| content |
HEADER HYDROLASE 16-MAY-08 2VTV
TITLE PHAZ7 DEPOLYMERASE FROM PAUCIMONAS LEMOIGNEI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHB DEPOLYMERASE PHAZ7;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 39-380;
COMPND 5 EC: 3.1.1.75
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: PAUCIMONAS LEMOIGNEI
KEYWDS HYDROLASE, POLYMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.C.PAPAGEORGIOU,S.HERMAWAN,C.B.SINGH,D.JENDROSSEK
REVDAT 1 26-AUG-08 2VTV 0
JRNL AUTH A.C.PAPAGEORGIOU,S.HERMAWAN,C.B.SINGH,D.JENDROSSEK
JRNL TITL STRUCTURAL BASIS OF POLY(3-HYDROXYBUTYRATE)
JRNL TITL 2 HYDROLYSIS BY PHAZ7 DEPOLYMERASE FROM PAUCIMONAS
JRNL TITL 3 LEMOIGNEI.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH E.G.KAPETANIOU,R.BRAAZ,D.JENDROSSEK,
REMARK 1 AUTH 2 A.C.PAPAGEORGIOU
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY ANALYSIS OF
REMARK 1 TITL 2 A NOVEL THERMOALKALOPHILIC POLY(3-HYDROXYBUTYRATE)
REMARK 1 TITL 3 DEPOLYMERASE (PHAZ7) FROM PAUCIMONAS LEMOIGNEI.
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.F V. 61 479 2005
REMARK 1 REFN ASTM ACSFCL DK ISSN 1744-3091
REMARK 2
REMARK 2 RESOLUTION. 1.9 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 87.04
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.34
REMARK 3 NUMBER OF REFLECTIONS : 51068
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) : 0.14459
REMARK 3 R VALUE (WORKING SET) : 0.14239
REMARK 3 FREE R VALUE : 0.18758
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.9
REMARK 3 FREE R VALUE TEST SET COUNT : 2609
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) : 1.904
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.954
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3427
REMARK 3 BIN R VALUE (WORKING SET) : 0.165
REMARK 3 BIN FREE R VALUE SET COUNT : 176
REMARK 3 BIN FREE R VALUE : 0.214
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5083
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 1001
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.464
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.59
REMARK 3 B22 (A**2) : -0.80
REMARK 3 B33 (A**2) : 0.14
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : -0.20
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.132
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.126
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.077
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.553
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.939
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED (A): 5233 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED (DEGREES): 7120 ; 1.227 ; 1.920
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 688 ; 5.927 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 214 ;34.737 ;23.738
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 735 ;11.423 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;20.355 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 748 ; 0.102 ; 0.200
REMARK 3 GENERAL PLANES REFINED (A): 4080 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED (A): 2872 ; 0.196 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED (A): 3633 ; 0.311 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED (A): 917 ; 0.146 ; 0.200
REMARK 3 SYMMETRY VDW REFINED (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED (A): 65 ; 0.160 ; 0.200
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED (A**2): 3397 ; 0.616 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED (A**2): 5316 ; 1.012 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED (A**2): 2163 ; 1.666 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED (A**2): 1798 ; 2.068 ; 4.500
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF 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: RESIDUES 293 AND 294 FROM BOTH
REMARK 3 SUBUNITS HAVE NOT BEEN MODELLED DUE TO LACK OF DENSITY
REMARK 4
REMARK 4 2VTV COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 16-MAY-2008.
REMARK 100 THE EBI ID CODE IS EBI-36285.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53749
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.90
REMARK 200 RESOLUTION RANGE LOW (A) : 99.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 15
REMARK 200 R MERGE (I) : 0.06
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 30.10
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.22
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 6.50
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.4
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.2
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MICRODIALYSIS, PH 10.5, NACL
REMARK 280 150 MM
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 1/2+X,1/2+Y,Z
REMARK 290 4555 1/2-X,1/2+Y,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 88.19150
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.19000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 88.19150
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 23.19000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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: PQS
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 HOH B2463 LIES ON A SPECIAL POSITION.
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 TYR A 293
REMARK 465 ASN A 294
REMARK 465 TYR B 293
REMARK 465 ASN B 294
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 B 2009 - O HOH B 2018 2.19
REMARK 500 O HOH B 2107 - O HOH B 2364 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCELIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 SER A 250 N - CA - C ANGL. DEV. = 17.3 DEGREES
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 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 55 -8.41 -58.56
REMARK 500 ALA A 181 67.78 -153.52
REMARK 500 SER A 186 -153.05 -86.47
REMARK 500 ASN A 210 78.93 -156.73
REMARK 500 PHE A 251 -24.96 122.32
REMARK 500 THR B 2 67.40 97.72
REMARK 500 SER B 55 -6.16 -59.79
REMARK 500 SER B 136 -132.28 56.58
REMARK 500 ALA B 181 63.69 -150.55
REMARK 500 SER B 186 -162.10 -77.15
REMARK 500 ASN B 210 83.66 -155.28
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1343
DBREF 2VTV A 1 342 UNP Q939Q9 Q939Q9_PSELE 39 380
DBREF 2VTV B 1 342 UNP Q939Q9 Q939Q9_PSELE 39 380
SEQRES 1 A 342 LEU THR CYS GLY THR ASN SER GLY PHE VAL CYS LYS GLY
SEQRES 2 A 342 THR GLN THR GLN TYR ALA GLY GLY PHE ALA PRO GLY VAL
SEQRES 3 A 342 GLY TYR GLY GLY PHE GLY GLY GLY SER CYS THR ALA THR
SEQRES 4 A 342 LYS THR PRO VAL ILE PHE ILE HIS GLY ASN GLY ASP ASN
SEQRES 5 A 342 ALA ILE SER PHE ASP MET PRO PRO GLY ASN VAL SER GLY
SEQRES 6 A 342 TYR GLY THR PRO ALA ARG SER VAL TYR ALA GLU LEU LYS
SEQRES 7 A 342 ALA ARG GLY TYR ASN ASP CYS GLU ILE PHE GLY VAL THR
SEQRES 8 A 342 TYR LEU SER SER SER GLU GLN GLY SER ALA GLN TYR ASN
SEQRES 9 A 342 TYR HIS SER SER THR LYS TYR ALA ILE ILE LYS THR PHE
SEQRES 10 A 342 ILE ASP LYS VAL LYS ALA TYR THR GLY LYS SER GLN VAL
SEQRES 11 A 342 ASP ILE VAL ALA HIS SER MET GLY VAL SER MET SER LEU
SEQRES 12 A 342 ALA THR LEU GLN TYR TYR ASN ASN TRP THR SER VAL ARG
SEQRES 13 A 342 LYS PHE ILE ASN LEU ALA GLY GLY ILE ARG GLY LEU TYR
SEQRES 14 A 342 SER CYS TYR TYR THR GLY TYR ALA ASN ALA ALA ALA PRO
SEQRES 15 A 342 THR CYS GLY SER GLN ASN TYR TYR ASN SER TYR THR PHE
SEQRES 16 A 342 GLY PHE PHE PRO GLU GLY TRP TYR TYR GLY VAL TRP VAL
SEQRES 17 A 342 SER ASN PRO TRP THR GLY SER GLY SER THR ASN SER MET
SEQRES 18 A 342 ARG ASP MET PRO ALA LYS ARG THR ALA VAL SER PHE TYR
SEQRES 19 A 342 THR LEU SER ALA GLY PHE LYS ASP GLN VAL GLY CYS ALA
SEQRES 20 A 342 THR ALA SER PHE TRP ALA GLY CYS ASP SER ALA ALA LYS
SEQRES 21 A 342 PHE ALA SER THR THR SER ASN VAL LYS ALA GLN ILE ASN
SEQRES 22 A 342 VAL GLY ALA GLY SER ASN ALA THR GLN ALA ASP TYR ASP
SEQRES 23 A 342 TRP ALA ASP GLY MET PRO TYR ASN ALA GLY GLY GLY ASP
SEQRES 24 A 342 THR THR ASN GLY VAL GLY HIS PHE ARG THR LYS THR ASN
SEQRES 25 A 342 THR GLY ALA ILE ILE GLN ARG MET LEU LEU THR THR CYS
SEQRES 26 A 342 THR GLY LEU ASP CYS ALA ALA GLU TYR THR THR GLY PRO
SEQRES 27 A 342 LYS ALA ALA TYR
SEQRES 1 B 342 LEU THR CYS GLY THR ASN SER GLY PHE VAL CYS LYS GLY
SEQRES 2 B 342 THR GLN THR GLN TYR ALA GLY GLY PHE ALA PRO GLY VAL
SEQRES 3 B 342 GLY TYR GLY GLY PHE GLY GLY GLY SER CYS THR ALA THR
SEQRES 4 B 342 LYS THR PRO VAL ILE PHE ILE HIS GLY ASN GLY ASP ASN
SEQRES 5 B 342 ALA ILE SER PHE ASP MET PRO PRO GLY ASN VAL SER GLY
SEQRES 6 B 342 TYR GLY THR PRO ALA ARG SER VAL TYR ALA GLU LEU LYS
SEQRES 7 B 342 ALA ARG GLY TYR ASN ASP CYS GLU ILE PHE GLY VAL THR
SEQRES 8 B 342 TYR LEU SER SER SER GLU GLN GLY SER ALA GLN TYR ASN
SEQRES 9 B 342 TYR HIS SER SER THR LYS TYR ALA ILE ILE LYS THR PHE
SEQRES 10 B 342 ILE ASP LYS VAL LYS ALA TYR THR GLY LYS SER GLN VAL
SEQRES 11 B 342 ASP ILE VAL ALA HIS SER MET GLY VAL SER MET SER LEU
SEQRES 12 B 342 ALA THR LEU GLN TYR TYR ASN ASN TRP THR SER VAL ARG
SEQRES 13 B 342 LYS PHE ILE ASN LEU ALA GLY GLY ILE ARG GLY LEU TYR
SEQRES 14 B 342 SER CYS TYR TYR THR GLY TYR ALA ASN ALA ALA ALA PRO
SEQRES 15 B 342 THR CYS GLY SER GLN ASN TYR TYR ASN SER TYR THR PHE
SEQRES 16 B 342 GLY PHE PHE PRO GLU GLY TRP TYR TYR GLY VAL TRP VAL
SEQRES 17 B 342 SER ASN PRO TRP THR GLY SER GLY SER THR ASN SER MET
SEQRES 18 B 342 ARG ASP MET PRO ALA LYS ARG THR ALA VAL SER PHE TYR
SEQRES 19 B 342 THR LEU SER ALA GLY PHE LYS ASP GLN VAL GLY CYS ALA
SEQRES 20 B 342 THR ALA SER PHE TRP ALA GLY CYS ASP SER ALA ALA LYS
SEQRES 21 B 342 PHE ALA SER THR THR SER ASN VAL LYS ALA GLN ILE ASN
SEQRES 22 B 342 VAL GLY ALA GLY SER ASN ALA THR GLN ALA ASP TYR ASP
SEQRES 23 B 342 TRP ALA ASP GLY MET PRO TYR ASN ALA GLY GLY GLY ASP
SEQRES 24 B 342 THR THR ASN GLY VAL GLY HIS PHE ARG THR LYS THR ASN
SEQRES 25 B 342 THR GLY ALA ILE ILE GLN ARG MET LEU LEU THR THR CYS
SEQRES 26 B 342 THR GLY LEU ASP CYS ALA ALA GLU TYR THR THR GLY PRO
SEQRES 27 B 342 LYS ALA ALA TYR
HET GOL A1343 6
HETNAM GOL GLYCEROL
FORMUL 3 GOL C3 H8 O3
FORMUL 4 HOH *1001(H2 O1)
HELIX 1 1 ASN A 52 MET A 58 5 7
HELIX 2 2 SER A 72 ARG A 80 1 9
HELIX 3 3 SER A 94 SER A 100 1 7
HELIX 4 4 ALA A 101 ASN A 104 5 4
HELIX 5 5 SER A 107 GLY A 126 1 20
HELIX 6 6 SER A 136 ASN A 150 1 15
HELIX 7 7 ASN A 151 THR A 153 5 3
HELIX 8 8 TYR A 169 GLY A 175 1 7
HELIX 9 9 ALA A 181 GLY A 185 5 5
HELIX 10 10 SER A 220 ARG A 222 5 3
HELIX 11 11 ASP A 223 ARG A 228 1 6
HELIX 12 12 ALA A 238 ASP A 242 5 5
HELIX 13 13 GLY A 254 ALA A 258 5 5
HELIX 14 14 ASP A 286 GLY A 290 5 5
HELIX 15 15 PHE A 307 ASN A 312 1 6
HELIX 16 16 THR A 313 THR A 323 1 11
HELIX 17 17 THR A 326 ALA A 332 5 7
HELIX 18 18 ASN B 52 MET B 58 5 7
HELIX 19 19 SER B 72 ARG B 80 1 9
HELIX 20 20 SER B 94 GLY B 99 1 6
HELIX 21 21 SER B 100 ASN B 104 5 5
HELIX 22 22 SER B 107 GLY B 126 1 20
HELIX 23 23 SER B 136 ASN B 150 1 15
HELIX 24 24 ASN B 151 THR B 153 5 3
HELIX 25 25 SER B 170 GLY B 175 1 6
HELIX 26 26 ALA B 181 GLY B 185 5 5
HELIX 27 27 SER B 220 ARG B 222 5 3
HELIX 28 28 ASP B 223 ARG B 228 1 6
HELIX 29 29 ALA B 238 LYS B 241 5 4
HELIX 30 30 ASP B 242 ALA B 247 1 6
HELIX 31 31 GLY B 254 ALA B 258 5 5
HELIX 32 32 ASP B 286 GLY B 290 5 5
HELIX 33 33 PHE B 307 ASN B 312 1 6
HELIX 34 34 THR B 313 THR B 323 1 11
HELIX 35 35 THR B 326 ALA B 332 5 7
SHEET 1 AA 9 THR A 16 TYR A 18 0
SHEET 2 AA 9 GLY A 30 GLY A 32 1 O GLY A 30 N GLN A 17
SHEET 3 AA 9 ILE A 87 VAL A 90 -1 O GLY A 89 N PHE A 31
SHEET 4 AA 9 VAL A 43 ILE A 46 1 O VAL A 43 N PHE A 88
SHEET 5 AA 9 VAL A 130 HIS A 135 1 O ASP A 131 N ILE A 44
SHEET 6 AA 9 VAL A 155 LEU A 161 1 N ARG A 156 O VAL A 130
SHEET 7 AA 9 SER A 232 SER A 237 1 O SER A 232 N PHE A 158
SHEET 8 AA 9 VAL A 268 ASN A 273 1 N LYS A 269 O PHE A 233
SHEET 9 AA 9 ALA A 340 ALA A 341 -1 O ALA A 340 N ASN A 273
SHEET 1 AB 2 GLY A 201 TYR A 203 0
SHEET 2 AB 2 VAL A 206 VAL A 208 -1 O VAL A 206 N TYR A 203
SHEET 1 BA 9 THR B 16 TYR B 18 0
SHEET 2 BA 9 GLY B 30 GLY B 32 1 O GLY B 30 N GLN B 17
SHEET 3 BA 9 ILE B 87 VAL B 90 -1 O GLY B 89 N PHE B 31
SHEET 4 BA 9 VAL B 43 ILE B 46 1 O VAL B 43 N PHE B 88
SHEET 5 BA 9 VAL B 130 HIS B 135 1 O ASP B 131 N ILE B 44
SHEET 6 BA 9 VAL B 155 LEU B 161 1 N ARG B 156 O VAL B 130
SHEET 7 BA 9 SER B 232 SER B 237 1 O SER B 232 N PHE B 158
SHEET 8 BA 9 VAL B 268 ASN B 273 1 N LYS B 269 O PHE B 233
SHEET 9 BA 9 ALA B 340 ALA B 341 -1 O ALA B 340 N ASN B 273
SHEET 1 BB 2 GLY B 201 TYR B 203 0
SHEET 2 BB 2 VAL B 206 VAL B 208 -1 O VAL B 206 N TYR B 203
SSBOND 1 CYS A 3 CYS A 11 1555 1555 2.07
SSBOND 2 CYS A 246 CYS A 255 1555 1555 2.07
SSBOND 3 CYS A 325 CYS A 330 1555 1555 2.11
SSBOND 4 CYS B 3 CYS B 11 1555 1555 2.06
SSBOND 5 CYS B 171 CYS B 184 1555 1555 2.10
SSBOND 6 CYS B 246 CYS B 255 1555 1555 2.07
SSBOND 7 CYS B 325 CYS B 330 1555 1555 2.09
CISPEP 1 SER A 250 PHE A 251 0 -23.71
CISPEP 2 LEU B 1 THR B 2 0 -28.97
SITE 1 AC1 10 ARG A 166 SER A 257 LYS A 260 HOH A2302
SITE 2 AC1 10 HOH A2523 HOH A2524 ARG B 166 SER B 257
SITE 3 AC1 10 LYS B 260 HOH B2268
CRYST1 176.383 46.380 85.779 90.00 99.78 90.00 C 1 2 1 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 0.005669 0.000000 0.000977 0.00000
SCALE2 0.000000 0.021561 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011830 0.00000
TER 2549 TYR A 342
TER 5085 TYR B 342
MASTER 320 0 1 35 22 0 3 6 6090 2 20 54
END |