| content |
HEADER HYDROLASE 27-JUN-24 9CFJ
TITLE FLUVIRUCIN THIOESTERASE DOMAIN (FLUC TE)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FLUC;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ACTINOMADURA VULGARIS;
SOURCE 3 ORGANISM_TAXID: 1233071;
SOURCE 4 GENE: FLUC;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS THIOESTERASE DOMAIN, NATURAL PRODUCTS, PKS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.CHOUDHARY,J.L.SMITH
REVDAT 1 18-SEP-24 9CFJ 0
JRNL AUTH T.M.MCCULLOUGH,V.CHOUDHARY,D.L.AKEY,M.A.SKIBA,S.M.BERNARD,
JRNL AUTH 2 J.D.KITTENDORF,J.J.SCHMIDT,D.H.SHERMAN,J.L.SMITH
JRNL TITL SUBSTRATE TRAPPING IN POLYKETIDE SYNTHASE THIOESTERASE
JRNL TITL 2 DOMAINS: STRUCTURAL BASIS FOR MACROLACTONE FORMATION
JRNL REF ACS CATALYSIS V. 14 2024
JRNL REFN ESSN 2155-5435
JRNL DOI 10.1021/ACSCATAL.4C03637
REMARK 2
REMARK 2 RESOLUTION. 1.44 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.21_5207
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.44
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.32
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 88675
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.157
REMARK 3 R VALUE (WORKING SET) : 0.156
REMARK 3 FREE R VALUE : 0.184
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.890
REMARK 3 FREE R VALUE TEST SET COUNT : 4339
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 38.3200 - 4.4700 1.00 2989 122 0.1615 0.1778
REMARK 3 2 4.4700 - 3.5500 1.00 2881 147 0.1435 0.1512
REMARK 3 3 3.5500 - 3.1000 1.00 2873 131 0.1559 0.1693
REMARK 3 4 3.1000 - 2.8200 1.00 2841 146 0.1559 0.1871
REMARK 3 5 2.8200 - 2.6100 1.00 2849 140 0.1536 0.1920
REMARK 3 6 2.6100 - 2.4600 1.00 2826 138 0.1489 0.1968
REMARK 3 7 2.4600 - 2.3400 1.00 2826 154 0.1433 0.1734
REMARK 3 8 2.3400 - 2.2400 1.00 2795 157 0.1314 0.1728
REMARK 3 9 2.2400 - 2.1500 1.00 2848 142 0.1319 0.1624
REMARK 3 10 2.1500 - 2.0800 1.00 2803 142 0.1342 0.1817
REMARK 3 11 2.0800 - 2.0100 1.00 2808 121 0.1305 0.1520
REMARK 3 12 2.0100 - 1.9500 1.00 2835 141 0.1254 0.1633
REMARK 3 13 1.9500 - 1.9000 1.00 2837 132 0.1319 0.1544
REMARK 3 14 1.9000 - 1.8500 1.00 2772 164 0.1346 0.1673
REMARK 3 15 1.8500 - 1.8100 1.00 2787 168 0.1297 0.1687
REMARK 3 16 1.8100 - 1.7700 1.00 2802 156 0.1321 0.1697
REMARK 3 17 1.7700 - 1.7400 1.00 2787 150 0.1353 0.1767
REMARK 3 18 1.7400 - 1.7100 1.00 2858 128 0.1360 0.2301
REMARK 3 19 1.7100 - 1.6800 1.00 2795 140 0.1499 0.1847
REMARK 3 20 1.6800 - 1.6500 1.00 2814 117 0.2463 0.2883
REMARK 3 21 1.6500 - 1.6200 1.00 2784 133 0.2255 0.2556
REMARK 3 22 1.6200 - 1.6000 1.00 2846 137 0.2054 0.2360
REMARK 3 23 1.6000 - 1.5700 1.00 2752 169 0.1988 0.2545
REMARK 3 24 1.5700 - 1.5500 1.00 2795 163 0.2111 0.2439
REMARK 3 25 1.5500 - 1.5300 1.00 2809 143 0.2370 0.2476
REMARK 3 26 1.5300 - 1.5100 1.00 2762 161 0.2850 0.3085
REMARK 3 27 1.5100 - 1.4900 1.00 2775 163 0.3255 0.3078
REMARK 3 28 1.4900 - 1.4700 1.00 2775 153 0.4275 0.4383
REMARK 3 29 1.4700 - 1.4600 1.00 2796 146 0.5055 0.5495
REMARK 3 30 1.4600 - 1.4400 0.93 2616 135 0.6091 0.5974
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) : 0.248
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.652
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.61
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.76
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 : 0.005 2495
REMARK 3 ANGLE : 0.750 3414
REMARK 3 CHIRALITY : 0.075 348
REMARK 3 PLANARITY : 0.006 473
REMARK 3 DIHEDRAL : 14.879 966
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 9CFJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUN-24.
REMARK 100 THE DEPOSITION ID IS D_1000285333.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-JUL-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.033
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 88675
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.440
REMARK 200 RESOLUTION RANGE LOW (A) : 38.320
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 19.70
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 26.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.44
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.53
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM ACETATE, 30% (V/V) PEG
REMARK 280 400, 100 MM MES PH 6.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A2720 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2740 LIES ON A SPECIAL POSITION.
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLN A 2380 N CA C O CB CG CD
REMARK 480 GLN A 2380 OE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 2502 O HOH A 2725 2.03
REMARK 500 O HOH A 2540 O HOH A 2552 2.06
REMARK 500 O HOH A 2669 O HOH A 2836 2.07
REMARK 500 O HOH A 2572 O HOH A 2752 2.11
REMARK 500 O HOH A 2711 O HOH A 2755 2.13
REMARK 500 O HOH A 2503 O HOH A 2744 2.13
REMARK 500 O HOH A 2540 O HOH A 2756 2.14
REMARK 500 O HOH A 2672 O HOH A 2755 2.18
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 OCS A2243 -129.57 55.80
REMARK 500 ASP A2277 30.58 -93.54
REMARK 500 GLU A2372 -112.54 -112.35
REMARK 500 LYS A2387 87.35 -151.82
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 1PE A 2401
DBREF 9CFJ A 2114 2389 UNP K4I6L4 K4I6L4_9ACTN 2114 2389
SEQRES 1 A 276 GLY GLY SER LEU SER SER LEU VAL ARG ALA ALA ALA PRO
SEQRES 2 A 276 ALA GLY LYS LEU GLN GLU GLY LEU ASP MET LEU GLU ALA
SEQRES 3 A 276 ALA ALA ARG LEU ARG PRO GLY PHE ARG THR LEU ASP GLU
SEQRES 4 A 276 LEU ASP ARG ALA TYR PRO PRO LEU ALA LEU ALA SER GLY
SEQRES 5 A 276 PRO ALA ARG PRO LYS LEU PHE CYS PHE SER THR PRO MET
SEQRES 6 A 276 ALA LEU GLY GLY ALA ALA GLN PHE ALA ARG LEU ALA VAL
SEQRES 7 A 276 HIS PHE GLN GLY VAL ARG ASP LEU TYR ALA LEU GLN VAL
SEQRES 8 A 276 PRO GLY TYR ALA PRO ASP ASP SER LEU PRO ASP ASN VAL
SEQRES 9 A 276 ASP VAL VAL VAL ARG MET TRP ALA GLU SER ILE ARG GLU
SEQRES 10 A 276 ALA ALA GLY ASP ASP PRO PHE VAL VAL MET GLY TYR OCS
SEQRES 11 A 276 GLY GLY GLY ASN PHE ALA HIS ALA ALA VAL SER TYR LEU
SEQRES 12 A 276 GLU ARG ASN GLY VAL ARG PRO GLU GLY LEU ILE LEU LEU
SEQRES 13 A 276 ASP THR PHE LEU PRO ASP SER ASP VAL ILE ASP GLU LEU
SEQRES 14 A 276 GLY GLY GLN MET LEU GLU GLY MET PHE ASP ARG ALA GLU
SEQRES 15 A 276 VAL TYR GLY PRO PHE SER ASP THR ARG MET THR ALA MET
SEQRES 16 A 276 GLY ARG TYR TYR ARG LEU PHE ARG GLU THR VAL VAL GLU
SEQRES 17 A 276 ASP ILE GLU THR PRO VAL LEU PHE LEU ARG PRO ASP THR
SEQRES 18 A 276 PRO LEU PRO SER GLY PRO ASP GLY GLU ARG SER ARG GLU
SEQRES 19 A 276 GLY ASN TRP ARG ALA SER TRP HIS LEU LYS HIS ASP LEU
SEQRES 20 A 276 CYS GLU VAL ARG GLY ASP HIS LEU THR MET LEU GLU GLY
SEQRES 21 A 276 GLU ALA GLY SER ILE ALA GLN ALA VAL GLU GLU TRP LEU
SEQRES 22 A 276 LYS PRO SER
MODRES 9CFJ OCS A 2243 CYS MODIFIED RESIDUE
HET OCS A2243 9
HET 1PE A2401 8
HET 1PE A2402 16
HET GOL A2403 6
HET GOL A2404 6
HET GOL A2405 6
HETNAM OCS CYSTEINESULFONIC ACID
HETNAM 1PE PENTAETHYLENE GLYCOL
HETNAM GOL GLYCEROL
HETSYN 1PE PEG400
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 OCS C3 H7 N O5 S
FORMUL 2 1PE 2(C10 H22 O6)
FORMUL 4 GOL 3(C3 H8 O3)
FORMUL 7 HOH *375(H2 O)
HELIX 1 AA1 SER A 2116 ALA A 2125 1 10
HELIX 2 AA2 LYS A 2129 ARG A 2142 1 14
HELIX 3 AA3 THR A 2149 LEU A 2153 5 5
HELIX 4 AA4 GLY A 2182 HIS A 2192 1 11
HELIX 5 AA5 ASN A 2216 GLY A 2233 1 18
HELIX 6 AA6 OCS A 2243 ASN A 2259 1 17
HELIX 7 AA7 ASP A 2277 ASP A 2292 1 16
HELIX 8 AA8 ARG A 2293 GLY A 2298 1 6
HELIX 9 AA9 SER A 2301 THR A 2318 1 18
HELIX 10 AB1 LEU A 2368 GLU A 2372 5 5
HELIX 11 AB2 GLU A 2374 LYS A 2387 1 14
SHEET 1 AA1 2 GLY A2146 PHE A2147 0
SHEET 2 AA1 2 LEU A2213 PRO A2214 1 O LEU A2213 N PHE A2147
SHEET 1 AA2 7 LEU A2160 PRO A2166 0
SHEET 2 AA2 7 ARG A2197 ALA A2201 -1 O ALA A2201 N LEU A2160
SHEET 3 AA2 7 LYS A2170 PHE A2174 1 N LEU A2171 O TYR A2200
SHEET 4 AA2 7 PHE A2237 TYR A2242 1 O MET A2240 N PHE A2174
SHEET 5 AA2 7 GLY A2265 LEU A2269 1 O ILE A2267 N VAL A2239
SHEET 6 AA2 7 VAL A2327 PRO A2332 1 O LEU A2330 N LEU A2268
SHEET 7 AA2 7 ASP A2359 VAL A2363 1 O ASP A2359 N PHE A2329
LINK C TYR A2242 N OCS A2243 1555 1555 1.34
LINK C OCS A2243 N GLY A2244 1555 1555 1.34
CISPEP 1 ARG A 2168 PRO A 2169 0 -2.53
CISPEP 2 ARG A 2168 PRO A 2169 0 1.85
CISPEP 3 GLY A 2298 PRO A 2299 0 -0.23
CRYST1 132.752 132.752 48.493 90.00 90.00 120.00 P 3 2 1 6
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 0.007533 0.004349 0.000000 0.00000
SCALE2 0.000000 0.008698 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020622 0.00000
TER 2378 SER A2389
MASTER 288 0 6 11 9 0 0 6 2540 1 53 22
END |