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HEADER OXIDOREDUCTASE 06-MAY-07 2PSJ
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 2PSJ 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. 1.80 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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 3 NUMBER OF REFLECTIONS : 55608
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) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2915
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3976
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.22
REMARK 3 BIN R VALUE (WORKING SET) : 0.2650
REMARK 3 BIN FREE R VALUE SET COUNT : 183
REMARK 3 BIN FREE R VALUE : 0.2990
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 5521
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.44
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.09000
REMARK 3 B22 (A**2) : -0.66000
REMARK 3 B33 (A**2) : -0.57000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.31000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.141
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.126
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.087
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.418
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
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): 5214 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 3634 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7054 ; 1.194 ; 1.968
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8826 ; 0.860 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 608 ; 5.624 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 250 ;35.266 ;24.080
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 906 ;13.039 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;14.747 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 728 ; 0.074 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5726 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1086 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1116 ; 0.209 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 3817 ; 0.193 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2554 ; 0.184 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 2460 ; 0.083 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 397 ; 0.135 ; 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): 17 ; 0.136 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 42 ; 0.124 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 25 ; 0.148 ; 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): 3975 ; 0.642 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1220 ; 0.120 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4958 ; 0.708 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2621 ; 1.331 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2096 ; 1.928 ; 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): 4303 ; 0.12 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 4303 ; 0.30 ; 2.00
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 3 A 309
REMARK 3 RESIDUE RANGE : 1 1
REMARK 3 ORIGIN FOR THE GROUP (A): -1.1074 -10.0625 38.7146
REMARK 3 T TENSOR
REMARK 3 T11: -0.1318 T22: -0.1140
REMARK 3 T33: -0.1189 T12: -0.0057
REMARK 3 T13: 0.0049 T23: -0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 0.6188 L22: 1.6413
REMARK 3 L33: 1.9107 L12: 0.0544
REMARK 3 L13: -0.0080 L23: 0.5003
REMARK 3 S TENSOR
REMARK 3 S11: 0.0415 S12: -0.0403 S13: 0.0376
REMARK 3 S21: 0.0015 S22: -0.0108 S23: 0.0445
REMARK 3 S31: -0.0537 S32: -0.0254 S33: -0.0307
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 10 B 310
REMARK 3 RESIDUE RANGE : 1 1
REMARK 3 ORIGIN FOR THE GROUP (A): 6.0839 -39.9402 8.8130
REMARK 3 T TENSOR
REMARK 3 T11: -0.1347 T22: -0.1238
REMARK 3 T33: -0.1335 T12: 0.0109
REMARK 3 T13: -0.0141 T23: -0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 0.8763 L22: 1.5129
REMARK 3 L33: 1.5562 L12: -0.2278
REMARK 3 L13: -0.2786 L23: 0.0800
REMARK 3 S TENSOR
REMARK 3 S11: 0.0027 S12: 0.0634 S13: -0.0285
REMARK 3 S21: -0.0759 S22: 0.0067 S23: 0.0347
REMARK 3 S31: 0.0373 S32: -0.0085 S33: -0.0094
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 2PSJ 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 RCSB042734.
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 : 55608
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
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 (%): 44.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, 10% V/V ISOPROPANOL
REMARK 280 WITH 6MG/ML COELENTERAZINE, 15% W/V PEG 3350, PH 7.5, VAPOR
REMARK 280 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 37.23650
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 TRP A 153
REMARK 465 ASP A 154
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 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: 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 OD2 ASP A 135 O HOH 333 2.16
REMARK 500 O HOH 152 O HOH 333 2.17
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 PRO B 224 CB PRO B 224 CG -0.056
REMARK 500 PRO B 251 CB PRO B 251 CG -0.057
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 LEU A 287 CA - CB - CG ANGL. DEV. = 10.7 DEGREES
REMARK 500 LYS A 308 N - CA - C ANGL. DEV. =-10.0 DEGREES
REMARK 500 MET B 27 CB - CG - SD ANGL. DEV. = -7.4 DEGREES
REMARK 500 TYR B 240 CA - CB - CG ANGL. DEV. = 7.4 DEGREES
REMARK 500 LEU B 287 CA - CB - CG ANGL. DEV. = 8.4 DEGREES
REMARK 500 LYS B 308 N - CA - C ANGL. DEV. = -9.1 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 -50.45 71.76
REMARK 500 ASN A 309 -50.25 72.29
REMARK 500 LEU B 30 -118.07 52.27
REMARK 500 GLU B 40 -52.51 68.66
REMARK 500 ASN B 309 -50.42 71.58
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: 2PSH RELATED DB: PDB
REMARK 900 RELATED ID: 2PSL RELATED DB: PDB
DBREF 2PSJ A 1 311 UNP P27652 LUCI_RENRE 1 311
DBREF 2PSJ B 1 311 UNP P27652 LUCI_RENRE 1 311
SEQADV 2PSJ ALA A 2 UNP P27652 THR 2 ENGINEERED
SEQADV 2PSJ THR A 55 UNP P27652 ALA 55 ENGINEERED
SEQADV 2PSJ ALA A 124 UNP P27652 CYS 124 ENGINEERED
SEQADV 2PSJ ALA A 130 UNP P27652 SER 130 ENGINEERED
SEQADV 2PSJ ARG A 136 UNP P27652 LYS 136 ENGINEERED
SEQADV 2PSJ MET A 143 UNP P27652 ALA 143 ENGINEERED
SEQADV 2PSJ VAL A 185 UNP P27652 MET 185 ENGINEERED
SEQADV 2PSJ LEU A 253 UNP P27652 MET 253 ENGINEERED
SEQADV 2PSJ LEU A 287 UNP P27652 SER 287 ENGINEERED
SEQADV 2PSJ VAL A 312 UNP P27652 CLONING ARTIFACT
SEQADV 2PSJ ASP A 313 UNP P27652 CLONING ARTIFACT
SEQADV 2PSJ HIS A 314 UNP P27652 HIS TAG
SEQADV 2PSJ HIS A 315 UNP P27652 HIS TAG
SEQADV 2PSJ HIS A 316 UNP P27652 HIS TAG
SEQADV 2PSJ HIS A 317 UNP P27652 HIS TAG
SEQADV 2PSJ HIS A 318 UNP P27652 HIS TAG
SEQADV 2PSJ HIS A 319 UNP P27652 HIS TAG
SEQADV 2PSJ ALA B 2 UNP P27652 THR 2 ENGINEERED
SEQADV 2PSJ THR B 55 UNP P27652 ALA 55 ENGINEERED
SEQADV 2PSJ ALA B 124 UNP P27652 CYS 124 ENGINEERED
SEQADV 2PSJ ALA B 130 UNP P27652 SER 130 ENGINEERED
SEQADV 2PSJ ARG B 136 UNP P27652 LYS 136 ENGINEERED
SEQADV 2PSJ MET B 143 UNP P27652 ALA 143 ENGINEERED
SEQADV 2PSJ VAL B 185 UNP P27652 MET 185 ENGINEERED
SEQADV 2PSJ LEU B 253 UNP P27652 MET 253 ENGINEERED
SEQADV 2PSJ LEU B 287 UNP P27652 SER 287 ENGINEERED
SEQADV 2PSJ VAL B 312 UNP P27652 CLONING ARTIFACT
SEQADV 2PSJ ASP B 313 UNP P27652 CLONING ARTIFACT
SEQADV 2PSJ HIS B 314 UNP P27652 HIS TAG
SEQADV 2PSJ HIS B 315 UNP P27652 HIS TAG
SEQADV 2PSJ HIS B 316 UNP P27652 HIS TAG
SEQADV 2PSJ HIS B 317 UNP P27652 HIS TAG
SEQADV 2PSJ HIS B 318 UNP P27652 HIS TAG
SEQADV 2PSJ 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 LYS 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 GLU 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 LYS 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 GLU 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
HET CEI 501 31
HET CEI 502 31
HETNAM CEI N-[3-BENZYL-5-(4-HYDROXYPHENYL)PYRAZIN-2-YL]-2-(4-
HETNAM 2 CEI HYDROXYPHENYL)ACETAMIDE
HETSYN CEI COELENTERAMIDE
FORMUL 3 CEI 2(C25 H21 N3 O3)
FORMUL 5 HOH *453(H2 O)
HELIX 1 1 GLN A 10 MET A 14 5 5
HELIX 2 2 THR A 16 ARG A 23 1 8
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 TRP A 121 HIS A 133 1 13
HELIX 7 7 ASP A 158 SER A 168 1 11
HELIX 8 8 SER A 168 LEU A 176 1 9
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 SER A 263 LYS A 271 1 9
HELIX 17 17 PHE A 286 ASP A 290 5 5
HELIX 18 18 ALA A 291 LYS A 308 1 18
HELIX 19 19 GLN B 10 MET B 14 5 5
HELIX 20 20 THR B 16 ARG B 23 1 8
HELIX 21 21 SER B 56 ARG B 61 5 6
HELIX 22 22 VAL B 63 GLU B 68 1 6
HELIX 23 23 ARG B 93 GLU B 106 1 14
HELIX 24 24 TRP B 121 HIS B 133 1 13
HELIX 25 25 ASP B 158 SER B 168 1 11
HELIX 26 26 SER B 168 GLU B 177 1 10
HELIX 27 27 ASN B 179 THR B 184 1 6
HELIX 28 28 THR B 184 LYS B 189 1 6
HELIX 29 29 GLU B 195 GLU B 204 1 10
HELIX 30 30 PRO B 205 LYS B 207 5 3
HELIX 31 31 GLY B 210 VAL B 212 5 3
HELIX 32 32 ARG B 213 GLU B 222 1 10
HELIX 33 33 LYS B 230 ARG B 245 1 16
HELIX 34 34 SER B 263 LYS B 271 1 9
HELIX 35 35 PHE B 286 ASP B 290 5 5
HELIX 36 36 ALA B 291 LYS B 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 ASP A 120 1 O VAL A 117 N LEU A 50
SHEET 6 A 8 ILE A 137 SER A 145 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 LYS B 25 VAL B 29 0
SHEET 2 B 8 SER B 32 ASP B 38 -1 O TYR B 36 N LYS 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 ASP B 120 1 O VAL B 117 N LEU B 50
SHEET 6 B 8 ILE B 137 SER B 145 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 5.75
CISPEP 2 ASP B 258 PRO B 259 0 5.89
CRYST1 51.329 74.473 89.249 90.00 103.45 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 0.019482 0.000000 0.004659 0.00000
SCALE2 0.000000 0.013428 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011521 0.00000
TER 2504 GLU A 310
TER 5008 GLU B 310
MASTER 377 0 2 36 16 0 0 6 5521 2 62 50
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