LinkDB: 2PSD 2PSE 2PSF 2PSH 2PSJ 2RH7
Original site: 2PSD 2PSE 2PSF 2PSH 2PSJ 2RH7
HEADER OXIDOREDUCTASE 06-MAY-07 2PSD TITLE CRYSTAL STRUCTURES OF THE LUCIFERASE AND GREEN FLUORESCENT PROTEIN TITLE 2 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_TAXID: 6136; SOURCE 4 GENE: RLUC; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: LMG194; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PBAD KEYWDS ALPHA/BETA-HYDROLASE, LUCIFERASE, OXIDOREDUCTASE EXPDTA X-RAY DIFFRACTION AUTHOR A.M.LOENING,T.D.FENN,S.S.GAMBHIR REVDAT 6 21-FEB-24 2PSD 1 REMARK REVDAT 5 20-OCT-21 2PSD 1 REMARK SEQADV REVDAT 4 13-JUL-11 2PSD 1 VERSN REVDAT 3 24-FEB-09 2PSD 1 VERSN REVDAT 2 27-NOV-07 2PSD 1 JRNL 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 FLUORESCENT JRNL TITL 2 PROTEIN FROM RENILLA RENIFORMIS. JRNL REF J.MOL.BIOL. V. 374 1017 2007 JRNL REFN ISSN 0022-2836 JRNL PMID 17980388 JRNL DOI 10.1016/J.JMB.2007.09.078 REMARK 2 REMARK 2 RESOLUTION. 1.40 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2.0005 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN 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 (A) : 1.40 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 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 PROTEIN ATOMS : 2502 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 10 REMARK 3 SOLVENT ATOMS : 384 REMARK 3 REMARK 3 B VALUES. REMARK 3 B VALUE TYPE : LIKELY RESIDUAL 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 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1277 ; 1.746 ; 3.000 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1027 ; 2.468 ; 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 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 RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 2PSD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-MAY-07. REMARK 100 THE DEPOSITION ID IS D_1000042730. 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 REMARK 200 PH : 8.0 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 <I/SIGMA(I)> 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 <I/SIGMA(I)> 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 PHOSPHATE, REMARK 280 0.1M IMIDAZOLE, PH 8.0, VAPOR DIFFUSION, HANGING DROP, REMARK 280 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,Z+1/3 REMARK 290 3555 -X+Y,-X,Z+2/3 REMARK 290 4555 -X,-Y,Z+1/2 REMARK 290 5555 Y,-X+Y,Z+5/6 REMARK 290 6555 X-Y,X,Z+1/6 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 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 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: 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 PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 LEU A 287 CA - CB - CG ANGL. DEV. = 13.9 DEGREES REMARK 500 LEU A 287 CB - CG - CD1 ANGL. DEV. = 10.5 DEGREES REMARK 500 REMARK 500 REMARK: NULL 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 30 -125.14 49.87 REMARK 500 SER A 32 -147.68 -149.29 REMARK 500 GLU A 40 -54.00 74.87 REMARK 500 ALA A 54 -19.43 80.30 REMARK 500 THR A 55 -161.92 -114.65 REMARK 500 ASP A 120 -133.52 58.76 REMARK 500 GLU A 144 53.84 39.02 REMARK 500 PHE A 261 -65.66 -109.96 REMARK 500 LEU A 284 -116.50 -114.64 REMARK 500 ALA A 291 48.56 -140.70 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 401 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 402 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 EXPRESSION TAG SEQADV 2PSD THR A 55 UNP P27652 ALA 55 ENGINEERED MUTATION SEQADV 2PSD ALA A 124 UNP P27652 CYS 124 ENGINEERED MUTATION SEQADV 2PSD ALA A 130 UNP P27652 SER 130 ENGINEERED MUTATION SEQADV 2PSD ARG A 136 UNP P27652 LYS 136 ENGINEERED MUTATION SEQADV 2PSD MET A 143 UNP P27652 ALA 143 ENGINEERED MUTATION SEQADV 2PSD VAL A 185 UNP P27652 MET 185 ENGINEERED MUTATION SEQADV 2PSD LEU A 253 UNP P27652 MET 253 ENGINEERED MUTATION SEQADV 2PSD LEU A 287 UNP P27652 SER 287 ENGINEERED MUTATION SEQADV 2PSD VAL A 312 UNP P27652 EXPRESSION TAG SEQADV 2PSD ASP A 313 UNP P27652 EXPRESSION TAG SEQADV 2PSD HIS A 314 UNP P27652 EXPRESSION TAG SEQADV 2PSD HIS A 315 UNP P27652 EXPRESSION TAG SEQADV 2PSD HIS A 316 UNP P27652 EXPRESSION TAG SEQADV 2PSD HIS A 317 UNP P27652 EXPRESSION TAG SEQADV 2PSD HIS A 318 UNP P27652 EXPRESSION TAG SEQADV 2PSD HIS A 319 UNP P27652 EXPRESSION 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 A 401 5 HET IMD A 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 SITE 1 AC1 2 ASP A 162 HOH A 534 SITE 1 AC2 6 SER A 145 VAL A 146 TRP A 156 PHE A 262 SITE 2 AC2 6 HOH A 431 HOH A 587 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 (ATOM LINES ARE NOT SHOWN.) END
HEADER OXIDOREDUCTASE 06-MAY-07 2PSE TITLE CRYSTAL STRUCTURES OF THE LUCIFERASE AND GREEN FLUORESCENT PROTEIN TITLE 2 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_TAXID: 6136; SOURCE 4 GENE: RLUC; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: LMG194; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PBAD KEYWDS ALPHA/BETA-HYDROLASE, LUCIFERASE, OXIDOREDUCTASE EXPDTA X-RAY DIFFRACTION AUTHOR A.M.LOENING,T.D.FENN,S.S.GAMBHIR REVDAT 5 21-FEB-24 2PSE 1 REMARK REVDAT 4 20-OCT-21 2PSE 1 REMARK SEQADV REVDAT 3 24-FEB-09 2PSE 1 VERSN REVDAT 2 27-NOV-07 2PSE 1 JRNL REVDAT 1 22-MAY-07 2PSE 0 JRNL AUTH A.M.LOENING,T.D.FENN,S.S.GAMBHIR JRNL TITL CRYSTAL STRUCTURES OF THE LUCIFERASE AND GREEN FLUORESCENT JRNL TITL 2 PROTEIN FROM RENILLA RENIFORMIS. JRNL REF J.MOL.BIOL. V. 374 1017 2007 JRNL REFN ISSN 0022-2836 JRNL PMID 17980388 JRNL DOI 10.1016/J.JMB.2007.09.078 REMARK 2 REMARK 2 RESOLUTION. 2.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2.0019 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.56 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 89.2 REMARK 3 NUMBER OF REFLECTIONS : 11477 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) : 0.193 REMARK 3 R VALUE (WORKING SET) : 0.191 REMARK 3 FREE R VALUE : 0.232 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 604 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) : 2.50 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.56 REMARK 3 REFLECTION IN BIN (WORKING SET) : 727 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 77.57 REMARK 3 BIN R VALUE (WORKING SET) : 0.3090 REMARK 3 BIN FREE R VALUE SET COUNT : 34 REMARK 3 BIN FREE R VALUE : 0.4090 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2502 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 5 REMARK 3 SOLVENT ATOMS : 76 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.20 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.53000 REMARK 3 B22 (A**2) : 0.53000 REMARK 3 B33 (A**2) : -0.79000 REMARK 3 B12 (A**2) : 0.26000 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): 0.760 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.291 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.202 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.232 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.939 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.916 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2580 ; 0.017 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 1804 ; 0.002 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3492 ; 1.588 ; 1.954 REMARK 3 BOND ANGLES OTHERS (DEGREES): 4383 ; 0.957 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 304 ; 6.744 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 125 ;35.875 ;24.000 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 451 ;16.591 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;17.540 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 363 ; 0.089 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2837 ; 0.006 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 539 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 627 ; 0.228 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1944 ; 0.205 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1258 ; 0.194 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): 1272 ; 0.093 ; 0.200 REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 110 ; 0.190 ; 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 ; 0.147 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): 24 ; 0.339 ; 0.200 REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 5 ; 0.135 ; 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): 1953 ; 0.836 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 608 ; 0.139 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2474 ; 1.061 ; 2.000 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1267 ; 1.662 ; 3.000 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1018 ; 2.425 ; 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 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL 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 RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 2PSE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-MAY-07. REMARK 100 THE DEPOSITION ID IS D_1000042731. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 17-MAY-05 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.4 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 : 11477 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500 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 <I/SIGMA(I)> 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 <I/SIGMA(I)> 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 (%): 53.98 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.15 KSCN, 15% W/V PEG 6000, 0.1 M REMARK 280 TRIS-HCL, PH 7.4, VAPOR DIFFUSION, HANGING 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,Z+1/3 REMARK 290 3555 -X+Y,-X,Z+2/3 REMARK 290 4555 -X,-Y,Z+1/2 REMARK 290 5555 Y,-X+Y,Z+5/6 REMARK 290 6555 X-Y,X,Z+1/6 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 16.01600 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 32.03200 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 24.02400 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 40.04000 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 8.00800 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 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 DISTANCE REMARK 500 O LYS A 167 O HOH A 385 2.02 REMARK 500 NZ LYS A 193 O HOH A 390 2.14 REMARK 500 REMARK 500 REMARK: NULL 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 PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ARG A 221 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES REMARK 500 ARG A 221 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES REMARK 500 REMARK 500 REMARK: NULL 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 MET A 14 126.31 -33.03 REMARK 500 LEU A 30 -121.21 43.95 REMARK 500 SER A 32 -153.42 -144.54 REMARK 500 GLU A 40 -55.43 66.37 REMARK 500 HIS A 42 48.24 74.65 REMARK 500 ALA A 54 -13.10 87.49 REMARK 500 THR A 55 -159.88 -130.79 REMARK 500 ASP A 120 -129.02 51.05 REMARK 500 GLU A 144 61.29 37.32 REMARK 500 SER A 152 141.69 -175.60 REMARK 500 ASP A 158 80.68 -69.63 REMARK 500 LEU A 284 -117.39 -103.39 REMARK 500 ALA A 291 40.62 -141.92 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 320 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2PSD 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 2PSE A 3 311 UNP P27652 LUCI_RENRE 3 311 SEQADV 2PSE ALA A 2 UNP P27652 EXPRESSION TAG SEQADV 2PSE THR A 55 UNP P27652 ALA 55 ENGINEERED MUTATION SEQADV 2PSE ALA A 124 UNP P27652 CYS 124 ENGINEERED MUTATION SEQADV 2PSE ALA A 130 UNP P27652 SER 130 ENGINEERED MUTATION SEQADV 2PSE ARG A 136 UNP P27652 LYS 136 ENGINEERED MUTATION SEQADV 2PSE MET A 143 UNP P27652 ALA 143 ENGINEERED MUTATION SEQADV 2PSE VAL A 185 UNP P27652 MET 185 ENGINEERED MUTATION SEQADV 2PSE LEU A 253 UNP P27652 MET 253 ENGINEERED MUTATION SEQADV 2PSE LEU A 287 UNP P27652 SER 287 ENGINEERED MUTATION SEQADV 2PSE VAL A 312 UNP P27652 EXPRESSION TAG SEQADV 2PSE ASP A 313 UNP P27652 EXPRESSION TAG SEQADV 2PSE HIS A 314 UNP P27652 EXPRESSION TAG SEQADV 2PSE HIS A 315 UNP P27652 EXPRESSION TAG SEQADV 2PSE HIS A 316 UNP P27652 EXPRESSION TAG SEQADV 2PSE HIS A 317 UNP P27652 EXPRESSION TAG SEQADV 2PSE HIS A 318 UNP P27652 EXPRESSION TAG SEQADV 2PSE HIS A 319 UNP P27652 EXPRESSION 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 A 320 5 HETNAM IMD IMIDAZOLE FORMUL 2 IMD C3 H5 N2 1+ FORMUL 3 HOH *76(H2 O) HELIX 1 1 GLU A 9 MET A 14 1 6 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 GLU A 68 1 6 HELIX 5 5 PRO A 69 ALA A 71 5 3 HELIX 6 6 ARG A 93 GLU A 106 1 14 HELIX 7 7 ASP A 120 GLU A 132 1 13 HELIX 8 8 ILE A 159 SER A 168 1 10 HELIX 9 9 GLU A 170 LEU A 176 1 7 HELIX 10 10 ASN A 179 THR A 184 1 6 HELIX 11 11 THR A 184 LYS A 189 1 6 HELIX 12 12 GLU A 195 GLU A 204 1 10 HELIX 13 13 PRO A 205 LYS A 207 5 3 HELIX 14 14 GLY A 210 VAL A 212 5 3 HELIX 15 15 ARG A 213 GLU A 222 1 10 HELIX 16 16 LYS A 230 ALA A 246 1 17 HELIX 17 17 PHE A 262 LYS A 272 1 11 HELIX 18 18 PHE A 286 ASP A 290 5 5 HELIX 19 19 ALA A 291 LYS A 308 1 18 SHEET 1 A 2 ASN A 28 VAL A 29 0 SHEET 2 A 2 SER A 32 PHE A 33 -1 O SER A 32 N VAL A 29 SHEET 1 B 7 TYR A 36 ASP A 38 0 SHEET 2 B 7 ARG A 72 PRO A 76 -1 O ILE A 75 N TYR A 37 SHEET 3 B 7 ALA A 46 LEU A 50 1 N VAL A 47 O ARG A 72 SHEET 4 B 7 ILE A 114 HIS A 119 1 O VAL A 117 N LEU A 50 SHEET 5 B 7 ILE A 137 MET A 143 1 O LYS A 138 N ILE A 114 SHEET 6 B 7 LYS A 252 PRO A 259 1 O LEU A 253 N HIS A 142 SHEET 7 B 7 THR A 276 GLY A 283 1 O VAL A 279 N GLU A 256 CISPEP 1 ASP A 258 PRO A 259 0 7.10 SITE 1 AC1 2 ASP A 162 VAL A 185 CRYST1 119.443 119.443 48.048 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 0.008372 0.004834 0.000000 0.00000 SCALE2 0.000000 0.009667 0.000000 0.00000 SCALE3 0.000000 0.000000 0.020813 0.00000 (ATOM LINES ARE NOT SHOWN.) END
HEADER OXIDOREDUCTASE 06-MAY-07 2PSF TITLE CRYSTAL STRUCTURES OF THE LUCIFERASE AND GREEN FLUORESCENT PROTEIN TITLE 2 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_TAXID: 6136; SOURCE 4 GENE: RLUC; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: LMG194; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PBAD KEYWDS ALPHA/BETA-HYDROLASE, LUCIFERASE, OXIDOREDUCTASE EXPDTA X-RAY DIFFRACTION AUTHOR A.M.LOENING,T.D.FENN,S.S.GAMBHIR REVDAT 6 21-FEB-24 2PSF 1 REMARK REVDAT 5 20-OCT-21 2PSF 1 SEQADV REVDAT 4 13-JUL-11 2PSF 1 VERSN REVDAT 3 24-FEB-09 2PSF 1 VERSN REVDAT 2 27-NOV-07 2PSF 1 JRNL REVDAT 1 22-MAY-07 2PSF 0 JRNL AUTH A.M.LOENING,T.D.FENN,S.S.GAMBHIR JRNL TITL CRYSTAL STRUCTURES OF THE LUCIFERASE AND GREEN FLUORESCENT JRNL TITL 2 PROTEIN FROM RENILLA RENIFORMIS. JRNL REF J.MOL.BIOL. V. 374 1017 2007 JRNL REFN ISSN 0022-2836 JRNL PMID 17980388 JRNL DOI 10.1016/J.JMB.2007.09.078 REMARK 2 REMARK 2 RESOLUTION. 1.40 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2.0019 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN 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 (%) : 98.3 REMARK 3 NUMBER OF REFLECTIONS : 111557 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) : 0.174 REMARK 3 R VALUE (WORKING SET) : 0.173 REMARK 3 FREE R VALUE : 0.194 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 5879 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) : 1.40 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.44 REMARK 3 REFLECTION IN BIN (WORKING SET) : 7585 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.47 REMARK 3 BIN R VALUE (WORKING SET) : 0.2800 REMARK 3 BIN FREE R VALUE SET COUNT : 406 REMARK 3 BIN FREE R VALUE : 0.2890 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4983 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 790 REMARK 3 REMARK 3 B VALUES. REMARK 3 B VALUE TYPE : LIKELY RESIDUAL REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.56 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.06000 REMARK 3 B22 (A**2) : -0.28000 REMARK 3 B33 (A**2) : 0.22000 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): 0.063 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.063 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.040 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.980 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.957 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5127 ; 0.007 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 3578 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6942 ; 1.209 ; 1.951 REMARK 3 BOND ANGLES OTHERS (DEGREES): 8697 ; 0.882 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 606 ; 5.522 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 250 ;34.561 ;24.040 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 898 ;12.162 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;14.842 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 723 ; 0.078 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5645 ; 0.004 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1063 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1084 ; 0.213 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 3870 ; 0.193 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2515 ; 0.184 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): 2440 ; 0.083 ; 0.200 REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 552 ; 0.113 ; 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): 7 ; 0.126 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): 38 ; 0.186 ; 0.200 REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 48 ; 0.107 ; 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): 3949 ; 0.710 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1213 ; 0.121 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4928 ; 0.807 ; 2.000 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2514 ; 1.584 ; 3.000 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2014 ; 2.159 ; 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 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 2 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 3 A 309 REMARK 3 ORIGIN FOR THE GROUP (A): 38.7062 10.7135 10.6740 REMARK 3 T TENSOR REMARK 3 T11: -0.1185 T22: -0.1306 REMARK 3 T33: -0.1229 T12: 0.0066 REMARK 3 T13: 0.0076 T23: 0.0072 REMARK 3 L TENSOR REMARK 3 L11: 0.5407 L22: 0.9246 REMARK 3 L33: 1.2508 L12: -0.0927 REMARK 3 L13: 0.0429 L23: 0.1969 REMARK 3 S TENSOR REMARK 3 S11: 0.0211 S12: 0.0105 S13: 0.0475 REMARK 3 S21: 0.0113 S22: 0.0046 S23: -0.0319 REMARK 3 S31: -0.1100 S32: 0.0357 S33: -0.0258 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 : B 10 B 310 REMARK 3 ORIGIN FOR THE GROUP (A): 36.8687 -24.9450 -12.8322 REMARK 3 T TENSOR REMARK 3 T11: -0.1195 T22: -0.1257 REMARK 3 T33: -0.1093 T12: 0.0062 REMARK 3 T13: -0.0064 T23: -0.0044 REMARK 3 L TENSOR REMARK 3 L11: 0.8653 L22: 1.4255 REMARK 3 L33: 1.2525 L12: 0.2394 REMARK 3 L13: -0.0018 L23: -0.0027 REMARK 3 S TENSOR REMARK 3 S11: -0.0112 S12: -0.0082 S13: -0.1398 REMARK 3 S21: 0.0386 S22: 0.0439 S23: -0.0838 REMARK 3 S31: 0.1235 S32: 0.0184 S33: -0.0327 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 RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 2PSF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-MAY-07. REMARK 100 THE DEPOSITION ID IS D_1000042732. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 17-SEP-05 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.4 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 : 111557 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 <I/SIGMA(I)> 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 <I/SIGMA(I)> 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 (%): 41.38 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.4M SODIUM ACETATE, 20% W/V PEG 3350, REMARK 280 1.8MM N-DECYL-BETA-D-THIOMALTOSIDE, PH 7.4, VAPOR DIFFUSION, REMARK 280 HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 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 40.58900 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.18950 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.13950 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 45.18950 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 40.58900 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.13950 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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 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 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC 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 GLY A 2 REMARK 465 GLU A 310 REMARK 465 GLN A 311 REMARK 465 GLY B 2 REMARK 465 SER B 3 REMARK 465 LYS B 4 REMARK 465 VAL B 5 REMARK 465 TYR B 6 REMARK 465 ASP B 7 REMARK 465 PRO B 8 REMARK 465 GLU B 9 REMARK 465 GLN B 311 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 DISTANCE REMARK 500 NZ LYS B 193 O HOH B 667 1.99 REMARK 500 REMARK 500 REMARK: NULL 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 30 -123.97 50.63 REMARK 500 SER A 32 -151.57 -145.25 REMARK 500 GLU A 40 -51.20 70.84 REMARK 500 ALA A 54 -16.63 78.05 REMARK 500 THR A 55 -165.18 -115.35 REMARK 500 ASP A 120 -131.40 55.16 REMARK 500 PHE A 261 -75.86 -116.47 REMARK 500 LEU A 284 -98.92 -104.80 REMARK 500 ALA A 291 52.97 -147.97 REMARK 500 LEU B 30 -118.80 53.87 REMARK 500 SER B 32 -151.44 -150.69 REMARK 500 GLU B 40 -49.60 73.83 REMARK 500 ALA B 54 -18.32 79.03 REMARK 500 THR B 55 -164.36 -114.09 REMARK 500 ASP B 120 -132.61 57.86 REMARK 500 GLU B 144 55.18 37.69 REMARK 500 ASP B 158 -87.26 -48.65 REMARK 500 ILE B 159 10.07 39.73 REMARK 500 LEU B 284 -107.81 -107.99 REMARK 500 ALA B 291 51.38 -145.66 REMARK 500 REMARK 500 REMARK: NULL 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: 2PSH RELATED DB: PDB REMARK 900 RELATED ID: 2PSJ RELATED DB: PDB REMARK 900 RELATED ID: 2PSL RELATED DB: PDB DBREF 2PSF A 3 311 UNP P27652 LUCI_RENRE 3 311 DBREF 2PSF B 3 311 UNP P27652 LUCI_RENRE 3 311 SEQADV 2PSF GLY A 2 UNP P27652 EXPRESSION TAG SEQADV 2PSF THR A 55 UNP P27652 ALA 55 ENGINEERED MUTATION SEQADV 2PSF ALA A 124 UNP P27652 CYS 124 ENGINEERED MUTATION SEQADV 2PSF ALA A 130 UNP P27652 SER 130 ENGINEERED MUTATION SEQADV 2PSF ARG A 136 UNP P27652 LYS 136 ENGINEERED MUTATION SEQADV 2PSF MET A 143 UNP P27652 ALA 143 ENGINEERED MUTATION SEQADV 2PSF VAL A 185 UNP P27652 MET 185 ENGINEERED MUTATION SEQADV 2PSF LEU A 253 UNP P27652 MET 253 ENGINEERED MUTATION SEQADV 2PSF LEU A 287 UNP P27652 SER 287 ENGINEERED MUTATION SEQADV 2PSF GLY B 2 UNP P27652 EXPRESSION TAG SEQADV 2PSF THR B 55 UNP P27652 ALA 55 ENGINEERED MUTATION SEQADV 2PSF ALA B 124 UNP P27652 CYS 124 ENGINEERED MUTATION SEQADV 2PSF ALA B 130 UNP P27652 SER 130 ENGINEERED MUTATION SEQADV 2PSF ARG B 136 UNP P27652 LYS 136 ENGINEERED MUTATION SEQADV 2PSF MET B 143 UNP P27652 ALA 143 ENGINEERED MUTATION SEQADV 2PSF VAL B 185 UNP P27652 MET 185 ENGINEERED MUTATION SEQADV 2PSF LEU B 253 UNP P27652 MET 253 ENGINEERED MUTATION SEQADV 2PSF LEU B 287 UNP P27652 SER 287 ENGINEERED MUTATION SEQRES 1 A 310 GLY SER LYS VAL TYR ASP PRO GLU GLN ARG LYS ARG MET SEQRES 2 A 310 ILE THR GLY PRO GLN TRP TRP ALA ARG CYS LYS GLN MET SEQRES 3 A 310 ASN VAL LEU ASP SER PHE ILE ASN TYR TYR ASP SER GLU SEQRES 4 A 310 LYS HIS ALA GLU ASN ALA VAL ILE PHE LEU HIS GLY ASN SEQRES 5 A 310 ALA THR SER SER TYR LEU TRP ARG HIS VAL VAL PRO HIS SEQRES 6 A 310 ILE GLU PRO VAL ALA ARG CYS ILE ILE PRO ASP LEU ILE SEQRES 7 A 310 GLY MET GLY LYS SER GLY LYS SER GLY ASN GLY SER TYR SEQRES 8 A 310 ARG LEU LEU ASP HIS TYR LYS TYR LEU THR ALA TRP PHE SEQRES 9 A 310 GLU LEU LEU ASN LEU PRO LYS LYS ILE ILE PHE VAL GLY SEQRES 10 A 310 HIS ASP TRP GLY ALA ALA LEU ALA PHE HIS TYR ALA TYR SEQRES 11 A 310 GLU HIS GLN ASP ARG ILE LYS ALA ILE VAL HIS MET GLU SEQRES 12 A 310 SER VAL VAL ASP VAL ILE GLU SER TRP ASP GLU TRP PRO SEQRES 13 A 310 ASP ILE GLU GLU ASP ILE ALA LEU ILE LYS SER GLU GLU SEQRES 14 A 310 GLY GLU LYS MET VAL LEU GLU ASN ASN PHE PHE VAL GLU SEQRES 15 A 310 THR VAL LEU PRO SER LYS ILE MET ARG LYS LEU GLU PRO SEQRES 16 A 310 GLU GLU PHE ALA ALA TYR LEU GLU PRO PHE LYS GLU LYS SEQRES 17 A 310 GLY GLU VAL ARG ARG PRO THR LEU SER TRP PRO ARG GLU SEQRES 18 A 310 ILE PRO LEU VAL LYS GLY GLY LYS PRO ASP VAL VAL GLN SEQRES 19 A 310 ILE VAL ARG ASN TYR ASN ALA TYR LEU ARG ALA SER ASP SEQRES 20 A 310 ASP LEU PRO LYS LEU PHE ILE GLU SER ASP PRO GLY PHE SEQRES 21 A 310 PHE SER ASN ALA ILE VAL GLU GLY ALA LYS LYS PHE PRO SEQRES 22 A 310 ASN THR GLU PHE VAL LYS VAL LYS GLY LEU HIS PHE LEU SEQRES 23 A 310 GLN GLU ASP ALA PRO ASP GLU MET GLY LYS TYR ILE LYS SEQRES 24 A 310 SER PHE VAL GLU ARG VAL LEU LYS ASN GLU GLN SEQRES 1 B 310 GLY SER LYS VAL TYR ASP PRO GLU GLN ARG LYS ARG MET SEQRES 2 B 310 ILE THR GLY PRO GLN TRP TRP ALA ARG CYS LYS GLN MET SEQRES 3 B 310 ASN VAL LEU ASP SER PHE ILE ASN TYR TYR ASP SER GLU SEQRES 4 B 310 LYS HIS ALA GLU ASN ALA VAL ILE PHE LEU HIS GLY ASN SEQRES 5 B 310 ALA THR SER SER TYR LEU TRP ARG HIS VAL VAL PRO HIS SEQRES 6 B 310 ILE GLU PRO VAL ALA ARG CYS ILE ILE PRO ASP LEU ILE SEQRES 7 B 310 GLY MET GLY LYS SER GLY LYS SER GLY ASN GLY SER TYR SEQRES 8 B 310 ARG LEU LEU ASP HIS TYR LYS TYR LEU THR ALA TRP PHE SEQRES 9 B 310 GLU LEU LEU ASN LEU PRO LYS LYS ILE ILE PHE VAL GLY SEQRES 10 B 310 HIS ASP TRP GLY ALA ALA LEU ALA PHE HIS TYR ALA TYR SEQRES 11 B 310 GLU HIS GLN ASP ARG ILE LYS ALA ILE VAL HIS MET GLU SEQRES 12 B 310 SER VAL VAL ASP VAL ILE GLU SER TRP ASP GLU TRP PRO SEQRES 13 B 310 ASP ILE GLU GLU ASP ILE ALA LEU ILE LYS SER GLU GLU SEQRES 14 B 310 GLY GLU LYS MET VAL LEU GLU ASN ASN PHE PHE VAL GLU SEQRES 15 B 310 THR VAL LEU PRO SER LYS ILE MET ARG LYS LEU GLU PRO SEQRES 16 B 310 GLU GLU PHE ALA ALA TYR LEU GLU PRO PHE LYS GLU LYS SEQRES 17 B 310 GLY GLU VAL ARG ARG PRO THR LEU SER TRP PRO ARG GLU SEQRES 18 B 310 ILE PRO LEU VAL LYS GLY GLY LYS PRO ASP VAL VAL GLN SEQRES 19 B 310 ILE VAL ARG ASN TYR ASN ALA TYR LEU ARG ALA SER ASP SEQRES 20 B 310 ASP LEU PRO LYS LEU PHE ILE GLU SER ASP PRO GLY PHE SEQRES 21 B 310 PHE SER ASN ALA ILE VAL GLU GLY ALA LYS LYS PHE PRO SEQRES 22 B 310 ASN THR GLU PHE VAL LYS VAL LYS GLY LEU HIS PHE LEU SEQRES 23 B 310 GLN GLU ASP ALA PRO ASP GLU MET GLY LYS TYR ILE LYS SEQRES 24 B 310 SER PHE VAL GLU ARG VAL LEU LYS ASN GLU GLN FORMUL 3 HOH *790(H2 O) HELIX 1 1 PRO A 8 ARG A 13 1 6 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 ASP A 120 HIS A 133 1 14 HELIX 7 7 ASP A 158 SER A 168 1 11 HELIX 8 8 SER A 168 GLU A 177 1 10 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 ASN A 309 1 19 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 ILE B 159 SER B 168 1 10 HELIX 25 25 GLU B 169 GLU B 177 1 9 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 PHE B 262 LYS B 271 1 10 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 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 ILE A 115 N ILE A 48 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 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 HIS B 119 1 O ILE B 115 N ILE B 48 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 5.59 CISPEP 2 ASP B 258 PRO B 259 0 5.02 CRYST1 81.178 82.279 90.379 90.00 90.00 90.00 P 21 21 21 8 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 0.012319 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012154 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011065 0.00000 (ATOM LINES ARE NOT SHOWN.) END
HEADER OXIDOREDUCTASE 06-MAY-07 2PSH TITLE CRYSTAL STRUCTURES OF THE LUCIFERASE AND GREEN FLUORESCENT PROTEIN TITLE 2 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_TAXID: 6136; SOURCE 4 GENE: RLUC; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: LMG194; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PBAD KEYWDS ALPHA/BETA-HYDROLASE, LUCIFERASE, OXIDOREDUCTASE EXPDTA X-RAY DIFFRACTION AUTHOR A.M.LOENING,T.D.FENN,S.S.GAMBHIR REVDAT 5 21-FEB-24 2PSH 1 REMARK REVDAT 4 20-OCT-21 2PSH 1 SEQADV REVDAT 3 24-FEB-09 2PSH 1 VERSN REVDAT 2 27-NOV-07 2PSH 1 JRNL 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 FLUORESCENT JRNL TITL 2 PROTEIN FROM RENILLA RENIFORMIS. JRNL REF J.MOL.BIOL. V. 374 1017 2007 JRNL REFN ISSN 0022-2836 JRNL PMID 17980388 JRNL DOI 10.1016/J.JMB.2007.09.078 REMARK 2 REMARK 2 RESOLUTION. 1.79 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2.0019 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN 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 (%) : 97.6 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 (A) : 1.79 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 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 PROTEIN ATOMS : 4860 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 476 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 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2434 ; 1.395 ; 3.000 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1934 ; 1.994 ; 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 : 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 : NULL 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 RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 2PSH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-MAY-07. REMARK 100 THE DEPOSITION ID IS D_1000042733. 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 REMARK 200 PH : 7.5 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 <I/SIGMA(I)> 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 <I/SIGMA(I)> 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 WITH REMARK 280 6MG/ML BENZYL-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,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 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 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 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 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC 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 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 PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ARG A 192 NE - CZ - NH1 ANGL. DEV. = 5.1 DEGREES REMARK 500 ARG A 192 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES REMARK 500 REMARK 500 REMARK: NULL 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 30 -123.32 51.12 REMARK 500 SER A 32 -150.78 -141.02 REMARK 500 GLU A 40 -50.80 69.14 REMARK 500 ALA A 54 -17.50 78.42 REMARK 500 THR A 55 -164.88 -115.08 REMARK 500 ASP A 120 -134.12 58.50 REMARK 500 HIS A 133 58.35 -142.05 REMARK 500 LEU A 284 -91.29 -100.09 REMARK 500 ALA A 291 50.42 -140.69 REMARK 500 LEU B 30 -125.36 52.62 REMARK 500 SER B 32 -151.16 -153.28 REMARK 500 GLU B 40 -56.04 72.28 REMARK 500 ALA B 54 -11.34 74.72 REMARK 500 THR B 55 -165.30 -113.41 REMARK 500 ASP B 120 -132.57 58.73 REMARK 500 HIS B 133 59.29 -142.36 REMARK 500 GLU B 151 2.89 109.88 REMARK 500 ASN B 179 68.19 3.57 REMARK 500 LEU B 284 -92.64 -98.63 REMARK 500 ALA B 291 53.42 -141.87 REMARK 500 REMARK 500 REMARK: NULL 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 MUTATION SEQADV 2PSH ALA A 25 UNP P27652 LYS 25 ENGINEERED MUTATION SEQADV 2PSH THR A 55 UNP P27652 ALA 55 ENGINEERED MUTATION SEQADV 2PSH ALA A 124 UNP P27652 CYS 124 ENGINEERED MUTATION SEQADV 2PSH ALA A 130 UNP P27652 SER 130 ENGINEERED MUTATION SEQADV 2PSH ARG A 136 UNP P27652 LYS 136 ENGINEERED MUTATION SEQADV 2PSH MET A 143 UNP P27652 ALA 143 ENGINEERED MUTATION SEQADV 2PSH VAL A 185 UNP P27652 MET 185 ENGINEERED MUTATION SEQADV 2PSH LEU A 253 UNP P27652 MET 253 ENGINEERED MUTATION SEQADV 2PSH ALA A 277 UNP P27652 GLU 277 ENGINEERED MUTATION SEQADV 2PSH LEU A 287 UNP P27652 SER 287 ENGINEERED MUTATION SEQADV 2PSH VAL A 312 UNP P27652 EXPRESSION TAG SEQADV 2PSH ASP A 313 UNP P27652 EXPRESSION TAG SEQADV 2PSH HIS A 314 UNP P27652 EXPRESSION TAG SEQADV 2PSH HIS A 315 UNP P27652 EXPRESSION TAG SEQADV 2PSH HIS A 316 UNP P27652 EXPRESSION TAG SEQADV 2PSH HIS A 317 UNP P27652 EXPRESSION TAG SEQADV 2PSH HIS A 318 UNP P27652 EXPRESSION TAG SEQADV 2PSH HIS A 319 UNP P27652 EXPRESSION TAG SEQADV 2PSH ALA B 2 UNP P27652 THR 2 ENGINEERED MUTATION SEQADV 2PSH ALA B 25 UNP P27652 LYS 25 ENGINEERED MUTATION SEQADV 2PSH THR B 55 UNP P27652 ALA 55 ENGINEERED MUTATION SEQADV 2PSH ALA B 124 UNP P27652 CYS 124 ENGINEERED MUTATION SEQADV 2PSH ALA B 130 UNP P27652 SER 130 ENGINEERED MUTATION SEQADV 2PSH ARG B 136 UNP P27652 LYS 136 ENGINEERED MUTATION SEQADV 2PSH MET B 143 UNP P27652 ALA 143 ENGINEERED MUTATION SEQADV 2PSH VAL B 185 UNP P27652 MET 185 ENGINEERED MUTATION SEQADV 2PSH LEU B 253 UNP P27652 MET 253 ENGINEERED MUTATION SEQADV 2PSH ALA B 277 UNP P27652 GLU 277 ENGINEERED MUTATION SEQADV 2PSH LEU B 287 UNP P27652 SER 287 ENGINEERED MUTATION SEQADV 2PSH VAL B 312 UNP P27652 EXPRESSION TAG SEQADV 2PSH ASP B 313 UNP P27652 EXPRESSION TAG SEQADV 2PSH HIS B 314 UNP P27652 EXPRESSION TAG SEQADV 2PSH HIS B 315 UNP P27652 EXPRESSION TAG SEQADV 2PSH HIS B 316 UNP P27652 EXPRESSION TAG SEQADV 2PSH HIS B 317 UNP P27652 EXPRESSION TAG SEQADV 2PSH HIS B 318 UNP P27652 EXPRESSION TAG SEQADV 2PSH HIS B 319 UNP P27652 EXPRESSION 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 (ATOM LINES ARE NOT SHOWN.) END
HEADER OXIDOREDUCTASE 06-MAY-07 2PSJ TITLE CRYSTAL STRUCTURES OF THE LUCIFERASE AND GREEN FLUORESCENT PROTEIN TITLE 2 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_TAXID: 6136; SOURCE 4 GENE: RLUC; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: LMG194; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PBAD KEYWDS ALPHA/BETA-HYDROLASE, LUCIFERASE, OXIDOREDUCTASE EXPDTA X-RAY DIFFRACTION AUTHOR A.M.LOENING,T.D.FENN,S.S.GAMBHIR REVDAT 6 21-FEB-24 2PSJ 1 REMARK REVDAT 5 20-OCT-21 2PSJ 1 REMARK SEQADV REVDAT 4 13-JUL-11 2PSJ 1 VERSN REVDAT 3 24-FEB-09 2PSJ 1 VERSN REVDAT 2 27-NOV-07 2PSJ 1 JRNL 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 FLUORESCENT JRNL TITL 2 PROTEIN FROM RENILLA RENIFORMIS. JRNL REF J.MOL.BIOL. V. 374 1017 2007 JRNL REFN ISSN 0022-2836 JRNL PMID 17980388 JRNL DOI 10.1016/J.JMB.2007.09.078 REMARK 2 REMARK 2 RESOLUTION. 1.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2.0019 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN 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 (A) : 1.80 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 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 PROTEIN ATOMS : 5006 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 62 REMARK 3 SOLVENT ATOMS : 453 REMARK 3 REMARK 3 B VALUES. REMARK 3 B VALUE TYPE : LIKELY RESIDUAL 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 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2621 ; 1.331 ; 3.000 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2096 ; 1.928 ; 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 : 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 : A 501 A 501 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 : B 502 B 502 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 RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 2PSJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-MAY-07. REMARK 100 THE DEPOSITION ID IS D_1000042734. 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 REMARK 200 PH : 7.5 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 <I/SIGMA(I)> 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 <I/SIGMA(I)> 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 WITH REMARK 280 6MG/ML COELENTERAZINE, 15% W/V PEG 3350, PH 7.5, VAPOR DIFFUSION, REMARK 280 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,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 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 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 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 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC 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 DISTANCE REMARK 500 OD2 ASP A 135 O HOH A 669 2.16 REMARK 500 O HOH A 669 O HOH B 574 2.17 REMARK 500 REMARK 500 REMARK: NULL 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 30 -125.68 54.23 REMARK 500 SER A 32 -149.30 -142.62 REMARK 500 GLU A 40 -50.45 71.76 REMARK 500 ALA A 54 -10.85 75.39 REMARK 500 THR A 55 -165.38 -116.30 REMARK 500 ASP A 120 -133.34 59.07 REMARK 500 LEU A 284 -88.40 -102.81 REMARK 500 ALA A 291 51.65 -144.56 REMARK 500 ASN A 309 -50.25 72.29 REMARK 500 LEU B 30 -118.07 52.27 REMARK 500 SER B 32 -147.25 -139.30 REMARK 500 GLU B 40 -52.51 68.66 REMARK 500 ALA B 54 -11.23 75.49 REMARK 500 THR B 55 -164.63 -116.83 REMARK 500 ASP B 120 -133.10 59.24 REMARK 500 ASP B 158 34.68 -96.32 REMARK 500 LEU B 284 -90.91 -104.93 REMARK 500 ALA B 291 53.25 -143.83 REMARK 500 ASN B 309 -50.42 71.58 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CEI A 501 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CEI B 502 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 MUTATION SEQADV 2PSJ THR A 55 UNP P27652 ALA 55 ENGINEERED MUTATION SEQADV 2PSJ ALA A 124 UNP P27652 CYS 124 ENGINEERED MUTATION SEQADV 2PSJ ALA A 130 UNP P27652 SER 130 ENGINEERED MUTATION SEQADV 2PSJ ARG A 136 UNP P27652 LYS 136 ENGINEERED MUTATION SEQADV 2PSJ MET A 143 UNP P27652 ALA 143 ENGINEERED MUTATION SEQADV 2PSJ VAL A 185 UNP P27652 MET 185 ENGINEERED MUTATION SEQADV 2PSJ LEU A 253 UNP P27652 MET 253 ENGINEERED MUTATION SEQADV 2PSJ LEU A 287 UNP P27652 SER 287 ENGINEERED MUTATION SEQADV 2PSJ VAL A 312 UNP P27652 EXPRESSION TAG SEQADV 2PSJ ASP A 313 UNP P27652 EXPRESSION TAG SEQADV 2PSJ HIS A 314 UNP P27652 EXPRESSION TAG SEQADV 2PSJ HIS A 315 UNP P27652 EXPRESSION TAG SEQADV 2PSJ HIS A 316 UNP P27652 EXPRESSION TAG SEQADV 2PSJ HIS A 317 UNP P27652 EXPRESSION TAG SEQADV 2PSJ HIS A 318 UNP P27652 EXPRESSION TAG SEQADV 2PSJ HIS A 319 UNP P27652 EXPRESSION TAG SEQADV 2PSJ ALA B 2 UNP P27652 THR 2 ENGINEERED MUTATION SEQADV 2PSJ THR B 55 UNP P27652 ALA 55 ENGINEERED MUTATION SEQADV 2PSJ ALA B 124 UNP P27652 CYS 124 ENGINEERED MUTATION SEQADV 2PSJ ALA B 130 UNP P27652 SER 130 ENGINEERED MUTATION SEQADV 2PSJ ARG B 136 UNP P27652 LYS 136 ENGINEERED MUTATION SEQADV 2PSJ MET B 143 UNP P27652 ALA 143 ENGINEERED MUTATION SEQADV 2PSJ VAL B 185 UNP P27652 MET 185 ENGINEERED MUTATION SEQADV 2PSJ LEU B 253 UNP P27652 MET 253 ENGINEERED MUTATION SEQADV 2PSJ LEU B 287 UNP P27652 SER 287 ENGINEERED MUTATION SEQADV 2PSJ VAL B 312 UNP P27652 EXPRESSION TAG SEQADV 2PSJ ASP B 313 UNP P27652 EXPRESSION TAG SEQADV 2PSJ HIS B 314 UNP P27652 EXPRESSION TAG SEQADV 2PSJ HIS B 315 UNP P27652 EXPRESSION TAG SEQADV 2PSJ HIS B 316 UNP P27652 EXPRESSION TAG SEQADV 2PSJ HIS B 317 UNP P27652 EXPRESSION TAG SEQADV 2PSJ HIS B 318 UNP P27652 EXPRESSION TAG SEQADV 2PSJ HIS B 319 UNP P27652 EXPRESSION 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 A 501 31 HET CEI B 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 SITE 1 AC1 6 TRP A 156 ASP A 162 MET A 174 PHE A 180 SITE 2 AC1 6 HIS A 285 HOH A 655 SITE 1 AC2 8 TRP B 156 ASP B 162 MET B 174 PHE B 180 SITE 2 AC2 8 PHE B 261 HIS B 285 HOH B 680 HOH B 698 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 (ATOM LINES ARE NOT SHOWN.) END
HEADER FLUORESCENT PROTEIN 06-OCT-07 2RH7 TITLE CRYSTAL STRUCTURES OF THE LUCIFERASE AND GREEN FLUORESCENT PROTEIN TITLE 2 FROM RENILLA RENIFORMIS COMPND MOL_ID: 1; COMPND 2 MOLECULE: GREEN FLUORESCENT PROTEIN; COMPND 3 CHAIN: A, B, C, D; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RENILLA RENIFORMIS; SOURCE 3 ORGANISM_TAXID: 6136; SOURCE 4 GENE: GFP; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: LMG194; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PBAD KEYWDS FLUORESCENT PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR A.M.LOENING,T.D.FENN,S.S.GAMBHIR REVDAT 5 15-NOV-23 2RH7 1 REMARK REVDAT 4 30-AUG-23 2RH7 1 SEQADV REVDAT 3 24-FEB-09 2RH7 1 VERSN REVDAT 2 27-NOV-07 2RH7 1 JRNL REVDAT 1 23-OCT-07 2RH7 0 SPRSDE 23-OCT-07 2RH7 2PSL JRNL AUTH A.M.LOENING,T.D.FENN,S.S.GAMBHIR JRNL TITL CRYSTAL STRUCTURES OF THE LUCIFERASE AND GREEN FLUORESCENT JRNL TITL 2 PROTEIN FROM RENILLA RENIFORMIS. JRNL REF J.MOL.BIOL. V. 374 1017 2007 JRNL REFN ISSN 0022-2836 JRNL PMID 17980388 JRNL DOI 10.1016/J.JMB.2007.09.078 REMARK 2 REMARK 2 RESOLUTION. 1.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 76.8 REMARK 3 NUMBER OF REFLECTIONS : 123752 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.291 REMARK 3 FREE R VALUE : 0.325 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 6229 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6776 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 537 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL 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): NULL REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA REMARK 3 BOND LENGTH (A) : NULL ; NULL REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL REMARK 3 REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL REMARK 3 REMARK 3 NON-BONDED CONTACT RESTRAINTS. REMARK 3 SINGLE TORSION (A) : NULL ; NULL REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL REMARK 3 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS. REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL REMARK 3 PLANAR (DEGREES) : NULL ; NULL REMARK 3 STAGGERED (DEGREES) : NULL ; NULL REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2RH7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-OCT-07. REMARK 100 THE DEPOSITION ID IS D_1000044855. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 17-SEP-05 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.0 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 : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 123752 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500 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 <I/SIGMA(I)> 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 <I/SIGMA(I)> 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: HYBRID OF PDB ENTRIES 1MOV, 1MOU, 1XSS AND 1GGX REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 46.63 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0M AMMONIUM SULFATE, 5% V/V REMARK 280 ISOPROPANOL, PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE REMARK 280 293K 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 36.87200 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.70250 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.87200 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.70250 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3900 ANGSTROM**2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3820 ANGSTROM**2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D 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 ASP A 2 REMARK 465 LEU A 3 REMARK 465 ALA A 4 REMARK 465 LYS A 5 REMARK 465 LEU A 6 REMARK 465 ASP A 115 REMARK 465 ASP A 206 REMARK 465 THR A 207 REMARK 465 ALA A 208 REMARK 465 SER A 209 REMARK 465 GLY A 210 REMARK 465 LYS A 227 REMARK 465 ILE A 228 REMARK 465 GLU A 229 REMARK 465 GLY A 230 REMARK 465 SER A 231 REMARK 465 LEU A 232 REMARK 465 PRO A 233 REMARK 465 VAL A 234 REMARK 465 ASP A 235 REMARK 465 HIS A 236 REMARK 465 HIS A 237 REMARK 465 HIS A 238 REMARK 465 HIS A 239 REMARK 465 HIS A 240 REMARK 465 HIS A 241 REMARK 465 MET B 1 REMARK 465 ASP B 2 REMARK 465 LEU B 3 REMARK 465 ALA B 4 REMARK 465 LYS B 5 REMARK 465 LEU B 6 REMARK 465 ASP B 206 REMARK 465 THR B 207 REMARK 465 ALA B 208 REMARK 465 SER B 209 REMARK 465 GLY B 210 REMARK 465 LYS B 227 REMARK 465 ILE B 228 REMARK 465 GLU B 229 REMARK 465 GLY B 230 REMARK 465 SER B 231 REMARK 465 LEU B 232 REMARK 465 PRO B 233 REMARK 465 VAL B 234 REMARK 465 ASP B 235 REMARK 465 HIS B 236 REMARK 465 HIS B 237 REMARK 465 HIS B 238 REMARK 465 HIS B 239 REMARK 465 HIS B 240 REMARK 465 HIS B 241 REMARK 465 MET C 1 REMARK 465 ASP C 2 REMARK 465 LEU C 3 REMARK 465 ALA C 4 REMARK 465 LYS C 5 REMARK 465 LEU C 6 REMARK 465 ASP C 115 REMARK 465 ASP C 206 REMARK 465 THR C 207 REMARK 465 ALA C 208 REMARK 465 SER C 209 REMARK 465 GLY C 210 REMARK 465 LYS C 227 REMARK 465 ILE C 228 REMARK 465 GLU C 229 REMARK 465 GLY C 230 REMARK 465 SER C 231 REMARK 465 LEU C 232 REMARK 465 PRO C 233 REMARK 465 VAL C 234 REMARK 465 ASP C 235 REMARK 465 HIS C 236 REMARK 465 HIS C 237 REMARK 465 HIS C 238 REMARK 465 HIS C 239 REMARK 465 HIS C 240 REMARK 465 HIS C 241 REMARK 465 MET D 1 REMARK 465 ASP D 2 REMARK 465 LEU D 3 REMARK 465 ALA D 4 REMARK 465 LYS D 5 REMARK 465 LEU D 6 REMARK 465 ASP D 115 REMARK 465 ASP D 206 REMARK 465 THR D 207 REMARK 465 ALA D 208 REMARK 465 SER D 209 REMARK 465 GLY D 210 REMARK 465 LYS D 227 REMARK 465 ILE D 228 REMARK 465 GLU D 229 REMARK 465 GLY D 230 REMARK 465 SER D 231 REMARK 465 LEU D 232 REMARK 465 PRO D 233 REMARK 465 VAL D 234 REMARK 465 ASP D 235 REMARK 465 HIS D 236 REMARK 465 HIS D 237 REMARK 465 HIS D 238 REMARK 465 HIS D 239 REMARK 465 HIS D 240 REMARK 465 HIS D 241 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 CRO A 66 CG1 REMARK 470 CRO B 66 CG1 REMARK 470 CRO C 66 CG1 REMARK 470 CRO D 66 CG1 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 DISTANCE REMARK 500 O HOH C 328 O HOH C 329 2.06 REMARK 500 O SER D 62 N1 CRO D 66 2.08 REMARK 500 REMARK 500 REMARK: NULL 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 PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 TYR A 211 N - CA - C ANGL. DEV. = -19.1 DEGREES REMARK 500 TYR B 211 N - CA - C ANGL. DEV. = -17.4 DEGREES REMARK 500 TYR C 211 N - CA - C ANGL. DEV. = -22.2 DEGREES REMARK 500 REMARK 500 REMARK: NULL 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 VAL A 154 -105.20 61.02 REMARK 500 GLU A 188 -79.03 -51.25 REMARK 500 LYS B 50 135.52 -175.63 REMARK 500 ASP B 115 -142.25 62.82 REMARK 500 VAL B 154 -119.98 65.87 REMARK 500 ASN B 204 125.27 176.22 REMARK 500 ASP C 128 30.61 72.43 REMARK 500 VAL C 154 -103.42 58.58 REMARK 500 LYS C 184 37.50 -90.72 REMARK 500 LYS C 185 142.37 -176.52 REMARK 500 ARG D 70 4.00 -66.92 REMARK 500 GLU D 114 1.44 -153.31 REMARK 500 VAL D 154 -110.77 58.13 REMARK 500 CYS D 161 148.82 -174.38 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 TYR A 211 VAL A 212 -140.34 REMARK 500 TYR B 211 VAL B 212 -138.10 REMARK 500 TYR C 211 VAL C 212 -145.02 REMARK 500 TYR D 211 VAL D 212 -145.72 REMARK 500 REMARK 500 REMARK: NULL DBREF 2RH7 A 1 233 UNP Q963I9 Q963I9_RENRE 1 233 DBREF 2RH7 B 1 233 UNP Q963I9 Q963I9_RENRE 1 233 DBREF 2RH7 C 1 233 UNP Q963I9 Q963I9_RENRE 1 233 DBREF 2RH7 D 1 233 UNP Q963I9 Q963I9_RENRE 1 233 SEQADV 2RH7 CRO A 66 UNP Q963I9 SER 66 CHROMOPHORE SEQADV 2RH7 CRO A 66 UNP Q963I9 TYR 67 CHROMOPHORE SEQADV 2RH7 CRO A 66 UNP Q963I9 GLY 68 CHROMOPHORE SEQADV 2RH7 VAL A 234 UNP Q963I9 EXPRESSION TAG SEQADV 2RH7 ASP A 235 UNP Q963I9 EXPRESSION TAG SEQADV 2RH7 HIS A 236 UNP Q963I9 EXPRESSION TAG SEQADV 2RH7 HIS A 237 UNP Q963I9 EXPRESSION TAG SEQADV 2RH7 HIS A 238 UNP Q963I9 EXPRESSION TAG SEQADV 2RH7 HIS A 239 UNP Q963I9 EXPRESSION TAG SEQADV 2RH7 HIS A 240 UNP Q963I9 EXPRESSION TAG SEQADV 2RH7 HIS A 241 UNP Q963I9 EXPRESSION TAG SEQADV 2RH7 CRO B 66 UNP Q963I9 SER 66 CHROMOPHORE SEQADV 2RH7 CRO B 66 UNP Q963I9 TYR 67 CHROMOPHORE SEQADV 2RH7 CRO B 66 UNP Q963I9 GLY 68 CHROMOPHORE SEQADV 2RH7 VAL B 234 UNP Q963I9 EXPRESSION TAG SEQADV 2RH7 ASP B 235 UNP Q963I9 EXPRESSION TAG SEQADV 2RH7 HIS B 236 UNP Q963I9 EXPRESSION TAG SEQADV 2RH7 HIS B 237 UNP Q963I9 EXPRESSION TAG SEQADV 2RH7 HIS B 238 UNP Q963I9 EXPRESSION TAG SEQADV 2RH7 HIS B 239 UNP Q963I9 EXPRESSION TAG SEQADV 2RH7 HIS B 240 UNP Q963I9 EXPRESSION TAG SEQADV 2RH7 HIS B 241 UNP Q963I9 EXPRESSION TAG SEQADV 2RH7 CRO C 66 UNP Q963I9 SER 66 CHROMOPHORE SEQADV 2RH7 CRO C 66 UNP Q963I9 TYR 67 CHROMOPHORE SEQADV 2RH7 CRO C 66 UNP Q963I9 GLY 68 CHROMOPHORE SEQADV 2RH7 VAL C 234 UNP Q963I9 EXPRESSION TAG SEQADV 2RH7 ASP C 235 UNP Q963I9 EXPRESSION TAG SEQADV 2RH7 HIS C 236 UNP Q963I9 EXPRESSION TAG SEQADV 2RH7 HIS C 237 UNP Q963I9 EXPRESSION TAG SEQADV 2RH7 HIS C 238 UNP Q963I9 EXPRESSION TAG SEQADV 2RH7 HIS C 239 UNP Q963I9 EXPRESSION TAG SEQADV 2RH7 HIS C 240 UNP Q963I9 EXPRESSION TAG SEQADV 2RH7 HIS C 241 UNP Q963I9 EXPRESSION TAG SEQADV 2RH7 CRO D 66 UNP Q963I9 SER 66 CHROMOPHORE SEQADV 2RH7 CRO D 66 UNP Q963I9 TYR 67 CHROMOPHORE SEQADV 2RH7 CRO D 66 UNP Q963I9 GLY 68 CHROMOPHORE SEQADV 2RH7 VAL D 234 UNP Q963I9 EXPRESSION TAG SEQADV 2RH7 ASP D 235 UNP Q963I9 EXPRESSION TAG SEQADV 2RH7 HIS D 236 UNP Q963I9 EXPRESSION TAG SEQADV 2RH7 HIS D 237 UNP Q963I9 EXPRESSION TAG SEQADV 2RH7 HIS D 238 UNP Q963I9 EXPRESSION TAG SEQADV 2RH7 HIS D 239 UNP Q963I9 EXPRESSION TAG SEQADV 2RH7 HIS D 240 UNP Q963I9 EXPRESSION TAG SEQADV 2RH7 HIS D 241 UNP Q963I9 EXPRESSION TAG SEQRES 1 A 239 MET ASP LEU ALA LYS LEU GLY LEU LYS GLU VAL MET PRO SEQRES 2 A 239 THR LYS ILE ASN LEU GLU GLY LEU VAL GLY ASP HIS ALA SEQRES 3 A 239 PHE SER MET GLU GLY VAL GLY GLU GLY ASN ILE LEU GLU SEQRES 4 A 239 GLY THR GLN GLU VAL LYS ILE SER VAL THR LYS GLY ALA SEQRES 5 A 239 PRO LEU PRO PHE ALA PHE ASP ILE VAL SER VAL ALA PHE SEQRES 6 A 239 CRO ASN ARG ALA TYR THR GLY TYR PRO GLU GLU ILE SER SEQRES 7 A 239 ASP TYR PHE LEU GLN SER PHE PRO GLU GLY PHE THR TYR SEQRES 8 A 239 GLU ARG ASN ILE ARG TYR GLN ASP GLY GLY THR ALA ILE SEQRES 9 A 239 VAL LYS SER ASP ILE SER LEU GLU ASP GLY LYS PHE ILE SEQRES 10 A 239 VAL ASN VAL ASP PHE LYS ALA LYS ASP LEU ARG ARG MET SEQRES 11 A 239 GLY PRO VAL MET GLN GLN ASP ILE VAL GLY MET GLN PRO SEQRES 12 A 239 SER TYR GLU SER MET TYR THR ASN VAL THR SER VAL ILE SEQRES 13 A 239 GLY GLU CYS ILE ILE ALA PHE LYS LEU GLN THR GLY LYS SEQRES 14 A 239 HIS PHE THR TYR HIS MET ARG THR VAL TYR LYS SER LYS SEQRES 15 A 239 LYS PRO VAL GLU THR MET PRO LEU TYR HIS PHE ILE GLN SEQRES 16 A 239 HIS ARG LEU VAL LYS THR ASN VAL ASP THR ALA SER GLY SEQRES 17 A 239 TYR VAL VAL GLN HIS GLU THR ALA ILE ALA ALA HIS SER SEQRES 18 A 239 THR ILE LYS LYS ILE GLU GLY SER LEU PRO VAL ASP HIS SEQRES 19 A 239 HIS HIS HIS HIS HIS SEQRES 1 B 239 MET ASP LEU ALA LYS LEU GLY LEU LYS GLU VAL MET PRO SEQRES 2 B 239 THR LYS ILE ASN LEU GLU GLY LEU VAL GLY ASP HIS ALA SEQRES 3 B 239 PHE SER MET GLU GLY VAL GLY GLU GLY ASN ILE LEU GLU SEQRES 4 B 239 GLY THR GLN GLU VAL LYS ILE SER VAL THR LYS GLY ALA SEQRES 5 B 239 PRO LEU PRO PHE ALA PHE ASP ILE VAL SER VAL ALA PHE SEQRES 6 B 239 CRO ASN ARG ALA TYR THR GLY TYR PRO GLU GLU ILE SER SEQRES 7 B 239 ASP TYR PHE LEU GLN SER PHE PRO GLU GLY PHE THR TYR SEQRES 8 B 239 GLU ARG ASN ILE ARG TYR GLN ASP GLY GLY THR ALA ILE SEQRES 9 B 239 VAL LYS SER ASP ILE SER LEU GLU ASP GLY LYS PHE ILE SEQRES 10 B 239 VAL ASN VAL ASP PHE LYS ALA LYS ASP LEU ARG ARG MET SEQRES 11 B 239 GLY PRO VAL MET GLN GLN ASP ILE VAL GLY MET GLN PRO SEQRES 12 B 239 SER TYR GLU SER MET TYR THR ASN VAL THR SER VAL ILE SEQRES 13 B 239 GLY GLU CYS ILE ILE ALA PHE LYS LEU GLN THR GLY LYS SEQRES 14 B 239 HIS PHE THR TYR HIS MET ARG THR VAL TYR LYS SER LYS SEQRES 15 B 239 LYS PRO VAL GLU THR MET PRO LEU TYR HIS PHE ILE GLN SEQRES 16 B 239 HIS ARG LEU VAL LYS THR ASN VAL ASP THR ALA SER GLY SEQRES 17 B 239 TYR VAL VAL GLN HIS GLU THR ALA ILE ALA ALA HIS SER SEQRES 18 B 239 THR ILE LYS LYS ILE GLU GLY SER LEU PRO VAL ASP HIS SEQRES 19 B 239 HIS HIS HIS HIS HIS SEQRES 1 C 239 MET ASP LEU ALA LYS LEU GLY LEU LYS GLU VAL MET PRO SEQRES 2 C 239 THR LYS ILE ASN LEU GLU GLY LEU VAL GLY ASP HIS ALA SEQRES 3 C 239 PHE SER MET GLU GLY VAL GLY GLU GLY ASN ILE LEU GLU SEQRES 4 C 239 GLY THR GLN GLU VAL LYS ILE SER VAL THR LYS GLY ALA SEQRES 5 C 239 PRO LEU PRO PHE ALA PHE ASP ILE VAL SER VAL ALA PHE SEQRES 6 C 239 CRO ASN ARG ALA TYR THR GLY TYR PRO GLU GLU ILE SER SEQRES 7 C 239 ASP TYR PHE LEU GLN SER PHE PRO GLU GLY PHE THR TYR SEQRES 8 C 239 GLU ARG ASN ILE ARG TYR GLN ASP GLY GLY THR ALA ILE SEQRES 9 C 239 VAL LYS SER ASP ILE SER LEU GLU ASP GLY LYS PHE ILE SEQRES 10 C 239 VAL ASN VAL ASP PHE LYS ALA LYS ASP LEU ARG ARG MET SEQRES 11 C 239 GLY PRO VAL MET GLN GLN ASP ILE VAL GLY MET GLN PRO SEQRES 12 C 239 SER TYR GLU SER MET TYR THR ASN VAL THR SER VAL ILE SEQRES 13 C 239 GLY GLU CYS ILE ILE ALA PHE LYS LEU GLN THR GLY LYS SEQRES 14 C 239 HIS PHE THR TYR HIS MET ARG THR VAL TYR LYS SER LYS SEQRES 15 C 239 LYS PRO VAL GLU THR MET PRO LEU TYR HIS PHE ILE GLN SEQRES 16 C 239 HIS ARG LEU VAL LYS THR ASN VAL ASP THR ALA SER GLY SEQRES 17 C 239 TYR VAL VAL GLN HIS GLU THR ALA ILE ALA ALA HIS SER SEQRES 18 C 239 THR ILE LYS LYS ILE GLU GLY SER LEU PRO VAL ASP HIS SEQRES 19 C 239 HIS HIS HIS HIS HIS SEQRES 1 D 239 MET ASP LEU ALA LYS LEU GLY LEU LYS GLU VAL MET PRO SEQRES 2 D 239 THR LYS ILE ASN LEU GLU GLY LEU VAL GLY ASP HIS ALA SEQRES 3 D 239 PHE SER MET GLU GLY VAL GLY GLU GLY ASN ILE LEU GLU SEQRES 4 D 239 GLY THR GLN GLU VAL LYS ILE SER VAL THR LYS GLY ALA SEQRES 5 D 239 PRO LEU PRO PHE ALA PHE ASP ILE VAL SER VAL ALA PHE SEQRES 6 D 239 CRO ASN ARG ALA TYR THR GLY TYR PRO GLU GLU ILE SER SEQRES 7 D 239 ASP TYR PHE LEU GLN SER PHE PRO GLU GLY PHE THR TYR SEQRES 8 D 239 GLU ARG ASN ILE ARG TYR GLN ASP GLY GLY THR ALA ILE SEQRES 9 D 239 VAL LYS SER ASP ILE SER LEU GLU ASP GLY LYS PHE ILE SEQRES 10 D 239 VAL ASN VAL ASP PHE LYS ALA LYS ASP LEU ARG ARG MET SEQRES 11 D 239 GLY PRO VAL MET GLN GLN ASP ILE VAL GLY MET GLN PRO SEQRES 12 D 239 SER TYR GLU SER MET TYR THR ASN VAL THR SER VAL ILE SEQRES 13 D 239 GLY GLU CYS ILE ILE ALA PHE LYS LEU GLN THR GLY LYS SEQRES 14 D 239 HIS PHE THR TYR HIS MET ARG THR VAL TYR LYS SER LYS SEQRES 15 D 239 LYS PRO VAL GLU THR MET PRO LEU TYR HIS PHE ILE GLN SEQRES 16 D 239 HIS ARG LEU VAL LYS THR ASN VAL ASP THR ALA SER GLY SEQRES 17 D 239 TYR VAL VAL GLN HIS GLU THR ALA ILE ALA ALA HIS SER SEQRES 18 D 239 THR ILE LYS LYS ILE GLU GLY SER LEU PRO VAL ASP HIS SEQRES 19 D 239 HIS HIS HIS HIS HIS MODRES 2RH7 CRO A 66 GLY MODRES 2RH7 CRO A 66 TYR MODRES 2RH7 CRO A 66 GLY MODRES 2RH7 CRO B 66 GLY MODRES 2RH7 CRO B 66 TYR MODRES 2RH7 CRO B 66 GLY MODRES 2RH7 CRO C 66 GLY MODRES 2RH7 CRO C 66 TYR MODRES 2RH7 CRO C 66 GLY MODRES 2RH7 CRO D 66 GLY MODRES 2RH7 CRO D 66 TYR MODRES 2RH7 CRO D 66 GLY HET CRO A 66 21 HET CRO B 66 21 HET CRO C 66 21 HET CRO D 66 21 HETNAM CRO {2-[(1R,2R)-1-AMINO-2-HYDROXYPROPYL]-4-(4- HETNAM 2 CRO HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1- HETNAM 3 CRO YL}ACETIC ACID HETSYN CRO PEPTIDE DERIVED CHROMOPHORE FORMUL 1 CRO 4(C15 H17 N3 O5) FORMUL 5 HOH *537(H2 O) HELIX 1 1 ALA A 57 SER A 62 5 6 HELIX 2 2 PHE A 83 PHE A 87 5 5 HELIX 3 3 ALA B 57 SER B 62 5 6 HELIX 4 4 PHE B 83 PHE B 87 5 5 HELIX 5 5 GLY B 133 GLN B 138 1 6 HELIX 6 6 ALA C 57 SER C 62 5 6 HELIX 7 7 PHE C 83 PHE C 87 5 5 HELIX 8 8 ALA D 57 SER D 62 5 6 HELIX 9 9 ASP D 81 PHE D 87 1 7 SHEET 1 A13 ILE A 140 MET A 143 0 SHEET 2 A13 SER A 156 LEU A 167 -1 O LYS A 166 N GLY A 142 SHEET 3 A13 HIS A 172 SER A 183 -1 O PHE A 173 N PHE A 165 SHEET 4 A13 PHE A 91 TYR A 99 -1 N GLU A 94 O VAL A 180 SHEET 5 A13 THR A 104 LEU A 113 -1 O ILE A 111 N PHE A 91 SHEET 6 A13 PHE A 118 LYS A 127 -1 O ASP A 123 N LYS A 108 SHEET 7 A13 VAL A 11 VAL A 22 1 N ASN A 17 O VAL A 120 SHEET 8 A13 HIS A 25 ASN A 36 -1 O PHE A 27 N GLY A 20 SHEET 9 A13 THR A 41 LYS A 50 -1 O LYS A 45 N VAL A 32 SHEET 10 A13 VAL A 213 ALA A 221 -1 O GLN A 214 N VAL A 44 SHEET 11 A13 HIS A 194 ASN A 204 -1 N VAL A 201 O HIS A 215 SHEET 12 A13 SER A 146 ASN A 153 -1 N MET A 150 O HIS A 194 SHEET 13 A13 SER A 156 LEU A 167 -1 O GLU A 160 N SER A 149 SHEET 1 B13 ILE B 140 MET B 143 0 SHEET 2 B13 SER B 156 LEU B 167 -1 O LYS B 166 N VAL B 141 SHEET 3 B13 HIS B 172 SER B 183 -1 O TYR B 181 N VAL B 157 SHEET 4 B13 PHE B 91 TYR B 99 -1 N ASN B 96 O ARG B 178 SHEET 5 B13 THR B 104 GLU B 114 -1 O ILE B 111 N PHE B 91 SHEET 6 B13 LYS B 117 LYS B 127 -1 O ILE B 119 N SER B 112 SHEET 7 B13 VAL B 11 VAL B 22 1 N ASN B 17 O VAL B 120 SHEET 8 B13 HIS B 25 ASN B 36 -1 O GLY B 35 N MET B 12 SHEET 9 B13 THR B 41 LYS B 50 -1 O LYS B 45 N VAL B 32 SHEET 10 B13 VAL B 212 ALA B 221 -1 O VAL B 212 N ILE B 46 SHEET 11 B13 HIS B 194 ASN B 204 -1 N VAL B 201 O HIS B 215 SHEET 12 B13 SER B 146 ASN B 153 -1 N MET B 150 O HIS B 194 SHEET 13 B13 SER B 156 LEU B 167 -1 O ILE B 158 N TYR B 151 SHEET 1 C13 ILE C 140 MET C 143 0 SHEET 2 C13 SER C 156 LEU C 167 -1 O LYS C 166 N VAL C 141 SHEET 3 C13 HIS C 172 SER C 183 -1 O PHE C 173 N PHE C 165 SHEET 4 C13 PHE C 91 TYR C 99 -1 N GLU C 94 O VAL C 180 SHEET 5 C13 THR C 104 LEU C 113 -1 O ILE C 111 N PHE C 91 SHEET 6 C13 PHE C 118 LYS C 127 -1 O LYS C 125 N ILE C 106 SHEET 7 C13 VAL C 11 VAL C 22 1 N ASN C 17 O VAL C 120 SHEET 8 C13 HIS C 25 ASN C 36 -1 O HIS C 25 N VAL C 22 SHEET 9 C13 THR C 41 LYS C 50 -1 O LYS C 45 N VAL C 32 SHEET 10 C13 VAL C 213 ALA C 221 -1 O GLN C 214 N VAL C 44 SHEET 11 C13 HIS C 194 ASN C 204 -1 N ASN C 204 O VAL C 213 SHEET 12 C13 SER C 146 ASN C 153 -1 N GLU C 148 O ILE C 196 SHEET 13 C13 SER C 156 LEU C 167 -1 O GLU C 160 N SER C 149 SHEET 1 D13 ILE D 140 MET D 143 0 SHEET 2 D13 SER D 156 LEU D 167 -1 O LYS D 166 N VAL D 141 SHEET 3 D13 HIS D 172 SER D 183 -1 O TYR D 181 N VAL D 157 SHEET 4 D13 PHE D 91 TYR D 99 -1 N ASN D 96 O ARG D 178 SHEET 5 D13 THR D 104 SER D 112 -1 O VAL D 107 N ARG D 95 SHEET 6 D13 PHE D 118 LYS D 127 -1 O ASP D 123 N LYS D 108 SHEET 7 D13 VAL D 11 VAL D 22 1 N LYS D 15 O VAL D 120 SHEET 8 D13 HIS D 25 ASN D 36 -1 O GLY D 35 N MET D 12 SHEET 9 D13 THR D 41 LYS D 50 -1 O LYS D 45 N VAL D 32 SHEET 10 D13 VAL D 213 ALA D 221 -1 O GLN D 214 N VAL D 44 SHEET 11 D13 HIS D 194 ASN D 204 -1 N ASN D 204 O VAL D 213 SHEET 12 D13 SER D 146 ASN D 153 -1 N MET D 150 O HIS D 194 SHEET 13 D13 SER D 156 LEU D 167 -1 O SER D 156 N ASN D 153 CISPEP 1 ALA A 52 PRO A 53 0 -5.30 CISPEP 2 PHE A 87 PRO A 88 0 9.33 CISPEP 3 ALA B 52 PRO B 53 0 -1.04 CISPEP 4 PHE B 87 PRO B 88 0 8.20 CISPEP 5 ALA C 52 PRO C 53 0 0.35 CISPEP 6 PHE C 87 PRO C 88 0 8.94 CISPEP 7 ALA D 52 PRO D 53 0 -0.69 CISPEP 8 PHE D 87 PRO D 88 0 5.89 CISPEP 9 GLU D 114 GLY D 116 0 -2.97 CRYST1 73.744 85.405 158.425 90.00 90.00 90.00 P 21 21 2 16 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 0.013560 0.000000 0.000000 0.00000 SCALE2 0.000000 0.011709 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006312 0.00000 (ATOM LINES ARE NOT SHOWN.) END