3QH4-pdb | HEADER HYDROLASE 25-JAN-11 3QH4
TITLE CRYSTAL STRUCTURE OF ESTERASE LIPW FROM MYCOBACTERIUM MARINUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE LIPW;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM MARINUM;
SOURCE 3 ORGANISM_TAXID: 216594;
SOURCE 4 STRAIN: ATCC BAA-535 / M;
SOURCE 5 GENE: LIPW, MMAR_0404;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: AVA0421
KEYWDS STRUCTURAL GENOMICS, SSGCID, SEATTLE STRUCTURAL GENOMICS CENTER FOR
KEYWDS 2 INFECTIOUS DISEASE, MYCOBACTERIUM, TUBERCULOSIS, MARINUM, ORTHOLOG,
KEYWDS 3 LIPW, ESTERASE, HEROIN ESTERASE, MULTIDRUG RESISTANCE, TB, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)
REVDAT 1 09-FEB-11 3QH4 0
JRNL AUTH T.E.EDWARDS,J.ABENDROTH,
JRNL AUTH 2 SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE
JRNL AUTH 3 (SSGCID)
JRNL TITL CRYSTAL STRUCTURE OF ESTERASE LIPW FROM MYCOBACTERIUM
JRNL TITL 2 MARINUM
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 30076
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) : 0.147
REMARK 3 R VALUE (WORKING SET) : 0.144
REMARK 3 FREE R VALUE : 0.188
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1515
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) : 1.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.79
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1967
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.40
REMARK 3 BIN R VALUE (WORKING SET) : 0.1650
REMARK 3 BIN FREE R VALUE SET COUNT : 122
REMARK 3 BIN FREE R VALUE : 0.2090
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2336
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 419
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.91
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 11.44
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.17000
REMARK 3 B22 (A**2) : 0.45000
REMARK 3 B33 (A**2) : -0.28000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
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): 0.105
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.057
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.834
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
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 ATOMS (A): 2417 ; 0.014 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3317 ; 1.400 ; 1.961
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 323 ; 5.577 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 104 ;32.432 ;22.212
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 336 ;11.076 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 25 ;18.718 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 380 ; 0.096 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1908 ; 0.008 ; 0.021
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): 1585 ; 0.733 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2534 ; 1.287 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 832 ; 2.101 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 778 ; 3.308 ; 4.500
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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A -10 A 9999
REMARK 3 ORIGIN FOR THE GROUP (A): 61.8631 13.3035 36.1235
REMARK 3 T TENSOR
REMARK 3 T11: 0.0143 T22: 0.0077
REMARK 3 T33: 0.0074 T12: 0.0059
REMARK 3 T13: 0.0018 T23: -0.0027
REMARK 3 L TENSOR
REMARK 3 L11: 0.3364 L22: 0.1920
REMARK 3 L33: 0.2835 L12: -0.1242
REMARK 3 L13: -0.0166 L23: 0.0868
REMARK 3 S TENSOR
REMARK 3 S11: 0.0048 S12: 0.0211 S13: -0.0036
REMARK 3 S21: -0.0027 S22: -0.0213 S23: -0.0021
REMARK 3 S31: -0.0426 S32: -0.0292 S33: 0.0165
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : RESIDUAL ONLY
REMARK 4
REMARK 4 3QH4 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-FEB-11.
REMARK 100 THE RCSB ID CODE IS RCSB063637.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-JAN-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E+ SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944+
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30172
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.03800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 21.7600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.0
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : 0.07300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 9.130
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1LZK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN AT 55.6 MG/ML, 0.2 M MGCL2,
REMARK 280 0.1 M TRIS, 20 % PEG 6000, CRYO-PROTECTED WITH 25 % ETHYLENE
REMARK 280 GLYCOL, PH 8.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289 K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 36.63500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.49500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.63500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.49500
REMARK 290 SMTRY3 4 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: 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 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 GLY A -3
REMARK 465 PRO A -2
REMARK 465 GLY A -1
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 MET A 1 CG SD CE
REMARK 470 GLU A 28 CG CD OE1 OE2
REMARK 470 ARG A 42 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 43 CG CD OE1 OE2
REMARK 470 THR A 62 OG1 CG2
REMARK 470 ARG A 67 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 154 CG CD NE CZ NH1 NH2
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 PHE A 92 -8.66 68.85
REMARK 500 ASN A 96 -161.18 -167.32
REMARK 500 PRO A 129 30.19 -99.87
REMARK 500 SER A 162 -128.64 60.20
REMARK 500 GLN A 190 54.79 34.23
REMARK 500 PHE A 204 46.29 -100.40
REMARK 500 ALA A 206 26.48 -148.29
REMARK 500 ALA A 209 -54.82 75.65
REMARK 500 ILE A 253 68.06 -101.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MYMAA.00277.C RELATED DB: TARGETDB
DBREF 3QH4 A 3 313 UNP B2HLX2 B2HLX2_MYCMM 2 312
SEQADV 3QH4 GLY A -3 UNP B2HLX2 EXPRESSION TAG
SEQADV 3QH4 PRO A -2 UNP B2HLX2 EXPRESSION TAG
SEQADV 3QH4 GLY A -1 UNP B2HLX2 EXPRESSION TAG
SEQADV 3QH4 SER A 0 UNP B2HLX2 EXPRESSION TAG
SEQADV 3QH4 MET A 1 UNP B2HLX2 EXPRESSION TAG
SEQADV 3QH4 VAL A 2 UNP B2HLX2 EXPRESSION TAG
SEQRES 1 A 317 GLY PRO GLY SER MET VAL THR GLN PRO GLU ALA VAL ASP
SEQRES 2 A 317 ARG LEU ASP PRO LEU LEU ARG ALA VAL ALA THR ALA ARG
SEQRES 3 A 317 ILE ASP PHE THR ALA GLU SER ILE LEU THR ILE ARG GLU
SEQRES 4 A 317 SER MET ASN GLN ARG ARG ARG GLU ALA ALA ALA THR GLU
SEQRES 5 A 317 THR ALA ALA ALA GLY VAL ALA VAL ALA ASP ASP VAL VAL
SEQRES 6 A 317 THR GLY GLU ALA GLY ARG PRO VAL PRO VAL ARG ILE TYR
SEQRES 7 A 317 ARG ALA ALA PRO THR PRO ALA PRO VAL VAL VAL TYR CYS
SEQRES 8 A 317 HIS ALA GLY GLY PHE ALA LEU GLY ASN LEU ASP THR ASP
SEQRES 9 A 317 HIS ARG GLN CYS LEU GLU LEU ALA ARG ARG ALA ARG CYS
SEQRES 10 A 317 ALA VAL VAL SER VAL ASP TYR ARG LEU ALA PRO GLU HIS
SEQRES 11 A 317 PRO TYR PRO ALA ALA LEU HIS ASP ALA ILE GLU VAL LEU
SEQRES 12 A 317 THR TRP VAL VAL GLY ASN ALA THR ARG LEU GLY PHE ASP
SEQRES 13 A 317 ALA ARG ARG LEU ALA VAL ALA GLY SER SER ALA GLY ALA
SEQRES 14 A 317 THR LEU ALA ALA GLY LEU ALA HIS GLY ALA ALA ASP GLY
SEQRES 15 A 317 SER LEU PRO PRO VAL ILE PHE GLN LEU LEU HIS GLN PRO
SEQRES 16 A 317 VAL LEU ASP ASP ARG PRO THR ALA SER ARG SER GLU PHE
SEQRES 17 A 317 ARG ALA THR PRO ALA PHE ASP GLY GLU ALA ALA SER LEU
SEQRES 18 A 317 MET TRP ARG HIS TYR LEU ALA GLY GLN THR PRO SER PRO
SEQRES 19 A 317 GLU SER VAL PRO GLY ARG ARG GLY GLN LEU ALA GLY LEU
SEQRES 20 A 317 PRO ALA THR LEU ILE THR CYS GLY GLU ILE ASP PRO PHE
SEQRES 21 A 317 ARG ASP GLU VAL LEU ASP TYR ALA GLN ARG LEU LEU GLY
SEQRES 22 A 317 ALA GLY VAL SER THR GLU LEU HIS ILE PHE PRO ARG ALA
SEQRES 23 A 317 CYS HIS GLY PHE ASP SER LEU LEU PRO GLU TRP THR THR
SEQRES 24 A 317 SER GLN ARG LEU PHE ALA MET GLN GLY HIS ALA LEU ALA
SEQRES 25 A 317 ASP ALA PHE TYR PRO
FORMUL 2 HOH *419(H2 O)
HELIX 1 1 ALA A 7 LEU A 11 5 5
HELIX 2 2 ASP A 12 ALA A 17 1 6
HELIX 3 3 THR A 26 GLY A 53 1 28
HELIX 4 4 ASP A 100 ARG A 112 1 13
HELIX 5 5 PRO A 129 ASN A 145 1 17
HELIX 6 6 ASN A 145 GLY A 150 1 6
HELIX 7 7 SER A 162 ASP A 177 1 16
HELIX 8 8 THR A 198 PHE A 204 1 7
HELIX 9 9 ASP A 211 ALA A 224 1 14
HELIX 10 10 VAL A 233 ARG A 237 5 5
HELIX 11 11 PHE A 256 ALA A 270 1 15
HELIX 12 12 GLY A 285 LEU A 290 1 6
HELIX 13 13 TRP A 293 TYR A 312 1 20
SHEET 1 A 8 ALA A 55 THR A 62 0
SHEET 2 A 8 PRO A 68 ARG A 75 -1 O VAL A 69 N VAL A 61
SHEET 3 A 8 ALA A 114 VAL A 118 -1 O VAL A 115 N TYR A 74
SHEET 4 A 8 ALA A 81 CYS A 87 1 N VAL A 84 O VAL A 116
SHEET 5 A 8 PHE A 151 SER A 161 1 O ASP A 152 N ALA A 81
SHEET 6 A 8 PHE A 185 HIS A 189 1 O HIS A 189 N GLY A 160
SHEET 7 A 8 THR A 246 ILE A 253 1 O LEU A 247 N LEU A 188
SHEET 8 A 8 THR A 274 CYS A 283 1 O GLU A 275 N ILE A 248
CISPEP 1 THR A 79 PRO A 80 0 -8.56
CISPEP 2 ALA A 123 PRO A 124 0 -0.34
CISPEP 3 TYR A 128 PRO A 129 0 3.38
CRYST1 73.270 86.990 46.190 90.00 90.00 90.00 P 21 21 2 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 0.013648 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011496 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021650 0.00000
TER 2357 PRO A 313
MASTER 301 0 0 13 8 0 0 6 2755 1 0 25
END
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