRES 18 A 537 LEU ALA HIS TYR LEU LEU GLY LEU PRO TRP GLN TRP GLY SEQRES 19 A 537 PHE ILE LEU GLY PHE VAL LEU GLY ALA VAL SER PRO ALA SEQRES 20 A 537 VAL VAL VAL PRO SER MET LEU LEU LEU GLN GLY GLY GLY SEQRES 21 A 537 TYR GLY VAL GLU LYS GLY VAL PRO THR LEU LEU MET ALA SEQRES 22 A 537 ALA GLY SER PHE ASP ASP ILE LEU ALA ILE THR GLY PHE SEQRES 23 A 537 ASN THR CYS LEU GLY ILE ALA PHE SER THR GLY SER THR SEQRES 24 A 537 VAL PHE ASN VAL LEU ARG GLY VAL LEU GLU VAL VAL ILE SEQRES 25 A 537 GLY VAL ALA THR GLY SER VAL LEU GLY PHE PHE ILE GLN SEQRES 26 A 537 TYR PHE PRO SER ARG ASP GLN ASP LYS LEU VAL CYS LYS SEQRES 27 A 537 ARG THR PHE LEU VAL LEU GLY LEU SER VAL LEU ALA VAL SEQRES 28 A 537 PHE SER SER VAL HIS PHE GLY PHE PRO GLY SER GLY GLY SEQRES 29 A 537 LEU CYS THR LEU VAL MET ALA PHE LEU ALA GLY MET GLY SEQRES 30 A 537 TRP THR SER GLU LYS ALA GLU VAL GLU LYS ILE ILE ALA SEQRES 31 A 537 VAL ALA TRP ASP ILE PHE GLN PRO LEU LEU PHE GLY LEU SEQRES 32 A 537 ILE GLY ALA GLU VAL SER ILE ALA SER LEU ARG PRO GLU SEQRES 33 A 537 THR VAL GLY LEU CYS VAL ALA THR VAL GLY ILE ALA VAL SEQRES 34 A 537 LEU ILE ARG ILE LEU THR THR PHE LEU MET VAL CYS PHE SEQRES 35 A 537 ALA GLY PHE ASN LEU LYS GLU LYS ILE PHE ILE SER PHE SEQRES 36 A 537 ALA TRP LEU PRO LYS ALA THR VAL GLN ALA ALA ILE GLY SEQRES 37 A 537 SER VAL ALA LEU ASP THR ALA ARG SER HIS GLY GLU LYS SEQRES 38 A 537 GLN LEU GLU ASP TYR GLY MET ASP VAL LEU THR VAL ALA SEQRES 39 A 537 PHE LEU SER ILE LEU ILE THR ALA PRO ILE GLY SER LEU SEQRES 40 A 537 LEU ILE GLY LEU LEU GLY PRO ARG LEU LEU GLN LYS VAL SEQRES 41 A 537 GLU HIS GLN ASN LYS ASP GLU GLU VAL GLN GLY GLU THR SEQRES 42 A 537 SER VAL GLN VAL SEQRES 1 B 537 MET GLY ASP GLU ASP LYS ARG ILE THR TYR GLU ASP SER SEQRES 2 B 537 GLU PRO SER THR GLY MET ASN TYR THR PRO SER MET HIS SEQRES 3 B 537 GLN GLU ALA GLN GLU GLU THR VAL MET LYS LEU LYS GLY SEQRES 4 B 537 ILE ASP ALA ASN GLU PRO THR GLU GLY SER ILE LEU LEU SEQRES 5 B 537 LYS SER SER GLU LYS LYS LEU GLN GLU THR PRO THR GLU SEQRES 6 B 537 ALA ASN HIS VAL GLN ARG LEU ARG GLN MET LEU ALA CYS SEQRES 7 B 537 PRO PRO HIS GLY LEU LEU ASP ARG VAL ILE THR ASN VAL SEQRES 8 B 537 THR ILE ILE VAL LEU LEU TRP ALA VAL VAL TRP SER ILE SEQRES 9 B 537 THR GLY SER GLU CYS LEU PRO GLY GLY ASN LEU PHE GLY SEQRES 10 B 537 ILE ILE ILE LEU PHE TYR CYS ALA ILE ILE GLY GLY LYS SEQRES 11 B 537 LEU LEU GLY LEU ILE LYS LEU PRO THR LEU PRO PRO LEU SEQRES 12 B 537 PRO SER LEU LEU GLY MET LEU LEU ALA GLY PHE LEU ILE SEQRES 13 B 537 ARG ASN ILE PRO VAL ILE ASN ASP ASN VAL GLN ILE LYS SEQRES 14 B 537 HIS LYS TRP SER SER SER LEU ARG SER ILE ALA LEU SER SEQRES 15 B 537 ILE ILE LEU VAL ARG ALA GLY LEU GLY LEU ASP SER LYS SEQRES 16 B 537 ALA LEU LYS LYS LEU LYS GLY VAL CYS VAL ARG LEU SER SEQRES 17 B 537 MET GLY PRO CYS ILE VAL GLU ALA CYS THR SER ALA LEU SEQRES 18 B 537 LEU ALA HIS TYR LEU LEU GLY LEU PRO TRP GLN TRP GLY SEQRES 19 B 537 PHE ILE LEU GLY PHE VAL LEU GLY ALA VAL SER PRO ALA SEQRES 20 B 537 VAL VAL VAL PRO SER MET LEU LEU LEU GLN GLY GLY GLY SEQRES 21 B 537 TYR GLY VAL GLU LYS GLY VAL PRO THR LEU LEU MET ALA SEQRES 22 B 537 ALA GLY SER PHE ASP ASP ILE LEU ALA ILE THR GLY PHE SEQRES 23 B 537 ASN THR CYS LEU GLY ILE ALA PHE SER THR GLY SER THR SEQRES 24 B 537 VAL PHE ASN VAL LEU ARG GLY VAL LEU GLU VAL VAL ILE SEQRES 25 B 537 GLY VAL ALA THR GLY SER VAL LEU GLY PHE PHE ILE GLN SEQRES 26 B 537 TYR PHE PRO SER ARG ASP GLN ASP LYS LEU VAL CYS LYS SEQRES 27 B 537 ARG THR PHE LEU VAL LEU GLY LEU SER VAL LEU ALA VAL SEQRES 28 B 537 PHE SER SER VAL HIS PHE GLY PHE PRO GLY SER GLY GLY SEQRES 29 B 537 LEU CYS THR LEU VAL MET ALA PHE LEU ALA GLY MET GLY SEQRES 30 B 537 TRP THR SER GLU LYS ALA GLU VAL GLU LYS ILE ILE ALA SEQRES 31 B 537 VAL ALA TRP ASP ILE PHE GLN PRO LEU LEU PHE GLY LEU SEQRES 32 B 537 ILE GLY ALA GLU VAL SER ILE ALA SER LEU ARG PRO GLU SEQRES 33 B 537 THR VAL GLY LEU CYS VAL ALA THR VAL GLY ILE ALA VAL SEQRES 34 B 537 LEU ILE ARG ILE LEU THR THR PHE LEU MET VAL CYS PHE SEQRES 35 B 537 ALA GLY PHE ASN LEU LYS GLU LYS ILE PHE ILE SER PHE SEQRES 36 B 537 ALA TRP LEU PRO LYS ALA THR VAL GLN ALA ALA ILE GLY SEQRES 37 B 537 SER VAL ALA LEU ASP THR ALA ARG SER HIS GLY GLU LYS SEQRES 38 B 537 GLN LEU GLU ASP TYR GLY MET ASP VAL LEU THR VAL ALA SEQRES 39 B 537 PHE LEU SER ILE LEU ILE THR ALA PRO ILE GLY SER LEU SEQRES 40 B 537 LEU ILE GLY LEU LEU GLY PRO ARG LEU LEU GLN LYS VAL SEQRES 41 B 537 GLU HIS GLN ASN LYS ASP GLU GLU VAL GLN GLY GLU THR SEQRES 42 B 537 SER VAL GLN VAL SEQRES 1 C 214 ASP ILE VAL MET THR GLN THR THR SER SER LEU SER ALA SEQRES 2 C 214 SER LEU GLY ASP ARG VAL THR ILE SER CYS ARG ALA SER SEQRES 3 C 214 GLN ASP ILE SER ASN TYR LEU ASN TRP PHE GLN GLN LYS SEQRES 4 C 214 PRO ASP GLY THR VAL LYS LEU LEU ILE CYS TYR THR SER SEQRES 5 C 214 ARG LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 C 214 GLY SER GLY THR ASP TYR SER LEU THR ILE SER ASN LEU SEQRES 7 C 214 GLU GLN GLU ASP ILE ALA THR TYR PHE CYS GLN GLN ASP SEQRES 8 C 214 SER LYS HIS PRO TRP THR PHE GLY GLY GLY THR LYS LEU SEQRES 9 C 214 GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE SEQRES 10 C 214 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SEQRES 11 C 214 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP SEQRES 12 C 214 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN SEQRES 13 C 214 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS SEQRES 14 C 214 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR SEQRES 15 C 214 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU SEQRES 16 C 214 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER SEQRES 17 C 214 PHE ASN ARG ASN GLU CYS HET LPP A 601 111 HET G50 A 602 34 HET LPP B 601 111 HET G50 B 602 34 HETNAM LPP 2-(HEXADECANOYLOXY)-1-[(PHOSPHONOOXY)METHYL]ETHYL HETNAM 2 LPP HEXADECANOATE HETNAM G50 3-(4-HYDROXYPHENYL)-1-(2,4,6-TRIHYDROXYPHENYL)PROPAN-1- HETNAM 2 G50 ONE HETSYN LPP 1,2-DIPALMITOYL-SN-GLYCERO-3-PHOSPHATE; L-B,G- HETSYN 2 LPP DIPALMITOYL-A-PHOSPHATIDIC ACID DISODIUM SALT; 3-SN- HETSYN 3 LPP PHOSPHATIDIC ACID; 1,2-DIPALMITOYLDISODIUM SALT FORMUL 7 LPP 2(C35 H69 O8 P) FORMUL 8 G50 2(C15 H14 O5) HELIX 1 AA1 GLU E 79 ILE E 83 5 5 HELIX 2 AA2 SER E 121 GLY E 128 1 8 HELIX 3 AA3 ILE E 150 SER E 153 5 4 HELIX 4 AA4 THR E 182 ARG E 188 1 7 HELIX 5 AA5 THR D 28 TYR D 32 5 5 HELIX 6 AA6 GLU D 62 LYS D 65 5 4 HELIX 7 AA7 THR D 87 SER D 91 5 5 HELIX 8 AA8 GLY D 165 SER D 169 5 5 HELIX 9 AA9 THR F 28 TYR F 32 5 5 HELIX 10 AB1 GLU F 62 LYS F 65 5 4 HELIX 11 AB2 THR F 87 SER F 91 5 5 HELIX 12 AB3 GLY F 165 SER F 169 5 5 HELIX 13 AB4 GLY A 82 GLY A 106 1 25 HELIX 14 AB5 GLY A 113 ILE A 135 1 23 HELIX 15 AB6 PRO A 144 ILE A 159 1 16 HELIX 16 AB7 ILE A 159 VAL A 166 1 8 HELIX 17 AB8 LYS A 169 LEU A 192 1 24 HELIX 18 AB9 ASP A 193 LEU A 200 1 8 HELIX 19 AC1 LYS A 201 LEU A 226 1 26 HELIX 20 AC2 PRO A 230 LEU A 241 1 12 HELIX 21 AC3 SER A 245 GLY A 260 1 16 HELIX 22 AC4 GLY A 266 GLY A 275 1 10 HELIX 23 AC5 PHE A 277 SER A 295 1 19 HELIX 24 AC6 SER A 298 GLN A 325 1 28 HELIX 25 AC7 LYS A 334 PHE A 357 1 24 HELIX 26 AC8 GLY A 361 THR A 379 1 19 HELIX 27 AC9 GLU A 381 VAL A 408 1 28 HELIX 28 AD1 THR A 417 VAL A 440 1 24 HELIX 29 AD2 ASN A 446 ALA A 456 1 11 HELIX 30 AD3 VAL A 463 GLY A 468 1 6 HELIX 31 AD4 SER A 469 GLY A 479 1 11 HELIX 32 AD5 GLU A 480 LEU A 517 1 38 HELIX 33 AD6 GLY B 82 GLY B 106 1 25 HELIX 34 AD7 GLY B 113 ILE B 135 1 23 HELIX 35 AD8 PRO B 144 ILE B 159 1 16 HELIX 36 AD9 ILE B 159 VAL B 166 1 8 HELIX 37 AE1 LYS B 169 LEU B 192 1 24 HELIX 38 AE2 ASP B 193 LEU B 200 1 8 HELIX 39 AE3 LYS B 201 LEU B 226 1 26 HELIX 40 AE4 PRO B 230 LEU B 241 1 12 HELIX 41 AE5 SER B 245 GLY B 260 1 16 HELIX 42 AE6 GLY B 266 GLY B 275 1 10 HELIX 43 AE7 PHE B 277 SER B 295 1 19 HELIX 44 AE8 SER B 298 GLN B 325 1 28 HELIX 45 AE9 LYS B 334 PHE B 357 1 24 HELIX 46 AF1 GLY B 361 THR B 379 1 19 HELIX 47 AF2 GLU B 381 VAL B 408 1 28 HELIX 48 AF3 THR B 417 VAL B 440 1 24 HELIX 49 AF4 ASN B 446 ALA B 456 1 11 HELIX 50 AF5 VAL B 463 GLY B 468 1 6 HELIX 51 AF6 SER B 469 GLY B 479 1 11 HELIX 52 AF7 GLU B 480 LEU B 517 1 38 HELIX 53 AF8 GLU C 79 ILE C 83 5 5 HELIX 54 AF9 SER C 121 GLY C 128 1 8 HELIX 55 AG1 ILE C 150 SER C 153 5 4 HELIX 56 AG2 THR C 182 ARG C 188 1 7 SHEET 1 AA1 4 MET E 4 GLN E 6 0 SHEET 2 AA1 4 VAL E 19 ALA E 25 -1 O ARG E 24 N THR E 5 SHEET 3 AA1 4 ASP E 70 ILE E 75 -1 O LEU E 73 N ILE E 21 SHEET 4 AA1 4 PHE E 62 SER E 63 -1 N SER E 63 O THR E 74 SHEET 1 AA2 4 MET E 4 GLN E 6 0 SHEET 2 AA2 4 VAL E 19 ALA E 25 -1 O ARG E 24 N THR E 5 SHEET 3 AA2 4 ASP E 70 ILE E 75 -1 O LEU E 73 N ILE E 21 SHEET 4 AA2 4 GLY E 66 SER E 67 -1 N SER E 67 O ASP E 70 SHEET 1 AA3 6 SER E 10 ALA E 13 0 SHEET 2 AA3 6 THR E 102 ILE E 106 1 O GLU E 105 N ALA E 13 SHEET 3 AA3 6 THR E 85 GLN E 90 -1 N TYR E 86 O THR E 102 SHEET 4 AA3 6 TRP E 35 GLN E 38 -1 N GLN E 38 O THR E 85 SHEET 5 AA3 6 VAL E 44 CYS E 49 -1 O LYS E 45 N GLN E 37 SHEET 6 AA3 6 ARG E 53 LEU E 54 -1 O ARG E 53 N CYS E 49 SHEET 1 AA4 4 SER E 10 ALA E 13 0 SHEET 2 AA4 4 THR E 102 ILE E 106 1 O GLU E 105 N ALA E 13 SHEET 3 AA4 4 THR E 85 GLN E 90 -1 N TYR E 86 O THR E 102 SHEET 4 AA4 4 THR E 97 PHE E 98 -1 O THR E 97 N GLN E 90 SHEET 1 AA5 4 SER E 116 PHE E 118 0 SHEET 2 AA5 4 SER E 131 PHE E 139 -1 O PHE E 135 N SER E 116 SHEET 3 AA5 4 TYR E 173 THR E 180 -1 O LEU E 179 N VAL E 132 SHEET 4 AA5 4 VAL E 159 TRP E 163 -1 N LEU E 160 O THR E 178 SHEET 1 AA6 2 LYS E 147 TRP E 148 0 SHEET 2 AA6 2 CYS E 194 GLU E 195 -1 O GLU E 195 N LYS E 147 SHEET 1 AA7 4 GLN D 3 GLU D 6 0 SHEET 2 AA7 4 VAL D 18 SER D 25 -1 O LYS D 23 N GLN D 5 SHEET 3 AA7 4 THR D 78 LEU D 83 -1 O MET D 81 N MET D 20 SHEET 4 AA7 4 ALA D 68 ASP D 73 -1 N THR D 69 O GLU D 82 SHEET 1 AA8 2 GLU D 10 VAL D 12 0 SHEET 2 AA8 2 VAL D 117 VAL D 119 1 O THR D 118 N VAL D 12 SHEET 1 AA9 5 THR D 58 PHE D 60 0 SHEET 2 AA9 5 LEU D 45 ILE D 51 -1 N TYR D 50 O LYS D 59 SHEET 3 AA9 5 PHE D 33 GLN D 39 -1 N TRP D 36 O ILE D 48 SHEET 4 AA9 5 VAL D 93 CYS D 99 -1 O ALA D 97 N HIS D 35 SHEET 5 AA9 5 TYR D 110 TRP D 111 -1 O TYR D 110 N ARG D 98 SHEET 1 AB1 2 THR D 145 LEU D 146 0 SHEET 2 AB1 2 VAL D 189 THR D 190 -1 O VAL D 189 N LEU D 146 SHEET 1 AB2 2 THR D 161 TRP D 162 0 SHEET 2 AB2 2 CYS D 203 ASN D 204 -1 O ASN D 204 N THR D 161 SHEET 1 AB3 4 GLN F 3 GLU F 6 0 SHEET 2 AB3 4 VAL F 18 SER F 25 -1 O LYS F 23 N GLN F 5 SHEET 3 AB3 4 THR F 78 LEU F 83 -1 O MET F 81 N MET F 20 SHEET 4 AB3 4 ALA F 68 ASP F 73 -1 N THR F 71 O TYR F 80 SHEET 1 AB4 2 GLU F 10 VAL F 12 0 SHEET 2 AB4 2 VAL F 117 VAL F 119 1 O THR F 118 N VAL F 12 SHEET 1 AB5 4 THR F 58 PHE F 60 0 SHEET 2 AB5 4 TRP F 47 ILE F 51 -1 N TYR F 50 O LYS F 59 SHEET 3 AB5 4 PHE F 33 GLN F 39 -1 N TRP F 36 O GLY F 49 SHEET 4 AB5 4 VAL F 93 CYS F 99 -1 O ALA F 97 N HIS F 35 SHEET 1 AB6 2 THR F 145 LEU F 146 0 SHEET 2 AB6 2 VAL F 189 THR F 190 -1 O VAL F 189 N LEU F 146 SHEET 1 AB7 2 THR F 161 TRP F 162 0 SHEET 2 AB7 2 CYS F 203 ASN F 204 -1 O ASN F 204 N THR F 161 SHEET 1 AB8 4 MET C 4 GLN C 6 0 SHEET 2 AB8 4 VAL C 19 ALA C 25 -1 O ARG C 24 N THR C 5 SHEET 3 AB8 4 ASP C 70 ILE C 75 -1 O LEU C 73 N ILE C 21 SHEET 4 AB8 4 PHE C 62 SER C 63 -1 N SER C 63 O THR C 74 SHEET 1 AB9 4 MET C 4 GLN C 6 0 SHEET 2 AB9 4 VAL C 19 ALA C 25 -1 O ARG C 24 N THR C 5 SHEET 3 AB9 4 ASP C 70 ILE C 75 -1 O LEU C 73 N ILE C 21 SHEET 4 AB9 4 GLY C 66 SER C 67 -1 N SER C 67 O ASP C 70 SHEET 1 AC1 6 SER C 10 ALA C 13 0 SHEET 2 AC1 6 THR C 102 ILE C 106 1 O GLU C 105 N ALA C 13 SHEET 3 AC1 6 THR C 85 GLN C 90 -1 N TYR C 86 O THR C 102 SHEET 4 AC1 6 TRP C 35 GLN C 38 -1 N GLN C 38 O THR C 85 SHEET 5 AC1 6 VAL C 44 CYS C 49 -1 O LYS C 45 N GLN C 37 SHEET 6 AC1 6 ARG C 53 LEU C 54 -1 O ARG C 53 N CYS C 49 SHEET 1 AC2 4 SER C 10 ALA C 13 0 SHEET 2 AC2 4 THR C 102 ILE C 106 1 O GLU C 105 N ALA C 13 SHEET 3 AC2 4 THR C 85 GLN C 90 -1 N TYR C 86 O THR C 102 SHEET 4 AC2 4 THR C 97 PHE C 98 -1 O THR C 97 N GLN C 90 SHEET 1 AC3 4 SER C 116 PHE C 118 0 SHEET 2 AC3 4 SER C 131 PHE C 139 -1 O PHE C 135 N SER C 116 SHEET 3 AC3 4 TYR C 173 THR C 180 -1 O LEU C 179 N VAL C 132 SHEET 4 AC3 4 VAL C 159 TRP C 163 -1 N LEU C 160 O THR C 178 SHEET 1 AC4 2 LYS C 147 TRP C 148 0 SHEET 2 AC4 2 CYS C 194 GLU C 195 -1 O GLU C 195 N LYS C 147 SSBOND 1 CYS E 23 CYS E 88 1555 1555 2.03 SSBOND 2 CYS E 134 CYS E 194 1555 1555 2.03 SSBOND 3 CYS D 22 CYS D 96 1555 1555 2.03 SSBOND 4 CYS D 148 CYS D 203 1555 1555 2.03 SSBOND 5 CYS F 22 CYS F 96 1555 1555 2.03 SSBOND 6 CYS F 148 CYS F 203 1555 1555 2.03 SSBOND 7 CYS C 23 CYS C 88 1555 1555 2.03 SSBOND 8 CYS C 134 CYS C 194 1555 1555 2.03 CISPEP 1 TYR E 140 PRO E 141 0 -2.12 CISPEP 2 TYR C 140 PRO C 141 0 -2.05 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