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HEADER HYDROLASE 19-JUN-24 9CBD
TITLE PIKROMYCIN THIOESTERASE DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NARBONOLIDE/10-DEOXYMETHYNOLIDE SYNTHASE PIKA4, MODULE 6;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: NARBONOLIDE/10-DEOXYMETHYNOLIDE SYNTHASE PIKAIV,PIKROMYCIN
COMPND 5 POLYKETIDE SYNTHASE COMPONENT PIKAIV,PIKROMYCIN PKS COMPONENT PIKAIV,
COMPND 6 TYPE I MODULAR POLYKETIDE SYNTHASE PIKAIV,PKS;
COMPND 7 EC: 3.1.2.-;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES VENEZUELAE;
SOURCE 3 ORGANISM_TAXID: 54571;
SOURCE 4 GENE: PIKAIV;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS POLYKETIDE SYNTHASE, PKS, THIOESTERASE, TE, MACROLACTONIZATION,
KEYWDS 2 PIKROMYCIN, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.M.MCCULLOUGH,J.L.SMITH
REVDAT 1 18-SEP-24 9CBD 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 12551 2024
JRNL REFN ESSN 2155-5435
JRNL DOI 10.1021/ACSCATAL.4C03637
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.15.2_3472: ???)
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.04
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 92404
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.410
REMARK 3 FREE R VALUE TEST SET COUNT : 2230
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 48.0380 - 5.0379 1.00 5615 137 0.1582 0.1867
REMARK 3 2 5.0379 - 3.9994 0.99 5620 139 0.1526 0.1761
REMARK 3 3 3.9994 - 3.4940 1.00 5638 138 0.1665 0.1880
REMARK 3 4 3.4940 - 3.1746 1.00 5627 150 0.1975 0.2513
REMARK 3 5 3.1746 - 2.9471 1.00 5630 144 0.2000 0.2358
REMARK 3 6 2.9471 - 2.7734 1.00 5655 134 0.2165 0.2770
REMARK 3 7 2.7734 - 2.6345 0.99 5607 144 0.2235 0.2578
REMARK 3 8 2.6345 - 2.5198 1.00 5626 134 0.2303 0.2510
REMARK 3 9 2.5198 - 2.4228 1.00 5670 140 0.2358 0.2491
REMARK 3 10 2.4228 - 2.3392 1.00 5620 147 0.2387 0.2758
REMARK 3 11 2.3392 - 2.2661 1.00 5678 127 0.2453 0.2670
REMARK 3 12 2.2661 - 2.2013 1.00 5641 155 0.2719 0.3300
REMARK 3 13 2.2013 - 2.1433 1.00 5677 144 0.2905 0.2763
REMARK 3 14 2.1433 - 2.0910 1.00 5581 141 0.3052 0.3425
REMARK 3 15 2.0910 - 2.0435 1.00 5689 120 0.3131 0.3543
REMARK 3 16 2.0435 - 2.0000 1.00 5600 136 0.3211 0.3160
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
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) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.750
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 : 0.008 4300
REMARK 3 ANGLE : 0.871 5860
REMARK 3 CHIRALITY : 0.049 628
REMARK 3 PLANARITY : 0.006 794
REMARK 3 DIHEDRAL : 16.088 2544
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 9CBD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUN-24.
REMARK 100 THE DEPOSITION ID IS D_1000285012.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-MAR-23
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
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-B
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 EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48701
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 48.040
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 1.55000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.500
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 (%): 58.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2 M LITHIUM CHLORIDE, 25% W/V
REMARK 280 PEG4000, 100 MM HEPES, PH 8.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 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 29.28950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 57.02400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.96600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 57.02400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.28950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 52.96600
REMARK 290 SMTRY3 4 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23270 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
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 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 SER A 1054
REMARK 465 ASN A 1055
REMARK 465 ALA A 1056
REMARK 465 ARG A 1112
REMARK 465 ALA A 1113
REMARK 465 GLY A 1158
REMARK 465 THR A 1159
REMARK 465 GLY A 1160
REMARK 465 THR A 1161
REMARK 465 GLY A 1340
REMARK 465 ILE A 1341
REMARK 465 GLU A 1342
REMARK 465 GLY A 1343
REMARK 465 ALA A 1344
REMARK 465 GLY A 1345
REMARK 465 LYS A 1346
REMARK 465 SER B 1054
REMARK 465 ASN B 1055
REMARK 465 ALA B 1056
REMARK 465 ARG B 1112
REMARK 465 ALA B 1113
REMARK 465 GLY B 1158
REMARK 465 THR B 1159
REMARK 465 GLY B 1160
REMARK 465 THR B 1161
REMARK 465 GLY B 1340
REMARK 465 ILE B 1341
REMARK 465 GLU B 1342
REMARK 465 GLY B 1343
REMARK 465 ALA B 1344
REMARK 465 GLY B 1345
REMARK 465 LYS B 1346
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 NH2 ARG B 1321 O HOH B 1401 2.19
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 ASP A1101 108.65 -42.49
REMARK 500 SER A1196 -122.24 66.08
REMARK 500 TRP A1292 119.04 -160.70
REMARK 500 ARG A1321 -71.88 -98.40
REMARK 500 ALA B1095 0.95 -67.91
REMARK 500 LEU B1100 31.39 -92.09
REMARK 500 SER B1196 -121.91 59.26
REMARK 500 ALA B1301 157.40 -48.71
REMARK 500 ARG B1321 -93.99 -117.57
REMARK 500
REMARK 500 REMARK: NULL
DBREF 9CBD A 1057 1346 UNP Q9ZGI2 PIKA4_STRVZ 1057 1346
DBREF 9CBD B 1057 1346 UNP Q9ZGI2 PIKA4_STRVZ 1057 1346
SEQADV 9CBD SER A 1054 UNP Q9ZGI2 EXPRESSION TAG
SEQADV 9CBD ASN A 1055 UNP Q9ZGI2 EXPRESSION TAG
SEQADV 9CBD ALA A 1056 UNP Q9ZGI2 EXPRESSION TAG
SEQADV 9CBD SER B 1054 UNP Q9ZGI2 EXPRESSION TAG
SEQADV 9CBD ASN B 1055 UNP Q9ZGI2 EXPRESSION TAG
SEQADV 9CBD ALA B 1056 UNP Q9ZGI2 EXPRESSION TAG
SEQRES 1 A 293 SER ASN ALA ALA GLY MET PHE ARG ALA LEU PHE ARG GLN
SEQRES 2 A 293 ALA VAL GLU ASP ASP ARG TYR GLY GLU PHE LEU ASP VAL
SEQRES 3 A 293 LEU ALA GLU ALA SER ALA PHE ARG PRO GLN PHE ALA SER
SEQRES 4 A 293 PRO GLU ALA CYS SER GLU ARG LEU ASP PRO VAL LEU LEU
SEQRES 5 A 293 ALA GLY GLY PRO THR ASP ARG ALA GLU GLY ARG ALA VAL
SEQRES 6 A 293 LEU VAL GLY CYS THR GLY THR ALA ALA ASN GLY GLY PRO
SEQRES 7 A 293 HIS GLU PHE LEU ARG LEU SER THR SER PHE GLN GLU GLU
SEQRES 8 A 293 ARG ASP PHE LEU ALA VAL PRO LEU PRO GLY TYR GLY THR
SEQRES 9 A 293 GLY THR GLY THR GLY THR ALA LEU LEU PRO ALA ASP LEU
SEQRES 10 A 293 ASP THR ALA LEU ASP ALA GLN ALA ARG ALA ILE LEU ARG
SEQRES 11 A 293 ALA ALA GLY ASP ALA PRO VAL VAL LEU LEU GLY HIS SER
SEQRES 12 A 293 GLY GLY ALA LEU LEU ALA HIS GLU LEU ALA PHE ARG LEU
SEQRES 13 A 293 GLU ARG ALA HIS GLY ALA PRO PRO ALA GLY ILE VAL LEU
SEQRES 14 A 293 VAL ASP PRO TYR PRO PRO GLY HIS GLN GLU PRO ILE GLU
SEQRES 15 A 293 VAL TRP SER ARG GLN LEU GLY GLU GLY LEU PHE ALA GLY
SEQRES 16 A 293 GLU LEU GLU PRO MET SER ASP ALA ARG LEU LEU ALA MET
SEQRES 17 A 293 GLY ARG TYR ALA ARG PHE LEU ALA GLY PRO ARG PRO GLY
SEQRES 18 A 293 ARG SER SER ALA PRO VAL LEU LEU VAL ARG ALA SER GLU
SEQRES 19 A 293 PRO LEU GLY ASP TRP GLN GLU GLU ARG GLY ASP TRP ARG
SEQRES 20 A 293 ALA HIS TRP ASP LEU PRO HIS THR VAL ALA ASP VAL PRO
SEQRES 21 A 293 GLY ASP HIS PHE THR MET MET ARG ASP HIS ALA PRO ALA
SEQRES 22 A 293 VAL ALA GLU ALA VAL LEU SER TRP LEU ASP ALA ILE GLU
SEQRES 23 A 293 GLY ILE GLU GLY ALA GLY LYS
SEQRES 1 B 293 SER ASN ALA ALA GLY MET PHE ARG ALA LEU PHE ARG GLN
SEQRES 2 B 293 ALA VAL GLU ASP ASP ARG TYR GLY GLU PHE LEU ASP VAL
SEQRES 3 B 293 LEU ALA GLU ALA SER ALA PHE ARG PRO GLN PHE ALA SER
SEQRES 4 B 293 PRO GLU ALA CYS SER GLU ARG LEU ASP PRO VAL LEU LEU
SEQRES 5 B 293 ALA GLY GLY PRO THR ASP ARG ALA GLU GLY ARG ALA VAL
SEQRES 6 B 293 LEU VAL GLY CYS THR GLY THR ALA ALA ASN GLY GLY PRO
SEQRES 7 B 293 HIS GLU PHE LEU ARG LEU SER THR SER PHE GLN GLU GLU
SEQRES 8 B 293 ARG ASP PHE LEU ALA VAL PRO LEU PRO GLY TYR GLY THR
SEQRES 9 B 293 GLY THR GLY THR GLY THR ALA LEU LEU PRO ALA ASP LEU
SEQRES 10 B 293 ASP THR ALA LEU ASP ALA GLN ALA ARG ALA ILE LEU ARG
SEQRES 11 B 293 ALA ALA GLY ASP ALA PRO VAL VAL LEU LEU GLY HIS SER
SEQRES 12 B 293 GLY GLY ALA LEU LEU ALA HIS GLU LEU ALA PHE ARG LEU
SEQRES 13 B 293 GLU ARG ALA HIS GLY ALA PRO PRO ALA GLY ILE VAL LEU
SEQRES 14 B 293 VAL ASP PRO TYR PRO PRO GLY HIS GLN GLU PRO ILE GLU
SEQRES 15 B 293 VAL TRP SER ARG GLN LEU GLY GLU GLY LEU PHE ALA GLY
SEQRES 16 B 293 GLU LEU GLU PRO MET SER ASP ALA ARG LEU LEU ALA MET
SEQRES 17 B 293 GLY ARG TYR ALA ARG PHE LEU ALA GLY PRO ARG PRO GLY
SEQRES 18 B 293 ARG SER SER ALA PRO VAL LEU LEU VAL ARG ALA SER GLU
SEQRES 19 B 293 PRO LEU GLY ASP TRP GLN GLU GLU ARG GLY ASP TRP ARG
SEQRES 20 B 293 ALA HIS TRP ASP LEU PRO HIS THR VAL ALA ASP VAL PRO
SEQRES 21 B 293 GLY ASP HIS PHE THR MET MET ARG ASP HIS ALA PRO ALA
SEQRES 22 B 293 VAL ALA GLU ALA VAL LEU SER TRP LEU ASP ALA ILE GLU
SEQRES 23 B 293 GLY ILE GLU GLY ALA GLY LYS
FORMUL 3 HOH *305(H2 O)
HELIX 1 AA1 GLY A 1058 ASP A 1070 1 13
HELIX 2 AA2 ARG A 1072 ALA A 1085 1 14
HELIX 3 AA3 PHE A 1134 SER A 1140 1 7
HELIX 4 AA4 ASP A 1169 GLY A 1186 1 18
HELIX 5 AA5 SER A 1196 ALA A 1212 1 17
HELIX 6 AA6 GLN A 1231 TRP A 1237 1 7
HELIX 7 AA7 TRP A 1237 GLY A 1248 1 12
HELIX 8 AA8 SER A 1254 GLY A 1270 1 17
HELIX 9 AA9 GLN A 1293 GLY A 1297 5 5
HELIX 10 AB1 HIS A 1323 GLU A 1339 1 17
HELIX 11 AB2 GLY B 1058 ASP B 1070 1 13
HELIX 12 AB3 ARG B 1072 ALA B 1085 1 14
HELIX 13 AB4 SER B 1092 CYS B 1096 5 5
HELIX 14 AB5 PHE B 1134 SER B 1140 1 7
HELIX 15 AB6 ASP B 1169 GLY B 1186 1 18
HELIX 16 AB7 SER B 1196 GLY B 1214 1 19
HELIX 17 AB8 GLN B 1231 TRP B 1237 1 7
HELIX 18 AB9 TRP B 1237 GLY B 1248 1 12
HELIX 19 AC1 SER B 1254 GLY B 1270 1 17
HELIX 20 AC2 GLN B 1293 GLY B 1297 5 5
HELIX 21 AC3 PHE B 1317 ARG B 1321 5 5
HELIX 22 AC4 HIS B 1323 GLU B 1339 1 17
SHEET 1 AA1 2 GLN A1089 PHE A1090 0
SHEET 2 AA1 2 LEU A1166 PRO A1167 1 O LEU A1166 N PHE A1090
SHEET 1 AA2 7 VAL A1103 ALA A1106 0
SHEET 2 AA2 7 PHE A1147 VAL A1150 -1 O PHE A1147 N LEU A1105
SHEET 3 AA2 7 VAL A1118 CYS A1122 1 N GLY A1121 O LEU A1148
SHEET 4 AA2 7 VAL A1190 HIS A1195 1 O LEU A1193 N CYS A1122
SHEET 5 AA2 7 GLY A1219 VAL A1223 1 O VAL A1221 N LEU A1192
SHEET 6 AA2 7 VAL A1280 ALA A1285 1 O LEU A1281 N LEU A1222
SHEET 7 AA2 7 THR A1308 VAL A1312 1 O THR A1308 N LEU A1282
SHEET 1 AA3 2 GLN B1089 PHE B1090 0
SHEET 2 AA3 2 LEU B1166 PRO B1167 1 O LEU B1166 N PHE B1090
SHEET 1 AA4 7 VAL B1103 ALA B1106 0
SHEET 2 AA4 7 PHE B1147 VAL B1150 -1 O PHE B1147 N LEU B1105
SHEET 3 AA4 7 VAL B1118 CYS B1122 1 N GLY B1121 O LEU B1148
SHEET 4 AA4 7 VAL B1190 HIS B1195 1 O LEU B1193 N CYS B1122
SHEET 5 AA4 7 GLY B1219 VAL B1223 1 O VAL B1221 N LEU B1192
SHEET 6 AA4 7 VAL B1280 ALA B1285 1 O LEU B1281 N ILE B1220
SHEET 7 AA4 7 THR B1308 VAL B1312 1 O THR B1308 N LEU B1282
CRYST1 58.579 105.932 114.048 90.00 90.00 90.00 P 21 21 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 0.017071 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009440 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008768 0.00000
TER 2096 GLU A1339
TER 4192 GLU B1339
MASTER 283 0 0 22 18 0 0 6 4495 2 0 46
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