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HEADER HYDROLASE 05-FEB-07 2ORY
TITLE CRYSTAL STRUCTURE OF M37 LIPASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PHOTOBACTERIUM SP. M37;
SOURCE 3 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 4 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 5 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS ALPHA/BETA HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.K.JUNG,D.G.JEONG,S.J.KIM
REVDAT 1 29-JAN-08 2ORY 0
JRNL AUTH S.K.JUNG,D.G.JEONG,M.S.LEE,J.K.LEE,H.K.KIM,S.E.RYU,
JRNL AUTH 2 B.C.PARK,J.H.KIM,S.J.KIM
JRNL TITL STRUCTURAL BASIS FOR THE COLD ADAPTATION OF
JRNL TITL 2 PSYCHROPHILIC M37 LIPASE FROM PHOTOBACTERIUM
JRNL TITL 3 LIPOLYTICUM
JRNL REF PROTEINS 2008
JRNL REFN ASTM PSFGEY US ESSN 1097-0134
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.9
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 34410
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 SET) : 0.204
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1711
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
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) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5363
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 182
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.42
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.89
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPHIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2ORY COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ.
REMARK 100 THE RCSB ID CODE IS RCSB041511.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-JUL-2005
REMARK 200 TEMPERATURE (KELVIN) : 93.0
REMARK 200 PH : 5.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34410
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05200
REMARK 200 FOR THE DATA SET : 11.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.21500
REMARK 200 FOR SHELL : 3.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM ACETATE, 23-25% PEG
REMARK 280 3350, PH 5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-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 35.34700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.85000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.55100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 49.85000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.34700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 47.55100
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: MONOMER
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: MONOMER
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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSEQI
REMARK 465 MET A 1
REMARK 465 GLY A 24
REMARK 465 SER A 25
REMARK 465 ALA A 26
REMARK 465 LYS A 27
REMARK 465 HIS A 341
REMARK 465 HIS A 342
REMARK 465 HIS A 343
REMARK 465 HIS A 344
REMARK 465 HIS A 345
REMARK 465 HIS A 346
REMARK 465 MET B 1
REMARK 465 SER B 2
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 LEU A 41 -7.27 -58.00
REMARK 500 LEU A 101 -62.40 -100.87
REMARK 500 MET A 106 8.24 -65.12
REMARK 500 GLU A 148 126.11 -39.93
REMARK 500 SER A 174 -130.51 65.05
REMARK 500 VAL A 193 -55.89 -126.53
REMARK 500 LYS A 248 3.71 -69.10
REMARK 500 SER A 256 -149.40 -121.14
REMARK 500 PRO A 327 74.91 -67.97
REMARK 500 GLU A 333 -127.16 51.54
REMARK 500 ALA A 337 -97.29 3.04
REMARK 500 GLU B 82 -78.31 -56.34
REMARK 500 ALA B 116 148.28 -175.17
REMARK 500 HIS B 144 -2.95 80.68
REMARK 500 GLU B 148 134.02 -33.44
REMARK 500 SER B 174 -128.78 66.47
REMARK 500 SER B 256 -158.90 -157.94
REMARK 500 GLU B 257 104.36 -44.64
REMARK 500 GLN B 258 -25.33 58.95
REMARK 500 GLU B 333 173.20 68.78
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR B 316 0.08 SIDE_CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2ORY A 1 340 UNP Q5DRN8 Q5DRN8_9GAMM 1 340
DBREF 2ORY B 1 340 UNP Q5DRN8 Q5DRN8_9GAMM 1 340
SEQADV 2ORY HIS A 341 UNP Q5DRN8 EXPRESSION TAG
SEQADV 2ORY HIS A 342 UNP Q5DRN8 EXPRESSION TAG
SEQADV 2ORY HIS A 343 UNP Q5DRN8 EXPRESSION TAG
SEQADV 2ORY HIS A 344 UNP Q5DRN8 EXPRESSION TAG
SEQADV 2ORY HIS A 345 UNP Q5DRN8 EXPRESSION TAG
SEQADV 2ORY HIS A 346 UNP Q5DRN8 EXPRESSION TAG
SEQADV 2ORY HIS B 341 UNP Q5DRN8 EXPRESSION TAG
SEQADV 2ORY HIS B 342 UNP Q5DRN8 EXPRESSION TAG
SEQADV 2ORY HIS B 343 UNP Q5DRN8 EXPRESSION TAG
SEQADV 2ORY HIS B 344 UNP Q5DRN8 EXPRESSION TAG
SEQADV 2ORY HIS B 345 UNP Q5DRN8 EXPRESSION TAG
SEQADV 2ORY HIS B 346 UNP Q5DRN8 EXPRESSION TAG
SEQRES 1 A 346 MET SER TYR THR LYS GLU GLN LEU MET LEU ALA PHE SER
SEQRES 2 A 346 TYR MET SER TYR TYR GLY ILE THR HIS THR GLY SER ALA
SEQRES 3 A 346 LYS LYS ASN ALA GLU LEU ILE LEU LYS LYS MET LYS GLU
SEQRES 4 A 346 ALA LEU LYS THR TRP LYS PRO PHE GLN GLU ASP ASP TRP
SEQRES 5 A 346 GLU VAL VAL TRP GLY PRO ALA VAL TYR THR MET PRO PHE
SEQRES 6 A 346 THR ILE PHE ASN ASP ALA MET MET TYR VAL ILE GLN LYS
SEQRES 7 A 346 LYS GLY ALA GLU GLY GLU TYR VAL ILE ALA ILE ARG GLY
SEQRES 8 A 346 THR ASN PRO VAL SER ILE SER ASP TRP LEU PHE ASN ASP
SEQRES 9 A 346 PHE MET VAL SER ALA MET LYS LYS TRP PRO TYR ALA SER
SEQRES 10 A 346 VAL GLU GLY ARG ILE LEU LYS ILE SER GLU SER THR SER
SEQRES 11 A 346 TYR GLY LEU LYS THR LEU GLN LYS LEU LYS PRO LYS SER
SEQRES 12 A 346 HIS ILE PRO GLY GLU ASN LYS THR ILE LEU GLN PHE LEU
SEQRES 13 A 346 ASN GLU LYS ILE GLY PRO GLU GLY LYS ALA LYS ILE CYS
SEQRES 14 A 346 VAL THR GLY HIS SER LYS GLY GLY ALA LEU SER SER THR
SEQRES 15 A 346 LEU ALA LEU TRP LEU LYS ASP ILE GLN GLY VAL LYS LEU
SEQRES 16 A 346 SER GLN ASN ILE ASP ILE SER THR ILE PRO PHE ALA GLY
SEQRES 17 A 346 PRO THR ALA GLY ASN ALA ASP PHE ALA ASP TYR PHE ASP
SEQRES 18 A 346 ASP CYS LEU GLY ASP GLN CYS THR ARG ILE ALA ASN SER
SEQRES 19 A 346 LEU ASP ILE VAL PRO TYR ALA TRP ASN THR ASN SER LEU
SEQRES 20 A 346 LYS LYS LEU LYS SER ILE TYR ILE SER GLU GLN ALA SER
SEQRES 21 A 346 VAL LYS PRO LEU LEU TYR GLN ARG ALA LEU ILE ARG ALA
SEQRES 22 A 346 MET ILE ALA GLU THR LYS GLY LYS LYS TYR LYS GLN ILE
SEQRES 23 A 346 LYS ALA GLU THR PRO PRO LEU GLU GLY ASN ILE ASN PRO
SEQRES 24 A 346 ILE LEU ILE GLU TYR LEU VAL GLN ALA ALA TYR GLN HIS
SEQRES 25 A 346 VAL VAL GLY TYR PRO GLU LEU MET GLY MET MET ASP ASP
SEQRES 26 A 346 ILE PRO LEU THR ASP ILE PHE GLU ASP ALA ILE ALA GLY
SEQRES 27 A 346 LEU LEU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 346 MET SER TYR THR LYS GLU GLN LEU MET LEU ALA PHE SER
SEQRES 2 B 346 TYR MET SER TYR TYR GLY ILE THR HIS THR GLY SER ALA
SEQRES 3 B 346 LYS LYS ASN ALA GLU LEU ILE LEU LYS LYS MET LYS GLU
SEQRES 4 B 346 ALA LEU LYS THR TRP LYS PRO PHE GLN GLU ASP ASP TRP
SEQRES 5 B 346 GLU VAL VAL TRP GLY PRO ALA VAL TYR THR MET PRO PHE
SEQRES 6 B 346 THR ILE PHE ASN ASP ALA MET MET TYR VAL ILE GLN LYS
SEQRES 7 B 346 LYS GLY ALA GLU GLY GLU TYR VAL ILE ALA ILE ARG GLY
SEQRES 8 B 346 THR ASN PRO VAL SER ILE SER ASP TRP LEU PHE ASN ASP
SEQRES 9 B 346 PHE MET VAL SER ALA MET LYS LYS TRP PRO TYR ALA SER
SEQRES 10 B 346 VAL GLU GLY ARG ILE LEU LYS ILE SER GLU SER THR SER
SEQRES 11 B 346 TYR GLY LEU LYS THR LEU GLN LYS LEU LYS PRO LYS SER
SEQRES 12 B 346 HIS ILE PRO GLY GLU ASN LYS THR ILE LEU GLN PHE LEU
SEQRES 13 B 346 ASN GLU LYS ILE GLY PRO GLU GLY LYS ALA LYS ILE CYS
SEQRES 14 B 346 VAL THR GLY HIS SER LYS GLY GLY ALA LEU SER SER THR
SEQRES 15 B 346 LEU ALA LEU TRP LEU LYS ASP ILE GLN GLY VAL LYS LEU
SEQRES 16 B 346 SER GLN ASN ILE ASP ILE SER THR ILE PRO PHE ALA GLY
SEQRES 17 B 346 PRO THR ALA GLY ASN ALA ASP PHE ALA ASP TYR PHE ASP
SEQRES 18 B 346 ASP CYS LEU GLY ASP GLN CYS THR ARG ILE ALA ASN SER
SEQRES 19 B 346 LEU ASP ILE VAL PRO TYR ALA TRP ASN THR ASN SER LEU
SEQRES 20 B 346 LYS LYS LEU LYS SER ILE TYR ILE SER GLU GLN ALA SER
SEQRES 21 B 346 VAL LYS PRO LEU LEU TYR GLN ARG ALA LEU ILE ARG ALA
SEQRES 22 B 346 MET ILE ALA GLU THR LYS GLY LYS LYS TYR LYS GLN ILE
SEQRES 23 B 346 LYS ALA GLU THR PRO PRO LEU GLU GLY ASN ILE ASN PRO
SEQRES 24 B 346 ILE LEU ILE GLU TYR LEU VAL GLN ALA ALA TYR GLN HIS
SEQRES 25 B 346 VAL VAL GLY TYR PRO GLU LEU MET GLY MET MET ASP ASP
SEQRES 26 B 346 ILE PRO LEU THR ASP ILE PHE GLU ASP ALA ILE ALA GLY
SEQRES 27 B 346 LEU LEU HIS HIS HIS HIS HIS HIS
FORMUL 3 HOH *182(H2 O)
HELIX 1 1 THR A 4 SER A 16 1 13
HELIX 2 2 ASN A 29 TRP A 44 1 16
HELIX 3 3 LYS A 45 GLN A 48 5 4
HELIX 4 4 SER A 96 LEU A 101 1 6
HELIX 5 5 ASP A 104 SER A 108 5 5
HELIX 6 6 GLU A 127 LEU A 139 1 13
HELIX 7 7 THR A 151 GLY A 161 1 11
HELIX 8 8 SER A 174 ILE A 190 1 17
HELIX 9 9 ASN A 213 GLY A 225 1 13
HELIX 10 10 ASP A 226 CYS A 228 5 3
HELIX 11 11 ILE A 237 ALA A 241 5 5
HELIX 12 12 ASN A 243 LYS A 248 1 6
HELIX 13 13 LEU A 264 LYS A 279 1 16
HELIX 14 14 GLU A 303 VAL A 314 1 12
HELIX 15 15 VAL A 314 MET A 320 1 7
HELIX 16 16 PRO A 327 GLU A 333 1 7
HELIX 17 17 ASP A 334 ALA A 337 5 4
HELIX 18 18 THR B 4 SER B 16 1 13
HELIX 19 19 SER B 25 LYS B 28 5 4
HELIX 20 20 ASN B 29 TRP B 44 1 16
HELIX 21 21 LYS B 45 ASP B 50 5 6
HELIX 22 22 SER B 96 LEU B 101 1 6
HELIX 23 23 ASP B 104 SER B 108 5 5
HELIX 24 24 GLU B 127 LEU B 139 1 13
HELIX 25 25 THR B 151 GLY B 161 1 11
HELIX 26 26 SER B 174 GLN B 191 1 18
HELIX 27 27 ASN B 213 GLY B 225 1 13
HELIX 28 28 ASP B 226 CYS B 228 5 3
HELIX 29 29 ILE B 237 ALA B 241 5 5
HELIX 30 30 ASN B 243 LYS B 248 1 6
HELIX 31 31 LEU B 264 LYS B 279 1 16
HELIX 32 32 GLU B 303 VAL B 314 1 12
HELIX 33 33 VAL B 314 MET B 320 1 7
HELIX 34 34 PRO B 327 LEU B 340 1 14
HELIX 35 35 HIS B 341 HIS B 346 1 6
SHEET 1 A 5 TRP A 52 MET A 63 0
SHEET 2 A 5 THR A 66 LYS A 78 -1 O ALA A 71 N TYR A 61
SHEET 3 A 5 GLU A 84 ARG A 90 -1 O ARG A 90 N MET A 72
SHEET 4 A 5 ALA A 166 HIS A 173 1 O LYS A 167 N TYR A 85
SHEET 5 A 5 ILE A 199 PHE A 206 1 O ASP A 200 N ILE A 168
SHEET 1 B 2 MET A 110 LYS A 112 0
SHEET 2 B 2 LYS A 124 SER A 126 -1 O ILE A 125 N LYS A 111
SHEET 1 C 5 ASP B 51 TYR B 61 0
SHEET 2 C 5 ALA B 71 LYS B 79 -1 O LYS B 79 N ASP B 51
SHEET 3 C 5 GLU B 84 ARG B 90 -1 O ALA B 88 N TYR B 74
SHEET 4 C 5 ALA B 166 HIS B 173 1 O THR B 171 N ILE B 87
SHEET 5 C 5 ILE B 199 PHE B 206 1 O ASP B 200 N ILE B 168
SHEET 1 D 2 MET B 110 LYS B 112 0
SHEET 2 D 2 LYS B 124 SER B 126 -1 O ILE B 125 N LYS B 111
CISPEP 1 GLY A 57 PRO A 58 0 0.72
CISPEP 2 ALA A 241 TRP A 242 0 0.57
CISPEP 3 GLY B 57 PRO B 58 0 1.62
CISPEP 4 ALA B 241 TRP B 242 0 1.32
CRYST1 70.694 95.102 99.700 90.00 90.00 90.00 P 21 21 21 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 0.014145 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010515 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010030 0.00000
TER 2643 LEU A 340
TER 5365 HIS B 346
MASTER 289 0 0 35 14 0 0 6 5545 2 0 54
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