| content |
HEADER HYDROLASE 16-MAY-24 9FDE
TITLE LIPASE CALB CANDIDA ANTARCTICA WITH LYSINE LIGAND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE B;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CALB;
COMPND 5 EC: 3.1.1.3;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: LIPASE B;
COMPND 9 CHAIN: B;
COMPND 10 SYNONYM: CALB;
COMPND 11 EC: 3.1.1.3;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MOESZIOMYCES ANTARCTICUS;
SOURCE 3 ORGANISM_TAXID: 84753;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI B;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 37762;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: MOESZIOMYCES ANTARCTICUS;
SOURCE 8 ORGANISM_TAXID: 84753;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS LIPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.JELSCH,F.FAVIER,C.DIDIERJEAN
REVDAT 1 28-MAY-25 9FDE 0
JRNL AUTH C.JELSCH,F.FAVIER,C.DIDIERJEAN
JRNL TITL LIPASE CALB CANDIDA ANTARCTICA WITH LYSINE LIGAND
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0258
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.32
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 43867
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) : 0.205
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.691
REMARK 3 FREE R VALUE TEST SET COUNT : 2058
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3008
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.53
REMARK 3 BIN R VALUE (WORKING SET) : 0.2440
REMARK 3 BIN FREE R VALUE SET COUNT : 139
REMARK 3 BIN FREE R VALUE : 0.3380
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4633
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 11
REMARK 3 SOLVENT ATOMS : 129
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.89
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -6.21900
REMARK 3 B22 (A**2) : -16.92900
REMARK 3 B33 (A**2) : 23.14900
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 3.47100
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.041
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.038
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.116
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.023
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.890
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4799 ; 0.010 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 4362 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6600 ; 1.810 ; 1.645
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10192 ; 1.344 ; 1.561
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 640 ; 7.845 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 182 ;32.181 ;23.736
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 690 ;15.469 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;20.432 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 661 ; 0.081 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5441 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 895 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1180 ; 0.213 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 52 ; 0.217 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2422 ; 0.169 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 234 ; 0.205 ; 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): 2551 ; 1.769 ; 2.356
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2550 ; 1.766 ; 2.356
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3191 ; 2.262 ; 3.530
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3192 ; 2.262 ; 3.531
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2248 ; 1.659 ; 2.397
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2248 ; 1.659 ; 2.397
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3408 ; 2.180 ; 3.574
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3408 ; 2.178 ; 3.574
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 TWIN DETAILS
REMARK 3 NUMBER OF TWIN DOMAINS : 2
REMARK 3 TWIN DOMAIN : 1
REMARK 3 TWIN OPERATOR : H, K, L
REMARK 3 TWIN FRACTION : 0.4317
REMARK 3 TWIN DOMAIN : 2
REMARK 3 TWIN OPERATOR : -H,-K,L
REMARK 3 TWIN FRACTION : 0.5683
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 BULK SOLVENT
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 THEIR
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 9FDE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-MAY-24.
REMARK 100 THE DEPOSITION ID IS D_1292138420.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-NOV-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 : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.980121
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52748
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.870
REMARK 200 RESOLUTION RANGE LOW (A) : 45.320
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.14600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.87
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.91
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: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: PLATELET-SHAPED
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.23
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROPAN-2-OL 40 % (V/V), PEG 8000 18 %
REMARK 280 (W/V), 100MM IMIDAZOLE/HCL PH 6.2, VAPOR DIFFUSION, TEMPERATURE
REMARK 280 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 53.73800
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 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 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 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 ASN A 51 -95.74 -149.62
REMARK 500 ASP A 75 104.16 -32.91
REMARK 500 SER A 105 -124.98 42.65
REMARK 500 ARG A 127 156.41 174.04
REMARK 500 ASP A 134 68.06 -109.99
REMARK 500 ASN A 206 -11.00 77.95
REMARK 500 THR A 316 -52.31 -121.91
REMARK 500 PRO B 2 153.39 -40.20
REMARK 500 SER B 3 15.20 -149.45
REMARK 500 SER B 29 78.04 -172.58
REMARK 500 ASN B 51 -96.29 -146.39
REMARK 500 ASP B 75 117.76 -27.63
REMARK 500 SER B 105 -127.57 61.35
REMARK 500 ASP B 134 66.76 -107.36
REMARK 500 ASN B 206 -14.57 80.10
REMARK 500 ALA B 263 135.43 -34.08
REMARK 500 ALA B 305 47.70 -152.31
REMARK 500
REMARK 500 REMARK: NULL
DBREF 9FDE A 1 317 UNP P41365 LIPB_PSEA2 26 342
DBREF 9FDE B 1 315 UNP P41365 LIPB_PSEA2 26 340
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 315 LEU PRO SER GLY SER ASP PRO ALA PHE SER GLN PRO LYS
SEQRES 2 B 315 SER VAL LEU ASP ALA GLY LEU THR CYS GLN GLY ALA SER
SEQRES 3 B 315 PRO SER SER VAL SER LYS PRO ILE LEU LEU VAL PRO GLY
SEQRES 4 B 315 THR GLY THR THR GLY PRO GLN SER PHE ASP SER ASN TRP
SEQRES 5 B 315 ILE PRO LEU SER THR GLN LEU GLY TYR THR PRO CYS TRP
SEQRES 6 B 315 ILE SER PRO PRO PRO PHE MET LEU ASN ASP THR GLN VAL
SEQRES 7 B 315 ASN THR GLU TYR MET VAL ASN ALA ILE THR ALA LEU TYR
SEQRES 8 B 315 ALA GLY SER GLY ASN ASN LYS LEU PRO VAL LEU THR TRP
SEQRES 9 B 315 SER GLN GLY GLY LEU VAL ALA GLN TRP GLY LEU THR PHE
SEQRES 10 B 315 PHE PRO SER ILE ARG SER LYS VAL ASP ARG LEU MET ALA
SEQRES 11 B 315 PHE ALA PRO ASP TYR LYS GLY THR VAL LEU ALA GLY PRO
SEQRES 12 B 315 LEU ASP ALA LEU ALA VAL SER ALA PRO SER VAL TRP GLN
SEQRES 13 B 315 GLN THR THR GLY SER ALA LEU THR THR ALA LEU ARG ASN
SEQRES 14 B 315 ALA GLY GLY LEU THR GLN ILE VAL PRO THR THR ASN LEU
SEQRES 15 B 315 TYR SER ALA THR ASP GLU ILE VAL GLN PRO GLN VAL SER
SEQRES 16 B 315 ASN SER PRO LEU ASP SER SER TYR LEU PHE ASN GLY LYS
SEQRES 17 B 315 ASN VAL GLN ALA GLN ALA VAL CYS GLY PRO LEU PHE VAL
SEQRES 18 B 315 ILE ASP HIS ALA GLY SER LEU THR SER GLN PHE SER TYR
SEQRES 19 B 315 VAL VAL GLY ARG SER ALA LEU ARG SER THR THR GLY GLN
SEQRES 20 B 315 ALA ARG SER ALA ASP TYR GLY ILE THR ASP CYS ASN PRO
SEQRES 21 B 315 LEU PRO ALA ASN ASP LEU THR PRO GLU GLN LYS VAL ALA
SEQRES 22 B 315 ALA ALA ALA LEU LEU ALA PRO ALA ALA ALA ALA ILE VAL
SEQRES 23 B 315 ALA GLY PRO LYS GLN ASN CYS GLU PRO ASP LEU MET PRO
SEQRES 24 B 315 TYR ALA ARG PRO PHE ALA VAL GLY LYS ARG THR CYS SER
SEQRES 25 B 315 GLY ILE VAL
HET CL B 401 1
HET LYS B 402 10
HETNAM CL CHLORIDE ION
HETNAM LYS LYSINE
FORMUL 3 CL CL 1-
FORMUL 4 LYS C6 H15 N2 O2 1+
FORMUL 5 HOH *129(H2 O)
HELIX 1 AA1 PRO A 12 GLY A 19 1 8
HELIX 2 AA2 THR A 43 ASP A 49 1 7
HELIX 3 AA3 ASN A 51 LEU A 59 1 9
HELIX 4 AA4 ASP A 75 SER A 94 1 20
HELIX 5 AA5 SER A 105 PHE A 118 1 14
HELIX 6 AA6 PRO A 119 SER A 123 5 5
HELIX 7 AA7 THR A 138 LEU A 140 5 3
HELIX 8 AA8 ALA A 141 LEU A 147 1 7
HELIX 9 AA9 ALA A 151 GLN A 157 1 7
HELIX 10 AB1 SER A 161 ALA A 170 1 10
HELIX 11 AB2 ALA A 212 GLY A 217 1 6
HELIX 12 AB3 ALA A 225 SER A 230 1 6
HELIX 13 AB4 SER A 230 SER A 243 1 14
HELIX 14 AB5 ARG A 249 TYR A 253 5 5
HELIX 15 AB6 GLY A 254 CYS A 258 5 5
HELIX 16 AB7 THR A 267 ALA A 276 1 10
HELIX 17 AB8 LEU A 277 GLY A 288 1 12
HELIX 18 AB9 ALA A 301 ALA A 305 5 5
HELIX 19 AC1 PRO B 12 GLY B 19 1 8
HELIX 20 AC2 THR B 43 ASP B 49 1 7
HELIX 21 AC3 ASN B 51 LEU B 59 1 9
HELIX 22 AC4 ASP B 75 SER B 94 1 20
HELIX 23 AC5 SER B 105 PHE B 118 1 14
HELIX 24 AC6 PRO B 119 SER B 123 5 5
HELIX 25 AC7 THR B 138 LEU B 140 5 3
HELIX 26 AC8 ALA B 141 ALA B 146 1 6
HELIX 27 AC9 ALA B 151 GLN B 157 1 7
HELIX 28 AD1 SER B 161 ALA B 170 1 10
HELIX 29 AD2 ALA B 212 GLY B 217 1 6
HELIX 30 AD3 ALA B 225 SER B 230 1 6
HELIX 31 AD4 SER B 230 SER B 243 1 14
HELIX 32 AD5 ARG B 249 TYR B 253 5 5
HELIX 33 AD6 GLY B 254 CYS B 258 5 5
HELIX 34 AD7 THR B 267 ALA B 276 1 10
HELIX 35 AD8 LEU B 277 GLY B 288 1 12
HELIX 36 AD9 MET B 298 ALA B 305 5 8
SHEET 1 AA1 7 LEU A 20 CYS A 22 0
SHEET 2 AA1 7 THR A 62 ILE A 66 -1 O TRP A 65 N THR A 21
SHEET 3 AA1 7 PRO A 33 VAL A 37 1 N LEU A 36 O CYS A 64
SHEET 4 AA1 7 LEU A 99 TRP A 104 1 O LEU A 102 N LEU A 35
SHEET 5 AA1 7 VAL A 125 PHE A 131 1 O PHE A 131 N THR A 103
SHEET 6 AA1 7 THR A 179 TYR A 183 1 O THR A 180 N ALA A 130
SHEET 7 AA1 7 LYS A 208 GLN A 211 1 O LYS A 208 N THR A 179
SHEET 1 AA2 2 ARG A 309 THR A 310 0
SHEET 2 AA2 2 GLY A 313 ILE A 314 -1 O GLY A 313 N THR A 310
SHEET 1 AA3 7 LEU B 20 CYS B 22 0
SHEET 2 AA3 7 THR B 62 ILE B 66 -1 O TRP B 65 N THR B 21
SHEET 3 AA3 7 PRO B 33 VAL B 37 1 N LEU B 36 O CYS B 64
SHEET 4 AA3 7 LEU B 99 TRP B 104 1 O LEU B 102 N LEU B 35
SHEET 5 AA3 7 VAL B 125 PHE B 131 1 O MET B 129 N VAL B 101
SHEET 6 AA3 7 THR B 179 TYR B 183 1 O THR B 180 N ALA B 130
SHEET 7 AA3 7 LYS B 208 GLN B 211 1 O LYS B 208 N THR B 179
SHEET 1 AA4 2 ARG B 309 THR B 310 0
SHEET 2 AA4 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 1.98
SSBOND 3 CYS A 293 CYS A 311 1555 1555 2.05
SSBOND 4 CYS B 22 CYS B 64 1555 1555 2.04
SSBOND 5 CYS B 216 CYS B 258 1555 1555 2.09
SSBOND 6 CYS B 293 CYS B 311 1555 1555 2.13
CISPEP 1 PRO A 69 PRO A 70 0 -8.24
CISPEP 2 GLN A 191 PRO A 192 0 8.98
CISPEP 3 PRO B 69 PRO B 70 0 -13.56
CISPEP 4 GLN B 191 PRO B 192 0 6.75
CRYST1 45.318 107.476 68.235 90.00 90.04 90.00 P 1 21 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 0.022066 0.000000 0.000017 0.00000
SCALE2 0.000000 0.009304 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014655 0.00000
TER 2348 PRO A 317
TER 4664 VAL B 315
MASTER 277 0 2 36 18 0 0 6 4773 2 12 50
END |