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HEADER BIOSYNTHETIC PROTEIN 19-JAN-21 7DXO
TITLE THE MUTANT OF BIFUNCTIONAL THIOESTERASE CATALYZING EPIMERIZATION AND
TITLE 2 CYCLIZATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NON-RIBOSOMAL PEPTIDE SYNTHETASE 4;
COMPND 3 CHAIN: A, B, C;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES ABIETIS;
SOURCE 3 ORGANISM_TAXID: 1227734;
SOURCE 4 GENE: NRPS4;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS HYDROLASE FOLD, THIOESTERASE, EPIMERIZATION, CYCLIZATION,
KEYWDS 2 BIOSYNTHETIC PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.H.YU,J.SONG,C.B.CHI,M.MA
REVDAT 1 26-JAN-22 7DXO 0
JRNL AUTH J.H.YU,J.SONG,C.B.CHI,M.MA
JRNL TITL THE FUNCTIONAL CHARACTERIZATION AND CRYSTAL STRUCTURE OF THE
JRNL TITL 2 BIFUNCTIONAL THIOESTERASE CATALYZING EPIMERIZATION AND
JRNL TITL 3 CYCLIZATION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.17.1_3660
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 5.22
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 33113
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.226
REMARK 3 R VALUE (WORKING SET) : 0.223
REMARK 3 FREE R VALUE : 0.280
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1987
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 27.1300 - 5.7700 0.98 2325 140 0.1884 0.1883
REMARK 3 2 5.7700 - 4.5900 0.98 2250 142 0.1959 0.2267
REMARK 3 3 4.5800 - 4.0100 0.98 2180 143 0.1843 0.2185
REMARK 3 4 4.0100 - 3.6400 0.98 2251 141 0.1913 0.2407
REMARK 3 5 3.6400 - 3.3800 0.99 2201 143 0.2089 0.2635
REMARK 3 6 3.3800 - 3.1800 0.99 2210 146 0.2390 0.2769
REMARK 3 7 3.1800 - 3.0200 1.00 2241 142 0.2471 0.4116
REMARK 3 8 3.0200 - 2.8900 1.00 2235 134 0.2494 0.3620
REMARK 3 9 2.8900 - 2.7800 1.00 2223 146 0.2568 0.2951
REMARK 3 10 2.7800 - 2.6800 1.00 2186 145 0.2376 0.3171
REMARK 3 11 2.6800 - 2.6000 1.00 2191 139 0.2383 0.2884
REMARK 3 12 2.6000 - 2.5300 1.00 2220 142 0.2475 0.3266
REMARK 3 13 2.5300 - 2.4600 1.00 2203 142 0.2643 0.3009
REMARK 3 14 2.4600 - 2.4000 0.99 2210 142 0.2901 0.3774
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) : 0.380
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.000
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.82
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
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 7DXO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-JAN-21.
REMARK 100 THE DEPOSITION ID IS D_1300020267.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-JAN-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.540562
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : RIGAKU HYPIX-6000HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSALISPRO
REMARK 200 DATA SCALING SOFTWARE : CRYSALISPRO
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33187
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 27.130
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 11.90
REMARK 200 R MERGE (I) : 0.12600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 25.3700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.23400
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: 7CRN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 60% V/V TACSIMATE, PH 7.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 289K
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 105.19850
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 105.19850
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 33.97950
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 58.79100
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 33.97950
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 58.79100
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 105.19850
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 33.97950
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 58.79100
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 105.19850
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 33.97950
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 58.79100
REMARK 290 SMTRY3 8 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 1740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 -67.95900
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -105.19850
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 C 310 LIES ON A SPECIAL POSITION.
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 1
REMARK 465 ASN A 2
REMARK 465 ALA A 3
REMARK 465 ASN A 4
REMARK 465 ASP A 5
REMARK 465 THR A 6
REMARK 465 ASP A 7
REMARK 465 LEU A 159
REMARK 465 GLY A 160
REMARK 465 ASP A 161
REMARK 465 GLU A 162
REMARK 465 THR A 276
REMARK 465 SER A 277
REMARK 465 LYS A 278
REMARK 465 SER B 1
REMARK 465 ASN B 2
REMARK 465 ALA B 3
REMARK 465 ASN B 4
REMARK 465 ASP B 5
REMARK 465 THR B 6
REMARK 465 ASP B 7
REMARK 465 LEU B 159
REMARK 465 GLY B 160
REMARK 465 ASP B 161
REMARK 465 GLU B 162
REMARK 465 THR B 276
REMARK 465 SER B 277
REMARK 465 LYS B 278
REMARK 465 SER C 1
REMARK 465 ASN C 2
REMARK 465 ALA C 3
REMARK 465 ASN C 4
REMARK 465 ASP C 5
REMARK 465 THR C 6
REMARK 465 ASP C 7
REMARK 465 LEU C 159
REMARK 465 GLY C 160
REMARK 465 ASP C 161
REMARK 465 GLU C 162
REMARK 465 THR C 276
REMARK 465 SER C 277
REMARK 465 LYS C 278
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 PRO A 31 -167.71 -75.02
REMARK 500 LEU A 60 -72.85 -96.97
REMARK 500 SER A 88 -144.05 -141.56
REMARK 500 ALA A 97 -120.01 61.94
REMARK 500 THR A 224 6.02 -64.55
REMARK 500 ARG B 18 107.35 -161.44
REMARK 500 PRO B 31 -168.10 -76.43
REMARK 500 LEU B 60 -67.97 -101.35
REMARK 500 SER B 88 -138.75 -154.42
REMARK 500 ALA B 97 -117.49 59.38
REMARK 500 ASP B 211 45.65 -85.82
REMARK 500 ARG C 18 113.64 -161.39
REMARK 500 PRO C 31 -162.28 -74.60
REMARK 500 LEU C 60 -74.52 -95.25
REMARK 500 SER C 88 -152.78 -146.95
REMARK 500 ALA C 97 -114.28 51.36
REMARK 500 ASP C 157 64.49 -69.44
REMARK 500 ASP C 211 40.21 -90.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE ALA206 IN THE SEQUENCE IS DIFFERENT NATURALLY TO THE PUBLISHED
REMARK 999 HOMOLOGUES (A0A1J0R317). SEQUENCE USED IN THIS STUDY WAS DERIVED
REMARK 999 FROM STREPTOMYCES STRAIN ISOLATED FROM A MARINE CORAL SAMPLE, WHICH
REMARK 999 HAS NOT BEEN DEPOSITED TO ANY DATABASE AT THE TIME OF DATA
REMARK 999 ANNOTATION.
DBREF1 7DXO A 4 278 UNP A0A1J0R317_STRSQ
DBREF2 7DXO A A0A1J0R317 3634 3908
DBREF1 7DXO B 4 278 UNP A0A1J0R317_STRSQ
DBREF2 7DXO B A0A1J0R317 3634 3908
DBREF1 7DXO C 4 278 UNP A0A1J0R317_STRSQ
DBREF2 7DXO C A0A1J0R317 3634 3908
SEQADV 7DXO SER A 1 UNP A0A1J0R31 EXPRESSION TAG
SEQADV 7DXO ASN A 2 UNP A0A1J0R31 EXPRESSION TAG
SEQADV 7DXO ALA A 3 UNP A0A1J0R31 EXPRESSION TAG
SEQADV 7DXO ALA A 97 UNP A0A1J0R31 SER 3727 ENGINEERED MUTATION
SEQADV 7DXO ALA A 206 UNP A0A1J0R31 ASP 3836 CONFLICT
SEQADV 7DXO SER B 1 UNP A0A1J0R31 EXPRESSION TAG
SEQADV 7DXO ASN B 2 UNP A0A1J0R31 EXPRESSION TAG
SEQADV 7DXO ALA B 3 UNP A0A1J0R31 EXPRESSION TAG
SEQADV 7DXO ALA B 97 UNP A0A1J0R31 SER 3727 ENGINEERED MUTATION
SEQADV 7DXO ALA B 206 UNP A0A1J0R31 ASP 3836 CONFLICT
SEQADV 7DXO SER C 1 UNP A0A1J0R31 EXPRESSION TAG
SEQADV 7DXO ASN C 2 UNP A0A1J0R31 EXPRESSION TAG
SEQADV 7DXO ALA C 3 UNP A0A1J0R31 EXPRESSION TAG
SEQADV 7DXO ALA C 97 UNP A0A1J0R31 SER 3727 ENGINEERED MUTATION
SEQADV 7DXO ALA C 206 UNP A0A1J0R31 ASP 3836 CONFLICT
SEQRES 1 A 278 SER ASN ALA ASN ASP THR ASP GLY ASP THR LEU ASP VAL
SEQRES 2 A 278 LEU LEU PRO LEU ARG THR THR GLY GLU LYS ALA PRO LEU
SEQRES 3 A 278 PHE CYS VAL HIS PRO ALA GLY GLY LEU SER TRP VAL TYR
SEQRES 4 A 278 SER GLY LEU MET GLN HIS ILE GLY ALA ASP ARG PRO LEU
SEQRES 5 A 278 TYR GLY LEU GLN ALA ARG GLY LEU ALA ASP PRO SER ALA
SEQRES 6 A 278 THR LEU PRO SER SER ILE GLU GLU MET ALA ALA ASP TYR
SEQRES 7 A 278 VAL THR GLN ILE ARG GLY VAL GLN PRO SER GLY PRO TYR
SEQRES 8 A 278 HIS LEU LEU GLY TRP ALA LEU GLY SER LEU VAL ILE HIS
SEQRES 9 A 278 ALA MET ALA THR GLN LEU ARG ALA GLU GLY GLU GLU VAL
SEQRES 10 A 278 GLY LEU LEU VAL ASN LEU ASP GLN TYR PRO ILE ASP ARG
SEQRES 11 A 278 SER ARG PRO ALA PRO GLU SER GLN PRO ASP GLN GLN ASP
SEQRES 12 A 278 ALA LEU ARG ILE MET LEU ASP PHE VAL GLY TYR ASP MET
SEQRES 13 A 278 ASP SER LEU GLY ASP GLU PRO LEU ASP TYR ALA MET VAL
SEQRES 14 A 278 ALA ASP VAL LEU ARG GLU ARG GLN SER VAL PHE ALA ASN
SEQRES 15 A 278 LEU ASP GLU THR ALA ILE THR ALA LEU ALA ASN VAL PHE
SEQRES 16 A 278 ALA ASN SER ARG SER LEU PHE GLY SER PHE ALA PRO GLN
SEQRES 17 A 278 PRO LEU ASP SER ASP VAL LEU VAL ILE VAL ALA GLU PRO
SEQRES 18 A 278 ASP GLU THR VAL PRO ALA ALA GLU LEU ALA ALA ARG VAL
SEQRES 19 A 278 GLU GLN TRP ARG PRO PHE VAL THR GLY LYS ILE GLU TYR
SEQRES 20 A 278 GLN THR VAL ARG CYS SER HIS PRO HIS MET MET GLN PRO
SEQRES 21 A 278 GLU PRO ALA ALA GLU ILE GLY ARG LEU ILE ALA GLU LYS
SEQRES 22 A 278 LEU GLY THR SER LYS
SEQRES 1 B 278 SER ASN ALA ASN ASP THR ASP GLY ASP THR LEU ASP VAL
SEQRES 2 B 278 LEU LEU PRO LEU ARG THR THR GLY GLU LYS ALA PRO LEU
SEQRES 3 B 278 PHE CYS VAL HIS PRO ALA GLY GLY LEU SER TRP VAL TYR
SEQRES 4 B 278 SER GLY LEU MET GLN HIS ILE GLY ALA ASP ARG PRO LEU
SEQRES 5 B 278 TYR GLY LEU GLN ALA ARG GLY LEU ALA ASP PRO SER ALA
SEQRES 6 B 278 THR LEU PRO SER SER ILE GLU GLU MET ALA ALA ASP TYR
SEQRES 7 B 278 VAL THR GLN ILE ARG GLY VAL GLN PRO SER GLY PRO TYR
SEQRES 8 B 278 HIS LEU LEU GLY TRP ALA LEU GLY SER LEU VAL ILE HIS
SEQRES 9 B 278 ALA MET ALA THR GLN LEU ARG ALA GLU GLY GLU GLU VAL
SEQRES 10 B 278 GLY LEU LEU VAL ASN LEU ASP GLN TYR PRO ILE ASP ARG
SEQRES 11 B 278 SER ARG PRO ALA PRO GLU SER GLN PRO ASP GLN GLN ASP
SEQRES 12 B 278 ALA LEU ARG ILE MET LEU ASP PHE VAL GLY TYR ASP MET
SEQRES 13 B 278 ASP SER LEU GLY ASP GLU PRO LEU ASP TYR ALA MET VAL
SEQRES 14 B 278 ALA ASP VAL LEU ARG GLU ARG GLN SER VAL PHE ALA ASN
SEQRES 15 B 278 LEU ASP GLU THR ALA ILE THR ALA LEU ALA ASN VAL PHE
SEQRES 16 B 278 ALA ASN SER ARG SER LEU PHE GLY SER PHE ALA PRO GLN
SEQRES 17 B 278 PRO LEU ASP SER ASP VAL LEU VAL ILE VAL ALA GLU PRO
SEQRES 18 B 278 ASP GLU THR VAL PRO ALA ALA GLU LEU ALA ALA ARG VAL
SEQRES 19 B 278 GLU GLN TRP ARG PRO PHE VAL THR GLY LYS ILE GLU TYR
SEQRES 20 B 278 GLN THR VAL ARG CYS SER HIS PRO HIS MET MET GLN PRO
SEQRES 21 B 278 GLU PRO ALA ALA GLU ILE GLY ARG LEU ILE ALA GLU LYS
SEQRES 22 B 278 LEU GLY THR SER LYS
SEQRES 1 C 278 SER ASN ALA ASN ASP THR ASP GLY ASP THR LEU ASP VAL
SEQRES 2 C 278 LEU LEU PRO LEU ARG THR THR GLY GLU LYS ALA PRO LEU
SEQRES 3 C 278 PHE CYS VAL HIS PRO ALA GLY GLY LEU SER TRP VAL TYR
SEQRES 4 C 278 SER GLY LEU MET GLN HIS ILE GLY ALA ASP ARG PRO LEU
SEQRES 5 C 278 TYR GLY LEU GLN ALA ARG GLY LEU ALA ASP PRO SER ALA
SEQRES 6 C 278 THR LEU PRO SER SER ILE GLU GLU MET ALA ALA ASP TYR
SEQRES 7 C 278 VAL THR GLN ILE ARG GLY VAL GLN PRO SER GLY PRO TYR
SEQRES 8 C 278 HIS LEU LEU GLY TRP ALA LEU GLY SER LEU VAL ILE HIS
SEQRES 9 C 278 ALA MET ALA THR GLN LEU ARG ALA GLU GLY GLU GLU VAL
SEQRES 10 C 278 GLY LEU LEU VAL ASN LEU ASP GLN TYR PRO ILE ASP ARG
SEQRES 11 C 278 SER ARG PRO ALA PRO GLU SER GLN PRO ASP GLN GLN ASP
SEQRES 12 C 278 ALA LEU ARG ILE MET LEU ASP PHE VAL GLY TYR ASP MET
SEQRES 13 C 278 ASP SER LEU GLY ASP GLU PRO LEU ASP TYR ALA MET VAL
SEQRES 14 C 278 ALA ASP VAL LEU ARG GLU ARG GLN SER VAL PHE ALA ASN
SEQRES 15 C 278 LEU ASP GLU THR ALA ILE THR ALA LEU ALA ASN VAL PHE
SEQRES 16 C 278 ALA ASN SER ARG SER LEU PHE GLY SER PHE ALA PRO GLN
SEQRES 17 C 278 PRO LEU ASP SER ASP VAL LEU VAL ILE VAL ALA GLU PRO
SEQRES 18 C 278 ASP GLU THR VAL PRO ALA ALA GLU LEU ALA ALA ARG VAL
SEQRES 19 C 278 GLU GLN TRP ARG PRO PHE VAL THR GLY LYS ILE GLU TYR
SEQRES 20 C 278 GLN THR VAL ARG CYS SER HIS PRO HIS MET MET GLN PRO
SEQRES 21 C 278 GLU PRO ALA ALA GLU ILE GLY ARG LEU ILE ALA GLU LYS
SEQRES 22 C 278 LEU GLY THR SER LYS
FORMUL 4 HOH *191(H2 O)
HELIX 1 AA1 SER A 36 MET A 43 5 8
HELIX 2 AA2 SER A 70 GLN A 86 1 17
HELIX 3 AA3 ALA A 97 GLU A 113 1 17
HELIX 4 AA4 ASP A 140 VAL A 152 1 13
HELIX 5 AA5 ASP A 165 GLN A 177 1 13
HELIX 6 AA6 SER A 178 ALA A 181 5 4
HELIX 7 AA7 ASP A 184 PHE A 202 1 19
HELIX 8 AA8 PRO A 226 GLU A 235 1 10
HELIX 9 AA9 GLN A 236 ARG A 238 5 3
HELIX 10 AB1 SER A 253 MET A 257 5 5
HELIX 11 AB2 GLN A 259 GLY A 275 1 17
HELIX 12 AB3 SER B 36 MET B 43 5 8
HELIX 13 AB4 SER B 70 GLN B 86 1 17
HELIX 14 AB5 ALA B 97 GLU B 113 1 17
HELIX 15 AB6 ASP B 140 VAL B 152 1 13
HELIX 16 AB7 ASP B 165 GLN B 177 1 13
HELIX 17 AB8 ASP B 184 PHE B 202 1 19
HELIX 18 AB9 PRO B 226 GLU B 235 1 10
HELIX 19 AC1 GLN B 236 ARG B 238 5 3
HELIX 20 AC2 SER B 253 MET B 257 5 5
HELIX 21 AC3 GLN B 259 GLY B 275 1 17
HELIX 22 AC4 SER C 36 MET C 43 5 8
HELIX 23 AC5 SER C 70 GLN C 86 1 17
HELIX 24 AC6 ALA C 97 GLU C 113 1 17
HELIX 25 AC7 ASP C 140 VAL C 152 1 13
HELIX 26 AC8 ASP C 165 GLN C 177 1 13
HELIX 27 AC9 ASP C 184 PHE C 202 1 19
HELIX 28 AD1 PRO C 226 GLU C 235 1 10
HELIX 29 AD2 GLN C 236 ARG C 238 5 3
HELIX 30 AD3 SER C 253 MET C 257 5 5
HELIX 31 AD4 GLN C 259 GLY C 275 1 17
SHEET 1 AA1 7 LEU A 14 ARG A 18 0
SHEET 2 AA1 7 LEU A 52 LEU A 55 -1 O GLY A 54 N LEU A 15
SHEET 3 AA1 7 LEU A 26 VAL A 29 1 N CYS A 28 O TYR A 53
SHEET 4 AA1 7 PRO A 90 TRP A 96 1 O HIS A 92 N PHE A 27
SHEET 5 AA1 7 GLU A 116 LEU A 123 1 O GLU A 116 N TYR A 91
SHEET 6 AA1 7 VAL A 214 ALA A 219 1 O LEU A 215 N LEU A 120
SHEET 7 AA1 7 ILE A 245 VAL A 250 1 O GLU A 246 N VAL A 216
SHEET 1 AA2 7 LEU B 14 ARG B 18 0
SHEET 2 AA2 7 LEU B 52 LEU B 55 -1 O GLY B 54 N LEU B 15
SHEET 3 AA2 7 LEU B 26 VAL B 29 1 N CYS B 28 O TYR B 53
SHEET 4 AA2 7 TYR B 91 TRP B 96 1 O HIS B 92 N PHE B 27
SHEET 5 AA2 7 VAL B 117 LEU B 123 1 O LEU B 119 N LEU B 93
SHEET 6 AA2 7 VAL B 214 ALA B 219 1 O ILE B 217 N ASN B 122
SHEET 7 AA2 7 ILE B 245 VAL B 250 1 O GLN B 248 N VAL B 218
SHEET 1 AA3 7 LEU C 14 ARG C 18 0
SHEET 2 AA3 7 LEU C 52 LEU C 55 -1 O GLY C 54 N LEU C 15
SHEET 3 AA3 7 LEU C 26 VAL C 29 1 N CYS C 28 O TYR C 53
SHEET 4 AA3 7 TYR C 91 TRP C 96 1 O HIS C 92 N PHE C 27
SHEET 5 AA3 7 VAL C 117 LEU C 123 1 O VAL C 121 N LEU C 93
SHEET 6 AA3 7 VAL C 214 ALA C 219 1 O LEU C 215 N LEU C 120
SHEET 7 AA3 7 ILE C 245 VAL C 250 1 O GLU C 246 N VAL C 216
CRYST1 67.959 117.582 210.397 90.00 90.00 90.00 C 2 2 21 24
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 0.014715 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008505 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004753 0.00000
TER 2021 GLY A 275
TER 4042 GLY B 275
TER 6063 GLY C 275
MASTER 335 0 0 31 21 0 0 6 6251 3 0 66
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