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HEADER HYDROLASE 28-OCT-20 7AT2
TITLE CRYSTAL STRUCTURE OF INACTIVE ESTD11 S144A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTD11 S144A;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;
SOURCE 3 ORGANISM_TAXID: 77133;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PET22
KEYWDS ESTERASE HORMONE-SENSITIVE LIPASE METAGENOME LIBRARY CRYSTAL
KEYWDS 2 STRUCTURE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.MIGUEL-RUANO,I.RIVERA,J.A.HERMOSO
REVDAT 1 03-MAR-21 7AT2 0
JRNL AUTH V.MIGUEL-RUANO,I.RIVERA,J.RAJKOVIC,K.KNAPIK,A.TORRADO,
JRNL AUTH 2 J.M.OTERO,E.BENEVENTI,M.BECERRA,M.SANCHEZ-COSTA,A.HIDALGO,
JRNL AUTH 3 J.BERENGUER,M.I.GONZALEZ-SISO,J.CRUCES,M.L.RUA,J.A.HERMOSO
JRNL TITL BIOCHEMICAL AND STRUCTURAL CHARACTERIZATION OF A NOVEL
JRNL TITL 2 THERMOPHILIC ESTERASE ESTD11 PROVIDE CATALYTIC INSIGHTS FOR
JRNL TITL 3 THE HSL FAMILY
JRNL REF COMPUT STRUCT BIOTECHNOL J 2021
JRNL REFN ESSN 2001-0370
JRNL DOI 10.1016/J.CSBJ.2021.01.047
REMARK 2
REMARK 2 RESOLUTION. 1.44 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0267
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.44
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.77
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 96537
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) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.188
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 5150
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) : 1.44
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.48
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7058
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.85
REMARK 3 BIN R VALUE (WORKING SET) : 0.2380
REMARK 3 BIN FREE R VALUE SET COUNT : 392
REMARK 3 BIN FREE R VALUE : 0.2460
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4494
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 733
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.88
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.32000
REMARK 3 B22 (A**2) : -0.06000
REMARK 3 B33 (A**2) : -0.26000
REMARK 3 B12 (A**2) : 0.00000
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): 0.071
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.066
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.044
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.161
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.958
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4968 ; 0.006 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 4839 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6833 ; 1.325 ; 1.645
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11125 ; 1.361 ; 1.571
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 668 ; 5.791 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 266 ;26.607 ;19.624
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 817 ;13.808 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 59 ;19.981 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 642 ; 0.069 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5824 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1142 ; 0.002 ; 0.020
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 2 296 B 2 296 9913 0.100 0.050
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 : 1.20
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 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 7AT2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-OCT-20.
REMARK 100 THE DEPOSITION ID IS D_1292112030.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-AUG-17
REMARK 200 TEMPERATURE (KELVIN) : 291
REMARK 200 PH : 5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALBA
REMARK 200 BEAMLINE : XALOC
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.072
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 : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 101766
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.440
REMARK 200 RESOLUTION RANGE LOW (A) : 48.310
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 5.700
REMARK 200 R MERGE (I) : 0.08200
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) : 1.44
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.46
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.60
REMARK 200 R MERGE FOR SHELL (I) : 0.70300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.500
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: 4XVC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.2M SODIUM FORMATE + 0.1M CITRATE PH
REMARK 280 5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
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 24.09500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 72.47000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.06850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 72.47000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.09500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.06850
REMARK 290 SMTRY3 4 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: 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 MET A 1
REMARK 465 MET B 1
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 554 O HOH A 633 1.94
REMARK 500 O HOH B 610 O HOH B 643 1.94
REMARK 500 O ALA B 237 O HOH B 301 1.94
REMARK 500 O HOH A 428 O HOH A 546 2.14
REMARK 500 O HOH A 419 O HOH A 566 2.15
REMARK 500 O HOH B 319 O HOH B 534 2.16
REMARK 500 O HOH B 307 O HOH B 553 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH B 351 O HOH B 504 3654 1.96
REMARK 500 O HOH A 338 O HOH A 539 4445 2.00
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 SER A 38 78.65 -111.07
REMARK 500 SER A 38 78.65 -111.86
REMARK 500 ALA A 144 -122.42 61.78
REMARK 500 ALA A 237 50.07 -95.02
REMARK 500 ASP A 265 -1.63 73.37
REMARK 500 SER B 38 79.64 -111.12
REMARK 500 ALA B 144 -123.32 62.21
REMARK 500 ALA B 237 46.51 -95.05
REMARK 500 ASP B 265 -0.63 72.87
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 7AT0 RELATED DB: PDB
REMARK 900 RELATED ID: 7AT3 RELATED DB: PDB
REMARK 900 RELATED ID: 7AT4 RELATED DB: PDB
REMARK 900 RELATED ID: 7ATD RELATED DB: PDB
DBREF 7AT2 A 1 296 PDB 7AT2 7AT2 1 296
DBREF 7AT2 B 1 296 PDB 7AT2 7AT2 1 296
SEQRES 1 A 296 MET ALA SER GLU ALA LEU THR MET ILE VAL ASN LEU LEU
SEQRES 2 A 296 ARG SER GLN ARG PRO LEU GLN GLU PRO THR VAL GLU GLN
SEQRES 3 A 296 MET ARG ALA GLY LEU GLU ALA MET ALA GLN MET SER PRO
SEQRES 4 A 296 LEU PRO ALA ASP VAL GLU LEU THR THR VAL ASP ALA GLY
SEQRES 5 A 296 GLY VAL PRO GLY ALA TRP VAL ARG VAL PRO GLU SER ASP
SEQRES 6 A 296 PRO ASP ARG VAL VAL LEU TYR LEU HIS GLY GLY GLY TYR
SEQRES 7 A 296 VAL ILE GLY SER ILE ARG THR HIS ARG ASP LEU ALA GLN
SEQRES 8 A 296 ARG ILE ALA ARG ALA ALA ARG CYS ARG VAL LEU LEU ILE
SEQRES 9 A 296 ASP TYR ARG LEU ALA PRO GLU HIS PRO HIS PRO ALA ALA
SEQRES 10 A 296 VAL GLU ASP SER THR ARG ALA TYR ARG TRP LEU LEU GLU
SEQRES 11 A 296 THR GLY SER ASP PRO LYS ARG MET ALA ILE ALA GLY ASP
SEQRES 12 A 296 ALA ALA GLY GLY GLY LEU THR VAL ALA THR LEU VAL ALA
SEQRES 13 A 296 LEU ARG ASP ALA GLY VAL PRO LEU PRO ALA ALA ALA VAL
SEQRES 14 A 296 CYS LEU SER PRO TRP VAL ASP LEU GLU GLY ILE GLY GLU
SEQRES 15 A 296 SER MET THR THR LYS ALA ALA VAL ASP PRO MET VAL GLN
SEQRES 16 A 296 ARG GLU PRO LEU LEU ARG MET ALA SER MET TYR LEU ALA
SEQRES 17 A 296 GLY GLN ASP PRO ARG THR PRO LEU ALA ALA PRO LEU TYR
SEQRES 18 A 296 ALA ASP LEU ARG GLY LEU PRO PRO LEU LEU ILE GLN VAL
SEQRES 19 A 296 GLY THR ALA GLU THR LEU LEU ASP ASP SER VAL ARG LEU
SEQRES 20 A 296 ALA GLU ARG ALA ARG ALA ALA GLY VAL GLN VAL THR LEU
SEQRES 21 A 296 GLU PRO TRP GLU ASP MET ILE HIS VAL TRP GLN ALA PHE
SEQRES 22 A 296 ALA ALA MET LEU PRO GLU GLY GLN GLN ALA ILE GLU ARG
SEQRES 23 A 296 ILE GLY GLU PHE LEU ARG GLN HIS TRP GLN
SEQRES 1 B 296 MET ALA SER GLU ALA LEU THR MET ILE VAL ASN LEU LEU
SEQRES 2 B 296 ARG SER GLN ARG PRO LEU GLN GLU PRO THR VAL GLU GLN
SEQRES 3 B 296 MET ARG ALA GLY LEU GLU ALA MET ALA GLN MET SER PRO
SEQRES 4 B 296 LEU PRO ALA ASP VAL GLU LEU THR THR VAL ASP ALA GLY
SEQRES 5 B 296 GLY VAL PRO GLY ALA TRP VAL ARG VAL PRO GLU SER ASP
SEQRES 6 B 296 PRO ASP ARG VAL VAL LEU TYR LEU HIS GLY GLY GLY TYR
SEQRES 7 B 296 VAL ILE GLY SER ILE ARG THR HIS ARG ASP LEU ALA GLN
SEQRES 8 B 296 ARG ILE ALA ARG ALA ALA ARG CYS ARG VAL LEU LEU ILE
SEQRES 9 B 296 ASP TYR ARG LEU ALA PRO GLU HIS PRO HIS PRO ALA ALA
SEQRES 10 B 296 VAL GLU ASP SER THR ARG ALA TYR ARG TRP LEU LEU GLU
SEQRES 11 B 296 THR GLY SER ASP PRO LYS ARG MET ALA ILE ALA GLY ASP
SEQRES 12 B 296 ALA ALA GLY GLY GLY LEU THR VAL ALA THR LEU VAL ALA
SEQRES 13 B 296 LEU ARG ASP ALA GLY VAL PRO LEU PRO ALA ALA ALA VAL
SEQRES 14 B 296 CYS LEU SER PRO TRP VAL ASP LEU GLU GLY ILE GLY GLU
SEQRES 15 B 296 SER MET THR THR LYS ALA ALA VAL ASP PRO MET VAL GLN
SEQRES 16 B 296 ARG GLU PRO LEU LEU ARG MET ALA SER MET TYR LEU ALA
SEQRES 17 B 296 GLY GLN ASP PRO ARG THR PRO LEU ALA ALA PRO LEU TYR
SEQRES 18 B 296 ALA ASP LEU ARG GLY LEU PRO PRO LEU LEU ILE GLN VAL
SEQRES 19 B 296 GLY THR ALA GLU THR LEU LEU ASP ASP SER VAL ARG LEU
SEQRES 20 B 296 ALA GLU ARG ALA ARG ALA ALA GLY VAL GLN VAL THR LEU
SEQRES 21 B 296 GLU PRO TRP GLU ASP MET ILE HIS VAL TRP GLN ALA PHE
SEQRES 22 B 296 ALA ALA MET LEU PRO GLU GLY GLN GLN ALA ILE GLU ARG
SEQRES 23 B 296 ILE GLY GLU PHE LEU ARG GLN HIS TRP GLN
FORMUL 3 HOH *733(H2 O)
HELIX 1 AA1 GLU A 4 ARG A 17 1 14
HELIX 2 AA2 PRO A 18 GLU A 21 5 4
HELIX 3 AA3 THR A 23 GLN A 36 1 14
HELIX 4 AA4 SER A 82 ARG A 98 1 17
HELIX 5 AA5 PRO A 115 THR A 131 1 17
HELIX 6 AA6 ASP A 134 LYS A 136 5 3
HELIX 7 AA7 ALA A 144 ALA A 160 1 17
HELIX 8 AA8 GLU A 182 LYS A 187 1 6
HELIX 9 AA9 GLN A 195 ALA A 208 1 14
HELIX 10 AB1 ALA A 218 ALA A 222 5 5
HELIX 11 AB2 LEU A 240 ALA A 254 1 15
HELIX 12 AB3 VAL A 269 ALA A 274 5 6
HELIX 13 AB4 LEU A 277 GLN A 296 1 20
HELIX 14 AB5 SER B 3 ARG B 17 1 15
HELIX 15 AB6 PRO B 18 GLU B 21 5 4
HELIX 16 AB7 THR B 23 GLN B 36 1 14
HELIX 17 AB8 SER B 82 ARG B 98 1 17
HELIX 18 AB9 PRO B 115 THR B 131 1 17
HELIX 19 AC1 ASP B 134 LYS B 136 5 3
HELIX 20 AC2 ALA B 144 ALA B 160 1 17
HELIX 21 AC3 GLU B 182 LYS B 187 1 6
HELIX 22 AC4 GLN B 195 ALA B 208 1 14
HELIX 23 AC5 ALA B 218 ALA B 222 5 5
HELIX 24 AC6 LEU B 240 ALA B 254 1 15
HELIX 25 AC7 VAL B 269 ALA B 274 5 6
HELIX 26 AC8 LEU B 277 TRP B 295 1 19
SHEET 1 AA1 8 GLU A 45 ASP A 50 0
SHEET 2 AA1 8 PRO A 55 ARG A 60 -1 O ARG A 60 N GLU A 45
SHEET 3 AA1 8 CYS A 99 ILE A 104 -1 O VAL A 101 N VAL A 59
SHEET 4 AA1 8 ASP A 65 LEU A 73 1 N ARG A 68 O ARG A 100
SHEET 5 AA1 8 MET A 138 ASP A 143 1 O ALA A 141 N LEU A 73
SHEET 6 AA1 8 ALA A 167 LEU A 171 1 O LEU A 171 N GLY A 142
SHEET 7 AA1 8 LEU A 230 GLY A 235 1 O LEU A 231 N CYS A 170
SHEET 8 AA1 8 VAL A 258 TRP A 263 1 O GLU A 261 N ILE A 232
SHEET 1 AA2 8 GLU B 45 ASP B 50 0
SHEET 2 AA2 8 PRO B 55 ARG B 60 -1 O ARG B 60 N GLU B 45
SHEET 3 AA2 8 CYS B 99 ILE B 104 -1 O VAL B 101 N VAL B 59
SHEET 4 AA2 8 ASP B 65 LEU B 73 1 N TYR B 72 O LEU B 102
SHEET 5 AA2 8 MET B 138 ASP B 143 1 O ALA B 141 N LEU B 73
SHEET 6 AA2 8 ALA B 167 LEU B 171 1 O LEU B 171 N GLY B 142
SHEET 7 AA2 8 LEU B 230 GLY B 235 1 O LEU B 231 N CYS B 170
SHEET 8 AA2 8 VAL B 258 TRP B 263 1 O GLU B 261 N ILE B 232
CISPEP 1 ALA A 109 PRO A 110 0 -1.18
CISPEP 2 HIS A 114 PRO A 115 0 6.78
CISPEP 3 ALA B 109 PRO B 110 0 1.66
CISPEP 4 HIS B 114 PRO B 115 0 7.36
CRYST1 48.190 80.137 144.940 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 0.020751 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012479 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006899 0.00000
TER 2382 GLN A 296
TER 4836 GLN B 296
MASTER 321 0 0 26 16 0 0 6 5227 2 0 46
END |