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HEADER HYDROLASE 15-SEP-21 7VGB
TITLE CRYSTAL STRUCTURE OF APO PROLYL OLIGOPEPTIDASE FROM MICROBULBIFER
TITLE 2 ARENACEOUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLYL OLIGOPEPTIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.4.21.26;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MICROBULBIFER ARENACEOUS;
SOURCE 3 ORGANISM_TAXID: 210427;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 866768
KEYWDS S9A, PROLYL ENDOPEPTIDASE, SERINE PROTEASE, MENTAL DISORDER, AMNESIA,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.HUANG,Z.Q.JIANG
REVDAT 1 25-MAY-22 7VGB 0
JRNL AUTH P.HUANG,A.LV,Q.YAN,Z.JIANG,S.YANG
JRNL TITL THE STRUCTURE AND MOLECULAR DYNAMICS OF PROLYL
JRNL TITL 2 OLIGOPEPTIDASE FROM MICROBULBIFER ARENACEOUS PROVIDE
JRNL TITL 3 INSIGHTS INTO CATALYTIC AND REGULATORY MECHANISMS
JRNL REF ACTA CRYSTALLOGR.,SECT.D 2022
JRNL REFN ESSN 1399-0047
JRNL DOI 10.1107/S2059798322004247
REMARK 2
REMARK 2 RESOLUTION. 2.23 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.23
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.20
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 64531
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) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.152
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.001
REMARK 3 FREE R VALUE TEST SET COUNT : 3237
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) : 2.23
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.29
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4448
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.05
REMARK 3 BIN R VALUE (WORKING SET) : 0.2000
REMARK 3 BIN FREE R VALUE SET COUNT : 235
REMARK 3 BIN FREE R VALUE : 0.2450
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10892
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 105
REMARK 3 SOLVENT ATOMS : 1016
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.55
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.04800
REMARK 3 B22 (A**2) : -0.76700
REMARK 3 B33 (A**2) : 0.07300
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.48600
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.327
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.208
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.145
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.865
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.925
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 11286 ; 0.007 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 15308 ; 1.430 ; 1.638
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1360 ; 7.209 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 612 ;34.300 ;22.876
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1788 ;14.650 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 56 ;17.429 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1380 ; 0.111 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8760 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4960 ; 0.202 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 7594 ; 0.313 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 982 ; 0.148 ; 0.200
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): 5450 ; 1.547 ; 1.954
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6804 ; 2.451 ; 2.922
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5836 ; 2.315 ; 2.212
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 8504 ; 3.582 ; 3.194
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 : BABINET MODEL PLUS 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 NOT BEEN USED
REMARK 4
REMARK 4 7VGB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-SEP-21.
REMARK 100 THE DEPOSITION ID IS D_1300024638.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-JUN-20
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 : SSRF
REMARK 200 BEAMLINE : BL18U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 64538
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.227
REMARK 200 RESOLUTION RANGE LOW (A) : 44.198
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : 0.13980
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.5300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.23
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.31
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.30
REMARK 200 R MERGE FOR SHELL (I) : 0.52650
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.370
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: 3MUN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M TRIMETHYLAMINE N-OXIDE DIHYDRATE,
REMARK 280 0.1M TRIS PH 8.5, 20% (W/V) POLYETHYLENE GLYCOL MONOMETHYL ETHER
REMARK 280 2000, VAPOR DIFFUSION, SITTING 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 62.69750
REMARK 290 SMTRY3 2 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
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 ARG A 2
REMARK 465 LYS A 3
REMARK 465 PRO A 4
REMARK 465 ALA A 5
REMARK 465 ILE A 6
REMARK 465 ALA A 7
REMARK 465 LEU A 8
REMARK 465 VAL A 9
REMARK 465 ALA A 10
REMARK 465 ALA A 11
REMARK 465 CYS A 12
REMARK 465 ALA A 13
REMARK 465 ALA A 14
REMARK 465 VAL A 15
REMARK 465 ALA A 16
REMARK 465 ALA A 17
REMARK 465 ILE A 18
REMARK 465 ALA A 19
REMARK 465 VAL A 20
REMARK 465 THR A 21
REMARK 465 ARG A 22
REMARK 465 GLY A 23
REMARK 465 THR A 24
REMARK 465 ASP A 25
REMARK 465 THR A 26
REMARK 465 GLN A 27
REMARK 465 SER A 28
REMARK 465 GLU A 710
REMARK 465 LYS A 711
REMARK 465 MET B 1
REMARK 465 ARG B 2
REMARK 465 LYS B 3
REMARK 465 PRO B 4
REMARK 465 ALA B 5
REMARK 465 ILE B 6
REMARK 465 ALA B 7
REMARK 465 LEU B 8
REMARK 465 VAL B 9
REMARK 465 ALA B 10
REMARK 465 ALA B 11
REMARK 465 CYS B 12
REMARK 465 ALA B 13
REMARK 465 ALA B 14
REMARK 465 VAL B 15
REMARK 465 ALA B 16
REMARK 465 ALA B 17
REMARK 465 ILE B 18
REMARK 465 ALA B 19
REMARK 465 VAL B 20
REMARK 465 THR B 21
REMARK 465 ARG B 22
REMARK 465 GLY B 23
REMARK 465 THR B 24
REMARK 465 ASP B 25
REMARK 465 THR B 26
REMARK 465 GLN B 27
REMARK 465 SER B 28
REMARK 465 GLU B 710
REMARK 465 LYS B 711
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 LYS A 133 -168.54 -111.12
REMARK 500 THR A 185 -19.26 -160.43
REMARK 500 LYS A 197 -72.91 -115.17
REMARK 500 ASP A 274 32.12 -149.37
REMARK 500 ASP A 288 -36.17 -138.17
REMARK 500 ALA A 322 91.40 -162.18
REMARK 500 ALA A 369 0.65 80.65
REMARK 500 PRO A 389 -19.23 -43.38
REMARK 500 SER A 434 74.97 -153.36
REMARK 500 PRO A 438 24.46 -75.84
REMARK 500 LYS A 471 71.39 -110.65
REMARK 500 TYR A 482 -75.81 -130.24
REMARK 500 PRO A 491 49.80 -77.12
REMARK 500 LYS A 528 -121.15 55.22
REMARK 500 SER A 562 -116.96 69.38
REMARK 500 VAL A 586 45.21 37.43
REMARK 500 SER A 624 110.02 -38.25
REMARK 500 ILE B 189 103.42 60.55
REMARK 500 LYS B 197 -73.55 -115.38
REMARK 500 ASP B 274 36.16 -154.61
REMARK 500 GLU B 290 -46.52 -135.07
REMARK 500 ASP B 298 24.26 -141.68
REMARK 500 ALA B 322 91.33 -163.72
REMARK 500 ALA B 369 -4.37 75.90
REMARK 500 SER B 434 71.70 -153.76
REMARK 500 TYR B 482 -85.75 -123.69
REMARK 500 PRO B 491 46.93 -78.64
REMARK 500 LYS B 528 -121.31 58.96
REMARK 500 SER B 562 -120.95 72.15
REMARK 500
REMARK 500 REMARK: NULL
DBREF 7VGB A 1 711 PDB 7VGB 7VGB 1 711
DBREF 7VGB B 1 711 PDB 7VGB 7VGB 1 711
SEQRES 1 A 711 MET ARG LYS PRO ALA ILE ALA LEU VAL ALA ALA CYS ALA
SEQRES 2 A 711 ALA VAL ALA ALA ILE ALA VAL THR ARG GLY THR ASP THR
SEQRES 3 A 711 GLN SER SER HIS ASN TYR PRO ASP THR ALA THR VAL ASP
SEQRES 4 A 711 GLN GLN ASP ASP TYR PHE GLY THR ALA VAL THR ASP PRO
SEQRES 5 A 711 TYR ARG TRP LEU GLU GLN GLN ASP SER LYS LEU VAL LYS
SEQRES 6 A 711 ASP TRP VAL THR ALA GLN ASN ASP PHE SER LEU PRO THR
SEQRES 7 A 711 LEU LYS ALA LEU PRO HIS TRP GLN LYS ILE ASN ASP ARG
SEQRES 8 A 711 LEU THR GLU LEU TRP GLN TYR GLU ARG TYR GLY VAL PRO
SEQRES 9 A 711 TYR LYS LYS ALA GLY GLN VAL PHE TYR GLU TYR ASN ASP
SEQRES 10 A 711 GLY SER TRP ASP GLN SER VAL PHE TYR ARG THR ALA ASP
SEQRES 11 A 711 ILE HIS LYS ASP GLY HIS VAL ILE LEU ASP PRO ARG ALA
SEQRES 12 A 711 LEU SER LYS ASP GLY THR ILE ALA ALA LYS ARG TYR THR
SEQRES 13 A 711 VAL SER PRO ASN GLY ARG TYR LEU ALA TYR GLY THR SER
SEQRES 14 A 711 ASP GLY GLY THR ASP TRP THR ASP TYR ARG VAL ARG ASP
SEQRES 15 A 711 LEU LYS THR ARG ARG MET ILE PRO ASP HIS LEU THR GLY
SEQRES 16 A 711 ILE LYS PHE SER ASP ALA SER TRP ALA LYS ASP GLU SER
SEQRES 17 A 711 GLY PHE TYR TYR SER ARG TYR PRO PHE LYS GLU ASP GLY
SEQRES 18 A 711 SER ALA ASP ASP SER LYS GLN VAL SER VAL TYR PHE HIS
SEQRES 19 A 711 LYS ILE GLY GLU PRO GLN SER LYS ASP GLN LEU ILE TYR
SEQRES 20 A 711 LYS ILE THR ASP HIS PRO THR ARG ASN PRO GLY ALA GLN
SEQRES 21 A 711 VAL SER ASP ASP GLY LYS TYR LEU ILE LEU GLY VAL PHE
SEQRES 22 A 711 ASP GLY TYR ASP SER ASN GLY ILE TYR TYR LYS ASP LEU
SEQRES 23 A 711 GLN ASP GLY GLU SER ARG VAL VAL LYS LEU LEU ASP ASP
SEQRES 24 A 711 TRP ASP ALA LEU TYR THR TYR LEU GLY ASN GLN GLY LYS
SEQRES 25 A 711 THR PHE TYR PHE GLU THR ASN VAL ASP ALA THR ASN GLY
SEQRES 26 A 711 ARG ILE ILE ALA ILE ASP ILE ASP LYS PRO GLN LYS ASP
SEQRES 27 A 711 HIS TRP LYS ILE LEU VAL PRO GLU GLN LYS ASP ALA LEU
SEQRES 28 A 711 GLN SER ALA SER LEU ILE GLY GLY ARG PHE VAL LEU HIS
SEQRES 29 A 711 TYR LEU GLU ASP ALA LYS SER LYS VAL VAL VAL THR ASP
SEQRES 30 A 711 LEU ASP GLY LYS GLN GLN TYR ALA LEU LYS LEU PRO GLY
SEQRES 31 A 711 MET GLY THR VAL GLU GLY PHE THR GLY ASP PRO ASP ASP
SEQRES 32 A 711 PRO GLU THR TYR TYR ALA PHE SER ASN PHE LEU THR PRO
SEQRES 33 A 711 PRO SER ILE TYR LYS LEU ASN VAL HIS SER GLY ASN SER
SEQRES 34 A 711 GLU ILE VAL LYS SER PRO LYS TYR PRO ALA ASP PHE SER
SEQRES 35 A 711 ASP TYR VAL VAL SER GLN GLU PHE PHE THR SER LYS ASP
SEQRES 36 A 711 GLY THR ARG VAL PRO LEU PHE LEU VAL HIS LYS LYS GLY
SEQRES 37 A 711 LEU LYS LYS TYR GLY LYS ASN PRO THR LEU LEU TYR GLY
SEQRES 38 A 711 TYR GLY GLY PHE ASN ALA ALA GLN LEU PRO ARG PHE TYR
SEQRES 39 A 711 THR ARG PHE ALA GLY TRP LEU ASP MET GLY GLY THR PHE
SEQRES 40 A 711 ALA MET VAL ASN LEU ARG GLY GLY SER GLU TYR GLY GLY
SEQRES 41 A 711 ALA TRP HIS LYS ALA GLY THR LYS LEU GLN LYS GLN ASN
SEQRES 42 A 711 VAL PHE ASP ASP PHE ILE GLY ALA ALA GLU TRP LEU ILE
SEQRES 43 A 711 GLU GLU LYS ILE THR SER PRO GLU LYS LEU GLY ILE MET
SEQRES 44 A 711 GLY ARG SER ASN GLY GLY LEU LEU VAL GLY ALA THR GLU
SEQRES 45 A 711 VAL GLN ARG PRO GLU LEU PHE ALA VAL ALA LEU PRO ILE
SEQRES 46 A 711 VAL GLY VAL LEU ASP MET LEU ARG TYR HIS THR ALA SER
SEQRES 47 A 711 ALA ASN ALA ARG GLN TRP SER SER ASP TYR GLY LEU SER
SEQRES 48 A 711 GLU ASN LYS ALA GLU PHE ASN ALA LEU TYR ALA TYR SER
SEQRES 49 A 711 PRO VAL HIS ASN THR LYS LYS GLY THR CYS TYR PRO ALA
SEQRES 50 A 711 THR LEU ILE THR THR ALA ASP ARG ASP ASP ARG VAL VAL
SEQRES 51 A 711 PRO TRP HIS SER TYR LYS PHE ALA ALA SER LEU GLN ARG
SEQRES 52 A 711 ASP GLN GLY CYS ASP ASN PRO ILE TYR LEU ALA VAL GLU
SEQRES 53 A 711 THR ARG ALA GLY HIS GLY ALA GLY LYS PRO VAL TRP MET
SEQRES 54 A 711 GLN VAL GLU ASP PHE THR ASN GLN TYR ALA PHE LEU ALA
SEQRES 55 A 711 ASP GLN LEU GLY LEU GLN VAL GLU LYS
SEQRES 1 B 711 MET ARG LYS PRO ALA ILE ALA LEU VAL ALA ALA CYS ALA
SEQRES 2 B 711 ALA VAL ALA ALA ILE ALA VAL THR ARG GLY THR ASP THR
SEQRES 3 B 711 GLN SER SER HIS ASN TYR PRO ASP THR ALA THR VAL ASP
SEQRES 4 B 711 GLN GLN ASP ASP TYR PHE GLY THR ALA VAL THR ASP PRO
SEQRES 5 B 711 TYR ARG TRP LEU GLU GLN GLN ASP SER LYS LEU VAL LYS
SEQRES 6 B 711 ASP TRP VAL THR ALA GLN ASN ASP PHE SER LEU PRO THR
SEQRES 7 B 711 LEU LYS ALA LEU PRO HIS TRP GLN LYS ILE ASN ASP ARG
SEQRES 8 B 711 LEU THR GLU LEU TRP GLN TYR GLU ARG TYR GLY VAL PRO
SEQRES 9 B 711 TYR LYS LYS ALA GLY GLN VAL PHE TYR GLU TYR ASN ASP
SEQRES 10 B 711 GLY SER TRP ASP GLN SER VAL PHE TYR ARG THR ALA ASP
SEQRES 11 B 711 ILE HIS LYS ASP GLY HIS VAL ILE LEU ASP PRO ARG ALA
SEQRES 12 B 711 LEU SER LYS ASP GLY THR ILE ALA ALA LYS ARG TYR THR
SEQRES 13 B 711 VAL SER PRO ASN GLY ARG TYR LEU ALA TYR GLY THR SER
SEQRES 14 B 711 ASP GLY GLY THR ASP TRP THR ASP TYR ARG VAL ARG ASP
SEQRES 15 B 711 LEU LYS THR ARG ARG MET ILE PRO ASP HIS LEU THR GLY
SEQRES 16 B 711 ILE LYS PHE SER ASP ALA SER TRP ALA LYS ASP GLU SER
SEQRES 17 B 711 GLY PHE TYR TYR SER ARG TYR PRO PHE LYS GLU ASP GLY
SEQRES 18 B 711 SER ALA ASP ASP SER LYS GLN VAL SER VAL TYR PHE HIS
SEQRES 19 B 711 LYS ILE GLY GLU PRO GLN SER LYS ASP GLN LEU ILE TYR
SEQRES 20 B 711 LYS ILE THR ASP HIS PRO THR ARG ASN PRO GLY ALA GLN
SEQRES 21 B 711 VAL SER ASP ASP GLY LYS TYR LEU ILE LEU GLY VAL PHE
SEQRES 22 B 711 ASP GLY TYR ASP SER ASN GLY ILE TYR TYR LYS ASP LEU
SEQRES 23 B 711 GLN ASP GLY GLU SER ARG VAL VAL LYS LEU LEU ASP ASP
SEQRES 24 B 711 TRP ASP ALA LEU TYR THR TYR LEU GLY ASN GLN GLY LYS
SEQRES 25 B 711 THR PHE TYR PHE GLU THR ASN VAL ASP ALA THR ASN GLY
SEQRES 26 B 711 ARG ILE ILE ALA ILE ASP ILE ASP LYS PRO GLN LYS ASP
SEQRES 27 B 711 HIS TRP LYS ILE LEU VAL PRO GLU GLN LYS ASP ALA LEU
SEQRES 28 B 711 GLN SER ALA SER LEU ILE GLY GLY ARG PHE VAL LEU HIS
SEQRES 29 B 711 TYR LEU GLU ASP ALA LYS SER LYS VAL VAL VAL THR ASP
SEQRES 30 B 711 LEU ASP GLY LYS GLN GLN TYR ALA LEU LYS LEU PRO GLY
SEQRES 31 B 711 MET GLY THR VAL GLU GLY PHE THR GLY ASP PRO ASP ASP
SEQRES 32 B 711 PRO GLU THR TYR TYR ALA PHE SER ASN PHE LEU THR PRO
SEQRES 33 B 711 PRO SER ILE TYR LYS LEU ASN VAL HIS SER GLY ASN SER
SEQRES 34 B 711 GLU ILE VAL LYS SER PRO LYS TYR PRO ALA ASP PHE SER
SEQRES 35 B 711 ASP TYR VAL VAL SER GLN GLU PHE PHE THR SER LYS ASP
SEQRES 36 B 711 GLY THR ARG VAL PRO LEU PHE LEU VAL HIS LYS LYS GLY
SEQRES 37 B 711 LEU LYS LYS TYR GLY LYS ASN PRO THR LEU LEU TYR GLY
SEQRES 38 B 711 TYR GLY GLY PHE ASN ALA ALA GLN LEU PRO ARG PHE TYR
SEQRES 39 B 711 THR ARG PHE ALA GLY TRP LEU ASP MET GLY GLY THR PHE
SEQRES 40 B 711 ALA MET VAL ASN LEU ARG GLY GLY SER GLU TYR GLY GLY
SEQRES 41 B 711 ALA TRP HIS LYS ALA GLY THR LYS LEU GLN LYS GLN ASN
SEQRES 42 B 711 VAL PHE ASP ASP PHE ILE GLY ALA ALA GLU TRP LEU ILE
SEQRES 43 B 711 GLU GLU LYS ILE THR SER PRO GLU LYS LEU GLY ILE MET
SEQRES 44 B 711 GLY ARG SER ASN GLY GLY LEU LEU VAL GLY ALA THR GLU
SEQRES 45 B 711 VAL GLN ARG PRO GLU LEU PHE ALA VAL ALA LEU PRO ILE
SEQRES 46 B 711 VAL GLY VAL LEU ASP MET LEU ARG TYR HIS THR ALA SER
SEQRES 47 B 711 ALA ASN ALA ARG GLN TRP SER SER ASP TYR GLY LEU SER
SEQRES 48 B 711 GLU ASN LYS ALA GLU PHE ASN ALA LEU TYR ALA TYR SER
SEQRES 49 B 711 PRO VAL HIS ASN THR LYS LYS GLY THR CYS TYR PRO ALA
SEQRES 50 B 711 THR LEU ILE THR THR ALA ASP ARG ASP ASP ARG VAL VAL
SEQRES 51 B 711 PRO TRP HIS SER TYR LYS PHE ALA ALA SER LEU GLN ARG
SEQRES 52 B 711 ASP GLN GLY CYS ASP ASN PRO ILE TYR LEU ALA VAL GLU
SEQRES 53 B 711 THR ARG ALA GLY HIS GLY ALA GLY LYS PRO VAL TRP MET
SEQRES 54 B 711 GLN VAL GLU ASP PHE THR ASN GLN TYR ALA PHE LEU ALA
SEQRES 55 B 711 ASP GLN LEU GLY LEU GLN VAL GLU LYS
HET GOL A 801 6
HET GOL A 802 6
HET GOL A 803 6
HET GOL A 804 6
HET GOL A 805 6
HET IMD A 806 5
HET TRS A 807 8
HET TRS A 808 8
HET PEG A 809 7
HET PEG A 810 7
HET NI A 811 1
HET TMO A 812 5
HET GOL B 801 6
HET GOL B 802 6
HET TRS B 803 8
HET TRS B 804 8
HET NI B 805 1
HET TMO B 806 5
HETNAM GOL GLYCEROL
HETNAM IMD IMIDAZOLE
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM NI NICKEL (II) ION
HETNAM TMO TRIMETHYLAMINE OXIDE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN TRS TRIS BUFFER
FORMUL 3 GOL 7(C3 H8 O3)
FORMUL 8 IMD C3 H5 N2 1+
FORMUL 9 TRS 4(C4 H12 N O3 1+)
FORMUL 11 PEG 2(C4 H10 O3)
FORMUL 13 NI 2(NI 2+)
FORMUL 14 TMO 2(C3 H9 N O)
FORMUL 21 HOH *1016(H2 O)
HELIX 1 AA1 TYR A 53 GLN A 58 5 6
HELIX 2 AA2 SER A 61 ALA A 81 1 21
HELIX 3 AA3 HIS A 84 TRP A 96 1 13
HELIX 4 AA4 ASP A 140 SER A 145 5 6
HELIX 5 AA5 PRO A 239 ASP A 243 5 5
HELIX 6 AA6 GLN A 336 TRP A 340 5 5
HELIX 7 AA7 TYR A 494 MET A 503 1 10
HELIX 8 AA8 GLY A 519 ALA A 525 1 7
HELIX 9 AA9 GLY A 526 GLN A 530 5 5
HELIX 10 AB1 LYS A 531 GLU A 548 1 18
HELIX 11 AB2 SER A 552 GLU A 554 5 3
HELIX 12 AB3 SER A 562 ARG A 575 1 14
HELIX 13 AB4 PRO A 576 PHE A 579 5 4
HELIX 14 AB5 ARG A 593 ALA A 597 5 5
HELIX 15 AB6 SER A 598 GLN A 603 1 6
HELIX 16 AB7 TRP A 604 GLY A 609 1 6
HELIX 17 AB8 ASN A 613 SER A 624 1 12
HELIX 18 AB9 PRO A 625 ASN A 628 5 4
HELIX 19 AC1 PRO A 651 GLN A 665 1 15
HELIX 20 AC2 PRO A 686 GLY A 706 1 21
HELIX 21 AC3 TYR B 53 GLN B 58 5 6
HELIX 22 AC4 SER B 61 ALA B 81 1 21
HELIX 23 AC5 HIS B 84 TRP B 96 1 13
HELIX 24 AC6 ASP B 140 LEU B 144 5 5
HELIX 25 AC7 PRO B 239 ASP B 243 5 5
HELIX 26 AC8 GLN B 336 TRP B 340 5 5
HELIX 27 AC9 ASP B 440 SER B 442 5 3
HELIX 28 AD1 TYR B 494 MET B 503 1 10
HELIX 29 AD2 TYR B 518 ALA B 525 1 8
HELIX 30 AD3 GLY B 526 GLN B 530 5 5
HELIX 31 AD4 LYS B 531 GLU B 548 1 18
HELIX 32 AD5 SER B 552 GLU B 554 5 3
HELIX 33 AD6 SER B 562 ARG B 575 1 14
HELIX 34 AD7 PRO B 576 PHE B 579 5 4
HELIX 35 AD8 ARG B 593 ALA B 597 5 5
HELIX 36 AD9 SER B 598 GLN B 603 1 6
HELIX 37 AE1 TRP B 604 GLY B 609 1 6
HELIX 38 AE2 ASN B 613 SER B 624 1 12
HELIX 39 AE3 PRO B 625 ASN B 628 5 4
HELIX 40 AE4 PRO B 651 GLN B 665 1 15
HELIX 41 AE5 PRO B 686 GLY B 706 1 21
SHEET 1 AA1 2 GLN A 41 TYR A 44 0
SHEET 2 AA1 2 THR A 47 THR A 50 -1 O THR A 47 N TYR A 44
SHEET 1 AA2 3 ARG A 100 TYR A 101 0
SHEET 2 AA2 3 GLN A 110 ASN A 116 -1 O ASN A 116 N ARG A 100
SHEET 3 AA2 3 TYR A 105 LYS A 107 -1 N TYR A 105 O PHE A 112
SHEET 1 AA3 4 ARG A 100 TYR A 101 0
SHEET 2 AA3 4 GLN A 110 ASN A 116 -1 O ASN A 116 N ARG A 100
SHEET 3 AA3 4 VAL A 124 THR A 128 -1 O VAL A 124 N TYR A 115
SHEET 4 AA3 4 HIS A 136 LEU A 139 -1 O ILE A 138 N PHE A 125
SHEET 1 AA4 4 ILE A 150 VAL A 157 0
SHEET 2 AA4 4 TYR A 163 ASP A 170 -1 O ALA A 165 N THR A 156
SHEET 3 AA4 4 ASP A 177 ASP A 182 -1 O ARG A 179 N TYR A 166
SHEET 4 AA4 4 ARG A 187 MET A 188 -1 O ARG A 187 N ASP A 182
SHEET 1 AA5 4 SER A 202 TRP A 203 0
SHEET 2 AA5 4 GLY A 209 ARG A 214 -1 O TYR A 211 N SER A 202
SHEET 3 AA5 4 SER A 230 LYS A 235 -1 O HIS A 234 N PHE A 210
SHEET 4 AA5 4 GLN A 244 TYR A 247 -1 O ILE A 246 N VAL A 231
SHEET 1 AA6 4 ASN A 256 VAL A 261 0
SHEET 2 AA6 4 TYR A 267 PHE A 273 -1 O ILE A 269 N GLN A 260
SHEET 3 AA6 4 ASN A 279 ASP A 285 -1 O TYR A 282 N LEU A 270
SHEET 4 AA6 4 VAL A 294 LEU A 297 -1 O LEU A 297 N ILE A 281
SHEET 1 AA7 4 TYR A 304 GLN A 310 0
SHEET 2 AA7 4 THR A 313 THR A 318 -1 O GLU A 317 N THR A 305
SHEET 3 AA7 4 ARG A 326 ASP A 331 -1 O ILE A 330 N PHE A 314
SHEET 4 AA7 4 LYS A 341 VAL A 344 -1 O LYS A 341 N ALA A 329
SHEET 1 AA8 4 ALA A 350 ILE A 357 0
SHEET 2 AA8 4 ARG A 360 GLU A 367 -1 O HIS A 364 N SER A 353
SHEET 3 AA8 4 LYS A 370 THR A 376 -1 O LYS A 372 N TYR A 365
SHEET 4 AA8 4 GLN A 382 LEU A 386 -1 O GLN A 383 N VAL A 375
SHEET 1 AA9 4 THR A 393 GLY A 396 0
SHEET 2 AA9 4 GLU A 405 ASN A 412 -1 O SER A 411 N THR A 393
SHEET 3 AA9 4 THR A 415 ASN A 423 -1 O LEU A 422 N THR A 406
SHEET 4 AA9 4 SER A 429 LYS A 433 -1 O VAL A 432 N ILE A 419
SHEET 1 AB1 8 TYR A 444 THR A 452 0
SHEET 2 AB1 8 ARG A 458 LYS A 466 -1 O LEU A 463 N SER A 447
SHEET 3 AB1 8 THR A 506 VAL A 510 -1 O PHE A 507 N VAL A 464
SHEET 4 AB1 8 THR A 477 TYR A 480 1 N TYR A 480 O ALA A 508
SHEET 5 AB1 8 LEU A 556 ARG A 561 1 O GLY A 557 N LEU A 479
SHEET 6 AB1 8 VAL A 581 ILE A 585 1 O LEU A 583 N ILE A 558
SHEET 7 AB1 8 ALA A 637 ALA A 643 1 O THR A 641 N PRO A 584
SHEET 8 AB1 8 ILE A 671 GLU A 676 1 O TYR A 672 N THR A 638
SHEET 1 AB2 2 GLN B 41 TYR B 44 0
SHEET 2 AB2 2 THR B 47 THR B 50 -1 O THR B 47 N TYR B 44
SHEET 1 AB3 3 ARG B 100 TYR B 101 0
SHEET 2 AB3 3 GLN B 110 ASN B 116 -1 O ASN B 116 N ARG B 100
SHEET 3 AB3 3 TYR B 105 LYS B 107 -1 N TYR B 105 O PHE B 112
SHEET 1 AB4 4 ARG B 100 TYR B 101 0
SHEET 2 AB4 4 GLN B 110 ASN B 116 -1 O ASN B 116 N ARG B 100
SHEET 3 AB4 4 VAL B 124 THR B 128 -1 O THR B 128 N VAL B 111
SHEET 4 AB4 4 HIS B 136 LEU B 139 -1 O ILE B 138 N PHE B 125
SHEET 1 AB5 3 ILE B 150 VAL B 157 0
SHEET 2 AB5 3 TYR B 163 ASP B 170 -1 O ALA B 165 N THR B 156
SHEET 3 AB5 3 ASP B 177 ASP B 182 -1 O ARG B 181 N LEU B 164
SHEET 1 AB6 4 SER B 202 TRP B 203 0
SHEET 2 AB6 4 GLY B 209 ARG B 214 -1 O TYR B 211 N SER B 202
SHEET 3 AB6 4 SER B 230 LYS B 235 -1 O TYR B 232 N TYR B 212
SHEET 4 AB6 4 GLN B 244 TYR B 247 -1 O ILE B 246 N VAL B 231
SHEET 1 AB7 4 ASN B 256 VAL B 261 0
SHEET 2 AB7 4 TYR B 267 PHE B 273 -1 O ILE B 269 N GLN B 260
SHEET 3 AB7 4 ASN B 279 ASP B 285 -1 O TYR B 282 N LEU B 270
SHEET 4 AB7 4 VAL B 294 LEU B 297 -1 O LEU B 297 N ILE B 281
SHEET 1 AB8 4 TYR B 304 GLN B 310 0
SHEET 2 AB8 4 THR B 313 THR B 318 -1 O TYR B 315 N LEU B 307
SHEET 3 AB8 4 ARG B 326 ASP B 331 -1 O ILE B 330 N PHE B 314
SHEET 4 AB8 4 LYS B 341 VAL B 344 -1 O LYS B 341 N ALA B 329
SHEET 1 AB9 4 ALA B 350 ILE B 357 0
SHEET 2 AB9 4 ARG B 360 GLU B 367 -1 O ARG B 360 N ILE B 357
SHEET 3 AB9 4 LYS B 370 ASP B 377 -1 O LYS B 372 N TYR B 365
SHEET 4 AB9 4 GLN B 382 ALA B 385 -1 O GLN B 383 N VAL B 375
SHEET 1 AC1 4 THR B 393 GLY B 396 0
SHEET 2 AC1 4 GLU B 405 ASN B 412 -1 O SER B 411 N THR B 393
SHEET 3 AC1 4 THR B 415 ASN B 423 -1 O TYR B 420 N TYR B 408
SHEET 4 AC1 4 ASN B 428 LYS B 433 -1 O VAL B 432 N ILE B 419
SHEET 1 AC2 8 TYR B 444 THR B 452 0
SHEET 2 AC2 8 ARG B 458 LYS B 466 -1 O LEU B 463 N SER B 447
SHEET 3 AC2 8 THR B 506 VAL B 510 -1 O PHE B 507 N VAL B 464
SHEET 4 AC2 8 THR B 477 TYR B 480 1 N LEU B 478 O THR B 506
SHEET 5 AC2 8 LEU B 556 ARG B 561 1 O GLY B 557 N THR B 477
SHEET 6 AC2 8 VAL B 581 ILE B 585 1 O ILE B 585 N GLY B 560
SHEET 7 AC2 8 ALA B 637 ALA B 643 1 O ALA B 637 N ALA B 582
SHEET 8 AC2 8 ILE B 671 GLU B 676 1 O TYR B 672 N ILE B 640
SSBOND 1 CYS A 634 CYS A 667 1555 1555 2.11
SSBOND 2 CYS B 634 CYS B 667 1555 1555 2.09
CRYST1 60.390 125.395 89.848 90.00 96.84 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 0.016559 0.000000 0.001985 0.00000
SCALE2 0.000000 0.007975 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011210 0.00000
TER 5447 VAL A 709
TER 10894 VAL B 709
MASTER 356 0 18 41 81 0 0 612013 2 107 110
END |