HEADER TRANSPORT PROTEIN 30-JUN-23 8PNL TITLE OUTWARD-OPEN CONFORMATION OF A MAJOR FACILITATOR SUPERFAMILY (MFS) TITLE 2 TRANSPORTER MHAS2168, A HOMOLOGUE OF RV1410 FROM M. TUBERCULOSIS, IN TITLE 3 COMPLEX WITH AN ALPACA NANOBODY COMPND MOL_ID: 1; COMPND 2 MOLECULE: PUTATIVE TRIACYLGLYCERIDE TRANSPORTER; COMPND 3 CHAIN: A, C; COMPND 4 SYNONYM: SUGAR (AND OTHER) TRANSPORTER FAMILY PROTEIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: NB_H2; COMPND 8 CHAIN: B, D; COMPND 9 ENGINEERED: YES; COMPND 10 OTHER_DETAILS: NANOBODY SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MYCOLICIBACTERIUM HASSIACUM DSM 44199; SOURCE 3 ORGANISM_TAXID: 1122247; SOURCE 4 GENE: C731_2106, MHAS_02168; SOURCE 5 EXPRESSION_SYSTEM: MYCOLICIBACTERIUM SMEGMATIS MC2 155; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 246196; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PACE_C3GH_MHAS2168; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: VICUGNA PACOS; SOURCE 10 ORGANISM_TAXID: 30538; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI MC1061; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 1211845; SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PBXNPHM3_NB_H2 KEYWDS MAJOR FACILITATOR SUPERFAMILY TRANSPORTER, NANOBODY, OUTWARD-OPEN KEYWDS 2 CONFORMATION, TRIACYLGLYCERIDE EXTRACTION, TRANSPORT PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR S.REMM,J.SCHOEPPE,C.A.J.HUTTER,I.GONDA,M.A.SEEGER REVDAT 1 18-OCT-23 8PNL 0 JRNL AUTH S.REMM,D.DE VECCHIS,J.SCHOEPPE,C.A.J.HUTTER,I.GONDA,M.HOHL, JRNL AUTH 2 S.NEWSTEAD,L.V.SCHAEFER,M.A.SEEGER JRNL TITL STRUCTURAL BASIS FOR TRIACYLGLYCERIDE EXTRACTION FROM JRNL TITL 2 MYCOBACTERIAL INNER MEMBRANE BY MFS TRANSPORTER RV1410 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.20.1_4487: ???) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.70 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4 REMARK 3 NUMBER OF REFLECTIONS : 39014 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.247 REMARK 3 R VALUE (WORKING SET) : 0.245 REMARK 3 FREE R VALUE : 0.292 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1952 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 44.7000 - 6.5000 0.98 2643 140 0.2027 0.2214 REMARK 3 2 6.5000 - 5.1600 0.99 2643 140 0.2688 0.3058 REMARK 3 3 5.1600 - 4.5100 0.99 2658 140 0.2364 0.2933 REMARK 3 4 4.5100 - 4.1000 0.99 2632 138 0.2308 0.3116 REMARK 3 5 4.1000 - 3.8100 1.00 2663 140 0.2487 0.3395 REMARK 3 6 3.8000 - 3.5800 0.98 2611 138 0.2561 0.2940 REMARK 3 7 3.5800 - 3.4000 1.00 2636 138 0.2453 0.2808 REMARK 3 8 3.4000 - 3.2500 1.00 2662 140 0.2508 0.3044 REMARK 3 9 3.2500 - 3.1300 1.00 2654 140 0.2718 0.3020 REMARK 3 10 3.1300 - 3.0200 1.00 2633 139 0.2908 0.3332 REMARK 3 11 3.0200 - 2.9300 1.00 2679 141 0.2949 0.3705 REMARK 3 12 2.9300 - 2.8400 1.00 2655 139 0.2912 0.3170 REMARK 3 13 2.8400 - 2.7700 1.00 2620 138 0.3155 0.3262 REMARK 3 14 2.7700 - 2.7000 1.00 2673 141 0.3552 0.3914 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.390 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.660 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.003 NULL REMARK 3 ANGLE : 0.729 NULL REMARK 3 CHIRALITY : 0.042 1481 REMARK 3 PLANARITY : 0.009 1536 REMARK 3 DIHEDRAL : 12.615 3111 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 8PNL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-JUN-23. REMARK 100 THE DEPOSITION ID IS D_1292131586. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 24-AUG-19 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.7 REMARK 200 NUMBER OF CRYSTALS USED : 2 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SLS REMARK 200 BEAMLINE : X06SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.999 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39032 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700 REMARK 200 RESOLUTION RANGE LOW (A) : 44.700 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 200 DATA REDUNDANCY : 4.650 REMARK 200 R MERGE (I) : 0.09500 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.7700 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.77 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 1.63800 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 52.63 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 380 MM NAH2PO4, 0.1 M SODIUM CITRATE REMARK 280 (PH 5.7), 28% (V/V) PEG400, 2.4% (V/V) 1,4-BUTANEDIOLE, LIPIDIC REMARK 280 CUBIC PHASE, TEMPERATURE 293.15K. 420 MM NAH2PO4, 0.1 M SODIUM REMARK 280 CITRATE (PH 5.8), 28% (V/V) PEG400, 2.4% (V/V) 1,4-BUTANEDIOLE, REMARK 280 LIPIDIC CUBIC PHASE, TEMPERATURE 293.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 80.35000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D 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 ALA A 2 REMARK 465 PHE A 3 REMARK 465 PRO A 4 REMARK 465 GLN A 5 REMARK 465 THR A 6 REMARK 465 PRO A 7 REMARK 465 ASN A 8 REMARK 465 ARG A 9 REMARK 465 LEU A 10 REMARK 465 ILE A 11 REMARK 465 ARG A 12 REMARK 465 PRO A 13 REMARK 465 ARG A 14 REMARK 465 ARG A 15 REMARK 465 ASN A 55 REMARK 465 GLN A 56 REMARK 465 ILE A 57 REMARK 465 VAL A 203 REMARK 465 ARG A 204 REMARK 465 THR A 205 REMARK 465 GLU A 206 REMARK 465 GLU A 207 REMARK 465 PRO A 208 REMARK 465 GLU A 234 REMARK 465 PRO A 235 REMARK 465 ASP A 236 REMARK 465 ARG A 511 REMARK 465 ARG A 512 REMARK 465 GLU A 513 REMARK 465 HIS A 514 REMARK 465 ALA A 515 REMARK 465 GLU A 516 REMARK 465 GLU A 517 REMARK 465 SER A 518 REMARK 465 ALA A 519 REMARK 465 ASP A 520 REMARK 465 ALA A 521 REMARK 465 VAL A 522 REMARK 465 ASP A 523 REMARK 465 GLY A 524 REMARK 465 VAL A 525 REMARK 465 SER A 526 REMARK 465 ASN A 527 REMARK 465 ALA A 528 REMARK 465 ARG A 529 REMARK 465 ASP A 530 REMARK 465 ARG A 531 REMARK 465 ALA A 532 REMARK 465 PRO A 533 REMARK 465 SER A 534 REMARK 465 ALA A 535 REMARK 465 ALA A 536 REMARK 465 LEU A 537 REMARK 465 GLU A 538 REMARK 465 VAL A 539 REMARK 465 LEU A 540 REMARK 465 PHE A 541 REMARK 465 GLN A 542 REMARK 465 GLY B -2 REMARK 465 PRO B -1 REMARK 465 SER B 0 REMARK 465 ALA B 40 REMARK 465 PRO B 41 REMARK 465 GLY B 42 REMARK 465 LYS B 43 REMARK 465 GLU B 44 REMARK 465 SER B 117 REMARK 465 ALA B 118 REMARK 465 MET C 0 REMARK 465 SER C 1 REMARK 465 ALA C 2 REMARK 465 PHE C 3 REMARK 465 PRO C 4 REMARK 465 GLN C 5 REMARK 465 THR C 6 REMARK 465 PRO C 7 REMARK 465 ASN C 8 REMARK 465 ARG C 9 REMARK 465 LEU C 10 REMARK 465 ILE C 11 REMARK 465 ARG C 12 REMARK 465 PRO C 13 REMARK 465 ARG C 14 REMARK 465 ARG C 15 REMARK 465 VAL C 203 REMARK 465 ARG C 204 REMARK 465 THR C 205 REMARK 465 GLU C 206 REMARK 465 GLU C 207 REMARK 465 PRO C 208 REMARK 465 GLN C 209 REMARK 465 PRO C 235 REMARK 465 ASP C 236 REMARK 465 ARG C 511 REMARK 465 ARG C 512 REMARK 465 GLU C 513 REMARK 465 HIS C 514 REMARK 465 ALA C 515 REMARK 465 GLU C 516 REMARK 465 GLU C 517 REMARK 465 SER C 518 REMARK 465 ALA C 519 REMARK 465 ASP C 520 REMARK 465 ALA C 521 REMARK 465 VAL C 522 REMARK 465 ASP C 523 REMARK 465 GLY C 524 REMARK 465 VAL C 525 REMARK 465 SER C 526 REMARK 465 ASN C 527 REMARK 465 ALA C 528 REMARK 465 ARG C 529 REMARK 465 ASP C 530 REMARK 465 ARG C 531 REMARK 465 ALA C 532 REMARK 465 PRO C 533 REMARK 465 SER C 534 REMARK 465 ALA C 535 REMARK 465 ALA C 536 REMARK 465 LEU C 537 REMARK 465 GLU C 538 REMARK 465 VAL C 539 REMARK 465 LEU C 540 REMARK 465 PHE C 541 REMARK 465 GLN C 542 REMARK 465 GLY D -2 REMARK 465 PRO D -1 REMARK 465 SER D 0 REMARK 465 GLN D 1 REMARK 465 ALA D 40 REMARK 465 PRO D 41 REMARK 465 GLY D 42 REMARK 465 LYS D 43 REMARK 465 GLU D 44 REMARK 465 SER D 117 REMARK 465 ALA D 118 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 HZ1 LYS A 238 SD MET C 468 2555 1.51 REMARK 500 OE2 GLU A 243 OG1 THR C 16 1556 1.80 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 ARG A 84 -61.64 -91.51 REMARK 500 LYS A 238 36.39 -96.45 REMARK 500 ARG C 84 -60.58 -107.08 REMARK 500 HIS C 175 30.05 -83.79 REMARK 500 ARG C 264 -41.76 76.81 REMARK 500 LEU C 376 56.05 -143.78 REMARK 500 LEU D 4 70.45 -154.22 REMARK 500 LYS D 75 -140.04 55.04 REMARK 500 TRP D 108 -5.82 -148.48 REMARK 500 REMARK 500 REMARK: NULL DBREF 8PNL A 2 535 UNP K5B8L6 K5B8L6_MYCHD 2 535 DBREF 8PNL B -2 118 PDB 8PNL 8PNL -2 118 DBREF 8PNL C 2 535 UNP K5B8L6 K5B8L6_MYCHD 2 535 DBREF 8PNL D -2 118 PDB 8PNL 8PNL -2 118 SEQADV 8PNL MET A 0 UNP K5B8L6 INITIATING METHIONINE SEQADV 8PNL SER A 1 UNP K5B8L6 EXPRESSION TAG SEQADV 8PNL ALA A 536 UNP K5B8L6 EXPRESSION TAG SEQADV 8PNL LEU A 537 UNP K5B8L6 EXPRESSION TAG SEQADV 8PNL GLU A 538 UNP K5B8L6 EXPRESSION TAG SEQADV 8PNL VAL A 539 UNP K5B8L6 EXPRESSION TAG SEQADV 8PNL LEU A 540 UNP K5B8L6 EXPRESSION TAG SEQADV 8PNL PHE A 541 UNP K5B8L6 EXPRESSION TAG SEQADV 8PNL GLN A 542 UNP K5B8L6 EXPRESSION TAG SEQADV 8PNL MET C 0 UNP K5B8L6 INITIATING METHIONINE SEQADV 8PNL SER C 1 UNP K5B8L6 EXPRESSION TAG SEQADV 8PNL ALA C 536 UNP K5B8L6 EXPRESSION TAG SEQADV 8PNL LEU C 537 UNP K5B8L6 EXPRESSION TAG SEQADV 8PNL GLU C 538 UNP K5B8L6 EXPRESSION TAG SEQADV 8PNL VAL C 539 UNP K5B8L6 EXPRESSION TAG SEQADV 8PNL LEU C 540 UNP K5B8L6 EXPRESSION TAG SEQADV 8PNL PHE C 541 UNP K5B8L6 EXPRESSION TAG SEQADV 8PNL GLN C 542 UNP K5B8L6 EXPRESSION TAG SEQRES 1 A 543 MET SER ALA PHE PRO GLN THR PRO ASN ARG LEU ILE ARG SEQRES 2 A 543 PRO ARG ARG THR SER ARG GLY ILE ALA ILE SER ALA GLY SEQRES 3 A 543 GLY LEU ALA VAL LEU LEU GLY ALA LEU ASP THR TYR VAL SEQRES 4 A 543 VAL VAL SER ILE VAL THR ASP ILE MET ARG ASP VAL GLY SEQRES 5 A 543 ILE ALA VAL ASN GLN ILE GLN ARG VAL THR PRO ILE ILE SEQRES 6 A 543 THR GLY TYR LEU LEU GLY TYR ILE ALA ALA MET PRO LEU SEQRES 7 A 543 LEU GLY ARG ALA SER ASP ARG PHE GLY ARG LYS LEU LEU SEQRES 8 A 543 ILE GLN ILE SER LEU ALA GLY PHE ALA LEU GLY SER VAL SEQRES 9 A 543 ILE THR ALA LEU ALA THR ASN LEU ASP VAL LEU VAL ALA SEQRES 10 A 543 GLY ARG VAL ILE GLN GLY ALA ALA SER GLY ALA LEU LEU SEQRES 11 A 543 PRO VAL THR LEU ALA LEU ALA ALA ASP LEU TRP ALA THR SEQRES 12 A 543 HIS LYS ARG ALA ALA VAL LEU GLY GLY VAL GLY ALA ALA SEQRES 13 A 543 GLN GLU LEU GLY ALA VAL LEU GLY PRO ILE TYR GLY ILE SEQRES 14 A 543 PHE VAL VAL TRP LEU PHE HIS HIS TRP GLN ALA VAL PHE SEQRES 15 A 543 TRP VAL ASN VAL PRO LEU ALA LEU ILE ALA MET VAL LEU SEQRES 16 A 543 ILE HIS ILE SER LEU PRO PRO ARG VAL ARG THR GLU GLU SEQRES 17 A 543 PRO GLN ARG VAL ASP VAL THR GLY GLY LEU LEU LEU ALA SEQRES 18 A 543 LEU ALA LEU GLY LEU ALA THR ILE GLY LEU TYR ASN ALA SEQRES 19 A 543 GLU PRO ASP GLY LYS GLN VAL LEU PRO GLU TYR GLY PRO SEQRES 20 A 543 PRO LEU ILE ILE GLY ALA VAL ILE ALA ALA VAL ALA PHE SEQRES 21 A 543 LEU VAL TRP GLU ARG PHE ALA ARG THR ARG LEU LEU ASP SEQRES 22 A 543 PRO ALA GLY VAL ARG PHE ARG PRO PHE LEU ILE ALA LEU SEQRES 23 A 543 LEU VAL SER LEU VAL THR GLY GLY ALA LEU MET VAL THR SEQRES 24 A 543 LEU VAL ASN VAL GLU LEU PHE GLY GLN GLY VAL LEU GLY SEQRES 25 A 543 LEU ASP GLN ASP GLU ALA VAL PHE LEU LEU ALA ARG PHE SEQRES 26 A 543 LEU ILE ALA LEU PRO VAL GLY ALA LEU LEU GLY GLY TRP SEQRES 27 A 543 ILE ALA THR ARG VAL GLY ASP ARG ALA VAL THR ALA VAL SEQRES 28 A 543 GLY LEU LEU ILE ALA ALA GLY GLY PHE TYR LEU ILE ALA SEQRES 29 A 543 GLN TRP PRO ALA ASP VAL LEU GLU SER ARG HIS ASP LEU SEQRES 30 A 543 GLY PHE VAL SER LEU PRO THR LEU ASP THR ASP LEU ALA SEQRES 31 A 543 ILE ALA GLY PHE GLY LEU GLY LEU VAL ILE ALA PRO LEU SEQRES 32 A 543 THR SER ALA ALA LEU ARG VAL VAL PRO ALA ALA GLN HIS SEQRES 33 A 543 GLY ILE ALA SER ALA ALA VAL VAL VAL ALA ARG MET ILE SEQRES 34 A 543 GLY MET LEU ILE GLY ILE ALA ALA LEU SER ALA TRP GLY SEQRES 35 A 543 LEU TYR ARG PHE ASN GLN TYR LEU LYS GLU GLN LEU ALA SEQRES 36 A 543 ALA LEU PRO PRO ALA PRO ALA ASP PHE PRO GLY GLY GLN SEQRES 37 A 543 MET ALA GLY GLN MET MET ARG LEU ARG THR ALA THR VAL SEQRES 38 A 543 GLN ALA TYR VAL LEU GLN TYR GLY GLU ILE PHE ALA ILE SEQRES 39 A 543 THR ALA GLY LEU CYS VAL PHE GLY ALA VAL LEU GLY LEU SEQRES 40 A 543 PHE ILE ALA GLY ARG ARG GLU HIS ALA GLU GLU SER ALA SEQRES 41 A 543 ASP ALA VAL ASP GLY VAL SER ASN ALA ARG ASP ARG ALA SEQRES 42 A 543 PRO SER ALA ALA LEU GLU VAL LEU PHE GLN SEQRES 1 B 121 GLY PRO SER GLN GLY GLN LEU VAL GLU SER GLY GLY GLY SEQRES 2 B 121 LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA SEQRES 3 B 121 ASP ALA GLY SER ILE PHE ASN LYS PHE PRO MET ALA TRP SEQRES 4 B 121 TYR ARG GLN ALA PRO GLY LYS GLU ARG GLU LEU VAL ALA SEQRES 5 B 121 ARG ILE SER SER GLY GLY SER THR ASN TYR ALA ASP PHE SEQRES 6 B 121 VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS SEQRES 7 B 121 SER THR LEU TYR LEU GLN MET ASN SER LEU LYS PRO GLU SEQRES 8 B 121 ASP THR ALA MET TYR TYR CYS ALA ARG ILE ILE ASN SER SEQRES 9 B 121 ALA SER ASN ILE ALA TYR TRP GLY GLN GLY THR ARG VAL SEQRES 10 B 121 THR VAL SER ALA SEQRES 1 C 543 MET SER ALA PHE PRO GLN THR PRO ASN ARG LEU ILE ARG SEQRES 2 C 543 PRO ARG ARG THR SER ARG GLY ILE ALA ILE SER ALA GLY SEQRES 3 C 543 GLY LEU ALA VAL LEU LEU GLY ALA LEU ASP THR TYR VAL SEQRES 4 C 543 VAL VAL SER ILE VAL THR ASP ILE MET ARG ASP VAL GLY SEQRES 5 C 543 ILE ALA VAL ASN GLN ILE GLN ARG VAL THR PRO ILE ILE SEQRES 6 C 543 THR GLY TYR LEU LEU GLY TYR ILE ALA ALA MET PRO LEU SEQRES 7 C 543 LEU GLY ARG ALA SER ASP ARG PHE GLY ARG LYS LEU LEU SEQRES 8 C 543 ILE GLN ILE SER LEU ALA GLY PHE ALA LEU GLY SER VAL SEQRES 9 C 543 ILE THR ALA LEU ALA THR ASN LEU ASP VAL LEU VAL ALA SEQRES 10 C 543 GLY ARG VAL ILE GLN GLY ALA ALA SER GLY ALA LEU LEU SEQRES 11 C 543 PRO VAL THR LEU ALA LEU ALA ALA ASP LEU TRP ALA THR SEQRES 12 C 543 HIS LYS ARG ALA ALA VAL LEU GLY GLY VAL GLY ALA ALA SEQRES 13 C 543 GLN GLU LEU GLY ALA VAL LEU GLY PRO ILE TYR GLY ILE SEQRES 14 C 543 PHE VAL VAL TRP LEU PHE HIS HIS TRP GLN ALA VAL PHE SEQRES 15 C 543 TRP VAL ASN VAL PRO LEU ALA LEU ILE ALA MET VAL LEU SEQRES 16 C 543 ILE HIS ILE SER LEU PRO PRO ARG VAL ARG THR GLU GLU SEQRES 17 C 543 PRO GLN ARG VAL ASP VAL THR GLY GLY LEU LEU LEU ALA SEQRES 18 C 543 LEU ALA LEU GLY LEU ALA THR ILE GLY LEU TYR ASN ALA SEQRES 19 C 543 GLU PRO ASP GLY LYS GLN VAL LEU PRO GLU TYR GLY PRO SEQRES 20 C 543 PRO LEU ILE ILE GLY ALA VAL ILE ALA ALA VAL ALA PHE SEQRES 21 C 543 LEU VAL TRP GLU ARG PHE ALA ARG THR ARG LEU LEU ASP SEQRES 22 C 543 PRO ALA GLY VAL ARG PHE ARG PRO PHE LEU ILE ALA LEU SEQRES 23 C 543 LEU VAL SER LEU VAL THR GLY GLY ALA LEU MET VAL THR SEQRES 24 C 543 LEU VAL ASN VAL GLU LEU PHE GLY GLN GLY VAL LEU GLY SEQRES 25 C 543 LEU ASP GLN ASP GLU ALA VAL PHE LEU LEU ALA ARG PHE SEQRES 26 C 543 LEU ILE ALA LEU PRO VAL GLY ALA LEU LEU GLY GLY TRP SEQRES 27 C 543 ILE ALA THR ARG VAL GLY ASP ARG ALA VAL THR ALA VAL SEQRES 28 C 543 GLY LEU LEU ILE ALA ALA GLY GLY PHE TYR LEU ILE ALA SEQRES 29 C 543 GLN TRP PRO ALA ASP VAL LEU GLU SER ARG HIS ASP LEU SEQRES 30 C 543 GLY PHE VAL SER LEU PRO THR LEU ASP THR ASP LEU ALA SEQRES 31 C 543 ILE ALA GLY PHE GLY LEU GLY LEU VAL ILE ALA PRO LEU SEQRES 32 C 543 THR SER ALA ALA LEU ARG VAL VAL PRO ALA ALA GLN HIS SEQRES 33 C 543 GLY ILE ALA SER ALA ALA VAL VAL VAL ALA ARG MET ILE SEQRES 34 C 543 GLY MET LEU ILE GLY ILE ALA ALA LEU SER ALA TRP GLY SEQRES 35 C 543 LEU TYR ARG PHE ASN GLN TYR LEU LYS GLU GLN LEU ALA SEQRES 36 C 543 ALA LEU PRO PRO ALA PRO ALA ASP PHE PRO GLY GLY GLN SEQRES 37 C 543 MET ALA GLY GLN MET MET ARG LEU ARG THR ALA THR VAL SEQRES 38 C 543 GLN ALA TYR VAL LEU GLN TYR GLY GLU ILE PHE ALA ILE SEQRES 39 C 543 THR ALA GLY LEU CYS VAL PHE GLY ALA VAL LEU GLY LEU SEQRES 40 C 543 PHE ILE ALA GLY ARG ARG GLU HIS ALA GLU GLU SER ALA SEQRES 41 C 543 ASP ALA VAL ASP GLY VAL SER ASN ALA ARG ASP ARG ALA SEQRES 42 C 543 PRO SER ALA ALA LEU GLU VAL LEU PHE GLN SEQRES 1 D 121 GLY PRO SER GLN GLY GLN LEU VAL GLU SER GLY GLY GLY SEQRES 2 D 121 LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA SEQRES 3 D 121 ASP ALA GLY SER ILE PHE ASN LYS PHE PRO MET ALA TRP SEQRES 4 D 121 TYR ARG GLN ALA PRO GLY LYS GLU ARG GLU LEU VAL ALA SEQRES 5 D 121 ARG ILE SER SER GLY GLY SER THR ASN TYR ALA ASP PHE SEQRES 6 D 121 VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS SEQRES 7 D 121 SER THR LEU TYR LEU GLN MET ASN SER LEU LYS PRO GLU SEQRES 8 D 121 ASP THR ALA MET TYR TYR CYS ALA ARG ILE ILE ASN SER SEQRES 9 D 121 ALA SER ASN ILE ALA TYR TRP GLY GLN GLY THR ARG VAL SEQRES 10 D 121 THR VAL SER ALA HELIX 1 AA1 SER A 17 VAL A 38 1 22 HELIX 2 AA2 VAL A 39 SER A 41 5 3 HELIX 3 AA3 ILE A 42 GLY A 51 1 10 HELIX 4 AA4 THR A 61 ALA A 74 1 14 HELIX 5 AA5 ALA A 74 GLY A 86 1 13 HELIX 6 AA6 GLY A 86 LEU A 107 1 22 HELIX 7 AA7 ASN A 110 TRP A 140 1 31 HELIX 8 AA8 ALA A 141 HIS A 175 1 35 HELIX 9 AA9 TRP A 177 LEU A 199 1 23 HELIX 10 AB1 ASP A 212 TYR A 231 1 20 HELIX 11 AB2 TYR A 244 ALA A 266 1 23 HELIX 12 AB3 ARG A 277 VAL A 309 1 33 HELIX 13 AB4 ASP A 313 LEU A 320 1 8 HELIX 14 AB5 LEU A 321 GLY A 343 1 23 HELIX 15 AB6 GLY A 343 ALA A 363 1 21 HELIX 16 AB7 ASP A 368 GLU A 371 5 4 HELIX 17 AB8 THR A 383 VAL A 409 1 27 HELIX 18 AB9 GLN A 414 LEU A 456 1 43 HELIX 19 AC1 GLY A 466 GLY A 505 1 40 HELIX 20 AC2 LEU A 506 ILE A 508 5 3 HELIX 21 AC3 ASP B 61 LYS B 64 5 4 HELIX 22 AC4 LYS B 86 THR B 90 5 5 HELIX 23 AC5 SER C 17 TYR C 37 1 21 HELIX 24 AC6 VAL C 38 SER C 41 5 4 HELIX 25 AC7 ILE C 42 GLY C 51 1 10 HELIX 26 AC8 ALA C 53 VAL C 60 5 8 HELIX 27 AC9 THR C 61 ALA C 74 1 14 HELIX 28 AD1 ALA C 74 GLY C 86 1 13 HELIX 29 AD2 GLY C 86 LEU C 107 1 22 HELIX 30 AD3 ASN C 110 ALA C 127 1 18 HELIX 31 AD4 ALA C 127 TRP C 140 1 14 HELIX 32 AD5 ALA C 141 PHE C 174 1 34 HELIX 33 AD6 TRP C 177 LEU C 199 1 23 HELIX 34 AD7 ASP C 212 TYR C 231 1 20 HELIX 35 AD8 TYR C 244 GLU C 263 1 20 HELIX 36 AD9 ARG C 277 VAL C 309 1 33 HELIX 37 AE1 ASP C 313 LEU C 320 1 8 HELIX 38 AE2 LEU C 321 GLY C 343 1 23 HELIX 39 AE3 GLY C 343 ALA C 363 1 21 HELIX 40 AE4 ASP C 368 SER C 372 5 5 HELIX 41 AE5 PRO C 382 VAL C 398 1 17 HELIX 42 AE6 VAL C 398 ARG C 408 1 11 HELIX 43 AE7 GLN C 414 LEU C 456 1 43 HELIX 44 AE8 GLY C 466 LEU C 506 1 41 HELIX 45 AE9 ALA D 25 ASN D 30 1 6 HELIX 46 AF1 ASP D 61 LYS D 64 5 4 HELIX 47 AF2 LYS D 86 THR D 90 5 5 HELIX 48 AF3 SER D 101 ASN D 104 5 4 SHEET 1 AA1 2 ARG A 373 ASP A 375 0 SHEET 2 AA1 2 SER A 380 PRO A 382 -1 O LEU A 381 N HIS A 374 SHEET 1 AA2 4 VAL B 5 SER B 7 0 SHEET 2 AA2 4 LEU B 18 ALA B 23 -1 O SER B 21 N SER B 7 SHEET 3 AA2 4 THR B 77 MET B 82 -1 O MET B 82 N LEU B 18 SHEET 4 AA2 4 PHE B 67 ASP B 72 -1 N SER B 70 O TYR B 79 SHEET 1 AA3 5 THR B 57 TYR B 59 0 SHEET 2 AA3 5 GLU B 46 ILE B 51 -1 N ARG B 50 O ASN B 58 SHEET 3 AA3 5 MET B 34 GLN B 39 -1 N ARG B 38 O GLU B 46 SHEET 4 AA3 5 ALA B 91 ASN B 100 -1 O ALA B 96 N ALA B 35 SHEET 5 AA3 5 ILE B 105 TRP B 108 -1 O TYR B 107 N ARG B 97 SHEET 1 AA4 5 THR B 57 TYR B 59 0 SHEET 2 AA4 5 GLU B 46 ILE B 51 -1 N ARG B 50 O ASN B 58 SHEET 3 AA4 5 MET B 34 GLN B 39 -1 N ARG B 38 O GLU B 46 SHEET 4 AA4 5 ALA B 91 ASN B 100 -1 O ALA B 96 N ALA B 35 SHEET 5 AA4 5 THR B 112 VAL B 114 -1 O VAL B 114 N ALA B 91 SHEET 1 AA5 4 LEU D 4 SER D 7 0 SHEET 2 AA5 4 LEU D 18 ASP D 24 -1 O SER D 21 N SER D 7 SHEET 3 AA5 4 THR D 77 MET D 82 -1 O MET D 82 N LEU D 18 SHEET 4 AA5 4 PHE D 67 ASP D 72 -1 N THR D 68 O GLN D 81 SHEET 1 AA6 5 THR D 57 TYR D 59 0 SHEET 2 AA6 5 GLU D 46 ILE D 51 -1 N ARG D 50 O ASN D 58 SHEET 3 AA6 5 MET D 34 ARG D 38 -1 N ARG D 38 O GLU D 46 SHEET 4 AA6 5 ALA D 91 ASN D 100 -1 O TYR D 94 N TYR D 37 SHEET 5 AA6 5 ILE D 105 TYR D 107 -1 O ILE D 105 N ILE D 99 SHEET 1 AA7 5 THR D 57 TYR D 59 0 SHEET 2 AA7 5 GLU D 46 ILE D 51 -1 N ARG D 50 O ASN D 58 SHEET 3 AA7 5 MET D 34 ARG D 38 -1 N ARG D 38 O GLU D 46 SHEET 4 AA7 5 ALA D 91 ASN D 100 -1 O TYR D 94 N TYR D 37 SHEET 5 AA7 5 THR D 112 VAL D 114 -1 O THR D 112 N TYR D 93 SSBOND 1 CYS B 22 CYS B 95 1555 1555 2.03 SSBOND 2 CYS D 22 CYS D 95 1555 1555 2.03 CRYST1 57.780 160.700 82.960 90.00 109.01 90.00 P 1 21 1 4 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 0.017307 0.000000 0.005963 0.00000 SCALE2 0.000000 0.006223 0.000000 0.00000 SCALE3 0.000000 0.000000 0.012749 0.00000