HEADER TRANSPORT PROTEIN 25-JUL-24 9G9O TITLE LIPID III FLIPPASE WZXE WITH NB10 AND NB7 NANOBODIES IN OUTWARD-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 9G9O 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. 2.69 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) : 2.69 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.50 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 3 NUMBER OF REFLECTIONS : 26804 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.282 REMARK 3 R VALUE (WORKING SET) : 0.279 REMARK 3 FREE R VALUE : 0.338 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.830 REMARK 3 FREE R VALUE TEST SET COUNT : 1295 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 38.5000 - 5.5900 1.00 3012 176 0.2280 0.2615 REMARK 3 2 5.5900 - 4.4400 0.98 2835 145 0.2745 0.3942 REMARK 3 3 4.4400 - 3.8800 0.99 2838 134 0.2777 0.3292 REMARK 3 4 3.8800 - 3.5200 1.00 2813 162 0.2515 0.3134 REMARK 3 5 3.5200 - 3.2700 1.00 2830 141 0.2916 0.3747 REMARK 3 6 3.2700 - 3.0800 1.00 2845 120 0.3153 0.3501 REMARK 3 7 3.0800 - 2.9200 1.00 2813 159 0.3407 0.3936 REMARK 3 8 2.9200 - 2.8000 1.00 2784 129 0.3561 0.4130 REMARK 3 9 2.8000 - 2.6900 0.98 2739 129 0.3801 0.3883 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) : 0.530 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.540 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 5221 REMARK 3 ANGLE : 0.451 7098 REMARK 3 CHIRALITY : 0.035 811 REMARK 3 PLANARITY : 0.004 881 REMARK 3 DIHEDRAL : 3.755 734 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: (CHAIN 'A' AND RESID 1 THROUGH 414) REMARK 3 ORIGIN FOR THE GROUP (A): -4.6211 -34.6703 -46.4057 REMARK 3 T TENSOR REMARK 3 T11: 0.3634 T22: 0.2938 REMARK 3 T33: 0.3998 T12: 0.0013 REMARK 3 T13: 0.0315 T23: 0.0129 REMARK 3 L TENSOR REMARK 3 L11: 0.9364 L22: 0.7700 REMARK 3 L33: 0.9206 L12: -0.1642 REMARK 3 L13: 0.1805 L23: -0.1653 REMARK 3 S TENSOR REMARK 3 S11: -0.1087 S12: -0.0596 S13: -0.0950 REMARK 3 S21: 0.0853 S22: 0.1245 S23: 0.0700 REMARK 3 S31: -0.1149 S32: -0.0741 S33: -0.0153 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (CHAIN 'B' AND RESID 2 THROUGH 127) REMARK 3 ORIGIN FOR THE GROUP (A): -7.1460 -5.9632 -13.0028 REMARK 3 T TENSOR REMARK 3 T11: 0.5642 T22: 0.3530 REMARK 3 T33: 0.3358 T12: 0.0055 REMARK 3 T13: -0.0705 T23: 0.0027 REMARK 3 L TENSOR REMARK 3 L11: 4.2843 L22: 4.1301 REMARK 3 L33: 5.5310 L12: -1.3184 REMARK 3 L13: -2.5813 L23: 2.4463 REMARK 3 S TENSOR REMARK 3 S11: -0.0353 S12: 0.1339 S13: -0.0369 REMARK 3 S21: -0.2854 S22: 0.1137 S23: -0.0882 REMARK 3 S31: 0.3123 S32: 0.2168 S33: -0.1214 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: (CHAIN 'C' AND RESID 2 THROUGH 124) REMARK 3 ORIGIN FOR THE GROUP (A): 5.1049 -53.6130 -6.0493 REMARK 3 T TENSOR REMARK 3 T11: 0.5857 T22: 0.3090 REMARK 3 T33: 0.4831 T12: 0.0623 REMARK 3 T13: 0.0022 T23: -0.0042 REMARK 3 L TENSOR REMARK 3 L11: 2.2613 L22: 2.7678 REMARK 3 L33: 6.4389 L12: 0.2261 REMARK 3 L13: 0.8959 L23: -0.2350 REMARK 3 S TENSOR REMARK 3 S11: -0.0125 S12: -0.2784 S13: 0.2839 REMARK 3 S21: 0.7549 S22: 0.2335 S23: 0.1762 REMARK 3 S31: -0.2420 S32: -0.0953 S33: -0.1942 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 9G9O 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_1292140429. 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 : 5 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 : 26959 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.690 REMARK 200 RESOLUTION RANGE LOW (A) : 39.270 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 6.700 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 4.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.69 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.73 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3 REMARK 200 DATA REDUNDANCY IN SHELL : 6.90 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.400 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 (%): 59.93 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.07 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE, LITHIUM SULFATE, REMARK 280 SODIUM CHLORIDE, PEG300, E. COLI POLAR LIPIDS, MONOOLEIN, PH 5, REMARK 280 LIPIDIC CUBIC 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 144.04250 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 144.04250 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 21.16750 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 77.00950 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 21.16750 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 77.00950 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 144.04250 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 21.16750 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 77.00950 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 144.04250 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 21.16750 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 77.00950 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 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 SER B 128 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 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 ALA A 101 40.57 -98.46 REMARK 500 VAL A 229 -40.74 -133.70 REMARK 500 THR A 230 -75.57 -58.10 REMARK 500 TYR A 246 -148.51 -138.06 REMARK 500 TYR A 275 -53.45 -122.14 REMARK 500 LEU A 321 -69.75 -103.30 REMARK 500 THR A 328 2.05 -65.09 REMARK 500 LYS B 43 -156.16 -121.56 REMARK 500 VAL B 48 -68.29 -123.42 REMARK 500 PRO C 41 100.80 -58.18 REMARK 500 VAL C 48 -67.61 -120.06 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 DBREF 9G9O A 2 416 UNP P0AAA7 WZXE_ECOLI 2 416 DBREF 9G9O B -1 138 PDB 9G9O 9G9O -1 138 DBREF 9G9O C -1 134 PDB 9G9O 9G9O -1 134 SEQADV 9G9O MET A 0 UNP P0AAA7 INITIATING METHIONINE SEQADV 9G9O VAL A 1 UNP P0AAA7 CLONING ARTIFACT SEQADV 9G9O LEU A 417 UNP P0AAA7 EXPRESSION TAG SEQADV 9G9O GLU A 418 UNP P0AAA7 EXPRESSION TAG SEQADV 9G9O GLU A 419 UNP P0AAA7 EXPRESSION TAG SEQADV 9G9O ASN A 420 UNP P0AAA7 EXPRESSION TAG SEQADV 9G9O LEU A 421 UNP P0AAA7 EXPRESSION TAG SEQADV 9G9O TYR A 422 UNP P0AAA7 EXPRESSION TAG SEQADV 9G9O PHE A 423 UNP P0AAA7 EXPRESSION TAG SEQADV 9G9O 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 SER A 2 ALA A 40 1 39 HELIX 2 AA2 ALA A 40 ALA A 54 1 15 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 PHE A 110 1 10 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 ARG A 197 1 12 HELIX 10 AB1 PRO A 201 LYS A 206 5 6 HELIX 11 AB2 ASP A 210 SER A 228 1 19 HELIX 12 AB3 VAL A 229 TYR A 246 1 18 HELIX 13 AB4 SER A 247 SER A 273 1 27 HELIX 14 AB5 TYR A 275 LEU A 283 1 9 HELIX 15 AB6 GLU A 285 LEU A 314 1 30 HELIX 16 AB7 LEU A 314 LEU A 321 1 8 HELIX 17 AB8 PHE A 327 ARG A 331 5 5 HELIX 18 AB9 ASP A 332 LYS A 357 1 26 HELIX 19 AC1 SER A 359 ARG A 414 1 56 HELIX 20 AC2 THR B 28 TYR B 32 5 5 HELIX 21 AC3 ASN B 87 THR B 91 5 5 HELIX 22 AC4 LEU B 100 GLY B 105 1 6 HELIX 23 AC5 ARG B 111 TYR B 115 5 5 HELIX 24 AC6 THR C 28 TYR C 30 5 3 HELIX 25 AC7 ASP C 62 LYS C 65 5 4 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 LEU B 4 SER B 7 0 SHEET 2 AA1 4 LEU B 18 ALA B 24 -1 O SER B 21 N SER B 7 SHEET 3 AA1 4 THR B 78 MET B 83 -1 O MET B 83 N LEU B 18 SHEET 4 AA1 4 PHE B 68 ASP B 73 -1 N THR B 69 O GLN B 82 SHEET 1 AA2 6 LEU B 11 VAL B 12 0 SHEET 2 AA2 6 THR B 122 VAL B 126 1 O THR B 125 N VAL B 12 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 ALA B 49 N TRP B 36 SHEET 6 AA2 6 THR B 58 TYR B 60 -1 O ASP B 59 N ARG B 50 SHEET 1 AA3 4 LEU B 11 VAL B 12 0 SHEET 2 AA3 4 THR B 122 VAL B 126 1 O THR B 125 N VAL B 12 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 VAL C 2 SER C 7 0 SHEET 2 AA4 4 LEU C 18 GLY C 26 -1 O ALA C 23 N VAL C 5 SHEET 3 AA4 4 MET C 78 MET C 83 -1 O VAL C 79 N CYS C 22 SHEET 4 AA4 4 PHE C 68 ASP C 73 -1 N SER C 71 O TYR C 80 SHEET 1 AA5 6 GLY C 10 GLN C 13 0 SHEET 2 AA5 6 THR C 118 SER C 123 1 O THR C 121 N GLY C 10 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 GLN C 13 0 SHEET 2 AA6 4 THR C 118 SER C 123 1 O THR C 121 N GLY C 10 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 2.03 SSBOND 2 CYS C 22 CYS C 96 1555 1555 2.03 CRYST1 42.335 154.019 288.085 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 0.023621 0.000000 0.000000 0.00000 SCALE2 0.000000 0.006493 0.000000 0.00000 SCALE3 0.000000 0.000000 0.003471 0.00000