LongText Report for: 3W9U-pdb
| 3W9U-pdb | HEADER HYDROLASE 17-APR-13 3W9U
TITLE CRYSTAL STRUCTURE OF LIPK107
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE LIPASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PROTEUS MIRABILIS;
SOURCE 3 ORGANISM_TAXID: 529507;
SOURCE 4 STRAIN: HI4320;
SOURCE 5 GENE: PMI0999;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS LIPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.A.YUAN
REVDAT 1 04-DEC-13 3W9U 0
JRNL AUTH Y.A.YUAN
JRNL TITL CRYSTAL STRUCTURE OF LIPK107
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 19653
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) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1065
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1452
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.94
REMARK 3 BIN R VALUE (WORKING SET) : 0.1760
REMARK 3 BIN FREE R VALUE SET COUNT : 72
REMARK 3 BIN FREE R VALUE : 0.2290
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2137
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 155
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.54
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.42000
REMARK 3 B22 (A**2) : -0.42000
REMARK 3 B33 (A**2) : 0.63000
REMARK 3 B12 (A**2) : -0.21000
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): 0.171
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.149
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.100
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.883
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.935
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.917
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2181 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2956 ; 1.049 ; 1.943
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 271 ; 5.251 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 105 ;35.947 ;24.762
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 354 ;13.696 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;19.821 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 329 ; 0.073 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1670 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1052 ; 0.191 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1498 ; 0.304 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 144 ; 0.098 ; 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): 41 ; 0.168 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 14 ; 0.151 ; 0.200
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): 1387 ; 0.483 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2173 ; 0.788 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 894 ; 1.381 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 783 ; 2.062 ; 4.500
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 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 : 0.8243
REMARK 3 TWIN DOMAIN : 2
REMARK 3 TWIN OPERATOR : K, H, -L
REMARK 3 TWIN FRACTION : 0.1757
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 2 A 287
REMARK 3 ORIGIN FOR THE GROUP (A): 13.5586 -14.7268 4.3832
REMARK 3 T TENSOR
REMARK 3 T11: -0.0764 T22: -0.0613
REMARK 3 T33: -0.0499 T12: 0.0027
REMARK 3 T13: -0.0072 T23: -0.0029
REMARK 3 L TENSOR
REMARK 3 L11: 1.3980 L22: 0.9921
REMARK 3 L33: 1.1045 L12: -0.3036
REMARK 3 L13: -0.5584 L23: 0.0283
REMARK 3 S TENSOR
REMARK 3 S11: -0.0497 S12: -0.0790 S13: -0.1334
REMARK 3 S21: 0.0284 S22: -0.0255 S23: 0.0533
REMARK 3 S31: 0.0401 S32: 0.0233 S33: 0.0752
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3W9U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-APR-13.
REMARK 100 THE RCSB ID CODE IS RCSB096067.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-JUN-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.075
REMARK 200 MONOCHROMATOR : 360 DEGREE, 1 DEGREE OSCILLATION
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19653
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 56.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
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: PHASER
REMARK 200 STARTING MODEL: 1EX9
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE, PEG4000,2-PROPANOL, PH
REMARK 280 5.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 42.58067
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 21.29033
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 -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 HIS A 146
REMARK 465 ARG A 147
REMARK 465 GLY A 148
REMARK 465 ASP A 149
REMARK 465 PRO A 150
REMARK 465 GLN A 151
REMARK 465 ILE A 204
REMARK 465 ALA A 205
REMARK 465 GLY A 206
REMARK 465 GLU A 207
REMARK 465 LYS A 208
REMARK 465 GLY A 209
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 13 77.66 92.87
REMARK 500 PHE A 47 47.94 -98.04
REMARK 500 GLN A 69 19.15 58.18
REMARK 500 SER A 79 -105.89 64.19
REMARK 500 ILE A 246 -63.78 -92.68
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 419 DISTANCE = 5.67 ANGSTROMS
DBREF 3W9U A 1 287 UNP B4EVM3 B4EVM3_PROMH 1 287
SEQADV 3W9U GLY A -2 UNP B4EVM3 EXPRESSION TAG
SEQADV 3W9U SER A -1 UNP B4EVM3 EXPRESSION TAG
SEQADV 3W9U HIS A 0 UNP B4EVM3 EXPRESSION TAG
SEQRES 1 A 290 GLY SER HIS MET SER THR LYS TYR PRO ILE VAL LEU VAL
SEQRES 2 A 290 HIS GLY LEU ALA GLY PHE ASN GLU ILE VAL GLY PHE PRO
SEQRES 3 A 290 TYR PHE TYR GLY ILE ALA ASP ALA LEU ARG GLN ASP GLY
SEQRES 4 A 290 HIS GLN VAL PHE THR ALA SER LEU SER ALA PHE ASN SER
SEQRES 5 A 290 ASN GLU VAL ARG GLY LYS GLN LEU TRP GLN PHE VAL GLN
SEQRES 6 A 290 THR LEU LEU GLN GLU THR GLN ALA LYS LYS VAL ASN PHE
SEQRES 7 A 290 ILE GLY HIS SER GLN GLY PRO LEU ALA CYS ARG TYR VAL
SEQRES 8 A 290 ALA ALA ASN TYR PRO ASP SER VAL ALA SER VAL THR SER
SEQRES 9 A 290 ILE ASN GLY VAL ASN HIS GLY SER GLU ILE ALA ASP LEU
SEQRES 10 A 290 TYR ARG ARG ILE MET ARG LYS ASP SER ILE PRO GLU TYR
SEQRES 11 A 290 ILE VAL GLU LYS VAL LEU ASN ALA PHE GLY THR ILE ILE
SEQRES 12 A 290 SER THR PHE SER GLY HIS ARG GLY ASP PRO GLN ASP ALA
SEQRES 13 A 290 ILE ALA ALA LEU GLU SER LEU THR THR GLU GLN VAL THR
SEQRES 14 A 290 GLU PHE ASN ASN LYS TYR PRO GLN ALA LEU PRO LYS THR
SEQRES 15 A 290 PRO GLY GLY GLU GLY ASP GLU ILE VAL ASN GLY VAL HIS
SEQRES 16 A 290 TYR TYR CYS PHE GLY SER TYR ILE GLN GLY LEU ILE ALA
SEQRES 17 A 290 GLY GLU LYS GLY ASN LEU LEU ASP PRO THR HIS ALA ALA
SEQRES 18 A 290 MET ARG VAL LEU ASN THR PHE PHE THR GLU LYS GLN ASN
SEQRES 19 A 290 ASP GLY LEU VAL GLY ARG SER SER MET ARG LEU GLY LYS
SEQRES 20 A 290 LEU ILE LYS ASP ASP TYR ALA GLN ASP HIS ILE ASP MET
SEQRES 21 A 290 VAL ASN GLN VAL ALA GLY LEU VAL GLY TYR ASN GLU ASP
SEQRES 22 A 290 ILE VAL ALA ILE TYR THR GLN HIS ALA LYS TYR LEU ALA
SEQRES 23 A 290 SER LYS GLN LEU
FORMUL 2 HOH *155(H2 O)
HELIX 1 1 GLY A 15 GLY A 21 1 7
HELIX 2 2 GLY A 27 ASP A 35 1 9
HELIX 3 3 SER A 49 GLN A 69 1 21
HELIX 4 4 GLN A 80 TYR A 92 1 13
HELIX 5 5 SER A 109 ARG A 120 1 12
HELIX 6 6 PRO A 125 GLY A 145 1 21
HELIX 7 7 ALA A 153 GLU A 158 1 6
HELIX 8 8 THR A 161 TYR A 172 1 12
HELIX 9 9 ASP A 213 THR A 224 1 12
HELIX 10 10 ARG A 237 ARG A 241 5 5
HELIX 11 11 ILE A 255 ASN A 259 5 5
HELIX 12 12 ASP A 270 LYS A 285 1 16
SHEET 1 A 6 VAL A 39 LEU A 44 0
SHEET 2 A 6 ILE A 7 GLY A 12 1 N HIS A 11 O LEU A 44
SHEET 3 A 6 VAL A 73 HIS A 78 1 O ASN A 74 N VAL A 8
SHEET 4 A 6 VAL A 96 ILE A 102 1 O SER A 98 N PHE A 75
SHEET 5 A 6 VAL A 191 SER A 198 1 O PHE A 196 N SER A 101
SHEET 6 A 6 ILE A 187 VAL A 188 -1 N VAL A 188 O VAL A 191
SHEET 1 B 6 VAL A 39 LEU A 44 0
SHEET 2 B 6 ILE A 7 GLY A 12 1 N HIS A 11 O LEU A 44
SHEET 3 B 6 VAL A 73 HIS A 78 1 O ASN A 74 N VAL A 8
SHEET 4 B 6 VAL A 96 ILE A 102 1 O SER A 98 N PHE A 75
SHEET 5 B 6 VAL A 191 SER A 198 1 O PHE A 196 N SER A 101
SHEET 6 B 6 LYS A 244 TYR A 250 1 O LYS A 244 N TYR A 193
CISPEP 1 GLN A 260 VAL A 261 0 -1.38
CRYST1 65.484 65.484 63.871 90.00 90.00 120.00 P 32 3
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 0.015271 0.008817 0.000000 0.00000
SCALE2 0.000000 0.017633 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015657 0.00000
TER 2138 LEU A 287
MASTER 316 0 0 12 12 0 0 6 2292 1 0 23
END
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