| content |
HEADER HYDROLASE 03-MAR-23 8ILJ
TITLE S-FORMYLGLUTATHIONE HYDROLASE (BUSFGH) FROM BURKHOLDERIACEAE SP.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: S-FORMYLGLUTATHIONE HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.2.12;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BURKHOLDERIACEAE;
SOURCE 3 ORGANISM_TAXID: 119060;
SOURCE 4 GENE: PAMC26510_23250;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS S-FORMYLGLUTATHIONE HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.HWANG,J.H.LEE,H.DO
REVDAT 1 10-JAN-24 8ILJ 0
JRNL AUTH J.HWANG,H.DO,Y.S.SHIM,J.H.LEE
JRNL TITL CRYSTAL STRUCTURE AND FUNCTIONAL CHARACTERIZATION OF AN
JRNL TITL 2 S-FORMYLGLUTATHIONE HYDROLASE (BUSFGH) FROM BURKHOLDERIACEAE
JRNL TITL 3 SP.
JRNL REF CRYSTALS V. 13 2023
JRNL REFN ESSN 2073-4352
JRNL DOI 10.3390/CRYST13040621
REMARK 2
REMARK 2 RESOLUTION. 1.73 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0238
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.73
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.52
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 65527
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3277
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.73
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.76
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2613
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.14
REMARK 3 BIN R VALUE (WORKING SET) : 0.2350
REMARK 3 BIN FREE R VALUE SET COUNT : 138
REMARK 3 BIN FREE R VALUE : 0.2450
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4356
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 416
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.68
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.77
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.188
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : NULL
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL
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): 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 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 : FLAT BULK SOLVENT MODEL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.11
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 8ILJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-MAR-23.
REMARK 100 THE DEPOSITION ID IS D_1300035979.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-MAY-20
REMARK 200 TEMPERATURE (KELVIN) : 77
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 5C (4A)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9796
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 65529
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.730
REMARK 200 RESOLUTION RANGE LOW (A) : 29.520
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 12.50
REMARK 200 R MERGE (I) : 0.08096
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 20.6300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.73
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.39690
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: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM CITRATE PH 5.0 AND 20%
REMARK 280 (W/V) PEG 3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 296K
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 25.18500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.31000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.64500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 56.31000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.18500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.64500
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: 1890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 239 CD GLU A 239 OE2 -0.071
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 54 -6.18 72.77
REMARK 500 THR A 56 -169.50 -129.01
REMARK 500 ALA A 102 47.72 -152.81
REMARK 500 PHE A 104 16.13 56.66
REMARK 500 GLN A 125 -76.67 -120.42
REMARK 500 SER A 148 -114.15 60.41
REMARK 500 GLN A 232 -30.86 -139.45
REMARK 500 CYS B 10 119.63 -161.37
REMARK 500 THR B 54 -6.81 75.48
REMARK 500 ALA B 102 46.49 -151.24
REMARK 500 PHE B 104 15.79 58.27
REMARK 500 GLN B 125 -75.78 -119.88
REMARK 500 SER B 148 -109.70 59.61
REMARK 500 GLN B 232 -32.90 -131.56
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 8ILJ A 1 281 UNP A0A242MJ43_9BURK
DBREF2 8ILJ A A0A242MJ43 1 281
DBREF1 8ILJ B 1 281 UNP A0A242MJ43_9BURK
DBREF2 8ILJ B A0A242MJ43 1 281
SEQRES 1 A 281 MET LEU GLU LEU VAL GLU GLU HIS ARG CYS PHE SER GLY
SEQRES 2 A 281 VAL GLN ARG THR TYR LYS HIS ASP SER GLN THR ILE GLY
SEQRES 3 A 281 LEU PRO MET ARG PHE SER VAL PHE LEU PRO PRO GLN ALA
SEQRES 4 A 281 ALA HIS GLY LYS VAL PRO ALA LEU PHE TYR LEU ALA GLY
SEQRES 5 A 281 LEU THR CYS THR GLU GLU THR PHE ALA ILE LYS ALA GLY
SEQRES 6 A 281 ALA GLN ARG PHE ALA SER GLU HIS GLY ILE ALA LEU ILE
SEQRES 7 A 281 GLY PRO ASP THR SER PRO ARG GLY ALA GLY VAL PRO ASN
SEQRES 8 A 281 GLU GLY ALA ALA TRP ASP PHE GLY VAL GLY ALA GLY PHE
SEQRES 9 A 281 TYR VAL ASP ALA THR GLN GLU PRO TRP ALA ARG ASN TYR
SEQRES 10 A 281 ARG MET TYR SER TYR VAL THR GLN GLU LEU ARG THR THR
SEQRES 11 A 281 VAL LEU ALA GLU LEU PRO VAL ARG GLU ASP ARG LEU GLY
SEQRES 12 A 281 ILE PHE GLY HIS SER MET GLY GLY HIS GLY ALA LEU VAL
SEQRES 13 A 281 LEU ALA LEU ARG ASN PRO ASP ILE TYR LYS SER VAL SER
SEQRES 14 A 281 ALA PHE ALA PRO ILE ALA ALA PRO SER HIS CYS PRO TRP
SEQRES 15 A 281 GLY GLU LYS ALA PHE SER GLY TYR LEU GLY ASP ASP ARG
SEQRES 16 A 281 GLU THR TRP LYS GLN TYR ASP ALA SER GLU LEU VAL LYS
SEQRES 17 A 281 SER ALA LYS THR LYS PHE ASP ALA GLY ILE LEU ILE ASP
SEQRES 18 A 281 GLN GLY LEU ALA ASP ASN PHE LEU ALA THR GLN LEU HIS
SEQRES 19 A 281 PRO GLU ILE PHE GLU ALA ALA ALA LYS ALA ALA GLY GLN
SEQRES 20 A 281 ALA VAL THR LEU ARG ARG HIS GLU GLY TYR ASP HIS GLY
SEQRES 21 A 281 TYR TYR PHE ILE SER THR PHE ILE GLY GLU HIS VAL ALA
SEQRES 22 A 281 PHE HIS ALA ARG THR LEU CYS ALA
SEQRES 1 B 281 MET LEU GLU LEU VAL GLU GLU HIS ARG CYS PHE SER GLY
SEQRES 2 B 281 VAL GLN ARG THR TYR LYS HIS ASP SER GLN THR ILE GLY
SEQRES 3 B 281 LEU PRO MET ARG PHE SER VAL PHE LEU PRO PRO GLN ALA
SEQRES 4 B 281 ALA HIS GLY LYS VAL PRO ALA LEU PHE TYR LEU ALA GLY
SEQRES 5 B 281 LEU THR CYS THR GLU GLU THR PHE ALA ILE LYS ALA GLY
SEQRES 6 B 281 ALA GLN ARG PHE ALA SER GLU HIS GLY ILE ALA LEU ILE
SEQRES 7 B 281 GLY PRO ASP THR SER PRO ARG GLY ALA GLY VAL PRO ASN
SEQRES 8 B 281 GLU GLY ALA ALA TRP ASP PHE GLY VAL GLY ALA GLY PHE
SEQRES 9 B 281 TYR VAL ASP ALA THR GLN GLU PRO TRP ALA ARG ASN TYR
SEQRES 10 B 281 ARG MET TYR SER TYR VAL THR GLN GLU LEU ARG THR THR
SEQRES 11 B 281 VAL LEU ALA GLU LEU PRO VAL ARG GLU ASP ARG LEU GLY
SEQRES 12 B 281 ILE PHE GLY HIS SER MET GLY GLY HIS GLY ALA LEU VAL
SEQRES 13 B 281 LEU ALA LEU ARG ASN PRO ASP ILE TYR LYS SER VAL SER
SEQRES 14 B 281 ALA PHE ALA PRO ILE ALA ALA PRO SER HIS CYS PRO TRP
SEQRES 15 B 281 GLY GLU LYS ALA PHE SER GLY TYR LEU GLY ASP ASP ARG
SEQRES 16 B 281 GLU THR TRP LYS GLN TYR ASP ALA SER GLU LEU VAL LYS
SEQRES 17 B 281 SER ALA LYS THR LYS PHE ASP ALA GLY ILE LEU ILE ASP
SEQRES 18 B 281 GLN GLY LEU ALA ASP ASN PHE LEU ALA THR GLN LEU HIS
SEQRES 19 B 281 PRO GLU ILE PHE GLU ALA ALA ALA LYS ALA ALA GLY GLN
SEQRES 20 B 281 ALA VAL THR LEU ARG ARG HIS GLU GLY TYR ASP HIS GLY
SEQRES 21 B 281 TYR TYR PHE ILE SER THR PHE ILE GLY GLU HIS VAL ALA
SEQRES 22 B 281 PHE HIS ALA ARG THR LEU CYS ALA
FORMUL 3 HOH *416(H2 O)
HELIX 1 AA1 PRO A 36 HIS A 41 5 6
HELIX 2 AA2 GLU A 58 ALA A 64 1 7
HELIX 3 AA3 ALA A 66 GLY A 74 1 9
HELIX 4 AA4 ARG A 118 GLN A 125 1 8
HELIX 5 AA5 GLN A 125 LEU A 135 1 11
HELIX 6 AA6 SER A 148 ASN A 161 1 14
HELIX 7 AA7 ALA A 176 HIS A 179 5 4
HELIX 8 AA8 CYS A 180 GLY A 192 1 13
HELIX 9 AA9 ASP A 194 TYR A 201 5 8
HELIX 10 AB1 ASP A 202 ALA A 210 1 9
HELIX 11 AB2 HIS A 234 GLY A 246 1 13
HELIX 12 AB3 GLY A 260 CYS A 280 1 21
HELIX 13 AB4 PRO B 36 GLY B 42 5 7
HELIX 14 AB5 GLU B 58 ALA B 64 1 7
HELIX 15 AB6 ALA B 66 GLY B 74 1 9
HELIX 16 AB7 ARG B 118 GLN B 125 1 8
HELIX 17 AB8 GLN B 125 LEU B 135 1 11
HELIX 18 AB9 SER B 148 ASN B 161 1 14
HELIX 19 AC1 ALA B 176 HIS B 179 5 4
HELIX 20 AC2 CYS B 180 GLY B 192 1 13
HELIX 21 AC3 ASP B 194 TYR B 201 5 8
HELIX 22 AC4 ASP B 202 ALA B 210 1 9
HELIX 23 AC5 HIS B 234 GLY B 246 1 13
HELIX 24 AC6 GLY B 260 CYS B 280 1 21
SHEET 1 AA1 9 GLU A 3 CYS A 10 0
SHEET 2 AA1 9 GLY A 13 ASP A 21 -1 O LYS A 19 N GLU A 3
SHEET 3 AA1 9 PRO A 28 LEU A 35 -1 O VAL A 33 N ARG A 16
SHEET 4 AA1 9 ALA A 76 GLY A 79 -1 O LEU A 77 N PHE A 34
SHEET 5 AA1 9 VAL A 44 LEU A 50 1 N PRO A 45 O ALA A 76
SHEET 6 AA1 9 VAL A 137 GLY A 146 1 O ARG A 138 N VAL A 44
SHEET 7 AA1 9 TYR A 165 PHE A 171 1 O LYS A 166 N LEU A 142
SHEET 8 AA1 9 ILE A 218 GLY A 223 1 O ASP A 221 N ALA A 170
SHEET 9 AA1 9 VAL A 249 HIS A 254 1 O THR A 250 N ILE A 218
SHEET 1 AA2 9 GLU B 3 CYS B 10 0
SHEET 2 AA2 9 GLY B 13 SER B 22 -1 O GLN B 15 N HIS B 8
SHEET 3 AA2 9 LEU B 27 LEU B 35 -1 O VAL B 33 N ARG B 16
SHEET 4 AA2 9 ALA B 76 GLY B 79 -1 O LEU B 77 N PHE B 34
SHEET 5 AA2 9 VAL B 44 LEU B 50 1 N LEU B 47 O ILE B 78
SHEET 6 AA2 9 VAL B 137 GLY B 146 1 O PHE B 145 N PHE B 48
SHEET 7 AA2 9 TYR B 165 PHE B 171 1 O LYS B 166 N LEU B 142
SHEET 8 AA2 9 ILE B 218 GLY B 223 1 O ASP B 221 N ALA B 170
SHEET 9 AA2 9 VAL B 249 HIS B 254 1 O THR B 250 N ILE B 218
CISPEP 1 GLU A 111 PRO A 112 0 4.73
CISPEP 2 GLU B 111 PRO B 112 0 11.24
CRYST1 50.370 109.290 112.620 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 0.019853 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009150 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008879 0.00000
TER 2179 ALA A 281
TER 4358 ALA B 281
MASTER 288 0 0 24 18 0 0 6 4772 2 0 44
END |