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HEADER HYDROLASE 02-MAY-19 6JZL
TITLE S-FORMYLGLUTATHIONE HYDROLASE HOMOLOG FROM A PSYCHROPHILIC BACTERIUM
TITLE 2 OF SHEWANELLA FRIGIDIMARINA
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: SHEWANELLA FRIGIDIMARINA;
SOURCE 3 ORGANISM_TAXID: 56812;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS S-FORMYLGLUTATHIONE HYDROLASE, SHEWANELLA FRIGIDIMARINA, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.W.LEE,J.H.LEE
REVDAT 1 04-SEP-19 6JZL 0
JRNL AUTH C.W.LEE,W.YOO,S.H.PARK,L.T.H.L.LE,C.S.JEONG,B.H.RYU,
JRNL AUTH 2 S.C.SHIN,H.W.KIM,H.PARK,K.K.KIM,T.D.KIM,J.H.LEE
JRNL TITL STRUCTURAL AND FUNCTIONAL CHARACTERIZATION OF A NOVEL
JRNL TITL 2 COLD-ACTIVE S-FORMYLGLUTATHIONE HYDROLASE (SFSFGH) HOMOLOG
JRNL TITL 3 FROM SHEWANELLA FRIGIDIMARINA, A PSYCHROPHILIC BACTERIUM.
JRNL REF MICROB. CELL FACT. V. 18 140 2019
JRNL REFN ISSN 1475-2859
JRNL PMID 31426813
JRNL DOI 10.1186/S12934-019-1190-1
REMARK 2
REMARK 2 RESOLUTION. 2.32 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.32
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.81
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 18706
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) : 0.161
REMARK 3 R VALUE (WORKING SET) : 0.158
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 964
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) : 2.32
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.38
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1341
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.84
REMARK 3 BIN R VALUE (WORKING SET) : 0.1650
REMARK 3 BIN FREE R VALUE SET COUNT : 47
REMARK 3 BIN FREE R VALUE : 0.2390
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4341
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 208
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.88
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.02000
REMARK 3 B33 (A**2) : -0.01000
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): 1.121
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.276
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.187
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.723
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.911
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4459 ; 0.010 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 3947 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6054 ; 1.596 ; 1.635
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9175 ; 1.337 ; 1.571
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 552 ; 8.029 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 234 ;36.077 ;23.077
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 700 ;17.343 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;19.719 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 551 ; 0.076 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5078 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 958 ; 0.001 ; 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): 2214 ; 2.139 ; 2.605
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2212 ; 2.126 ; 2.603
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2764 ; 3.266 ; 3.902
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2764 ; 3.263 ; 3.902
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2245 ; 2.698 ; 2.896
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2246 ; 2.697 ; 2.897
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3291 ; 4.261 ; 4.208
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 5049 ; 5.674 ;30.356
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 5019 ; 5.617 ;30.222
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 : NULL
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
REMARK 4
REMARK 4 6JZL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-MAY-19.
REMARK 100 THE DEPOSITION ID IS D_1300012029.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JUL-17
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 : 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 : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19691
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.320
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 42.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.32
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.36
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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 : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.23
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M LITHIUM CHLORIDE AND 16% (W/V)
REMARK 280 PEG 3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 38.29700
REMARK 290 SMTRY3 2 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: 1680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 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 MET A 1
REMARK 465 THR A 2
REMARK 465 LYS A 279
REMARK 465 LYS B 279
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 56 -5.14 85.37
REMARK 500 THR A 58 -166.27 -110.15
REMARK 500 ALA A 103 45.77 -148.95
REMARK 500 PHE A 105 14.45 58.74
REMARK 500 ARG A 119 52.52 -115.52
REMARK 500 SER A 139 -176.36 -69.71
REMARK 500 SER A 148 -118.98 59.77
REMARK 500 PRO A 246 75.80 -68.71
REMARK 500 ASP A 256 -157.97 -104.57
REMARK 500 THR B 56 -10.95 81.26
REMARK 500 ALA B 103 40.51 -151.14
REMARK 500 HIS B 117 -31.12 -144.26
REMARK 500 ASP B 126 -70.96 -115.03
REMARK 500 SER B 139 -168.06 -70.15
REMARK 500 SER B 148 -109.83 65.70
REMARK 500 ASN B 161 50.41 -140.27
REMARK 500 ASP B 194 -71.35 52.90
REMARK 500 SER B 195 117.66 42.03
REMARK 500 THR B 211 -68.65 -99.36
REMARK 500 ASP B 256 -154.91 -95.90
REMARK 500
REMARK 500 REMARK: NULL
DBREF 6JZL A 1 279 UNP Q07XK4 Q07XK4_SHEFN 1 279
DBREF 6JZL B 1 279 UNP Q07XK4 Q07XK4_SHEFN 1 279
SEQRES 1 A 279 MET THR ILE GLU ASN MET SER VAL ASN LYS SER PHE GLY
SEQRES 2 A 279 GLY TRP HIS LYS GLN TYR SER HIS GLN SER GLN THR LEU
SEQRES 3 A 279 ASN CYS GLU MET ARG PHE ALA ILE TYR LEU PRO PRO GLN
SEQRES 4 A 279 ALA SER SER GLY LYS LYS VAL PRO VAL LEU TYR TRP LEU
SEQRES 5 A 279 SER GLY LEU THR CYS THR ASP GLU ASN PHE MET GLN LYS
SEQRES 6 A 279 ALA GLY ALA GLN ALA LEU ALA ALA GLU LEU GLY ILE ALA
SEQRES 7 A 279 ILE VAL ALA PRO ASP THR SER PRO ARG GLY GLU ASN VAL
SEQRES 8 A 279 ALA ASP ASP GLU GLY TYR ASP LEU GLY LYS GLY ALA GLY
SEQRES 9 A 279 PHE TYR VAL ASN ALA THR GLN ALA PRO TRP ASN ARG HIS
SEQRES 10 A 279 TYR ARG MET TYR ASP TYR VAL VAL ASP GLU LEU PRO LYS
SEQRES 11 A 279 LEU ILE GLU SER MET PHE PRO VAL SER ASP LYS ARG SER
SEQRES 12 A 279 ILE ALA GLY HIS SER MET GLY GLY HIS GLY ALA LEU VAL
SEQRES 13 A 279 ILE ALA LEU ARG ASN ALA ASP ALA TYR GLN SER VAL SER
SEQRES 14 A 279 ALA PHE SER PRO ILE SER ASN PRO ILE ASN CYS PRO TRP
SEQRES 15 A 279 GLY LYS LYS ALA LEU THR ALA TYR LEU GLY ARG ASP SER
SEQRES 16 A 279 ALA THR TRP MET GLU TYR ASP ALA SER VAL LEU MET ARG
SEQRES 17 A 279 GLN ALA THR GLN PHE VAL PRO ALA LEU VAL ASP GLN GLY
SEQRES 18 A 279 ASP ALA ASP ASN PHE LEU VAL GLU GLN LEU LYS PRO GLU
SEQRES 19 A 279 VAL LEU GLU ALA ALA ALA LYS VAL LYS GLY TYR PRO LEU
SEQRES 20 A 279 GLU LEU ASN TYR ARG GLU GLY TYR ASP HIS SER TYR TYR
SEQRES 21 A 279 PHE ILE SER SER PHE ILE GLU ASN HIS LEU ARG PHE HIS
SEQRES 22 A 279 ALA GLU HIS LEU GLY LYS
SEQRES 1 B 279 MET THR ILE GLU ASN MET SER VAL ASN LYS SER PHE GLY
SEQRES 2 B 279 GLY TRP HIS LYS GLN TYR SER HIS GLN SER GLN THR LEU
SEQRES 3 B 279 ASN CYS GLU MET ARG PHE ALA ILE TYR LEU PRO PRO GLN
SEQRES 4 B 279 ALA SER SER GLY LYS LYS VAL PRO VAL LEU TYR TRP LEU
SEQRES 5 B 279 SER GLY LEU THR CYS THR ASP GLU ASN PHE MET GLN LYS
SEQRES 6 B 279 ALA GLY ALA GLN ALA LEU ALA ALA GLU LEU GLY ILE ALA
SEQRES 7 B 279 ILE VAL ALA PRO ASP THR SER PRO ARG GLY GLU ASN VAL
SEQRES 8 B 279 ALA ASP ASP GLU GLY TYR ASP LEU GLY LYS GLY ALA GLY
SEQRES 9 B 279 PHE TYR VAL ASN ALA THR GLN ALA PRO TRP ASN ARG HIS
SEQRES 10 B 279 TYR ARG MET TYR ASP TYR VAL VAL ASP GLU LEU PRO LYS
SEQRES 11 B 279 LEU ILE GLU SER MET PHE PRO VAL SER ASP LYS ARG SER
SEQRES 12 B 279 ILE ALA GLY HIS SER MET GLY GLY HIS GLY ALA LEU VAL
SEQRES 13 B 279 ILE ALA LEU ARG ASN ALA ASP ALA TYR GLN SER VAL SER
SEQRES 14 B 279 ALA PHE SER PRO ILE SER ASN PRO ILE ASN CYS PRO TRP
SEQRES 15 B 279 GLY LYS LYS ALA LEU THR ALA TYR LEU GLY ARG ASP SER
SEQRES 16 B 279 ALA THR TRP MET GLU TYR ASP ALA SER VAL LEU MET ARG
SEQRES 17 B 279 GLN ALA THR GLN PHE VAL PRO ALA LEU VAL ASP GLN GLY
SEQRES 18 B 279 ASP ALA ASP ASN PHE LEU VAL GLU GLN LEU LYS PRO GLU
SEQRES 19 B 279 VAL LEU GLU ALA ALA ALA LYS VAL LYS GLY TYR PRO LEU
SEQRES 20 B 279 GLU LEU ASN TYR ARG GLU GLY TYR ASP HIS SER TYR TYR
SEQRES 21 B 279 PHE ILE SER SER PHE ILE GLU ASN HIS LEU ARG PHE HIS
SEQRES 22 B 279 ALA GLU HIS LEU GLY LYS
FORMUL 3 HOH *208(H2 O)
HELIX 1 AA1 PRO A 37 SER A 42 5 6
HELIX 2 AA2 ASP A 59 ALA A 66 1 8
HELIX 3 AA3 ALA A 68 GLY A 76 1 9
HELIX 4 AA4 PRO A 113 HIS A 117 5 5
HELIX 5 AA5 ARG A 119 ASP A 126 1 8
HELIX 6 AA6 ASP A 126 PHE A 136 1 11
HELIX 7 AA7 SER A 148 ASN A 161 1 14
HELIX 8 AA8 ASN A 176 ASN A 179 5 4
HELIX 9 AA9 CYS A 180 GLY A 192 1 13
HELIX 10 AB1 ASP A 194 TYR A 201 5 8
HELIX 11 AB2 ASP A 202 ALA A 210 1 9
HELIX 12 AB3 LYS A 232 VAL A 242 1 11
HELIX 13 AB4 SER A 258 GLY A 278 1 21
HELIX 14 AB5 PRO B 37 SER B 41 5 5
HELIX 15 AB6 ASP B 59 ALA B 66 1 8
HELIX 16 AB7 ALA B 68 GLY B 76 1 9
HELIX 17 AB8 PRO B 113 HIS B 117 5 5
HELIX 18 AB9 ARG B 119 ASP B 126 1 8
HELIX 19 AC1 ASP B 126 SER B 134 1 9
HELIX 20 AC2 SER B 148 ASN B 161 1 14
HELIX 21 AC3 ASN B 176 ASN B 179 5 4
HELIX 22 AC4 CYS B 180 GLY B 192 1 13
HELIX 23 AC5 SER B 195 TYR B 201 5 7
HELIX 24 AC6 ASP B 202 GLN B 209 1 8
HELIX 25 AC7 LYS B 232 GLY B 244 1 13
HELIX 26 AC8 SER B 258 GLY B 278 1 21
SHEET 1 AA1 9 GLU A 4 SER A 11 0
SHEET 2 AA1 9 GLY A 14 SER A 23 -1 O GLN A 18 N MET A 6
SHEET 3 AA1 9 CYS A 28 LEU A 36 -1 O MET A 30 N HIS A 21
SHEET 4 AA1 9 ALA A 78 PRO A 82 -1 O ILE A 79 N TYR A 35
SHEET 5 AA1 9 VAL A 46 LEU A 52 1 N TRP A 51 O VAL A 80
SHEET 6 AA1 9 VAL A 138 HIS A 147 1 O ALA A 145 N LEU A 52
SHEET 7 AA1 9 VAL A 168 PHE A 171 1 O PHE A 171 N GLY A 146
SHEET 8 AA1 9 ALA A 216 GLY A 221 1 O ASP A 219 N ALA A 170
SHEET 9 AA1 9 LEU A 247 ARG A 252 1 O ARG A 252 N GLN A 220
SHEET 1 AA2 6 ILE B 3 SER B 11 0
SHEET 2 AA2 6 GLY B 14 SER B 23 -1 O GLN B 18 N MET B 6
SHEET 3 AA2 6 CYS B 28 LEU B 36 -1 O ILE B 34 N LYS B 17
SHEET 4 AA2 6 ALA B 78 PRO B 82 -1 O ILE B 79 N TYR B 35
SHEET 5 AA2 6 VAL B 46 LEU B 52 1 N TRP B 51 O VAL B 80
SHEET 6 AA2 6 VAL B 138 GLY B 146 1 O SER B 139 N VAL B 46
SHEET 1 AA3 3 VAL B 168 PHE B 171 0
SHEET 2 AA3 3 ALA B 216 GLY B 221 1 O ASP B 219 N ALA B 170
SHEET 3 AA3 3 LEU B 247 ARG B 252 1 O ARG B 252 N GLN B 220
CISPEP 1 ALA A 112 PRO A 113 0 -3.82
CISPEP 2 ALA B 112 PRO B 113 0 0.50
CRYST1 49.356 76.594 64.725 90.00 105.32 90.00 P 1 21 1 4
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 0.020261 0.000000 0.005550 0.00000
SCALE2 0.000000 0.013056 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016019 0.00000
TER 2164 GLY A 278
TER 4343 GLY B 278
MASTER 279 0 0 26 18 0 0 6 4549 2 0 44
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