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HEADER HYDROLASE 01-JUL-15 5A6V
TITLE OPEN AND CLOSED CONFORMATIONS AND PROTONATION STATES OF
TITLE 2 CANDIDA ANTARCTICA LIPASE B: XENON COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE B;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 26-342;
COMPND 5 SYNONYM: CALB, CANDIDA ANTARCTICA LIPASE B;
COMPND 6 EC: 3.1.1.3;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOZYMA ANTARCTICA;
SOURCE 3 ORGANISM_TAXID: 84753;
SOURCE 4 EXPRESSION_SYSTEM: ASPERGILLUS ORYZAE;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 5062
KEYWDS HYDROLASE, LIPASE, CANDIDA ANTARCTICA, ATOMIC RESOLUTION, FREE FATTY
KEYWDS 2 ACIDS, LIPIDS, HYDROLASE FOLD, INTERFACIAL ACTIVATION
EXPDTA X-RAY DIFFRACTION
AUTHOR B.STAUCH,S.J.FISHER,M.CIANCI
REVDAT 1 21-OCT-15 5A6V 0
JRNL AUTH B.STAUCH,S.J.FISHER,M.CIANCI
JRNL TITL OPEN AND CLOSED STATES OF CANDIDA ANTARCTICA LIPASE B:
JRNL TITL 2 PROTONATION AND THE MECHANISM OF INTERFACIAL ACTIVATION.
JRNL REF J.LIPID RES. 2015
JRNL REFN ESSN 0022-2275
JRNL PMID 26447231
JRNL DOI 10.1194/JLR.M063388
REMARK 2
REMARK 2 RESOLUTION. 2.28 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0107
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,
REMARK 3 STEINER,NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.28
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 70.97
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.18
REMARK 3 NUMBER OF REFLECTIONS : 20233
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) : 0.14226
REMARK 3 R VALUE (WORKING SET) : 0.13930
REMARK 3 FREE R VALUE : 0.19480
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.1
REMARK 3 FREE R VALUE TEST SET COUNT : 1097
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) : 2.279
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.338
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1032
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 62.13
REMARK 3 BIN R VALUE (WORKING SET) : 0.267
REMARK 3 BIN FREE R VALUE SET COUNT : 49
REMARK 3 BIN FREE R VALUE : 0.396
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4639
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 70
REMARK 3 SOLVENT ATOMS : 484
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.381
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.05
REMARK 3 B22 (A**2) : 0.01
REMARK 3 B33 (A**2) : -0.12
REMARK 3 B12 (A**2) : 0.17
REMARK 3 B13 (A**2) : -0.11
REMARK 3 B23 (A**2) : -0.20
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): 0.235
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.156
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.494
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.922
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4828 ; 0.014 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6636 ; 1.416 ; 1.987
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 631 ; 6.235 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 166 ;34.209 ;25.060
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 680 ;13.606 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;18.545 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 785 ; 0.080 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3666 ; 0.008 ; 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): 2530 ; 1.021 ; 1.298
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3159 ; 1.530 ; 1.941
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2298 ; 1.585 ; 1.403
REMARK 3 SIDE-CHAIN ANGLE REFINED 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 ADDED IN THE
REMARK 3 RIDING POSITIONS.
REMARK 3 U VALUES REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5A6V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-JUL-15.
REMARK 100 THE PDBE ID CODE IS EBI-64234.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-MAR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.8
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PETRA III
REMARK 200 BEAMLINE : P13 (MX1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 2.25
REMARK 200 MONOCHROMATOR : SI(III)
REMARK 200 OPTICS : KB MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL (PILATUS 6M)
REMARK 200 DETECTOR MANUFACTURER : DECTRIS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21330
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.27
REMARK 200 RESOLUTION RANGE LOW (A) : 70.96
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 7.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.7
REMARK 200 DATA REDUNDANCY : 6.2
REMARK 200 R MERGE (I) : 0.06
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 29.50
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.27
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.36
REMARK 200 COMPLETENESS FOR SHELL (%) : 70.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.6
REMARK 200 R MERGE FOR SHELL (I) : 0.03
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 7.20
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: PDB ENTRY 1TCA
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CANDIDA ANTARCTICA LIPASE B
REMARK 280 (CALB) WAS PURCHASED BY HAMPTON RESEARCH AND CRYSTALLIZED
REMARK 280 WITHOUT FURTHER PURIFICATION. CRYSTALLIZATION TRIALS WERE
REMARK 280 PERFORMED AT 293 K USING THE HANGING-DROP METHOD USING A
REMARK 280 QUIAGEN EASYXTAL 15-WELL PLATE. 1 UL OF A 15 MG/ML CALB
REMARK 280 SOLUTION IN 20MM NA(CH3COO) PH = 4.8 WAS DILUTED WITH 1 UL
REMARK 280 OF THE PRECIPITANT SOLUTION, MADE OF 200MM NA(CH3COO) PH =
REMARK 280 4.8, 20% (W/V) PEG4000, AND 10-13% (V/V) 2-PROPANOL. THE
REMARK 280 DROP WAS EQUILIBRATED BY VAPOR DIFFUSION AGAINST 500 ML OF
REMARK 280 THE PRECIPITANT SOLUTION. PROTEIN CRYSTALS OF NATIVE CALB
REMARK 280 APPEARED WITHIN ONE WEEK AND GREW TO A SIZE OF 0.2 X 0.4 X
REMARK 280 0.5 MM3 IN THREE WEEKS
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,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
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: 3970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 5.6 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 PRO B 317
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 OD2 ASP B 252 O HOH B 2174 2.12
REMARK 500 O4 NAG B 1318 O HOH B 2235 2.15
REMARK 500 O HOH B 2065 O HOH B 2066 2.01
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 SER A 3 19.96 -147.19
REMARK 500 SER A 29 86.94 -156.88
REMARK 500 ASN A 51 -88.13 -143.11
REMARK 500 ASP A 75 120.84 -25.97
REMARK 500 SER A 105 -125.39 50.50
REMARK 500 ASP A 134 65.81 -115.09
REMARK 500 PRO A 198 -17.98 -49.76
REMARK 500 ALA A 305 34.37 -142.13
REMARK 500 THR A 310 -169.58 -120.62
REMARK 500 ASN B 51 -93.50 -156.36
REMARK 500 ASP B 75 121.60 -39.26
REMARK 500 SER B 105 -119.28 54.67
REMARK 500 ASP B 134 68.04 -110.30
REMARK 500 ASN B 206 -1.20 64.39
REMARK 500 ALA B 305 39.19 -146.66
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 IPA A1320
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA B1319
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XE A1321
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XE A1323
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XE B1320
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XE A1324
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE
REMARK 800 RESIDUES NAG A1318 THROUGH NAG A1319 BOUND TO ASN A 74
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE
REMARK 800 RESIDUES NAG B1317 THROUGH NAG B1318 BOUND TO ASN B 74
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5A71 RELATED DB: PDB
REMARK 900 OPEN AND CLOSED CONFORMATIONS AND PROTONATION STATES OF
REMARK 900 CANDIDA ANTARCTICA LIPASE B: ATOMIC RESOLUTION NATIVE
DBREF 5A6V A 1 317 UNP P41365 LIPB_CANAR 26 342
DBREF 5A6V B 1 317 UNP P41365 LIPB_CANAR 26 342
SEQRES 1 A 317 LEU PRO SER GLY SER ASP PRO ALA PHE SER GLN PRO LYS
SEQRES 2 A 317 SER VAL LEU ASP ALA GLY LEU THR CYS GLN GLY ALA SER
SEQRES 3 A 317 PRO SER SER VAL SER LYS PRO ILE LEU LEU VAL PRO GLY
SEQRES 4 A 317 THR GLY THR THR GLY PRO GLN SER PHE ASP SER ASN TRP
SEQRES 5 A 317 ILE PRO LEU SER THR GLN LEU GLY TYR THR PRO CYS TRP
SEQRES 6 A 317 ILE SER PRO PRO PRO PHE MET LEU ASN ASP THR GLN VAL
SEQRES 7 A 317 ASN THR GLU TYR MET VAL ASN ALA ILE THR ALA LEU TYR
SEQRES 8 A 317 ALA GLY SER GLY ASN ASN LYS LEU PRO VAL LEU THR TRP
SEQRES 9 A 317 SER GLN GLY GLY LEU VAL ALA GLN TRP GLY LEU THR PHE
SEQRES 10 A 317 PHE PRO SER ILE ARG SER LYS VAL ASP ARG LEU MET ALA
SEQRES 11 A 317 PHE ALA PRO ASP TYR LYS GLY THR VAL LEU ALA GLY PRO
SEQRES 12 A 317 LEU ASP ALA LEU ALA VAL SER ALA PRO SER VAL TRP GLN
SEQRES 13 A 317 GLN THR THR GLY SER ALA LEU THR THR ALA LEU ARG ASN
SEQRES 14 A 317 ALA GLY GLY LEU THR GLN ILE VAL PRO THR THR ASN LEU
SEQRES 15 A 317 TYR SER ALA THR ASP GLU ILE VAL GLN PRO GLN VAL SER
SEQRES 16 A 317 ASN SER PRO LEU ASP SER SER TYR LEU PHE ASN GLY LYS
SEQRES 17 A 317 ASN VAL GLN ALA GLN ALA VAL CYS GLY PRO LEU PHE VAL
SEQRES 18 A 317 ILE ASP HIS ALA GLY SER LEU THR SER GLN PHE SER TYR
SEQRES 19 A 317 VAL VAL GLY ARG SER ALA LEU ARG SER THR THR GLY GLN
SEQRES 20 A 317 ALA ARG SER ALA ASP TYR GLY ILE THR ASP CYS ASN PRO
SEQRES 21 A 317 LEU PRO ALA ASN ASP LEU THR PRO GLU GLN LYS VAL ALA
SEQRES 22 A 317 ALA ALA ALA LEU LEU ALA PRO ALA ALA ALA ALA ILE VAL
SEQRES 23 A 317 ALA GLY PRO LYS GLN ASN CYS GLU PRO ASP LEU MET PRO
SEQRES 24 A 317 TYR ALA ARG PRO PHE ALA VAL GLY LYS ARG THR CYS SER
SEQRES 25 A 317 GLY ILE VAL THR PRO
SEQRES 1 B 317 LEU PRO SER GLY SER ASP PRO ALA PHE SER GLN PRO LYS
SEQRES 2 B 317 SER VAL LEU ASP ALA GLY LEU THR CYS GLN GLY ALA SER
SEQRES 3 B 317 PRO SER SER VAL SER LYS PRO ILE LEU LEU VAL PRO GLY
SEQRES 4 B 317 THR GLY THR THR GLY PRO GLN SER PHE ASP SER ASN TRP
SEQRES 5 B 317 ILE PRO LEU SER THR GLN LEU GLY TYR THR PRO CYS TRP
SEQRES 6 B 317 ILE SER PRO PRO PRO PHE MET LEU ASN ASP THR GLN VAL
SEQRES 7 B 317 ASN THR GLU TYR MET VAL ASN ALA ILE THR ALA LEU TYR
SEQRES 8 B 317 ALA GLY SER GLY ASN ASN LYS LEU PRO VAL LEU THR TRP
SEQRES 9 B 317 SER GLN GLY GLY LEU VAL ALA GLN TRP GLY LEU THR PHE
SEQRES 10 B 317 PHE PRO SER ILE ARG SER LYS VAL ASP ARG LEU MET ALA
SEQRES 11 B 317 PHE ALA PRO ASP TYR LYS GLY THR VAL LEU ALA GLY PRO
SEQRES 12 B 317 LEU ASP ALA LEU ALA VAL SER ALA PRO SER VAL TRP GLN
SEQRES 13 B 317 GLN THR THR GLY SER ALA LEU THR THR ALA LEU ARG ASN
SEQRES 14 B 317 ALA GLY GLY LEU THR GLN ILE VAL PRO THR THR ASN LEU
SEQRES 15 B 317 TYR SER ALA THR ASP GLU ILE VAL GLN PRO GLN VAL SER
SEQRES 16 B 317 ASN SER PRO LEU ASP SER SER TYR LEU PHE ASN GLY LYS
SEQRES 17 B 317 ASN VAL GLN ALA GLN ALA VAL CYS GLY PRO LEU PHE VAL
SEQRES 18 B 317 ILE ASP HIS ALA GLY SER LEU THR SER GLN PHE SER TYR
SEQRES 19 B 317 VAL VAL GLY ARG SER ALA LEU ARG SER THR THR GLY GLN
SEQRES 20 B 317 ALA ARG SER ALA ASP TYR GLY ILE THR ASP CYS ASN PRO
SEQRES 21 B 317 LEU PRO ALA ASN ASP LEU THR PRO GLU GLN LYS VAL ALA
SEQRES 22 B 317 ALA ALA ALA LEU LEU ALA PRO ALA ALA ALA ALA ILE VAL
SEQRES 23 B 317 ALA GLY PRO LYS GLN ASN CYS GLU PRO ASP LEU MET PRO
SEQRES 24 B 317 TYR ALA ARG PRO PHE ALA VAL GLY LYS ARG THR CYS SER
SEQRES 25 B 317 GLY ILE VAL THR PRO
HET NAG A1318 14
HET NAG A1319 14
HET NAG B1317 14
HET NAG B1318 14
HET IPA A1320 4
HET IPA B1319 4
HET XE A1321 1
HET XE A1322 1
HET XE A1323 1
HET XE B1320 1
HET XE A1324 1
HET XE B1321 1
HETNAM IPA ISOPROPYL ALCOHOL
HETNAM XE XENON
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETSYN IPA 2-PROPANOL
FORMUL 3 IPA 2(C3 H8 O)
FORMUL 4 XE 6(XE)
FORMUL 5 NAG 4(C8 H15 N O6)
FORMUL 6 HOH *484(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 SER A 123 5 5
HELIX 7 7 ALA A 141 LEU A 147 1 7
HELIX 8 8 ALA A 151 GLN A 157 1 7
HELIX 9 9 SER A 161 ALA A 170 1 10
HELIX 10 10 ALA A 212 GLY A 217 1 6
HELIX 11 11 ALA A 225 SER A 230 1 6
HELIX 12 12 SER A 230 SER A 243 1 14
HELIX 13 13 ARG A 249 TYR A 253 5 5
HELIX 14 14 GLY A 254 CYS A 258 5 5
HELIX 15 15 THR A 267 ALA A 276 1 10
HELIX 16 16 LEU A 277 GLY A 288 1 12
HELIX 17 17 MET A 298 ALA A 305 5 8
HELIX 18 18 PRO B 12 GLY B 19 1 8
HELIX 19 19 THR B 43 ASP B 49 1 7
HELIX 20 20 ASN B 51 LEU B 59 1 9
HELIX 21 21 ASP B 75 SER B 94 1 20
HELIX 22 22 SER B 105 PHE B 118 1 14
HELIX 23 23 PRO B 119 SER B 123 5 5
HELIX 24 24 ALA B 151 GLN B 157 1 7
HELIX 25 25 SER B 161 GLY B 171 1 11
HELIX 26 26 ALA B 212 GLY B 217 1 6
HELIX 27 27 ALA B 225 SER B 230 1 6
HELIX 28 28 SER B 230 SER B 243 1 14
HELIX 29 29 ARG B 249 TYR B 253 5 5
HELIX 30 30 GLY B 254 CYS B 258 5 5
HELIX 31 31 THR B 267 ALA B 276 1 10
HELIX 32 32 LEU B 277 GLY B 288 1 12
HELIX 33 33 ALA B 301 ALA B 305 5 5
SHEET 1 AA 7 LEU A 20 CYS A 22 0
SHEET 2 AA 7 THR A 62 ILE A 66 -1 O TRP A 65 N THR A 21
SHEET 3 AA 7 PRO A 33 VAL A 37 1 O ILE A 34 N CYS A 64
SHEET 4 AA 7 LEU A 99 TRP A 104 1 O PRO A 100 N LEU A 35
SHEET 5 AA 7 VAL A 125 PHE A 131 1 N ASP A 126 O LEU A 99
SHEET 6 AA 7 THR A 179 TYR A 183 1 O THR A 180 N ALA A 130
SHEET 7 AA 7 LYS A 208 GLN A 211 1 O LYS A 208 N ASN A 181
SHEET 1 AB 2 ARG A 309 THR A 310 0
SHEET 2 AB 2 GLY A 313 ILE A 314 -1 O GLY A 313 N THR A 310
SHEET 1 BA 7 LEU B 20 CYS B 22 0
SHEET 2 BA 7 THR B 62 ILE B 66 -1 O TRP B 65 N THR B 21
SHEET 3 BA 7 PRO B 33 VAL B 37 1 O ILE B 34 N CYS B 64
SHEET 4 BA 7 LEU B 99 TRP B 104 1 O PRO B 100 N LEU B 35
SHEET 5 BA 7 VAL B 125 PHE B 131 1 N ASP B 126 O LEU B 99
SHEET 6 BA 7 THR B 179 TYR B 183 1 O THR B 180 N ALA B 130
SHEET 7 BA 7 LYS B 208 GLN B 211 1 O LYS B 208 N ASN B 181
SHEET 1 BB 2 ARG B 309 THR B 310 0
SHEET 2 BB 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 2.10
SSBOND 2 CYS A 216 CYS A 258 1555 1555 2.04
SSBOND 3 CYS A 293 CYS A 311 1555 1555 2.09
SSBOND 4 CYS B 22 CYS B 64 1555 1555 2.12
SSBOND 5 CYS B 216 CYS B 258 1555 1555 2.03
SSBOND 6 CYS B 293 CYS B 311 1555 1555 2.06
LINK ND2 ASN A 74 C1 NAG A1318 1555 1555 1.45
LINK O4 NAG A1318 C1 NAG A1319 1555 1555 1.45
LINK ND2 ASN B 74 C1 NAG B1317 1555 1555 1.43
LINK O4 NAG B1317 C1 NAG B1318 1555 1555 1.44
CISPEP 1 PRO A 69 PRO A 70 0 -15.16
CISPEP 2 GLN A 191 PRO A 192 0 4.84
CISPEP 3 PRO B 69 PRO B 70 0 -12.56
CISPEP 4 GLN B 191 PRO B 192 0 -1.08
SITE 1 AC1 5 THR A 40 ASP A 134 GLN A 157 XE A1323
SITE 2 AC1 5 HOH A2101
SITE 1 AC2 3 GLN B 157 HOH B2124 HOH B2237
SITE 1 AC3 3 LEU A 278 XE A1323 LEU B 219
SITE 1 AC4 3 ILE A 285 IPA A1320 XE A1321
SITE 1 AC5 2 ALA B 111 LEU B 115
SITE 1 AC6 2 VAL A 101 ALA A 111
SITE 1 AC7 10 SER A 10 GLN A 11 ASN A 74 ASP A 75
SITE 2 AC7 10 VAL A 78 TYR A 203 HOH A2019 HOH A2071
SITE 3 AC7 10 HOH A2237 HOH A2238
SITE 1 AC8 9 SER B 10 GLN B 11 ASN B 74 ASP B 75
SITE 2 AC8 9 VAL B 78 HOH B2018 HOH B2068 HOH B2234
SITE 3 AC8 9 HOH B2235
CRYST1 39.656 48.890 71.680 87.80 98.07 108.17 P 1 2
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 0.025217 0.008276 0.003623 0.00000
SCALE2 0.000000 0.021528 0.000123 0.00000
SCALE3 0.000000 0.000000 0.014091 0.00000
TER 2324 PRO A 317
TER 4641 THR B 316
MASTER 325 0 12 33 18 0 13 6 5193 2 78 50
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