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HEADER HYDROLASE 15-APR-13 4K6G
TITLE CRYSTAL STRUCTURE OF CALB FROM CANDIDA ANTARCTICA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE B;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CALB;
COMPND 5 EC: 3.1.1.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CANDIDA ANTARCTICA;
SOURCE 3 ORGANISM_COMMON: YEAST;
SOURCE 4 ORGANISM_TAXID: 34362;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: ROSETTA AODE3AI;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS LIPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.AN,Y.XIE,Y.FENG,G.WU
REVDAT 1 29-JAN-14 4K6G 0
JRNL AUTH Y.XIE,J.AN,G.YANG,G.WU,Y.ZHANG,L.CUI,Y.FENG
JRNL TITL ENHANCED ENZYME KINETIC STABILITY BY INCREASING RIGIDITY
JRNL TITL 2 WITHIN THE ACTIVE SITE
JRNL REF J.BIOL.CHEM. 2014
JRNL REFN ESSN 1083-351X
JRNL DOI 10.1074/JBC.M113.536045
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 86931
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) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4353
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) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5885
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.34
REMARK 3 BIN R VALUE (WORKING SET) : 0.2090
REMARK 3 BIN FREE R VALUE SET COUNT : 318
REMARK 3 BIN FREE R VALUE : 0.2220
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4644
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 8
REMARK 3 SOLVENT ATOMS : 402
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 11.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.09000
REMARK 3 B22 (A**2) : 0.33000
REMARK 3 B33 (A**2) : -0.44000
REMARK 3 B12 (A**2) : -0.00000
REMARK 3 B13 (A**2) : -0.10000
REMARK 3 B23 (A**2) : -0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.083
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.077
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.046
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.195
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4770 ; 0.005 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6550 ; 1.091 ; 1.973
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 631 ; 5.452 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 165 ;33.806 ;25.030
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 679 ;12.171 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;17.091 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 767 ; 0.068 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3632 ; 0.005 ; 0.022
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 : 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 USED IF PRESENT IN
REMARK 3 THE INPUT U VALUES: REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4K6G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-MAY-13.
REMARK 100 THE RCSB ID CODE IS RCSB078950.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-OCT-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 171636
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.09700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 18.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.55
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.18900
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 (%): 39.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 3350, 0.2M NAAC, 0.1M TRIS-BIS
REMARK 280 PH6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 287K
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 40.82100
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 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 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 ALA A 141
REMARK 465 GLY A 142
REMARK 465 PRO A 143
REMARK 465 LEU A 144
REMARK 465 ASP A 145
REMARK 465 ALA A 146
REMARK 465 LEU A 147
REMARK 465 HIS A 320
REMARK 465 HIS A 321
REMARK 465 HIS A 322
REMARK 465 HIS A 323
REMARK 465 HIS A 324
REMARK 465 HIS A 325
REMARK 465 MET B -1
REMARK 465 HIS B 320
REMARK 465 HIS B 321
REMARK 465 HIS B 322
REMARK 465 HIS B 323
REMARK 465 HIS B 324
REMARK 465 HIS B 325
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 319 CG CD OE1 OE2
REMARK 470 ALA B 0 N
REMARK 470 GLU B 319 CG CD OE1 OE2
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 29 87.07 -154.66
REMARK 500 ASN A 51 -90.38 -146.20
REMARK 500 SER A 105 -127.60 56.18
REMARK 500 ASN A 206 -0.91 74.23
REMARK 500 ALA A 305 36.29 -140.59
REMARK 500 SER B 29 86.22 -156.38
REMARK 500 ASN B 51 -92.47 -144.49
REMARK 500 SER B 105 -127.01 56.38
REMARK 500 ASP B 134 63.83 -102.25
REMARK 500 ASN B 206 -2.31 74.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4K5Q RELATED DB: PDB
REMARK 900 RELATED ID: 4K6H RELATED DB: PDB
REMARK 900 RELATED ID: 4K6K RELATED DB: PDB
DBREF 4K6G A 1 317 UNP P41365 LIPB_CANAR 26 342
DBREF 4K6G B 1 317 UNP P41365 LIPB_CANAR 26 342
SEQADV 4K6G MET A -1 UNP P41365 EXPRESSION TAG
SEQADV 4K6G ALA A 0 UNP P41365 EXPRESSION TAG
SEQADV 4K6G LEU A 318 UNP P41365 EXPRESSION TAG
SEQADV 4K6G GLU A 319 UNP P41365 EXPRESSION TAG
SEQADV 4K6G HIS A 320 UNP P41365 EXPRESSION TAG
SEQADV 4K6G HIS A 321 UNP P41365 EXPRESSION TAG
SEQADV 4K6G HIS A 322 UNP P41365 EXPRESSION TAG
SEQADV 4K6G HIS A 323 UNP P41365 EXPRESSION TAG
SEQADV 4K6G HIS A 324 UNP P41365 EXPRESSION TAG
SEQADV 4K6G HIS A 325 UNP P41365 EXPRESSION TAG
SEQADV 4K6G MET B -1 UNP P41365 EXPRESSION TAG
SEQADV 4K6G ALA B 0 UNP P41365 EXPRESSION TAG
SEQADV 4K6G LEU B 318 UNP P41365 EXPRESSION TAG
SEQADV 4K6G GLU B 319 UNP P41365 EXPRESSION TAG
SEQADV 4K6G HIS B 320 UNP P41365 EXPRESSION TAG
SEQADV 4K6G HIS B 321 UNP P41365 EXPRESSION TAG
SEQADV 4K6G HIS B 322 UNP P41365 EXPRESSION TAG
SEQADV 4K6G HIS B 323 UNP P41365 EXPRESSION TAG
SEQADV 4K6G HIS B 324 UNP P41365 EXPRESSION TAG
SEQADV 4K6G HIS B 325 UNP P41365 EXPRESSION TAG
SEQRES 1 A 327 MET ALA LEU PRO SER GLY SER ASP PRO ALA PHE SER GLN
SEQRES 2 A 327 PRO LYS SER VAL LEU ASP ALA GLY LEU THR CYS GLN GLY
SEQRES 3 A 327 ALA SER PRO SER SER VAL SER LYS PRO ILE LEU LEU VAL
SEQRES 4 A 327 PRO GLY THR GLY THR THR GLY PRO GLN SER PHE ASP SER
SEQRES 5 A 327 ASN TRP ILE PRO LEU SER THR GLN LEU GLY TYR THR PRO
SEQRES 6 A 327 CYS TRP ILE SER PRO PRO PRO PHE MET LEU ASN ASP THR
SEQRES 7 A 327 GLN VAL ASN THR GLU TYR MET VAL ASN ALA ILE THR ALA
SEQRES 8 A 327 LEU TYR ALA GLY SER GLY ASN ASN LYS LEU PRO VAL LEU
SEQRES 9 A 327 THR TRP SER GLN GLY GLY LEU VAL ALA GLN TRP GLY LEU
SEQRES 10 A 327 THR PHE PHE PRO SER ILE ARG SER LYS VAL ASP ARG LEU
SEQRES 11 A 327 MET ALA PHE ALA PRO ASP TYR LYS GLY THR VAL LEU ALA
SEQRES 12 A 327 GLY PRO LEU ASP ALA LEU ALA VAL SER ALA PRO SER VAL
SEQRES 13 A 327 TRP GLN GLN THR THR GLY SER ALA LEU THR THR ALA LEU
SEQRES 14 A 327 ARG ASN ALA GLY GLY LEU THR GLN ILE VAL PRO THR THR
SEQRES 15 A 327 ASN LEU TYR SER ALA THR ASP GLU ILE VAL GLN PRO GLN
SEQRES 16 A 327 VAL SER ASN SER PRO LEU ASP SER SER TYR LEU PHE ASN
SEQRES 17 A 327 GLY LYS ASN VAL GLN ALA GLN ALA VAL CYS GLY PRO LEU
SEQRES 18 A 327 PHE VAL ILE ASP HIS ALA GLY SER LEU THR SER GLN PHE
SEQRES 19 A 327 SER TYR VAL VAL GLY ARG SER ALA LEU ARG SER THR THR
SEQRES 20 A 327 GLY GLN ALA ARG SER ALA ASP TYR GLY ILE THR ASP CYS
SEQRES 21 A 327 ASN PRO LEU PRO ALA ASN ASP LEU THR PRO GLU GLN LYS
SEQRES 22 A 327 VAL ALA ALA ALA ALA LEU LEU ALA PRO ALA ALA ALA ALA
SEQRES 23 A 327 ILE VAL ALA GLY PRO LYS GLN ASN CYS GLU PRO ASP LEU
SEQRES 24 A 327 MET PRO TYR ALA ARG PRO PHE ALA VAL GLY LYS ARG THR
SEQRES 25 A 327 CYS SER GLY ILE VAL THR PRO LEU GLU HIS HIS HIS HIS
SEQRES 26 A 327 HIS HIS
SEQRES 1 B 327 MET ALA LEU PRO SER GLY SER ASP PRO ALA PHE SER GLN
SEQRES 2 B 327 PRO LYS SER VAL LEU ASP ALA GLY LEU THR CYS GLN GLY
SEQRES 3 B 327 ALA SER PRO SER SER VAL SER LYS PRO ILE LEU LEU VAL
SEQRES 4 B 327 PRO GLY THR GLY THR THR GLY PRO GLN SER PHE ASP SER
SEQRES 5 B 327 ASN TRP ILE PRO LEU SER THR GLN LEU GLY TYR THR PRO
SEQRES 6 B 327 CYS TRP ILE SER PRO PRO PRO PHE MET LEU ASN ASP THR
SEQRES 7 B 327 GLN VAL ASN THR GLU TYR MET VAL ASN ALA ILE THR ALA
SEQRES 8 B 327 LEU TYR ALA GLY SER GLY ASN ASN LYS LEU PRO VAL LEU
SEQRES 9 B 327 THR TRP SER GLN GLY GLY LEU VAL ALA GLN TRP GLY LEU
SEQRES 10 B 327 THR PHE PHE PRO SER ILE ARG SER LYS VAL ASP ARG LEU
SEQRES 11 B 327 MET ALA PHE ALA PRO ASP TYR LYS GLY THR VAL LEU ALA
SEQRES 12 B 327 GLY PRO LEU ASP ALA LEU ALA VAL SER ALA PRO SER VAL
SEQRES 13 B 327 TRP GLN GLN THR THR GLY SER ALA LEU THR THR ALA LEU
SEQRES 14 B 327 ARG ASN ALA GLY GLY LEU THR GLN ILE VAL PRO THR THR
SEQRES 15 B 327 ASN LEU TYR SER ALA THR ASP GLU ILE VAL GLN PRO GLN
SEQRES 16 B 327 VAL SER ASN SER PRO LEU ASP SER SER TYR LEU PHE ASN
SEQRES 17 B 327 GLY LYS ASN VAL GLN ALA GLN ALA VAL CYS GLY PRO LEU
SEQRES 18 B 327 PHE VAL ILE ASP HIS ALA GLY SER LEU THR SER GLN PHE
SEQRES 19 B 327 SER TYR VAL VAL GLY ARG SER ALA LEU ARG SER THR THR
SEQRES 20 B 327 GLY GLN ALA ARG SER ALA ASP TYR GLY ILE THR ASP CYS
SEQRES 21 B 327 ASN PRO LEU PRO ALA ASN ASP LEU THR PRO GLU GLN LYS
SEQRES 22 B 327 VAL ALA ALA ALA ALA LEU LEU ALA PRO ALA ALA ALA ALA
SEQRES 23 B 327 ILE VAL ALA GLY PRO LYS GLN ASN CYS GLU PRO ASP LEU
SEQRES 24 B 327 MET PRO TYR ALA ARG PRO PHE ALA VAL GLY LYS ARG THR
SEQRES 25 B 327 CYS SER GLY ILE VAL THR PRO LEU GLU HIS HIS HIS HIS
SEQRES 26 B 327 HIS HIS
HET EDO A 401 4
HET EDO A 402 4
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 EDO 2(C2 H6 O2)
FORMUL 5 HOH *402(H2 O)
HELIX 1 1 PRO A 12 GLY A 19 1 8
HELIX 2 2 THR A 43 ASP A 49 1 7
HELIX 3 3 ASN A 51 LEU A 59 1 9
HELIX 4 4 ASP A 75 SER A 94 1 20
HELIX 5 5 SER A 105 PHE A 118 1 14
HELIX 6 6 PRO A 119 ARG A 122 5 4
HELIX 7 7 ALA A 151 GLN A 157 1 7
HELIX 8 8 SER A 161 ALA A 170 1 10
HELIX 9 9 ALA A 212 GLY A 217 1 6
HELIX 10 10 ALA A 225 SER A 230 1 6
HELIX 11 11 SER A 230 SER A 243 1 14
HELIX 12 12 ARG A 249 TYR A 253 5 5
HELIX 13 13 GLY A 254 CYS A 258 5 5
HELIX 14 14 THR A 267 ALA A 276 1 10
HELIX 15 15 LEU A 277 GLY A 288 1 12
HELIX 16 16 ALA A 301 ALA A 305 5 5
HELIX 17 17 PRO B 12 GLY B 19 1 8
HELIX 18 18 THR B 43 ASP B 49 1 7
HELIX 19 19 ASN B 51 LEU B 59 1 9
HELIX 20 20 ASP B 75 SER B 94 1 20
HELIX 21 21 SER B 105 PHE B 118 1 14
HELIX 22 22 PRO B 119 ARG B 122 5 4
HELIX 23 23 THR B 138 GLY B 142 5 5
HELIX 24 24 PRO B 143 LEU B 147 5 5
HELIX 25 25 ALA B 151 GLN B 157 1 7
HELIX 26 26 SER B 161 ALA B 170 1 10
HELIX 27 27 ALA B 212 GLY B 217 1 6
HELIX 28 28 ALA B 225 SER B 230 1 6
HELIX 29 29 SER B 230 SER B 243 1 14
HELIX 30 30 ARG B 249 TYR B 253 5 5
HELIX 31 31 GLY B 254 CYS B 258 5 5
HELIX 32 32 THR B 267 ALA B 276 1 10
HELIX 33 33 LEU B 278 GLY B 288 1 11
HELIX 34 34 ALA B 301 ALA B 305 5 5
SHEET 1 A 7 LEU A 20 CYS A 22 0
SHEET 2 A 7 THR A 62 ILE A 66 -1 O TRP A 65 N THR A 21
SHEET 3 A 7 PRO A 33 VAL A 37 1 N LEU A 36 O CYS A 64
SHEET 4 A 7 LEU A 99 TRP A 104 1 O LEU A 102 N LEU A 35
SHEET 5 A 7 VAL A 125 PHE A 131 1 O MET A 129 N VAL A 101
SHEET 6 A 7 THR A 179 TYR A 183 1 O THR A 180 N ALA A 130
SHEET 7 A 7 LYS A 208 GLN A 211 1 O VAL A 210 N ASN A 181
SHEET 1 B 2 ARG A 309 THR A 310 0
SHEET 2 B 2 GLY A 313 ILE A 314 -1 O GLY A 313 N THR A 310
SHEET 1 C 7 LEU B 20 CYS B 22 0
SHEET 2 C 7 THR B 62 ILE B 66 -1 O TRP B 65 N THR B 21
SHEET 3 C 7 PRO B 33 VAL B 37 1 N LEU B 36 O CYS B 64
SHEET 4 C 7 LEU B 99 TRP B 104 1 O LEU B 102 N LEU B 35
SHEET 5 C 7 VAL B 125 PHE B 131 1 O MET B 129 N VAL B 101
SHEET 6 C 7 THR B 179 TYR B 183 1 O THR B 180 N ALA B 130
SHEET 7 C 7 LYS B 208 GLN B 211 1 O VAL B 210 N ASN B 181
SHEET 1 D 2 ARG B 309 THR B 310 0
SHEET 2 D 2 GLY B 313 ILE B 314 -1 O GLY B 313 N THR B 310
SSBOND 1 CYS A 22 CYS A 64 1555 1555 2.05
SSBOND 2 CYS A 216 CYS A 258 1555 1555 2.03
SSBOND 3 CYS A 293 CYS A 311 1555 1555 2.04
SSBOND 4 CYS B 22 CYS B 64 1555 1555 2.05
SSBOND 5 CYS B 216 CYS B 258 1555 1555 2.03
SSBOND 6 CYS B 293 CYS B 311 1555 1555 2.04
CISPEP 1 PRO A 69 PRO A 70 0 -10.35
CISPEP 2 GLN A 191 PRO A 192 0 2.57
CISPEP 3 PRO B 69 PRO B 70 0 -9.77
CISPEP 4 GLN B 191 PRO B 192 0 0.32
SITE 1 AC1 5 ASN A 169 PRO A 303 PHE A 304 ALA A 305
SITE 2 AC1 5 VAL A 306
SITE 1 AC2 6 THR A 40 TRP A 104 SER A 105 HIS A 224
SITE 2 AC2 6 LEU A 278 ALA A 281
CRYST1 47.699 81.642 71.652 90.00 95.87 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 0.020965 0.000000 0.002154 0.00000
SCALE2 0.000000 0.012249 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014030 0.00000
TER 2305 GLU A 319
TER 4646 GLU B 319
MASTER 313 0 2 34 18 0 4 6 5054 2 20 52
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