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HEADER HYDROLASE 05-JUN-24 8ZRO
TITLE ARABIDOPSIS CARBOXYLESTERASE CXE15
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: STRIGOLACTONES HYDROLASE CXE15;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CARBOXYLESTERASE 15,ATCXE15;
COMPND 5 EC: 3.1.1.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: THALE CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: CXE15, AT5G06570, F15M7.10;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 866768
KEYWDS CATABOLIC ENZYME, CXE15, STRIGOLACTOONE, CARBOXYLESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.T.AROLD,U.F.S.HAMEED
REVDAT 1 28-MAY-25 8ZRO 0
JRNL AUTH S.T.AROLD,U.F.S.HAMEED
JRNL TITL ARABIDOPSIS CARBOXYLESTERASE CXE15
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.09 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) : 3.09
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.70
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 70.2
REMARK 3 NUMBER OF REFLECTIONS : 8666
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.284
REMARK 3 R VALUE (WORKING SET) : 0.278
REMARK 3 FREE R VALUE : 0.339
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 867
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 49.7000 - 5.6100 1.00 1943 214 0.2407 0.3124
REMARK 3 2 5.6100 - 4.4600 1.00 1866 213 0.2786 0.3228
REMARK 3 3 4.4500 - 3.8900 1.00 1828 206 0.3049 0.3724
REMARK 3 4 3.8900 - 3.5400 0.65 1197 129 0.3463 0.3929
REMARK 3 5 3.5400 - 3.2800 0.34 618 67 0.3642 0.3786
REMARK 3 6 3.2800 - 3.0900 0.19 347 38 0.3827 0.4212
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) : 0.450
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 40.560
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 : 0.005 4889
REMARK 3 ANGLE : 1.048 6630
REMARK 3 CHIRALITY : 0.056 709
REMARK 3 PLANARITY : 0.009 871
REMARK 3 DIHEDRAL : 5.837 652
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 8ZRO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-JUN-24.
REMARK 100 THE DEPOSITION ID IS D_1300048425.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-DEC-22
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 : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.987
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8670
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.090
REMARK 200 RESOLUTION RANGE LOW (A) : 49.750
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 19.20
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.09
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.6
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 : 1.200
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: AF-Q9FG13-F1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 MSODIUM ACETATE TRIHYDRATE, 20%
REMARK 280 W/V PEG 3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 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+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 76.10733
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 38.05367
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 38.05367
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 76.10733
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: 2090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24510 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 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 GLN A 9
REMARK 465 VAL A 10
REMARK 465 GLU A 30
REMARK 465 SER A 31
REMARK 465 ILE A 32
REMARK 465 ASP A 33
REMARK 465 LEU A 34
REMARK 465 ILE A 35
REMARK 465 THR A 36
REMARK 465 GLN A 37
REMARK 465 GLN A 38
REMARK 465 ILE A 39
REMARK 465 PRO A 40
REMARK 465 PHE A 41
REMARK 465 LYS A 42
REMARK 465 GLU B 30
REMARK 465 SER B 31
REMARK 465 ILE B 32
REMARK 465 ASP B 33
REMARK 465 LEU B 34
REMARK 465 ILE B 35
REMARK 465 THR B 36
REMARK 465 GLN B 37
REMARK 465 GLN B 38
REMARK 465 ILE B 39
REMARK 465 PRO B 40
REMARK 465 PHE B 41
REMARK 465 LYS B 42
REMARK 465 ASN B 72
REMARK 465 ARG B 73
REMARK 465 THR B 74
REMARK 465 ALA B 75
REMARK 465 LEU B 76
REMARK 465 PRO B 77
REMARK 465 SER B 184
REMARK 465 GLY B 185
REMARK 465 SER B 186
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 ILE B 320 OD1 ASP B 323 1.29
REMARK 500 CE1 PHE B 182 OE1 GLU B 188 1.78
REMARK 500 O LEU A 189 O VAL A 192 1.80
REMARK 500 OG1 THR B 156 OD1 ASP B 159 1.83
REMARK 500 CD1 PHE B 182 OE1 GLU B 188 1.96
REMARK 500 NH2 ARG B 181 OE2 GLU B 188 1.99
REMARK 500 CG1 VAL B 158 N ASP B 161 2.11
REMARK 500 O ALA B 143 O SER B 145 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 GLY A 24 N - CA - C ANGL. DEV. = -17.5 DEGREES
REMARK 500 THR A 25 N - CA - CB ANGL. DEV. = 15.6 DEGREES
REMARK 500 ALA A 179 N - CA - C ANGL. DEV. = -23.4 DEGREES
REMARK 500 LEU A 189 N - CA - C ANGL. DEV. = -16.6 DEGREES
REMARK 500 SER B 145 CB - CA - C ANGL. DEV. = 17.9 DEGREES
REMARK 500 SER B 145 N - CA - C ANGL. DEV. = -37.9 DEGREES
REMARK 500 ASP B 159 N - CA - C ANGL. DEV. = -24.7 DEGREES
REMARK 500 LEU B 220 CB - CA - C ANGL. DEV. = -13.9 DEGREES
REMARK 500 LEU B 221 N - CA - CB ANGL. DEV. = 12.1 DEGREES
REMARK 500 SER B 306 CB - CA - C ANGL. DEV. = -22.8 DEGREES
REMARK 500 ASN B 307 N - CA - CB ANGL. DEV. = 16.4 DEGREES
REMARK 500 ASN B 307 N - CA - C ANGL. DEV. = -30.1 DEGREES
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 THR A 25 128.63 -176.27
REMARK 500 GLN A 45 -146.99 54.69
REMARK 500 THR A 46 -2.93 66.57
REMARK 500 THR A 74 -161.37 -163.27
REMARK 500 TRP A 94 151.05 -49.76
REMARK 500 ALA A 143 -60.38 -96.40
REMARK 500 ASP A 146 -125.37 44.28
REMARK 500 ASN A 149 -15.89 69.83
REMARK 500 ASP A 154 126.58 -39.65
REMARK 500 SER A 169 -118.44 49.93
REMARK 500 LEU A 178 -9.55 82.82
REMARK 500 SER A 186 -0.28 74.82
REMARK 500 ILE A 187 101.81 -0.83
REMARK 500 ASN A 211 -59.26 -1.87
REMARK 500 LEU A 220 -61.08 -93.22
REMARK 500 LEU A 255 -42.07 72.23
REMARK 500 SER A 310 5.61 55.46
REMARK 500 MET B 15 14.71 57.66
REMARK 500 VAL B 26 113.89 73.92
REMARK 500 THR B 46 -163.96 -129.04
REMARK 500 VAL B 47 167.52 60.55
REMARK 500 ILE B 68 -53.00 72.46
REMARK 500 TRP B 94 150.96 -49.44
REMARK 500 HIS B 150 9.54 54.88
REMARK 500 TRP B 151 -73.10 -127.33
REMARK 500 SER B 169 -118.69 50.36
REMARK 500 LEU B 189 53.32 32.36
REMARK 500 THR B 210 -90.52 -117.39
REMARK 500 ASN B 211 -37.74 -134.05
REMARK 500 LEU B 220 -15.93 72.70
REMARK 500 MET B 244 0.97 81.85
REMARK 500 ALA B 245 -58.04 -132.05
REMARK 500 SER B 306 36.20 38.62
REMARK 500 TYR B 308 62.94 20.84
REMARK 500 SER B 310 13.11 55.83
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG B 162 0.08 SIDE CHAIN
REMARK 500 ARG B 193 0.23 SIDE CHAIN
REMARK 500 ARG B 209 0.29 SIDE CHAIN
REMARK 500 ARG B 319 0.29 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 8ZR6 RELATED DB: PDB
DBREF 8ZRO A 9 329 UNP Q9FG13 CXE15_ARATH 9 329
DBREF 8ZRO B 9 329 UNP Q9FG13 CXE15_ARATH 9 329
SEQRES 1 A 321 GLN VAL ALA GLU ASP CYS MET GLY LEU LEU GLN LEU LEU
SEQRES 2 A 321 SER ASN GLY THR VAL LEU ARG SER GLU SER ILE ASP LEU
SEQRES 3 A 321 ILE THR GLN GLN ILE PRO PHE LYS ASN ASN GLN THR VAL
SEQRES 4 A 321 LEU PHE LYS ASP SER ILE TYR HIS LYS PRO ASN ASN LEU
SEQRES 5 A 321 HIS LEU ARG LEU TYR LYS PRO ILE SER ALA SER ASN ARG
SEQRES 6 A 321 THR ALA LEU PRO VAL VAL VAL PHE PHE HIS GLY GLY GLY
SEQRES 7 A 321 PHE CYS PHE GLY SER ARG SER TRP PRO HIS PHE HIS ASN
SEQRES 8 A 321 PHE CYS LEU THR LEU ALA SER SER LEU ASN ALA LEU VAL
SEQRES 9 A 321 VAL SER PRO ASP TYR ARG LEU ALA PRO GLU HIS ARG LEU
SEQRES 10 A 321 PRO ALA ALA PHE GLU ASP ALA GLU ALA VAL LEU THR TRP
SEQRES 11 A 321 LEU TRP ASP GLN ALA VAL SER ASP GLY VAL ASN HIS TRP
SEQRES 12 A 321 PHE GLU ASP GLY THR ASP VAL ASP PHE ASP ARG VAL PHE
SEQRES 13 A 321 VAL VAL GLY ASP SER SER GLY GLY ASN ILE ALA HIS GLN
SEQRES 14 A 321 LEU ALA VAL ARG PHE GLY SER GLY SER ILE GLU LEU THR
SEQRES 15 A 321 PRO VAL ARG VAL ARG GLY TYR VAL LEU MET GLY PRO PHE
SEQRES 16 A 321 PHE GLY GLY GLU GLU ARG THR ASN SER GLU ASN GLY PRO
SEQRES 17 A 321 SER GLU ALA LEU LEU SER LEU ASP LEU LEU ASP LYS PHE
SEQRES 18 A 321 TRP ARG LEU SER LEU PRO ASN GLY ALA THR ARG ASP HIS
SEQRES 19 A 321 HIS MET ALA ASN PRO PHE GLY PRO THR SER PRO THR LEU
SEQRES 20 A 321 GLU SER ILE SER LEU GLU PRO MET LEU VAL ILE VAL GLY
SEQRES 21 A 321 GLY SER GLU LEU LEU ARG ASP ARG ALA LYS GLU TYR ALA
SEQRES 22 A 321 TYR LYS LEU LYS LYS MET GLY GLY LYS ARG VAL ASP TYR
SEQRES 23 A 321 ILE GLU PHE GLU ASN LYS GLU HIS GLY PHE TYR SER ASN
SEQRES 24 A 321 TYR PRO SER SER GLU ALA ALA GLU GLN VAL LEU ARG ILE
SEQRES 25 A 321 ILE GLY ASP PHE MET ASN ASN LEU SER
SEQRES 1 B 321 GLN VAL ALA GLU ASP CYS MET GLY LEU LEU GLN LEU LEU
SEQRES 2 B 321 SER ASN GLY THR VAL LEU ARG SER GLU SER ILE ASP LEU
SEQRES 3 B 321 ILE THR GLN GLN ILE PRO PHE LYS ASN ASN GLN THR VAL
SEQRES 4 B 321 LEU PHE LYS ASP SER ILE TYR HIS LYS PRO ASN ASN LEU
SEQRES 5 B 321 HIS LEU ARG LEU TYR LYS PRO ILE SER ALA SER ASN ARG
SEQRES 6 B 321 THR ALA LEU PRO VAL VAL VAL PHE PHE HIS GLY GLY GLY
SEQRES 7 B 321 PHE CYS PHE GLY SER ARG SER TRP PRO HIS PHE HIS ASN
SEQRES 8 B 321 PHE CYS LEU THR LEU ALA SER SER LEU ASN ALA LEU VAL
SEQRES 9 B 321 VAL SER PRO ASP TYR ARG LEU ALA PRO GLU HIS ARG LEU
SEQRES 10 B 321 PRO ALA ALA PHE GLU ASP ALA GLU ALA VAL LEU THR TRP
SEQRES 11 B 321 LEU TRP ASP GLN ALA VAL SER ASP GLY VAL ASN HIS TRP
SEQRES 12 B 321 PHE GLU ASP GLY THR ASP VAL ASP PHE ASP ARG VAL PHE
SEQRES 13 B 321 VAL VAL GLY ASP SER SER GLY GLY ASN ILE ALA HIS GLN
SEQRES 14 B 321 LEU ALA VAL ARG PHE GLY SER GLY SER ILE GLU LEU THR
SEQRES 15 B 321 PRO VAL ARG VAL ARG GLY TYR VAL LEU MET GLY PRO PHE
SEQRES 16 B 321 PHE GLY GLY GLU GLU ARG THR ASN SER GLU ASN GLY PRO
SEQRES 17 B 321 SER GLU ALA LEU LEU SER LEU ASP LEU LEU ASP LYS PHE
SEQRES 18 B 321 TRP ARG LEU SER LEU PRO ASN GLY ALA THR ARG ASP HIS
SEQRES 19 B 321 HIS MET ALA ASN PRO PHE GLY PRO THR SER PRO THR LEU
SEQRES 20 B 321 GLU SER ILE SER LEU GLU PRO MET LEU VAL ILE VAL GLY
SEQRES 21 B 321 GLY SER GLU LEU LEU ARG ASP ARG ALA LYS GLU TYR ALA
SEQRES 22 B 321 TYR LYS LEU LYS LYS MET GLY GLY LYS ARG VAL ASP TYR
SEQRES 23 B 321 ILE GLU PHE GLU ASN LYS GLU HIS GLY PHE TYR SER ASN
SEQRES 24 B 321 TYR PRO SER SER GLU ALA ALA GLU GLN VAL LEU ARG ILE
SEQRES 25 B 321 ILE GLY ASP PHE MET ASN ASN LEU SER
HELIX 1 AA1 TRP A 94 ASN A 109 1 16
HELIX 2 AA2 PRO A 126 GLN A 142 1 17
HELIX 3 AA3 SER A 170 GLN A 177 1 8
HELIX 4 AA4 THR A 210 GLY A 215 1 6
HELIX 5 AA5 SER A 222 LEU A 234 1 13
HELIX 6 AA6 LEU A 273 MET A 287 1 15
HELIX 7 AA7 GLY A 303 TYR A 308 1 6
HELIX 8 AA8 SER A 311 LEU A 328 1 18
HELIX 9 AA9 TRP B 94 LEU B 108 1 15
HELIX 10 AB1 PRO B 126 VAL B 144 1 19
HELIX 11 AB2 SER B 170 PHE B 182 1 13
HELIX 12 AB3 SER B 222 LEU B 234 1 13
HELIX 13 AB4 LEU B 273 GLY B 288 1 16
HELIX 14 AB5 SER B 311 ASN B 327 1 17
SHEET 1 AA111 GLU A 12 CYS A 14 0
SHEET 2 AA111 LEU A 18 LEU A 20 -1 O LEU A 20 N GLU A 12
SHEET 3 AA111 VAL A 26 ARG A 28 -1 O LEU A 27 N GLN A 19
SHEET 4 AA111 LEU B 48 HIS B 55 -1 O ASP B 51 N ARG A 28
SHEET 5 AA111 LEU B 60 LYS B 66 -1 O LEU B 64 N LYS B 50
SHEET 6 AA111 VAL B 112 PRO B 115 -1 O SER B 114 N ARG B 63
SHEET 7 AA111 VAL B 79 PHE B 82 1 N VAL B 79 O VAL B 113
SHEET 8 AA111 VAL B 163 ASP B 168 1 O VAL B 166 N VAL B 80
SHEET 9 AA111 VAL B 194 MET B 200 1 O VAL B 198 N VAL B 165
SHEET 10 AA111 MET B 263 GLY B 268 1 O LEU B 264 N LEU B 199
SHEET 11 AA111 VAL B 292 PHE B 297 1 O ASP B 293 N VAL B 265
SHEET 1 AA211 VAL A 292 PHE A 297 0
SHEET 2 AA211 MET A 263 GLY A 268 1 N VAL A 265 O ASP A 293
SHEET 3 AA211 VAL A 194 MET A 200 1 N LEU A 199 O LEU A 264
SHEET 4 AA211 ASP A 157 ASP A 168 1 N VAL A 163 O ARG A 195
SHEET 5 AA211 ALA A 75 PHE A 82 1 N LEU A 76 O ASP A 157
SHEET 6 AA211 LEU A 111 PRO A 115 1 O LEU A 111 N VAL A 79
SHEET 7 AA211 LEU A 60 PRO A 67 -1 N ARG A 63 O SER A 114
SHEET 8 AA211 VAL A 47 HIS A 55 -1 N LEU A 48 O LYS A 66
SHEET 9 AA211 LEU B 27 ARG B 28 -1 O ARG B 28 N ASP A 51
SHEET 10 AA211 LEU B 18 LEU B 21 -1 N GLN B 19 O LEU B 27
SHEET 11 AA211 VAL B 10 CYS B 14 -1 N ALA B 11 O LEU B 20
CISPEP 1 ALA A 120 PRO A 121 0 -2.27
CISPEP 2 LEU A 125 PRO A 126 0 8.25
CISPEP 3 THR A 190 PRO A 191 0 6.62
CISPEP 4 GLY A 249 PRO A 250 0 -9.14
CISPEP 5 ALA B 120 PRO B 121 0 -2.08
CISPEP 6 LEU B 125 PRO B 126 0 7.10
CRYST1 99.399 99.399 114.161 90.00 90.00 120.00 P 32 2 1 12
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 0.010060 0.005808 0.000000 0.00000
SCALE2 0.000000 0.011617 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008760 0.00000
TER 2407 SER A 329
TER 4768 SER B 329
MASTER 370 0 0 14 22 0 0 6 4766 2 0 50
END |