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HEADER OXIDOREDUCTASE 06-MAY-07 2PSD
TITLE CRYSTAL STRUCTURES OF THE LUCIFERASE AND GREEN FLUORESCENT
TITLE 2 PROTEIN FROM RENILLA RENIFORMIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RENILLA-LUCIFERIN 2-MONOOXYGENASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: RENILLA-TYPE LUCIFERASE;
COMPND 5 EC: 1.13.12.5;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RENILLA RENIFORMIS;
SOURCE 3 ORGANISM_COMMON: SEA PANSY;
SOURCE 4 GENE: RLUC;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: LMG194;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PBAD
KEYWDS ALPHA/BETA-HYDROLASE, LUCIFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.M.LOENING,T.D.FENN,S.S.GAMBHIR
REVDAT 1 05-JUN-07 2PSD 0
JRNL AUTH A.M.LOENING,T.D.FENN,S.S.GAMBHIR
JRNL TITL CRYSTAL STRUCTURES OF THE LUCIFERASE AND GREEN
JRNL TITL 2 FLUORESCENT PROTEIN FROM RENILLA RENIFORMIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 73121
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) : 0.166
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.183
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3868
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.40
REMARK 3 BIN RESOLUTION RANGE LOW : 1.44
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5261
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.79
REMARK 3 BIN R VALUE (WORKING SET) : 0.3820
REMARK 3 BIN FREE R VALUE SET COUNT : 280
REMARK 3 BIN FREE R VALUE : 0.4140
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 2921
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.51000
REMARK 3 B22 (A**2) : 0.51000
REMARK 3 B33 (A**2) : -0.76000
REMARK 3 B12 (A**2) : 0.25000
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): 0.051
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.052
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.042
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.178
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.975
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.970
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2610 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2344 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3534 ; 1.372 ; 1.956
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5474 ; 0.843 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 310 ; 5.799 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 125 ;30.990 ;24.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 458 ;12.574 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;18.615 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 366 ; 0.093 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2884 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 550 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 564 ; 0.215 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2494 ; 0.189 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1309 ; 0.189 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1418 ; 0.082 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 272 ; 0.118 ; 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): 5 ; 0.058 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 26 ; 0.283 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 29 ; 0.178 ; 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): 2011 ; 0.802 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 617 ; 0.167 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2507 ; 0.891 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1277 ; 1.746 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1027 ; 2.468 ; 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 : 0
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 4 A 150
REMARK 3 RESIDUE RANGE : A 226 A 308
REMARK 3 ORIGIN FOR THE GROUP (A): 82.3974 0.7371 -0.3043
REMARK 3 T TENSOR
REMARK 3 T11: -0.1423 T22: -0.1421
REMARK 3 T33: -0.1361 T12: -0.0055
REMARK 3 T13: -0.0170 T23: 0.0385
REMARK 3 L TENSOR
REMARK 3 L11: 0.9198 L22: 1.4297
REMARK 3 L33: 1.9263 L12: 0.1018
REMARK 3 L13: 0.5379 L23: 0.0846
REMARK 3 S TENSOR
REMARK 3 S11: 0.1043 S12: 0.0341 S13: -0.0368
REMARK 3 S21: 0.1166 S22: -0.0218 S23: -0.0746
REMARK 3 S31: 0.1103 S32: 0.1128 S33: -0.0825
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 151 A 225
REMARK 3 ORIGIN FOR THE GROUP (A): 65.8187 5.4965 6.0514
REMARK 3 T TENSOR
REMARK 3 T11: -0.0975 T22: -0.0011
REMARK 3 T33: -0.0821 T12: -0.0123
REMARK 3 T13: 0.0411 T23: 0.0393
REMARK 3 L TENSOR
REMARK 3 L11: 1.1553 L22: 0.7535
REMARK 3 L33: 3.5203 L12: 0.1091
REMARK 3 L13: 0.6885 L23: 0.2047
REMARK 3 S TENSOR
REMARK 3 S11: 0.1027 S12: -0.1680 S13: 0.0052
REMARK 3 S21: 0.1866 S22: -0.0607 S23: 0.2024
REMARK 3 S31: 0.0561 S32: -0.6419 S33: -0.0420
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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 4
REMARK 4 2PSD COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006
REMARK 4
REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY.
REMARK 4 REMEDIATED DATA FILE REVISION 3.100 (2007-06-01)
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB .
REMARK 100 THE RCSB ID CODE IS RCSB042730.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 73121
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
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 (%) : NULL
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.3M NACL, 1.25M DIAMMONIUM
REMARK 280 PHOSPHATE, 0.1M IMIDAZOLE, PH 8.0, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,1/3+Z
REMARK 290 3555 -X+Y,-X,2/3+Z
REMARK 290 4555 -X,-Y,1/2+Z
REMARK 290 5555 Y,-X+Y,5/6+Z
REMARK 290 6555 X-Y,X,1/6+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 -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 15.99833
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 31.99667
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 23.99750
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 39.99583
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 7.99917
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 ALA A 2
REMARK 465 SER A 3
REMARK 465 ASN A 309
REMARK 465 GLU A 310
REMARK 465 GLN A 311
REMARK 465 VAL A 312
REMARK 465 ASP A 313
REMARK 465 HIS A 314
REMARK 465 HIS A 315
REMARK 465 HIS A 316
REMARK 465 HIS A 317
REMARK 465 HIS A 318
REMARK 465 HIS A 319
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
REMARK 500 O HOH 102 O HOH 103 2.13
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 TYR A 240 CA - CB - CG ANGL. DEV. = 8.4 DEGREES
REMARK 500 LEU A 287 CA - CB - CG ANGL. DEV. = 12.9 DEGREES
REMARK 500 LEU A 287 CB - CG - CD1 ANGL. DEV. = 10.8 DEGREES
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 M RES CSSEQI PSI PHI
REMARK 500 GLU A 40 -54.00 74.87
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2PSE RELATED DB: PDB
REMARK 900 RELATED ID: 2PSF RELATED DB: PDB
REMARK 900 RELATED ID: 2PSH RELATED DB: PDB
REMARK 900 RELATED ID: 2PSJ RELATED DB: PDB
REMARK 900 RELATED ID: 2PSL RELATED DB: PDB
DBREF 2PSD A 3 311 UNP P27652 LUCI_RENRE 3 311
SEQADV 2PSD ALA A 2 UNP P27652 CLONING ARTIFACT
SEQADV 2PSD THR A 55 UNP P27652 ALA 55 ENGINEERED
SEQADV 2PSD ALA A 124 UNP P27652 CYS 124 ENGINEERED
SEQADV 2PSD ALA A 130 UNP P27652 SER 130 ENGINEERED
SEQADV 2PSD ARG A 136 UNP P27652 LYS 136 ENGINEERED
SEQADV 2PSD MET A 143 UNP P27652 ALA 143 ENGINEERED
SEQADV 2PSD VAL A 185 UNP P27652 MET 185 ENGINEERED
SEQADV 2PSD LEU A 253 UNP P27652 MET 253 ENGINEERED
SEQADV 2PSD LEU A 287 UNP P27652 SER 287 ENGINEERED
SEQADV 2PSD VAL A 312 UNP P27652 CLONING ARTIFACT
SEQADV 2PSD ASP A 313 UNP P27652 CLONING ARTIFACT
SEQADV 2PSD HIS A 314 UNP P27652 HIS TAG
SEQADV 2PSD HIS A 315 UNP P27652 HIS TAG
SEQADV 2PSD HIS A 316 UNP P27652 HIS TAG
SEQADV 2PSD HIS A 317 UNP P27652 HIS TAG
SEQADV 2PSD HIS A 318 UNP P27652 HIS TAG
SEQADV 2PSD HIS A 319 UNP P27652 HIS TAG
SEQRES 1 A 318 ALA SER LYS VAL TYR ASP PRO GLU GLN ARG LYS ARG MET
SEQRES 2 A 318 ILE THR GLY PRO GLN TRP TRP ALA ARG CYS LYS GLN MET
SEQRES 3 A 318 ASN VAL LEU ASP SER PHE ILE ASN TYR TYR ASP SER GLU
SEQRES 4 A 318 LYS HIS ALA GLU ASN ALA VAL ILE PHE LEU HIS GLY ASN
SEQRES 5 A 318 ALA THR SER SER TYR LEU TRP ARG HIS VAL VAL PRO HIS
SEQRES 6 A 318 ILE GLU PRO VAL ALA ARG CYS ILE ILE PRO ASP LEU ILE
SEQRES 7 A 318 GLY MET GLY LYS SER GLY LYS SER GLY ASN GLY SER TYR
SEQRES 8 A 318 ARG LEU LEU ASP HIS TYR LYS TYR LEU THR ALA TRP PHE
SEQRES 9 A 318 GLU LEU LEU ASN LEU PRO LYS LYS ILE ILE PHE VAL GLY
SEQRES 10 A 318 HIS ASP TRP GLY ALA ALA LEU ALA PHE HIS TYR ALA TYR
SEQRES 11 A 318 GLU HIS GLN ASP ARG ILE LYS ALA ILE VAL HIS MET GLU
SEQRES 12 A 318 SER VAL VAL ASP VAL ILE GLU SER TRP ASP GLU TRP PRO
SEQRES 13 A 318 ASP ILE GLU GLU ASP ILE ALA LEU ILE LYS SER GLU GLU
SEQRES 14 A 318 GLY GLU LYS MET VAL LEU GLU ASN ASN PHE PHE VAL GLU
SEQRES 15 A 318 THR VAL LEU PRO SER LYS ILE MET ARG LYS LEU GLU PRO
SEQRES 16 A 318 GLU GLU PHE ALA ALA TYR LEU GLU PRO PHE LYS GLU LYS
SEQRES 17 A 318 GLY GLU VAL ARG ARG PRO THR LEU SER TRP PRO ARG GLU
SEQRES 18 A 318 ILE PRO LEU VAL LYS GLY GLY LYS PRO ASP VAL VAL GLN
SEQRES 19 A 318 ILE VAL ARG ASN TYR ASN ALA TYR LEU ARG ALA SER ASP
SEQRES 20 A 318 ASP LEU PRO LYS LEU PHE ILE GLU SER ASP PRO GLY PHE
SEQRES 21 A 318 PHE SER ASN ALA ILE VAL GLU GLY ALA LYS LYS PHE PRO
SEQRES 22 A 318 ASN THR GLU PHE VAL LYS VAL LYS GLY LEU HIS PHE LEU
SEQRES 23 A 318 GLN GLU ASP ALA PRO ASP GLU MET GLY LYS TYR ILE LYS
SEQRES 24 A 318 SER PHE VAL GLU ARG VAL LEU LYS ASN GLU GLN VAL ASP
SEQRES 25 A 318 HIS HIS HIS HIS HIS HIS
HET IMD 401 5
HET IMD 402 5
HETNAM IMD IMIDAZOLE
FORMUL 2 IMD 2(C3 H5 N2 1+)
FORMUL 4 HOH *384(H2 O)
HELIX 1 1 GLU A 9 MET A 14 1 6
HELIX 2 2 THR A 16 CYS A 24 1 9
HELIX 3 3 SER A 56 ARG A 61 5 6
HELIX 4 4 VAL A 63 ILE A 67 5 5
HELIX 5 5 ARG A 93 GLU A 106 1 14
HELIX 6 6 ASP A 120 HIS A 133 1 14
HELIX 7 7 ILE A 159 SER A 168 1 10
HELIX 8 8 GLU A 169 LEU A 176 1 8
HELIX 9 9 ASN A 179 THR A 184 1 6
HELIX 10 10 THR A 184 LYS A 189 1 6
HELIX 11 11 GLU A 195 GLU A 204 1 10
HELIX 12 12 PRO A 205 LYS A 207 5 3
HELIX 13 13 GLY A 210 VAL A 212 5 3
HELIX 14 14 ARG A 213 GLU A 222 1 10
HELIX 15 15 LYS A 230 ALA A 246 1 17
HELIX 16 16 PHE A 262 LYS A 271 1 10
HELIX 17 17 PHE A 286 ASP A 290 5 5
HELIX 18 18 ALA A 291 LYS A 308 1 18
SHEET 1 A 8 LYS A 25 VAL A 29 0
SHEET 2 A 8 SER A 32 ASP A 38 -1 O TYR A 36 N LYS A 25
SHEET 3 A 8 ARG A 72 PRO A 76 -1 O ILE A 75 N TYR A 37
SHEET 4 A 8 ALA A 46 LEU A 50 1 N VAL A 47 O ARG A 72
SHEET 5 A 8 ILE A 114 HIS A 119 1 O VAL A 117 N LEU A 50
SHEET 6 A 8 ILE A 137 MET A 143 1 O VAL A 141 N PHE A 116
SHEET 7 A 8 LYS A 252 PRO A 259 1 O LEU A 253 N HIS A 142
SHEET 8 A 8 THR A 276 GLY A 283 1 O GLU A 277 N PHE A 254
CISPEP 1 ASP A 258 PRO A 259 0 4.11
CRYST1 119.468 119.468 47.995 90.00 90.00 120.00 P 61 6
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 0.008370 0.004833 0.000000 0.00000
SCALE2 0.000000 0.009665 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020836 0.00000
TER 2525 LYS A 308
MASTER 339 0 2 18 8 0 0 6 2921 1 10 25
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