HEADER TRANSPORT PROTEIN 25-JUL-24 9G9P TITLE LIPID III FLIPPASE WZXE WITH NB10 AND NB7 NANOBODIES IN INWARD-FACING TITLE 2 CONFORMATION - CRYSTAL 2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: LIPID III FLIPPASE; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: NB10 NANOBODY; COMPND 7 CHAIN: B; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: NB7 NANOBODY; COMPND 11 CHAIN: C; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 562; SOURCE 4 GENE: WZXE, WZX, YIFJ, B3792, JW3766; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_VARIANT: C43; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 10 ORGANISM_TAXID: 9844; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 13 EXPRESSION_SYSTEM_STRAIN: WK6 SU-; SOURCE 14 MOL_ID: 3; SOURCE 15 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 16 ORGANISM_TAXID: 9844; SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 18 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 19 EXPRESSION_SYSTEM_STRAIN: WK6 SU- KEYWDS MEMBRANE PROTEIN, FLIPPASE, CELL WALL, ENTEROBACTERIAL COMMON KEYWDS 2 ANTIGEN, TRANSPORT PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR A.LE BAS,J.H.NAISMITH REVDAT 1 22-JAN-25 9G9P 0 JRNL AUTH A.LE BAS,B.R.CLARKE,T.TEELUCKSINGH,M.LEE,K.EL OMARI, JRNL AUTH 2 A.M.GILTRAP,S.A.MCMAHON,H.LIU,J.H.BEALE,V.MYKHAYLYK,R.DUMAN, JRNL AUTH 3 N.G.PATERSON,P.N.WARD,P.J.HARRISON,M.WECKENER,E.PARDON, JRNL AUTH 4 J.STEYAERT,H.LIU,A.QUIGLEY,B.G.DAVIS,A.WAGNER,C.WHITFIELD, JRNL AUTH 5 J.H.NAISMITH JRNL TITL STRUCTURE OF WZXE THE LIPID III FLIPPASE FOR ENTEROBACTERIAL JRNL TITL 2 COMMON ANTIGEN POLYSACCHARIDE. JRNL REF OPEN BIOLOGY V. 15 40310 2025 JRNL REFN ESSN 2046-2441 JRNL PMID 39772807 JRNL DOI 10.1098/RSOB.240310 REMARK 2 REMARK 2 RESOLUTION. 2.80 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) : 2.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.94 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 3 NUMBER OF REFLECTIONS : 20501 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.223 REMARK 3 R VALUE (WORKING SET) : 0.220 REMARK 3 FREE R VALUE : 0.274 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.920 REMARK 3 FREE R VALUE TEST SET COUNT : 1008 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 34.9400 - 5.3600 1.00 2923 156 0.2118 0.2432 REMARK 3 2 5.3600 - 4.2600 1.00 2803 141 0.2110 0.2381 REMARK 3 3 4.2600 - 3.7200 1.00 2818 127 0.1962 0.2591 REMARK 3 4 3.7200 - 3.3800 1.00 2741 154 0.2237 0.2939 REMARK 3 5 3.3800 - 3.1400 1.00 2775 135 0.2361 0.3412 REMARK 3 6 3.1400 - 2.9500 1.00 2743 146 0.2527 0.3301 REMARK 3 7 2.9500 - 2.8000 0.99 2690 149 0.2733 0.3355 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) : 0.330 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.210 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 : 0.002 5162 REMARK 3 ANGLE : 0.447 7017 REMARK 3 CHIRALITY : 0.036 801 REMARK 3 PLANARITY : 0.003 869 REMARK 3 DIHEDRAL : 3.672 723 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: (CHAIN 'C' AND RESID 4 THROUGH 124) REMARK 3 ORIGIN FOR THE GROUP (A): 24.4488 -39.4328 39.4692 REMARK 3 T TENSOR REMARK 3 T11: 0.7558 T22: 0.3277 REMARK 3 T33: 0.3403 T12: 0.1274 REMARK 3 T13: -0.0039 T23: 0.0299 REMARK 3 L TENSOR REMARK 3 L11: 3.3455 L22: 4.3390 REMARK 3 L33: 2.8964 L12: 2.2548 REMARK 3 L13: 1.0424 L23: -0.5220 REMARK 3 S TENSOR REMARK 3 S11: 0.0074 S12: -0.0183 S13: -0.3313 REMARK 3 S21: 0.4383 S22: -0.0752 S23: -0.2486 REMARK 3 S31: 0.2919 S32: 0.0723 S33: 0.0842 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (CHAIN 'A' AND RESID 7 THROUGH 414) REMARK 3 ORIGIN FOR THE GROUP (A): 20.1594 1.9517 25.0286 REMARK 3 T TENSOR REMARK 3 T11: 0.5620 T22: 0.2012 REMARK 3 T33: 0.4120 T12: -0.0086 REMARK 3 T13: 0.0272 T23: -0.0079 REMARK 3 L TENSOR REMARK 3 L11: 0.5303 L22: 0.2587 REMARK 3 L33: 1.0913 L12: 0.1322 REMARK 3 L13: -0.1001 L23: -0.2301 REMARK 3 S TENSOR REMARK 3 S11: 0.0097 S12: -0.0469 S13: 0.1227 REMARK 3 S21: 0.1197 S22: -0.0039 S23: -0.0444 REMARK 3 S31: -0.1105 S32: 0.0961 S33: -0.0078 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: (CHAIN 'B' AND RESID 3 THROUGH 128) REMARK 3 ORIGIN FOR THE GROUP (A): 18.1543 -34.4423 10.6718 REMARK 3 T TENSOR REMARK 3 T11: 0.7577 T22: 0.2416 REMARK 3 T33: 0.4345 T12: 0.0218 REMARK 3 T13: -0.0040 T23: -0.0198 REMARK 3 L TENSOR REMARK 3 L11: 1.6433 L22: 1.6719 REMARK 3 L33: 2.0403 L12: -1.3723 REMARK 3 L13: -0.6123 L23: 0.8975 REMARK 3 S TENSOR REMARK 3 S11: -0.0930 S12: 0.0535 S13: -0.0110 REMARK 3 S21: 0.1213 S22: 0.1590 S23: -0.2146 REMARK 3 S31: 0.4583 S32: -0.0697 S33: -0.0551 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 9G9P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-JUL-24. REMARK 100 THE DEPOSITION ID IS D_1292140441. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 28-SEP-22 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 3.8 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I24 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.6702 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X CDTE 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2 REMARK 200 DATA SCALING SOFTWARE : DIALS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20557 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800 REMARK 200 RESOLUTION RANGE LOW (A) : 36.020 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 6.800 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.2 REMARK 200 DATA REDUNDANCY IN SHELL : 7.00 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.800 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 (%): 54.15 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, GLYCINE, TRIETHYLENE REMARK 280 GLYCOL, E. COLI POLAR LIPIDS, MONOOLEIN, PH 3.8, LIPIDIC CUBIC REMARK 280 PHASE, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -X,Y,-Z+1/2 REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 X+1/2,-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 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 51.04350 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 51.04350 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 41.94200 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 95.84050 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 41.94200 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 95.84050 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 51.04350 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 41.94200 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 95.84050 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 51.04350 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 41.94200 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 95.84050 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 MET A 0 REMARK 465 VAL A 1 REMARK 465 SER A 2 REMARK 465 LEU A 3 REMARK 465 ALA A 4 REMARK 465 LYS A 5 REMARK 465 ARG A 415 REMARK 465 ALA A 416 REMARK 465 LEU A 417 REMARK 465 GLU A 418 REMARK 465 GLU A 419 REMARK 465 ASN A 420 REMARK 465 LEU A 421 REMARK 465 TYR A 422 REMARK 465 PHE A 423 REMARK 465 GLN A 424 REMARK 465 MET B -1 REMARK 465 ALA B 0 REMARK 465 HIS B 129 REMARK 465 HIS B 130 REMARK 465 HIS B 131 REMARK 465 HIS B 132 REMARK 465 HIS B 133 REMARK 465 HIS B 134 REMARK 465 GLU B 135 REMARK 465 PRO B 136 REMARK 465 GLU B 137 REMARK 465 ALA B 138 REMARK 465 MET C -1 REMARK 465 ALA C 0 REMARK 465 GLN C 1 REMARK 465 HIS C 125 REMARK 465 HIS C 126 REMARK 465 HIS C 127 REMARK 465 HIS C 128 REMARK 465 HIS C 129 REMARK 465 HIS C 130 REMARK 465 GLU C 131 REMARK 465 PRO C 132 REMARK 465 GLU C 133 REMARK 465 ALA C 134 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 ASP A 144 75.10 -111.42 REMARK 500 THR A 230 -95.86 -116.72 REMARK 500 TYR A 246 -88.62 -130.64 REMARK 500 SER A 273 -69.38 -105.14 REMARK 500 LEU A 323 -140.96 -114.53 REMARK 500 PRO B 41 107.89 -58.09 REMARK 500 VAL B 48 -65.75 -127.90 REMARK 500 SER B 54 -92.47 -113.63 REMARK 500 PRO C 41 106.94 -58.58 REMARK 500 ASN C 84 -72.40 -112.11 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 9G95 RELATED DB: PDB REMARK 900 RELATED ID: 9G97 RELATED DB: PDB REMARK 900 RELATED ID: 9G9M RELATED DB: PDB REMARK 900 RELATED ID: 9G9N RELATED DB: PDB REMARK 900 RELATED ID: 9G9O RELATED DB: PDB DBREF 9G9P A 2 416 UNP P0AAA7 WZXE_ECOLI 2 416 DBREF 9G9P B -1 138 PDB 9G9P 9G9P -1 138 DBREF 9G9P C -1 134 PDB 9G9P 9G9P -1 134 SEQADV 9G9P MET A 0 UNP P0AAA7 INITIATING METHIONINE SEQADV 9G9P VAL A 1 UNP P0AAA7 CLONING ARTIFACT SEQADV 9G9P LEU A 417 UNP P0AAA7 EXPRESSION TAG SEQADV 9G9P GLU A 418 UNP P0AAA7 EXPRESSION TAG SEQADV 9G9P GLU A 419 UNP P0AAA7 EXPRESSION TAG SEQADV 9G9P ASN A 420 UNP P0AAA7 EXPRESSION TAG SEQADV 9G9P LEU A 421 UNP P0AAA7 EXPRESSION TAG SEQADV 9G9P TYR A 422 UNP P0AAA7 EXPRESSION TAG SEQADV 9G9P PHE A 423 UNP P0AAA7 EXPRESSION TAG SEQADV 9G9P GLN A 424 UNP P0AAA7 EXPRESSION TAG SEQRES 1 A 425 MET VAL SER LEU ALA LYS ALA SER LEU TRP THR ALA ALA SEQRES 2 A 425 SER THR LEU VAL LYS ILE GLY ALA GLY LEU LEU VAL GLY SEQRES 3 A 425 LYS LEU LEU ALA VAL SER PHE GLY PRO ALA GLY LEU GLY SEQRES 4 A 425 LEU ALA ALA ASN PHE ARG GLN LEU ILE THR VAL LEU GLY SEQRES 5 A 425 VAL LEU ALA GLY ALA GLY ILE PHE ASN GLY VAL THR LYS SEQRES 6 A 425 TYR VAL ALA GLN TYR HIS ASP ASN PRO GLN GLN LEU ARG SEQRES 7 A 425 ARG VAL VAL GLY THR SER SER ALA MET VAL LEU GLY PHE SEQRES 8 A 425 SER THR LEU MET ALA LEU VAL PHE VAL LEU ALA ALA ALA SEQRES 9 A 425 PRO ILE SER GLN GLY LEU PHE GLY ASN THR ASP TYR GLN SEQRES 10 A 425 GLY LEU VAL ARG LEU VAL ALA LEU VAL GLN MET GLY ILE SEQRES 11 A 425 ALA TRP GLY ASN LEU LEU LEU ALA LEU MET LYS GLY PHE SEQRES 12 A 425 ARG ASP ALA ALA GLY ASN ALA LEU SER LEU ILE VAL GLY SEQRES 13 A 425 SER LEU ILE GLY VAL LEU ALA TYR TYR VAL SER TYR ARG SEQRES 14 A 425 LEU GLY GLY TYR GLU GLY ALA LEU LEU GLY LEU ALA LEU SEQRES 15 A 425 ILE PRO ALA LEU VAL VAL ILE PRO ALA ALA ILE MET LEU SEQRES 16 A 425 ILE LYS ARG GLY VAL ILE PRO LEU SER TYR LEU LYS PRO SEQRES 17 A 425 SER TRP ASP ASN GLY LEU ALA GLY GLN LEU SER LYS PHE SEQRES 18 A 425 THR LEU MET ALA LEU ILE THR SER VAL THR LEU PRO VAL SEQRES 19 A 425 ALA TYR ILE MET MET ARG LYS LEU LEU ALA ALA GLN TYR SEQRES 20 A 425 SER TRP ASP GLU VAL GLY ILE TRP GLN GLY VAL SER SER SEQRES 21 A 425 ILE SER ASP ALA TYR LEU GLN PHE ILE THR ALA SER PHE SEQRES 22 A 425 SER VAL TYR LEU LEU PRO THR LEU SER ARG LEU THR GLU SEQRES 23 A 425 LYS ARG ASP ILE THR ARG GLU VAL VAL LYS SER LEU LYS SEQRES 24 A 425 PHE VAL LEU PRO ALA VAL ALA ALA ALA SER PHE THR VAL SEQRES 25 A 425 TRP LEU LEU ARG ASP PHE ALA ILE TRP LEU LEU LEU SER SEQRES 26 A 425 ASN LYS PHE THR ALA MET ARG ASP LEU PHE ALA TRP GLN SEQRES 27 A 425 LEU VAL GLY ASP VAL LEU LYS VAL GLY ALA TYR VAL PHE SEQRES 28 A 425 GLY TYR LEU VAL ILE ALA LYS ALA SER LEU ARG PHE TYR SEQRES 29 A 425 ILE LEU ALA GLU VAL SER GLN PHE THR LEU LEU MET VAL SEQRES 30 A 425 PHE ALA HIS TRP LEU ILE PRO ALA HIS GLY ALA LEU GLY SEQRES 31 A 425 ALA ALA GLN ALA TYR MET ALA THR TYR ILE VAL TYR PHE SEQRES 32 A 425 SER LEU CYS CYS GLY VAL PHE LEU LEU TRP ARG ARG ARG SEQRES 33 A 425 ALA LEU GLU GLU ASN LEU TYR PHE GLN SEQRES 1 B 140 MET ALA GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU SEQRES 2 B 140 VAL GLN ALA GLY GLY SER LEU GLY LEU SER CYS ALA ALA SEQRES 3 B 140 SER GLY ARG THR PHE SER ASN TYR VAL MET ALA TRP PHE SEQRES 4 B 140 ARG GLN ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ARG SEQRES 5 B 140 ILE SER GLU SER ARG GLY THR THR ASP TYR ALA ASP SER SEQRES 6 B 140 VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS SEQRES 7 B 140 ASN THR ILE TYR LEU GLN MET ASN SER LEU ASN PRO GLY SEQRES 8 B 140 ASP THR ALA VAL TYR SER CYS ALA ALA THR LEU PRO ALA SEQRES 9 B 140 TRP THR GLY ILE ILE GLY GLY ARG ARG PRO GLY ASN TYR SEQRES 10 B 140 PRO TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER SEQRES 11 B 140 HIS HIS HIS HIS HIS HIS GLU PRO GLU ALA SEQRES 1 C 136 MET ALA GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU SEQRES 2 C 136 VAL GLN ALA GLY ASP SER LEU THR LEU SER CYS ALA ALA SEQRES 3 C 136 SER GLY ARG THR ALA TYR ARG TYR GLY MET GLY TRP PHE SEQRES 4 C 136 ARG GLN HIS PRO GLY LYS GLU ARG GLU PHE VAL ALA SER SEQRES 5 C 136 ILE TRP TRP THR GLY THR THR THR TYR TYR ALA ASP SER SEQRES 6 C 136 VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASP VAL LYS SEQRES 7 C 136 ASN MET VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU SEQRES 8 C 136 ASP THR ALA VAL TYR TYR CYS ALA ALA LYS PHE TYR GLY SEQRES 9 C 136 GLY ASN SER LYS ARG PRO GLY ASP TYR ALA TYR TRP GLY SEQRES 10 C 136 GLN GLY THR GLN VAL THR VAL SER SER HIS HIS HIS HIS SEQRES 11 C 136 HIS HIS GLU PRO GLU ALA HELIX 1 AA1 ALA A 6 LEU A 53 1 48 HELIX 2 AA2 ALA A 54 GLY A 57 5 4 HELIX 3 AA3 ILE A 58 TYR A 69 1 12 HELIX 4 AA4 ASN A 72 ALA A 101 1 30 HELIX 5 AA5 ALA A 101 GLY A 111 1 11 HELIX 6 AA6 TYR A 115 PHE A 142 1 28 HELIX 7 AA7 ASP A 144 GLY A 171 1 28 HELIX 8 AA8 GLY A 171 LEU A 185 1 15 HELIX 9 AA9 VAL A 186 GLY A 198 1 13 HELIX 10 AB1 PRO A 201 LYS A 206 5 6 HELIX 11 AB2 ASP A 210 VAL A 229 1 20 HELIX 12 AB3 THR A 230 TYR A 246 1 17 HELIX 13 AB4 SER A 247 PHE A 272 1 26 HELIX 14 AB5 LEU A 276 LEU A 283 1 8 HELIX 15 AB6 GLU A 285 LEU A 314 1 30 HELIX 16 AB7 LEU A 314 LEU A 323 1 10 HELIX 17 AB8 SER A 324 ARG A 331 5 8 HELIX 18 AB9 ASP A 332 LYS A 357 1 26 HELIX 19 AC1 SER A 359 GLY A 386 1 28 HELIX 20 AC2 GLY A 386 ARG A 414 1 29 HELIX 21 AC3 THR B 28 TYR B 32 5 5 HELIX 22 AC4 ASN B 87 THR B 91 5 5 HELIX 23 AC5 LEU B 100 GLY B 105 1 6 HELIX 24 AC6 ARG B 111 TYR B 115 5 5 HELIX 25 AC7 THR C 28 TYR C 30 5 3 HELIX 26 AC8 LYS C 87 THR C 91 5 5 HELIX 27 AC9 ARG C 107 TYR C 111 5 5 SHEET 1 AA1 4 GLN B 3 GLY B 8 0 SHEET 2 AA1 4 SER B 17 SER B 25 -1 O ALA B 23 N VAL B 5 SHEET 3 AA1 4 THR B 78 ASN B 84 -1 O MET B 83 N LEU B 18 SHEET 4 AA1 4 PHE B 68 ASP B 73 -1 N SER B 71 O TYR B 80 SHEET 1 AA2 6 GLY B 10 VAL B 12 0 SHEET 2 AA2 6 THR B 122 VAL B 126 1 O THR B 125 N GLY B 10 SHEET 3 AA2 6 ALA B 92 THR B 99 -1 N TYR B 94 O THR B 122 SHEET 4 AA2 6 VAL B 33 GLN B 39 -1 N VAL B 33 O THR B 99 SHEET 5 AA2 6 GLU B 46 ILE B 51 -1 O GLU B 46 N ARG B 38 SHEET 6 AA2 6 THR B 58 TYR B 60 -1 O ASP B 59 N ARG B 50 SHEET 1 AA3 4 GLY B 10 VAL B 12 0 SHEET 2 AA3 4 THR B 122 VAL B 126 1 O THR B 125 N GLY B 10 SHEET 3 AA3 4 ALA B 92 THR B 99 -1 N TYR B 94 O THR B 122 SHEET 4 AA3 4 TYR B 117 TRP B 118 -1 O TYR B 117 N ALA B 98 SHEET 1 AA4 4 GLN C 3 SER C 7 0 SHEET 2 AA4 4 LEU C 18 SER C 25 -1 O ALA C 23 N VAL C 5 SHEET 3 AA4 4 MET C 78 MET C 83 -1 O MET C 83 N LEU C 18 SHEET 4 AA4 4 THR C 69 ASP C 73 -1 N THR C 69 O GLN C 82 SHEET 1 AA5 6 GLY C 10 VAL C 12 0 SHEET 2 AA5 6 THR C 118 VAL C 122 1 O THR C 121 N VAL C 12 SHEET 3 AA5 6 ALA C 92 PHE C 100 -1 N TYR C 94 O THR C 118 SHEET 4 AA5 6 TYR C 32 GLN C 39 -1 N PHE C 37 O TYR C 95 SHEET 5 AA5 6 ARG C 45 ILE C 51 -1 O ALA C 49 N TRP C 36 SHEET 6 AA5 6 THR C 58 TYR C 60 -1 O TYR C 59 N SER C 50 SHEET 1 AA6 4 GLY C 10 VAL C 12 0 SHEET 2 AA6 4 THR C 118 VAL C 122 1 O THR C 121 N VAL C 12 SHEET 3 AA6 4 ALA C 92 PHE C 100 -1 N TYR C 94 O THR C 118 SHEET 4 AA6 4 TYR C 113 TRP C 114 -1 O TYR C 113 N ALA C 98 SSBOND 1 CYS B 22 CYS B 96 1555 1555 2.04 SSBOND 2 CYS C 22 CYS C 96 1555 1555 2.04 CRYST1 83.884 191.681 102.087 90.00 90.00 90.00 C 2 2 21 8 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 0.011921 0.000000 0.000000 0.00000 SCALE2 0.000000 0.005217 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009796 0.00000