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HEADER HYDROLASE 03-OCT-10 3P2M
TITLE CRYSTAL STRUCTURE OF A NOVEL ESTERASE RV0045C FROM MYCOBACTERIUM
TITLE 2 TUBERCULOSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POSSIBLE HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HYDROLASE RV0045C, PUTATIVE UNCHARACTERIZED PROTEIN;
COMPND 5 EC: 3.-.-.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 GENE: RV0045C;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-28A
KEYWDS ALPHA/BETA HYDROLASE SUPERFAMILY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.D.ZHENG,J.GUO,L.XU,H.LI,D.ZHANG,K.ZHANG,F.SUN,T.WEN,S.LIU,H.PANG
REVDAT 1 06-JUL-11 3P2M 0
JRNL AUTH X.D.ZHENG,J.GUO,L.XU,H.LI,D.ZHANG,K.ZHANG,F.SUN,T.WEN,S.LIU,
JRNL AUTH 2 H.PANG
JRNL TITL CRYSTAL STRUCTURE OF A NOVEL ESTERASE RV0045C FROM
JRNL TITL 2 MYCOBACTERIUM TUBERCULOSIS
JRNL REF PLOS ONE V. 6 E2050 2011
JRNL REFN ESSN 1932-6203
JRNL PMID 21637775
JRNL DOI 10.1371/JOURNAL.PONE.0020506
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0072
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.35
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 6810
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.220
REMARK 3 R VALUE (WORKING SET) : 0.217
REMARK 3 FREE R VALUE : 0.286
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.700
REMARK 3 FREE R VALUE TEST SET COUNT : 336
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.88
REMARK 3 REFLECTION IN BIN (WORKING SET) : 522
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.82
REMARK 3 BIN R VALUE (WORKING SET) : 0.2650
REMARK 3 BIN FREE R VALUE SET COUNT : 18
REMARK 3 BIN FREE R VALUE : 0.4100
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2136
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 36
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 80.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.99000
REMARK 3 B22 (A**2) : 0.99000
REMARK 3 B33 (A**2) : -1.49000
REMARK 3 B12 (A**2) : 0.50000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.460
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.396
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.082
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.929
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.882
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2183 ; 0.013 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2973 ; 1.570 ; 1.944
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 279 ; 7.139 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 103 ;32.805 ;23.107
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 328 ;23.287 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 21 ;24.410 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 333 ; 0.098 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1701 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1388 ; 0.726 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2213 ; 1.359 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 795 ; 1.543 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 760 ; 2.740 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3P2M COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-OCT-10.
REMARK 100 THE RCSB ID CODE IS RCSB061878.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JUN-09
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 : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.07176
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 7159
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07900
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) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.39700
REMARK 200 FOR SHELL : 3.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M MAGNESIUM CHLORIDE, 100 MM TRIS-
REMARK 280 HCL, 30% PEG 4000, PH 8.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,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 16.02100
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 32.04200
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 MET A 1
REMARK 465 GLY A 2
REMARK 465 SER A 3
REMARK 465 SER A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 HIS A 8
REMARK 465 HIS A 9
REMARK 465 HIS A 10
REMARK 465 SER A 11
REMARK 465 SER A 12
REMARK 465 GLY A 13
REMARK 465 LEU A 14
REMARK 465 VAL A 15
REMARK 465 PRO A 16
REMARK 465 ARG A 17
REMARK 465 GLY A 18
REMARK 465 SER A 19
REMARK 465 HIS A 20
REMARK 465 MET A 21
REMARK 465 ALA A 22
REMARK 465 SER A 23
REMARK 465 MET A 24
REMARK 465 THR A 25
REMARK 465 GLY A 26
REMARK 465 GLY A 27
REMARK 465 GLN A 28
REMARK 465 GLN A 29
REMARK 465 MET A 30
REMARK 465 GLY A 31
REMARK 465 ARG A 32
REMARK 465 VAL A 33
REMARK 465 LEU A 34
REMARK 465 SER A 35
REMARK 465 ASP A 36
REMARK 465 ASP A 37
REMARK 465 GLN A 194
REMARK 465 ARG A 195
REMARK 465 GLY A 196
REMARK 465 THR A 197
REMARK 465 VAL A 198
REMARK 465 ALA A 199
REMARK 465 LEU A 200
REMARK 465 MET A 201
REMARK 465 HIS A 202
REMARK 465 GLY A 203
REMARK 465 GLU A 204
REMARK 465 ARG A 330
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 SER A 80 55.26 32.71
REMARK 500 ALA A 81 -151.92 -164.82
REMARK 500 GLN A 92 -168.47 -104.80
REMARK 500 SER A 154 -119.41 49.48
REMARK 500 ALA A 167 62.80 -156.30
REMARK 500 ALA A 192 7.70 -65.69
REMARK 500 ALA A 221 73.34 -150.39
REMARK 500 LEU A 327 29.33 -77.04
REMARK 500 ASP A 328 -5.54 64.25
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLU A 123 ASP A 124 148.31
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3P2M A 34 330 UNP P71702 P71702_MYCTU 2 298
SEQADV 3P2M MET A 1 UNP P71702 EXPRESSION TAG
SEQADV 3P2M GLY A 2 UNP P71702 EXPRESSION TAG
SEQADV 3P2M SER A 3 UNP P71702 EXPRESSION TAG
SEQADV 3P2M SER A 4 UNP P71702 EXPRESSION TAG
SEQADV 3P2M HIS A 5 UNP P71702 EXPRESSION TAG
SEQADV 3P2M HIS A 6 UNP P71702 EXPRESSION TAG
SEQADV 3P2M HIS A 7 UNP P71702 EXPRESSION TAG
SEQADV 3P2M HIS A 8 UNP P71702 EXPRESSION TAG
SEQADV 3P2M HIS A 9 UNP P71702 EXPRESSION TAG
SEQADV 3P2M HIS A 10 UNP P71702 EXPRESSION TAG
SEQADV 3P2M SER A 11 UNP P71702 EXPRESSION TAG
SEQADV 3P2M SER A 12 UNP P71702 EXPRESSION TAG
SEQADV 3P2M GLY A 13 UNP P71702 EXPRESSION TAG
SEQADV 3P2M LEU A 14 UNP P71702 EXPRESSION TAG
SEQADV 3P2M VAL A 15 UNP P71702 EXPRESSION TAG
SEQADV 3P2M PRO A 16 UNP P71702 EXPRESSION TAG
SEQADV 3P2M ARG A 17 UNP P71702 EXPRESSION TAG
SEQADV 3P2M GLY A 18 UNP P71702 EXPRESSION TAG
SEQADV 3P2M SER A 19 UNP P71702 EXPRESSION TAG
SEQADV 3P2M HIS A 20 UNP P71702 EXPRESSION TAG
SEQADV 3P2M MET A 21 UNP P71702 EXPRESSION TAG
SEQADV 3P2M ALA A 22 UNP P71702 EXPRESSION TAG
SEQADV 3P2M SER A 23 UNP P71702 EXPRESSION TAG
SEQADV 3P2M MET A 24 UNP P71702 EXPRESSION TAG
SEQADV 3P2M THR A 25 UNP P71702 EXPRESSION TAG
SEQADV 3P2M GLY A 26 UNP P71702 EXPRESSION TAG
SEQADV 3P2M GLY A 27 UNP P71702 EXPRESSION TAG
SEQADV 3P2M GLN A 28 UNP P71702 EXPRESSION TAG
SEQADV 3P2M GLN A 29 UNP P71702 EXPRESSION TAG
SEQADV 3P2M MET A 30 UNP P71702 EXPRESSION TAG
SEQADV 3P2M GLY A 31 UNP P71702 EXPRESSION TAG
SEQADV 3P2M ARG A 32 UNP P71702 EXPRESSION TAG
SEQADV 3P2M VAL A 33 UNP P71702 EXPRESSION TAG
SEQRES 1 A 330 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 330 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY
SEQRES 3 A 330 GLY GLN GLN MET GLY ARG VAL LEU SER ASP ASP GLU LEU
SEQRES 4 A 330 THR GLY LEU ASP GLU PHE ALA LEU LEU ALA GLU ASN ALA
SEQRES 5 A 330 GLU GLN ALA GLY VAL ASN GLY PRO LEU PRO GLU VAL GLU
SEQRES 6 A 330 ARG VAL GLN ALA GLY ALA ILE SER ALA LEU ARG TRP GLY
SEQRES 7 A 330 GLY SER ALA PRO ARG VAL ILE PHE LEU HIS GLY GLY GLY
SEQRES 8 A 330 GLN ASN ALA HIS THR TRP ASP THR VAL ILE VAL GLY LEU
SEQRES 9 A 330 GLY GLU PRO ALA LEU ALA VAL ASP LEU PRO GLY HIS GLY
SEQRES 10 A 330 HIS SER ALA TRP ARG GLU ASP GLY ASN TYR SER PRO GLN
SEQRES 11 A 330 LEU ASN SER GLU THR LEU ALA PRO VAL LEU ARG GLU LEU
SEQRES 12 A 330 ALA PRO GLY ALA GLU PHE VAL VAL GLY MET SER LEU GLY
SEQRES 13 A 330 GLY LEU THR ALA ILE ARG LEU ALA ALA MET ALA PRO ASP
SEQRES 14 A 330 LEU VAL GLY GLU LEU VAL LEU VAL ASP VAL THR PRO SER
SEQRES 15 A 330 ALA LEU GLN ARG HIS ALA GLU LEU THR ALA GLU GLN ARG
SEQRES 16 A 330 GLY THR VAL ALA LEU MET HIS GLY GLU ARG GLU PHE PRO
SEQRES 17 A 330 SER PHE GLN ALA MET LEU ASP LEU THR ILE ALA ALA ALA
SEQRES 18 A 330 PRO HIS ARG ASP VAL LYS SER LEU ARG ARG GLY VAL PHE
SEQRES 19 A 330 HIS ASN SER ARG ARG LEU ASP ASN GLY ASN TRP VAL TRP
SEQRES 20 A 330 ARG TYR ASP ALA ILE ARG THR PHE GLY ASP PHE ALA GLY
SEQRES 21 A 330 LEU TRP ASP ASP VAL ASP ALA LEU SER ALA PRO ILE THR
SEQRES 22 A 330 LEU VAL ARG GLY GLY SER SER GLY PHE VAL THR ASP GLN
SEQRES 23 A 330 ASP THR ALA GLU LEU HIS ARG ARG ALA THR HIS PHE ARG
SEQRES 24 A 330 GLY VAL HIS ILE VAL GLU LYS SER GLY HIS SER VAL GLN
SEQRES 25 A 330 SER ASP GLN PRO ARG ALA LEU ILE GLU ILE VAL ARG GLY
SEQRES 26 A 330 VAL LEU ASP THR ARG
FORMUL 2 HOH *36(H2 O)
HELIX 1 1 LEU A 47 ALA A 55 1 9
HELIX 2 2 ASN A 93 THR A 96 5 4
HELIX 3 3 TRP A 97 LEU A 104 1 8
HELIX 4 4 SER A 128 LEU A 143 1 16
HELIX 5 5 SER A 154 ALA A 167 1 14
HELIX 6 6 THR A 180 THR A 191 1 12
HELIX 7 7 SER A 209 ALA A 221 1 13
HELIX 8 8 ASP A 225 HIS A 235 1 11
HELIX 9 9 ASP A 257 LEU A 268 1 12
HELIX 10 10 THR A 284 ALA A 295 1 12
HELIX 11 11 SER A 310 GLN A 315 1 6
HELIX 12 12 GLN A 315 LEU A 327 1 13
SHEET 1 A 8 VAL A 64 ALA A 69 0
SHEET 2 A 8 ILE A 72 TRP A 77 -1 O ALA A 74 N VAL A 67
SHEET 3 A 8 ALA A 108 VAL A 111 -1 O ALA A 108 N TRP A 77
SHEET 4 A 8 VAL A 84 LEU A 87 1 N PHE A 86 O LEU A 109
SHEET 5 A 8 PHE A 149 MET A 153 1 O VAL A 151 N LEU A 87
SHEET 6 A 8 GLU A 173 VAL A 177 1 O VAL A 177 N GLY A 152
SHEET 7 A 8 ILE A 272 GLY A 277 1 O THR A 273 N LEU A 176
SHEET 8 A 8 PHE A 298 VAL A 304 1 O ARG A 299 N ILE A 272
SHEET 1 B 2 SER A 237 ARG A 239 0
SHEET 2 B 2 TRP A 245 TRP A 247 -1 O VAL A 246 N ARG A 238
CISPEP 1 GLY A 70 ALA A 71 0 15.32
CISPEP 2 GLY A 79 SER A 80 0 7.04
CISPEP 3 ALA A 81 PRO A 82 0 -20.23
CRYST1 73.465 73.465 48.063 90.00 90.00 120.00 P 31 3
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 0.013612 0.007859 0.000000 0.00000
SCALE2 0.000000 0.015718 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020806 0.00000
TER 2137 THR A 329
MASTER 321 0 0 12 10 0 0 6 2172 1 0 26
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