| content |
HEADER OXIDOREDUCTASE 06-MAY-07 2PSH
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, B;
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 2PSH 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. 1.79 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) : 1.79
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 86.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 3 NUMBER OF REFLECTIONS : 58344
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) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3119
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.79
REMARK 3 BIN RESOLUTION RANGE LOW : 1.84
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3552
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 80.69
REMARK 3 BIN R VALUE (WORKING SET) : 0.2980
REMARK 3 BIN FREE R VALUE SET COUNT : 201
REMARK 3 BIN FREE R VALUE : 0.3530
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 5336
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.09
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.95000
REMARK 3 B22 (A**2) : 0.13000
REMARK 3 B33 (A**2) : -1.10000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.04000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.136
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.127
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.091
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.928
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.934
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4994 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 3487 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6755 ; 1.212 ; 1.952
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8473 ; 0.878 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 593 ; 5.642 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 238 ;34.843 ;23.824
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 872 ;12.784 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;16.897 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 710 ; 0.077 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5483 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1040 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1072 ; 0.212 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 3548 ; 0.193 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2446 ; 0.179 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 2337 ; 0.082 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 379 ; 0.125 ; 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): 2 ; 0.139 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 23 ; 0.169 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 28 ; 0.116 ; 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): 3864 ; 0.776 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1192 ; 0.122 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4821 ; 0.858 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2434 ; 1.395 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1934 ; 1.994 ; 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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 3 A 310 4
REMARK 3 1 B 3 B 310 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 4149 ; 0.42 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 4149 ; 0.42 ; 2.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 0
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 2PSH 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 RCSB042733.
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 : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.2
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 : 58344
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.790
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
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 (%): 46.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1~M HEPES, 10% V/V ISOPROPANOL
REMARK 280 WITH 6MG/ML BENZYL-COELENTERAZINE, 15% W/V PEG 3350, PH 7.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 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,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 37.82600
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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 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 350 BIOMOLECULE: 2
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; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 ASP A 154
REMARK 465 GLU A 155
REMARK 465 TRP A 156
REMARK 465 PRO A 157
REMARK 465 ASP A 158
REMARK 465 ILE A 159
REMARK 465 GLU A 160
REMARK 465 GLU A 161
REMARK 465 ASP A 162
REMARK 465 ILE A 163
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 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 TRP B 153
REMARK 465 ASP B 154
REMARK 465 GLU B 155
REMARK 465 TRP B 156
REMARK 465 PRO B 157
REMARK 465 ASP B 158
REMARK 465 ILE B 159
REMARK 465 GLU B 160
REMARK 465 GLU B 161
REMARK 465 GLN B 311
REMARK 465 VAL B 312
REMARK 465 ASP B 313
REMARK 465 HIS B 314
REMARK 465 HIS B 315
REMARK 465 HIS B 316
REMARK 465 HIS B 317
REMARK 465 HIS B 318
REMARK 465 HIS B 319
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 LYS A 272 CE LYS A 272 NZ 0.056
REMARK 500 ASN B 179 CB ASN B 179 CG -0.058
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 PRO A 65 C - N - CA ANGL. DEV. = -7.6 DEGREES
REMARK 500 PRO A 65 C - N - CD ANGL. DEV. = 8.7 DEGREES
REMARK 500 LEU A 287 CA - CB - CG ANGL. DEV. = 8.8 DEGREES
REMARK 500 TYR B 240 CA - CB - CG ANGL. DEV. = 8.1 DEGREES
REMARK 500 LEU B 287 CA - CB - CG ANGL. DEV. = 9.4 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 -50.80 69.14
REMARK 500 GLU B 40 -56.04 72.28
REMARK 500 ASN B 179 68.19 3.57
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2PSD RELATED DB: PDB
REMARK 900 RELATED ID: 2PSE RELATED DB: PDB
REMARK 900 RELATED ID: 2PSF RELATED DB: PDB
REMARK 900 RELATED ID: 2PSJ RELATED DB: PDB
REMARK 900 RELATED ID: 2PSL RELATED DB: PDB
DBREF 2PSH A 1 311 UNP P27652 LUCI_RENRE 1 311
DBREF 2PSH B 1 311 UNP P27652 LUCI_RENRE 1 311
SEQADV 2PSH ALA A 2 UNP P27652 THR 2 ENGINEERED
SEQADV 2PSH ALA A 25 UNP P27652 LYS 25 ENGINEERED
SEQADV 2PSH THR A 55 UNP P27652 ALA 55 ENGINEERED
SEQADV 2PSH ALA A 124 UNP P27652 CYS 124 ENGINEERED
SEQADV 2PSH ALA A 130 UNP P27652 SER 130 ENGINEERED
SEQADV 2PSH ARG A 136 UNP P27652 LYS 136 ENGINEERED
SEQADV 2PSH MET A 143 UNP P27652 ALA 143 ENGINEERED
SEQADV 2PSH VAL A 185 UNP P27652 MET 185 ENGINEERED
SEQADV 2PSH LEU A 253 UNP P27652 MET 253 ENGINEERED
SEQADV 2PSH ALA A 277 UNP P27652 GLU 277 ENGINEERED
SEQADV 2PSH LEU A 287 UNP P27652 SER 287 ENGINEERED
SEQADV 2PSH VAL A 312 UNP P27652 CLONING ARTIFACT
SEQADV 2PSH ASP A 313 UNP P27652 CLONING ARTIFACT
SEQADV 2PSH HIS A 314 UNP P27652 HIS TAG
SEQADV 2PSH HIS A 315 UNP P27652 HIS TAG
SEQADV 2PSH HIS A 316 UNP P27652 HIS TAG
SEQADV 2PSH HIS A 317 UNP P27652 HIS TAG
SEQADV 2PSH HIS A 318 UNP P27652 HIS TAG
SEQADV 2PSH HIS A 319 UNP P27652 HIS TAG
SEQADV 2PSH ALA B 2 UNP P27652 THR 2 ENGINEERED
SEQADV 2PSH ALA B 25 UNP P27652 LYS 25 ENGINEERED
SEQADV 2PSH THR B 55 UNP P27652 ALA 55 ENGINEERED
SEQADV 2PSH ALA B 124 UNP P27652 CYS 124 ENGINEERED
SEQADV 2PSH ALA B 130 UNP P27652 SER 130 ENGINEERED
SEQADV 2PSH ARG B 136 UNP P27652 LYS 136 ENGINEERED
SEQADV 2PSH MET B 143 UNP P27652 ALA 143 ENGINEERED
SEQADV 2PSH VAL B 185 UNP P27652 MET 185 ENGINEERED
SEQADV 2PSH LEU B 253 UNP P27652 MET 253 ENGINEERED
SEQADV 2PSH ALA B 277 UNP P27652 GLU 277 ENGINEERED
SEQADV 2PSH LEU B 287 UNP P27652 SER 287 ENGINEERED
SEQADV 2PSH VAL B 312 UNP P27652 CLONING ARTIFACT
SEQADV 2PSH ASP B 313 UNP P27652 CLONING ARTIFACT
SEQADV 2PSH HIS B 314 UNP P27652 HIS TAG
SEQADV 2PSH HIS B 315 UNP P27652 HIS TAG
SEQADV 2PSH HIS B 316 UNP P27652 HIS TAG
SEQADV 2PSH HIS B 317 UNP P27652 HIS TAG
SEQADV 2PSH HIS B 318 UNP P27652 HIS TAG
SEQADV 2PSH HIS B 319 UNP P27652 HIS TAG
SEQRES 1 A 319 MET ALA SER LYS VAL TYR ASP PRO GLU GLN ARG LYS ARG
SEQRES 2 A 319 MET ILE THR GLY PRO GLN TRP TRP ALA ARG CYS ALA GLN
SEQRES 3 A 319 MET ASN VAL LEU ASP SER PHE ILE ASN TYR TYR ASP SER
SEQRES 4 A 319 GLU LYS HIS ALA GLU ASN ALA VAL ILE PHE LEU HIS GLY
SEQRES 5 A 319 ASN ALA THR SER SER TYR LEU TRP ARG HIS VAL VAL PRO
SEQRES 6 A 319 HIS ILE GLU PRO VAL ALA ARG CYS ILE ILE PRO ASP LEU
SEQRES 7 A 319 ILE GLY MET GLY LYS SER GLY LYS SER GLY ASN GLY SER
SEQRES 8 A 319 TYR ARG LEU LEU ASP HIS TYR LYS TYR LEU THR ALA TRP
SEQRES 9 A 319 PHE GLU LEU LEU ASN LEU PRO LYS LYS ILE ILE PHE VAL
SEQRES 10 A 319 GLY HIS ASP TRP GLY ALA ALA LEU ALA PHE HIS TYR ALA
SEQRES 11 A 319 TYR GLU HIS GLN ASP ARG ILE LYS ALA ILE VAL HIS MET
SEQRES 12 A 319 GLU SER VAL VAL ASP VAL ILE GLU SER TRP ASP GLU TRP
SEQRES 13 A 319 PRO ASP ILE GLU GLU ASP ILE ALA LEU ILE LYS SER GLU
SEQRES 14 A 319 GLU GLY GLU LYS MET VAL LEU GLU ASN ASN PHE PHE VAL
SEQRES 15 A 319 GLU THR VAL LEU PRO SER LYS ILE MET ARG LYS LEU GLU
SEQRES 16 A 319 PRO GLU GLU PHE ALA ALA TYR LEU GLU PRO PHE LYS GLU
SEQRES 17 A 319 LYS GLY GLU VAL ARG ARG PRO THR LEU SER TRP PRO ARG
SEQRES 18 A 319 GLU ILE PRO LEU VAL LYS GLY GLY LYS PRO ASP VAL VAL
SEQRES 19 A 319 GLN ILE VAL ARG ASN TYR ASN ALA TYR LEU ARG ALA SER
SEQRES 20 A 319 ASP ASP LEU PRO LYS LEU PHE ILE GLU SER ASP PRO GLY
SEQRES 21 A 319 PHE PHE SER ASN ALA ILE VAL GLU GLY ALA LYS LYS PHE
SEQRES 22 A 319 PRO ASN THR ALA PHE VAL LYS VAL LYS GLY LEU HIS PHE
SEQRES 23 A 319 LEU GLN GLU ASP ALA PRO ASP GLU MET GLY LYS TYR ILE
SEQRES 24 A 319 LYS SER PHE VAL GLU ARG VAL LEU LYS ASN GLU GLN VAL
SEQRES 25 A 319 ASP HIS HIS HIS HIS HIS HIS
SEQRES 1 B 319 MET ALA SER LYS VAL TYR ASP PRO GLU GLN ARG LYS ARG
SEQRES 2 B 319 MET ILE THR GLY PRO GLN TRP TRP ALA ARG CYS ALA GLN
SEQRES 3 B 319 MET ASN VAL LEU ASP SER PHE ILE ASN TYR TYR ASP SER
SEQRES 4 B 319 GLU LYS HIS ALA GLU ASN ALA VAL ILE PHE LEU HIS GLY
SEQRES 5 B 319 ASN ALA THR SER SER TYR LEU TRP ARG HIS VAL VAL PRO
SEQRES 6 B 319 HIS ILE GLU PRO VAL ALA ARG CYS ILE ILE PRO ASP LEU
SEQRES 7 B 319 ILE GLY MET GLY LYS SER GLY LYS SER GLY ASN GLY SER
SEQRES 8 B 319 TYR ARG LEU LEU ASP HIS TYR LYS TYR LEU THR ALA TRP
SEQRES 9 B 319 PHE GLU LEU LEU ASN LEU PRO LYS LYS ILE ILE PHE VAL
SEQRES 10 B 319 GLY HIS ASP TRP GLY ALA ALA LEU ALA PHE HIS TYR ALA
SEQRES 11 B 319 TYR GLU HIS GLN ASP ARG ILE LYS ALA ILE VAL HIS MET
SEQRES 12 B 319 GLU SER VAL VAL ASP VAL ILE GLU SER TRP ASP GLU TRP
SEQRES 13 B 319 PRO ASP ILE GLU GLU ASP ILE ALA LEU ILE LYS SER GLU
SEQRES 14 B 319 GLU GLY GLU LYS MET VAL LEU GLU ASN ASN PHE PHE VAL
SEQRES 15 B 319 GLU THR VAL LEU PRO SER LYS ILE MET ARG LYS LEU GLU
SEQRES 16 B 319 PRO GLU GLU PHE ALA ALA TYR LEU GLU PRO PHE LYS GLU
SEQRES 17 B 319 LYS GLY GLU VAL ARG ARG PRO THR LEU SER TRP PRO ARG
SEQRES 18 B 319 GLU ILE PRO LEU VAL LYS GLY GLY LYS PRO ASP VAL VAL
SEQRES 19 B 319 GLN ILE VAL ARG ASN TYR ASN ALA TYR LEU ARG ALA SER
SEQRES 20 B 319 ASP ASP LEU PRO LYS LEU PHE ILE GLU SER ASP PRO GLY
SEQRES 21 B 319 PHE PHE SER ASN ALA ILE VAL GLU GLY ALA LYS LYS PHE
SEQRES 22 B 319 PRO ASN THR ALA PHE VAL LYS VAL LYS GLY LEU HIS PHE
SEQRES 23 B 319 LEU GLN GLU ASP ALA PRO ASP GLU MET GLY LYS TYR ILE
SEQRES 24 B 319 LYS SER PHE VAL GLU ARG VAL LEU LYS ASN GLU GLN VAL
SEQRES 25 B 319 ASP HIS HIS HIS HIS HIS HIS
FORMUL 3 HOH *476(H2 O)
HELIX 1 1 GLN A 10 MET A 14 5 5
HELIX 2 2 THR A 16 ALA A 22 1 7
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 SER A 168 GLU A 177 1 10
HELIX 8 8 ASN A 179 THR A 184 1 6
HELIX 9 9 THR A 184 LYS A 189 1 6
HELIX 10 10 GLU A 195 GLU A 204 1 10
HELIX 11 11 PRO A 205 LYS A 207 5 3
HELIX 12 12 GLY A 210 VAL A 212 5 3
HELIX 13 13 ARG A 213 GLU A 222 1 10
HELIX 14 14 LYS A 230 ALA A 246 1 17
HELIX 15 15 SER A 263 LYS A 271 1 9
HELIX 16 16 PHE A 286 ASP A 290 5 5
HELIX 17 17 ALA A 291 GLU A 310 1 20
HELIX 18 18 GLU B 9 ARG B 13 5 5
HELIX 19 19 THR B 16 ALA B 22 1 7
HELIX 20 20 SER B 56 ARG B 61 5 6
HELIX 21 21 VAL B 63 ILE B 67 5 5
HELIX 22 22 ARG B 93 GLU B 106 1 14
HELIX 23 23 ASP B 120 HIS B 133 1 14
HELIX 24 24 ASP B 162 SER B 168 1 7
HELIX 25 25 SER B 168 GLU B 177 1 10
HELIX 26 26 ASN B 179 THR B 184 1 6
HELIX 27 27 THR B 184 LYS B 189 1 6
HELIX 28 28 GLU B 195 GLU B 204 1 10
HELIX 29 29 PRO B 205 LYS B 207 5 3
HELIX 30 30 GLY B 210 VAL B 212 5 3
HELIX 31 31 ARG B 213 GLU B 222 1 10
HELIX 32 32 LYS B 230 ALA B 246 1 17
HELIX 33 33 SER B 263 LYS B 271 1 9
HELIX 34 34 PHE B 286 ASP B 290 5 5
HELIX 35 35 ALA B 291 GLU B 310 1 20
SHEET 1 A 8 ALA A 25 VAL A 29 0
SHEET 2 A 8 SER A 32 ASP A 38 -1 O TYR A 36 N ALA 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 VAL A 279 N GLU A 256
SHEET 1 B 8 ALA B 25 VAL B 29 0
SHEET 2 B 8 SER B 32 ASP B 38 -1 O TYR B 36 N ALA B 25
SHEET 3 B 8 ARG B 72 PRO B 76 -1 O ILE B 75 N TYR B 37
SHEET 4 B 8 ALA B 46 LEU B 50 1 N VAL B 47 O ARG B 72
SHEET 5 B 8 ILE B 114 HIS B 119 1 O VAL B 117 N LEU B 50
SHEET 6 B 8 ILE B 137 MET B 143 1 O VAL B 141 N PHE B 116
SHEET 7 B 8 LYS B 252 PRO B 259 1 O LEU B 253 N HIS B 142
SHEET 8 B 8 THR B 276 GLY B 283 1 O VAL B 279 N GLU B 256
CISPEP 1 ASP A 258 PRO A 259 0 8.16
CISPEP 2 ASP B 258 PRO B 259 0 9.24
CRYST1 51.776 75.652 89.185 90.00 76.48 90.00 P 1 21 1 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 0.019314 0.000000 -0.004645 0.00000
SCALE2 0.000000 0.013218 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011532 0.00000
TER 2430 GLU A 310
TER 4862 GLU B 310
MASTER 342 0 0 35 16 0 0 6 5336 2 0 50
END |