HEADER FLUORESCENT PROTEIN 30-JUL-10 3O78
TITLE THE STRUCTURE OF CA2+ SENSOR (CASE-12)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MYOSIN LIGHT CHAIN KINASE, SMOOTH MUSCLE,GREEN FLUORESCENT
COMPND 3 PROTEIN,GREEN FLUORESCENT PROTEIN,CALMODULIN-1;
COMPND 4 CHAIN: A, B;
COMPND 5 SYNONYM: MLCK,TELOKIN;
COMPND 6 EC: 2.7.11.18;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 OTHER_DETAILS: CHIMERA PROTEIN OF PEPTIDE OF M13 (RESIDUES 1730-1749,
COMPND 10 UNP P11799), C-TERMINAL DOMAIN OF GREEN FLUORESCENT PROTEIN (RESIDUES
COMPND 11 147-238, UNP P42212), LINKER, N-TERMINAL OF GREEN FLUORESCENT PROTEIN
COMPND 12 (RESIDUES 2-146, UNP P42212) AND RESIDUES 3-149 OF CALMODULIN (UNP
COMPND 13 P0DP23)
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS, AEQUOREA VICTORIA, HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: CHICKEN, JELLYFISH, HUMAN;
SOURCE 4 ORGANISM_TAXID: 9031, 6100, 9606;
SOURCE 5 GENE: MYLK, GFP, CALM1, CALM, CAM, CAM1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) TUNER;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET41
KEYWDS CIRCULAR PERMUTATED GREEN FLUORESCENT PROTEIN, GENETICALLY ENCODED,
KEYWDS 2 GFP CALMODULIN M13-PEPTIDE, CALCIUM SENSOR, M13-PEPTIDE, GYG
KEYWDS 3 NATURALLY MODIFIED TRIPEPTIDE ACTS AS CHROMOPHORE, FLUORESCENT
KEYWDS 4 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR L.LEDER,W.STARK,F.FREULER,M.MARSH,M.MEYERHOFER,T.STETTLER,L.M.MAYR,
AUTHOR 2 O.V.BRITANOVA,L.A.STRUKOVA,D.M.CHUDAKOV
REVDAT 6 06-DEC-23 3O78 1 REMARK
REVDAT 5 01-NOV-23 3O78 1 REMARK LINK
REVDAT 4 21-JUN-17 3O78 1 COMPND SOURCE
REVDAT 3 13-JUN-12 3O78 1 SEQADV
REVDAT 2 25-APR-12 3O78 1 JRNL VERSN
REVDAT 1 29-SEP-10 3O78 0
JRNL AUTH L.LEDER,W.STARK,F.FREULER,M.MARSH,M.MEYERHOFER,T.STETTLER,
JRNL AUTH 2 L.M.MAYR,O.V.BRITANOVA,L.A.STRUKOVA,D.M.CHUDAKOV,
JRNL AUTH 3 E.A.SOUSLOVA
JRNL TITL THE STRUCTURE OF CA2+ SENSOR CASE16 REVEALS THE MECHANISM OF
JRNL TITL 2 REACTION TO LOW CA2+ CONCENTRATIONS
JRNL REF SENSORS (BASEL) V. 10 8143 2010
JRNL REFN ESSN 1424-8220
JRNL PMID 22163646
JRNL DOI 10.3390/S100908143
REMARK 2
REMARK 2 RESOLUTION. 2.60 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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.83
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 22288
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) : 0.245
REMARK 3 R VALUE (WORKING SET) : 0.242
REMARK 3 FREE R VALUE : 0.316
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1173
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1627
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.77
REMARK 3 BIN R VALUE (WORKING SET) : 0.3400
REMARK 3 BIN FREE R VALUE SET COUNT : 85
REMARK 3 BIN FREE R VALUE : 0.4530
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6338
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 8
REMARK 3 SOLVENT ATOMS : 77
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 41.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.43
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.01000
REMARK 3 B22 (A**2) : 0.32000
REMARK 3 B33 (A**2) : 0.69000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.06000
REMARK 3 B23 (A**2) : 0.00000
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): 0.450
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.376
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 24.100
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.904
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.840
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6445 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8674 ; 1.726 ; 1.968
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 795 ; 8.346 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 322 ;35.786 ;25.280
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1163 ;21.239 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 34 ;20.667 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 935 ; 0.106 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4908 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3511 ; 0.268 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4392 ; 0.319 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 352 ; 0.205 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 25 ; 0.178 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 88 ; 0.328 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 8 ; 0.372 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 3
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 25 A 270 1
REMARK 3 1 B 25 B 270 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 1793 ; 0.07 ; 0.05
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
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 271 A 340 1
REMARK 3 1 B 271 B 340 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 A (A): 542 ; 0.07 ; 0.05
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 341 A 411 1
REMARK 3 1 B 341 B 411 1
REMARK 3 2 A 1 A 24 1
REMARK 3 2 B 1 B 24 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 3 A (A): 754 ; 0.09 ; 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3O78 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-AUG-10.
REMARK 100 THE DEPOSITION ID IS D_1000060752.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-AUG-07
REMARK 200 TEMPERATURE (KELVIN) : 77
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54179
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23464
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.71
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.51700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 3O77
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: RESERVOIR: 100MM TRIS HCL (PH 5.5),
REMARK 280 100MM (NH4)2SO4, 21% PEG 3350; PROTEIN STOCK: 7.6 MG/ML PROTEIN,
REMARK 280 50MM TRIS HCL (PH 7.4), 150MM NACL; SEED STOCK SOLUTION: 20MM
REMARK 280 CACL2, 20% PEG 3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 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 50.81750
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, 3
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -46.0 KCAL/MOL
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 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 110
REMARK 465 MET A 111
REMARK 465 ASP A 112
REMARK 465 GLU A 113
REMARK 465 LEU A 114
REMARK 465 TYR A 115
REMARK 465 ASN A 116
REMARK 465 VAL A 117
REMARK 465 ASP A 118
REMARK 465 GLY A 119
REMARK 465 GLY A 120
REMARK 465 SER A 121
REMARK 465 ASP B 112
REMARK 465 GLU B 113
REMARK 465 LEU B 114
REMARK 465 TYR B 115
REMARK 465 ASN B 116
REMARK 465 VAL B 117
REMARK 465 ASP B 118
REMARK 465 GLY B 119
REMARK 465 GLY B 120
REMARK 465 SER B 121
REMARK 465 GLY B 122
REMARK 465 GLY B 123
REMARK 465 THR B 124
REMARK 465 GLY B 125
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 ILE A 107 CG1 CG2 CD1
REMARK 470 THR A 108 OG1 CG2
REMARK 470 LEU A 109 CG CD1 CD2
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 NH1 ARG A 6 OE2 GLU B 396 1.80
REMARK 500 OE1 GLU A 141 NH1 ARG A 246 2.11
REMARK 500 OE1 GLN A 61 NH2 ARG A 220 2.12
REMARK 500 OE1 GLN B 272 O HOH B 419 2.15
REMARK 500 N VAL A 71 O HOH A 447 2.15
REMARK 500 OE1 GLU B 141 NH1 ARG B 246 2.19
REMARK 500 N GLY A 1 O LYS B 384 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OD1 ASN B 37 OE1 GLU B 50 1455 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 TRP A 9 CB TRP A 9 CG -0.111
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 270 NE - CZ - NH1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG A 270 NE - CZ - NH2 ANGL. DEV. = 5.1 DEGREES
REMARK 500 ARG A 395 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 395 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG B 270 NE - CZ - NH1 ANGL. DEV. = 3.3 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 LYS A 34 -34.01 -34.97
REMARK 500 ASN A 37 46.97 33.44
REMARK 500 ASP A 51 33.46 -97.62
REMARK 500 SER A 53 -166.62 -64.78
REMARK 500 VAL A 71 143.39 58.80
REMARK 500 THR A 124 -94.74 105.91
REMARK 500 THR A 133 -41.00 -29.69
REMARK 500 LYS A 203 0.14 -67.02
REMARK 500 ASP A 226 13.24 59.00
REMARK 500 GLU A 256 1.19 -61.55
REMARK 500 ASP A 257 12.30 -143.81
REMARK 500 ASN A 268 150.64 71.49
REMARK 500 ASP A 289 66.02 -69.53
REMARK 500 ALA A 326 -67.72 -28.40
REMARK 500 ASP A 347 1.36 -47.93
REMARK 500 ASP A 398 68.71 -66.04
REMARK 500 ASP A 400 3.78 -64.74
REMARK 500 SER B 4 156.16 118.61
REMARK 500 SER B 5 119.10 -34.12
REMARK 500 ARG B 6 -164.41 102.77
REMARK 500 ARG B 7 -15.42 66.10
REMARK 500 GLN B 35 25.16 -67.75
REMARK 500 LYS B 36 21.53 -165.55
REMARK 500 ASN B 37 46.65 36.51
REMARK 500 ASP B 51 9.95 -65.61
REMARK 500 VAL B 71 155.35 -0.05
REMARK 500 LEU B 109 101.54 108.62
REMARK 500 LYS B 203 6.51 -66.81
REMARK 500 GLU B 256 -2.76 -57.78
REMARK 500 LYS B 264 0.26 -68.22
REMARK 500 ASN B 268 151.72 68.75
REMARK 500 ASP B 347 -2.92 -53.02
REMARK 500 ASP B 398 68.01 -67.30
REMARK 500 ASP B 400 6.29 -62.38
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 MET A 212 PRO A 213 95.64
REMARK 500 THR A 415 ALA A 416 147.16
REMARK 500 MET B 212 PRO B 213 108.05
REMARK 500 ASN B 268 THR B 269 146.82
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 289 OD1
REMARK 620 2 ASP A 291 OD1 79.7
REMARK 620 3 ASP A 293 OD1 67.5 85.3
REMARK 620 4 THR A 295 O 58.7 136.7 68.9
REMARK 620 5 GLU A 300 OE1 94.0 122.4 144.5 75.6
REMARK 620 6 GLU A 300 OE2 93.3 73.2 153.7 117.4 49.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 502 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 325 OD2
REMARK 620 2 ASP A 327 OD1 63.9
REMARK 620 3 ASN A 329 OD1 76.0 63.7
REMARK 620 4 THR A 331 O 80.9 133.1 79.1
REMARK 620 5 GLU A 336 OE1 80.5 84.8 146.6 120.3
REMARK 620 6 GLU A 336 OE2 91.1 131.4 153.1 75.6 48.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 503 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 362 OD2
REMARK 620 2 ASP A 364 OD2 75.1
REMARK 620 3 ASN A 366 OD1 90.8 90.0
REMARK 620 4 TYR A 368 O 97.3 171.2 85.8
REMARK 620 5 GLU A 373 OE2 113.6 111.6 150.4 75.1
REMARK 620 6 GLU A 373 OE1 83.7 66.3 156.3 117.8 49.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 504 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 398 OD1
REMARK 620 2 ASP A 400 OD2 95.7
REMARK 620 3 ASP A 402 OD1 89.9 87.0
REMARK 620 4 GLN A 404 O 97.0 153.8 70.3
REMARK 620 5 GLU A 409 OE2 125.3 102.8 141.4 88.2
REMARK 620 6 GLU A 409 OE1 104.7 62.9 147.3 134.3 46.5
REMARK 620 7 HOH A 448 O 151.2 60.2 74.3 99.9 78.6 79.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 289 OD1
REMARK 620 2 ASP B 291 OD1 80.3
REMARK 620 3 ASP B 293 OD1 68.1 84.7
REMARK 620 4 THR B 295 O 70.2 146.5 70.0
REMARK 620 5 GLU B 300 OE1 103.6 121.6 151.7 81.7
REMARK 620 6 GLU B 300 OE2 102.3 68.5 152.9 132.3 53.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 502 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 325 OD2
REMARK 620 2 ASP B 327 OD1 66.4
REMARK 620 3 ASN B 329 OD1 70.3 58.7
REMARK 620 4 THR B 331 O 86.7 128.2 71.1
REMARK 620 5 GLU B 336 OE1 89.6 89.9 147.2 135.2
REMARK 620 6 GLU B 336 OE2 103.6 144.8 152.8 82.2 55.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 503 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 362 OD2
REMARK 620 2 ASP B 364 OD2 77.5
REMARK 620 3 ASN B 366 OD1 81.7 77.5
REMARK 620 4 TYR B 368 O 91.8 151.0 74.3
REMARK 620 5 GLU B 373 OE1 92.3 73.3 150.8 134.7
REMARK 620 6 GLU B 373 OE2 119.3 128.3 147.8 80.5 58.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 504 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 398 OD1
REMARK 620 2 ASP B 400 OD2 92.6
REMARK 620 3 ASP B 402 OD1 84.6 94.6
REMARK 620 4 GLN B 404 O 85.5 163.6 69.0
REMARK 620 5 GLU B 409 OE2 114.5 112.3 145.2 83.1
REMARK 620 6 GLU B 409 OE1 105.2 62.1 154.6 134.1 51.6
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 504
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3O77 RELATED DB: PDB
REMARK 900 RELATED ID: 3EK4 RELATED DB: PDB
REMARK 900 RELATED ID: 3EK7 RELATED DB: PDB
REMARK 900 RELATED ID: 3EK8 RELATED DB: PDB
REMARK 900 RELATED ID: 3EKH RELATED DB: PDB
REMARK 900 RELATED ID: 3EKJ RELATED DB: PDB
REMARK 900 RELATED ID: 3EVP RELATED DB: PDB
REMARK 900 RELATED ID: 3EVR RELATED DB: PDB
REMARK 900 RELATED ID: 3EVU RELATED DB: PDB
REMARK 900 RELATED ID: 3EVV RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 UNP RESIDUE 65 SER AND 72 SER OF GREEN FLUORESCENT PROTEIN IN
REMARK 999 DATABASE UNP P42212 (GFP_AEQVI) SHOULD BE GLY. RESIDUE S65G FORM
REMARK 999 THE CHROMOPHORE CR2 190. RESIDUE S72G (RESIDUE NUMBER 196 IN THE
REMARK 999 COORDINATES RESPECTIVELY) IS MUTAGENESIS. THESE SEQUENCE WERE BASED
REMARK 999 ON REFERENCES IN THE DATABASE UNP P42212.
DBREF 3O78 A 5 24 UNP P11799 MYLK_CHICK 1730 1749
DBREF 3O78 A 25 116 UNP P42212 GFP_AEQVI 147 238
DBREF 3O78 A 126 270 UNP P42212 GFP_AEQVI 2 146
DBREF 3O78 A 271 417 UNP P0DP23 CALM1_HUMAN 3 149
DBREF 3O78 B 5 24 UNP P11799 MYLK_CHICK 1730 1749
DBREF 3O78 B 25 116 UNP P42212 GFP_AEQVI 147 238
DBREF 3O78 B 126 270 UNP P42212 GFP_AEQVI 2 146
DBREF 3O78 B 271 417 UNP P0DP23 CALM1_HUMAN 3 149
SEQADV 3O78 GLY A 1 UNP P11799 EXPRESSION TAG
SEQADV 3O78 PRO A 2 UNP P11799 EXPRESSION TAG
SEQADV 3O78 GLY A 3 UNP P11799 EXPRESSION TAG
SEQADV 3O78 SER A 4 UNP P11799 EXPRESSION TAG
SEQADV 3O78 SER A 5 UNP P11799 ALA 1730 ENGINEERED MUTATION
SEQADV 3O78 ASN A 10 UNP P11799 GLN 1735 ENGINEERED MUTATION
SEQADV 3O78 LEU A 25 UNP P42212 SER 147 ENGINEERED MUTATION
SEQADV 3O78 GLU A 26 UNP P42212 HIS 148 ENGINEERED MUTATION
SEQADV 3O78 ALA A 41 UNP P42212 VAL 163 ENGINEERED MUTATION
SEQADV 3O78 VAL A 49 UNP P42212 ILE 171 ENGINEERED MUTATION
SEQADV 3O78 PHE A 81 UNP P42212 THR 203 ENGINEERED MUTATION
SEQADV 3O78 VAL A 84 UNP P42212 ALA 206 ENGINEERED MUTATION
SEQADV 3O78 LEU A 109 UNP P42212 HIS 231 ENGINEERED MUTATION
SEQADV 3O78 ASN A 116 UNP P42212 LYS 238 ENGINEERED MUTATION
SEQADV 3O78 VAL A 117 UNP P42212 LINKER
SEQADV 3O78 ASP A 118 UNP P42212 LINKER
SEQADV 3O78 GLY A 119 UNP P42212 LINKER
SEQADV 3O78 GLY A 120 UNP P42212 LINKER
SEQADV 3O78 SER A 121 UNP P42212 LINKER
SEQADV 3O78 GLY A 122 UNP P42212 LINKER
SEQADV 3O78 GLY A 123 UNP P42212 LINKER
SEQADV 3O78 THR A 124 UNP P42212 LINKER
SEQADV 3O78 GLY A 125 UNP P42212 LINKER
SEQADV 3O78 LEU A 170 UNP P42212 PHE 46 ENGINEERED MUTATION
SEQADV 3O78 LEU A 188 UNP P42212 PHE 64 ENGINEERED MUTATION
SEQADV 3O78 CR2 A 190 UNP P42212 SER 65 CHROMOPHORE
SEQADV 3O78 CR2 A 190 UNP P42212 TYR 66 CHROMOPHORE
SEQADV 3O78 CR2 A 190 UNP P42212 GLY 67 CHROMOPHORE
SEQADV 3O78 LEU A 192 UNP P42212 VAL 68 ENGINEERED MUTATION
SEQADV 3O78 LYS A 193 UNP P42212 GLN 69 ENGINEERED MUTATION
SEQADV 3O78 ALA A 196 UNP P42212 SER 72 SEE SEQUENCE DETAILS
SEQADV 3O78 GLY A 253 UNP P42212 ASP 129 ENGINEERED MUTATION
SEQADV 3O78 THR A 269 UNP P42212 TYR 145 ENGINEERED MUTATION
SEQADV 3O78 ARG A 270 UNP P42212 ASN 146 ENGINEERED MUTATION
SEQADV 3O78 GLY B 1 UNP P11799 EXPRESSION TAG
SEQADV 3O78 PRO B 2 UNP P11799 EXPRESSION TAG
SEQADV 3O78 GLY B 3 UNP P11799 EXPRESSION TAG
SEQADV 3O78 SER B 4 UNP P11799 EXPRESSION TAG
SEQADV 3O78 SER B 5 UNP P11799 ALA 1730 ENGINEERED MUTATION
SEQADV 3O78 ASN B 10 UNP P11799 GLN 1735 ENGINEERED MUTATION
SEQADV 3O78 LEU B 25 UNP P42212 SER 147 ENGINEERED MUTATION
SEQADV 3O78 GLU B 26 UNP P42212 HIS 148 ENGINEERED MUTATION
SEQADV 3O78 ALA B 41 UNP P42212 VAL 163 ENGINEERED MUTATION
SEQADV 3O78 VAL B 49 UNP P42212 ILE 171 ENGINEERED MUTATION
SEQADV 3O78 PHE B 81 UNP P42212 THR 203 ENGINEERED MUTATION
SEQADV 3O78 VAL B 84 UNP P42212 ALA 206 ENGINEERED MUTATION
SEQADV 3O78 LEU B 109 UNP P42212 HIS 231 ENGINEERED MUTATION
SEQADV 3O78 ASN B 116 UNP P42212 LYS 238 ENGINEERED MUTATION
SEQADV 3O78 VAL B 117 UNP P42212 LINKER
SEQADV 3O78 ASP B 118 UNP P42212 LINKER
SEQADV 3O78 GLY B 119 UNP P42212 LINKER
SEQADV 3O78 GLY B 120 UNP P42212 LINKER
SEQADV 3O78 SER B 121 UNP P42212 LINKER
SEQADV 3O78 GLY B 122 UNP P42212 LINKER
SEQADV 3O78 GLY B 123 UNP P42212 LINKER
SEQADV 3O78 THR B 124 UNP P42212 LINKER
SEQADV 3O78 GLY B 125 UNP P42212 LINKER
SEQADV 3O78 LEU B 170 UNP P42212 PHE 46 ENGINEERED MUTATION
SEQADV 3O78 LEU B 188 UNP P42212 PHE 64 ENGINEERED MUTATION
SEQADV 3O78 CR2 B 190 UNP P42212 SER 65 CHROMOPHORE
SEQADV 3O78 CR2 B 190 UNP P42212 TYR 66 CHROMOPHORE
SEQADV 3O78 CR2 B 190 UNP P42212 GLY 67 CHROMOPHORE
SEQADV 3O78 LEU B 192 UNP P42212 VAL 68 ENGINEERED MUTATION
SEQADV 3O78 LYS B 193 UNP P42212 GLN 69 ENGINEERED MUTATION
SEQADV 3O78 ALA B 196 UNP P42212 SER 72 SEE SEQUENCE DETAILS
SEQADV 3O78 GLY B 253 UNP P42212 ASP 129 ENGINEERED MUTATION
SEQADV 3O78 THR B 269 UNP P42212 TYR 145 ENGINEERED MUTATION
SEQADV 3O78 ARG B 270 UNP P42212 ASN 146 ENGINEERED MUTATION
SEQRES 1 A 415 GLY PRO GLY SER SER ARG ARG LYS TRP ASN LYS THR GLY
SEQRES 2 A 415 HIS ALA VAL ARG ALA ILE GLY ARG LEU SER SER LEU GLU
SEQRES 3 A 415 ASN VAL TYR ILE MET ALA ASP LYS GLN LYS ASN GLY ILE
SEQRES 4 A 415 LYS ALA ASN PHE LYS ILE ARG HIS ASN VAL GLU ASP GLY
SEQRES 5 A 415 SER VAL GLN LEU ALA ASP HIS TYR GLN GLN ASN THR PRO
SEQRES 6 A 415 ILE GLY ASP GLY PRO VAL LEU LEU PRO ASP ASN HIS TYR
SEQRES 7 A 415 LEU SER PHE GLN SER VAL LEU SER LYS ASP PRO ASN GLU
SEQRES 8 A 415 LYS ARG ASP HIS MET VAL LEU LEU GLU PHE VAL THR ALA
SEQRES 9 A 415 ALA GLY ILE THR LEU GLY MET ASP GLU LEU TYR ASN VAL
SEQRES 10 A 415 ASP GLY GLY SER GLY GLY THR GLY SER LYS GLY GLU GLU
SEQRES 11 A 415 LEU PHE THR GLY VAL VAL PRO ILE LEU VAL GLU LEU ASP
SEQRES 12 A 415 GLY ASP VAL ASN GLY HIS LYS PHE SER VAL SER GLY GLU
SEQRES 13 A 415 GLY GLU GLY ASP ALA THR TYR GLY LYS LEU THR LEU LYS
SEQRES 14 A 415 LEU ILE CYS THR THR GLY LYS LEU PRO VAL PRO TRP PRO
SEQRES 15 A 415 THR LEU VAL THR THR LEU CR2 LEU LYS CYS PHE ALA ARG
SEQRES 16 A 415 TYR PRO ASP HIS MET LYS GLN HIS ASP PHE PHE LYS SER
SEQRES 17 A 415 ALA MET PRO GLU GLY TYR VAL GLN GLU ARG THR ILE PHE
SEQRES 18 A 415 PHE LYS ASP ASP GLY ASN TYR LYS THR ARG ALA GLU VAL
SEQRES 19 A 415 LYS PHE GLU GLY ASP THR LEU VAL ASN ARG ILE GLU LEU
SEQRES 20 A 415 LYS GLY ILE GLY PHE LYS GLU ASP GLY ASN ILE LEU GLY
SEQRES 21 A 415 HIS LYS LEU GLU TYR ASN THR ARG ASP GLN LEU THR GLU
SEQRES 22 A 415 GLU GLN ILE ALA GLU PHE LYS GLU ALA PHE SER LEU PHE
SEQRES 23 A 415 ASP LYS ASP GLY ASP GLY THR ILE THR THR LYS GLU LEU
SEQRES 24 A 415 GLY THR VAL MET ARG SER LEU GLY GLN ASN PRO THR GLU
SEQRES 25 A 415 ALA GLU LEU GLN ASP MET ILE ASN GLU VAL ASP ALA ASP
SEQRES 26 A 415 GLY ASN GLY THR ILE ASP PHE PRO GLU PHE LEU THR MET
SEQRES 27 A 415 MET ALA ARG LYS MET LYS ASP THR ASP SER GLU GLU GLU
SEQRES 28 A 415 ILE ARG GLU ALA PHE ARG VAL PHE ASP LYS ASP GLY ASN
SEQRES 29 A 415 GLY TYR ILE SER ALA ALA GLU LEU ARG HIS VAL MET THR
SEQRES 30 A 415 ASN LEU GLY GLU LYS LEU THR ASP GLU GLU VAL ASP GLU
SEQRES 31 A 415 MET ILE ARG GLU ALA ASP ILE ASP GLY ASP GLY GLN VAL
SEQRES 32 A 415 ASN TYR GLU GLU PHE VAL GLN MET MET THR ALA LYS
SEQRES 1 B 415 GLY PRO GLY SER SER ARG ARG LYS TRP ASN LYS THR GLY
SEQRES 2 B 415 HIS ALA VAL ARG ALA ILE GLY ARG LEU SER SER LEU GLU
SEQRES 3 B 415 ASN VAL TYR ILE MET ALA ASP LYS GLN LYS ASN GLY ILE
SEQRES 4 B 415 LYS ALA ASN PHE LYS ILE ARG HIS ASN VAL GLU ASP GLY
SEQRES 5 B 415 SER VAL GLN LEU ALA ASP HIS TYR GLN GLN ASN THR PRO
SEQRES 6 B 415 ILE GLY ASP GLY PRO VAL LEU LEU PRO ASP ASN HIS TYR
SEQRES 7 B 415 LEU SER PHE GLN SER VAL LEU SER LYS ASP PRO ASN GLU
SEQRES 8 B 415 LYS ARG ASP HIS MET VAL LEU LEU GLU PHE VAL THR ALA
SEQRES 9 B 415 ALA GLY ILE THR LEU GLY MET ASP GLU LEU TYR ASN VAL
SEQRES 10 B 415 ASP GLY GLY SER GLY GLY THR GLY SER LYS GLY GLU GLU
SEQRES 11 B 415 LEU PHE THR GLY VAL VAL PRO ILE LEU VAL GLU LEU ASP
SEQRES 12 B 415 GLY ASP VAL ASN GLY HIS LYS PHE SER VAL SER GLY GLU
SEQRES 13 B 415 GLY GLU GLY ASP ALA THR TYR GLY LYS LEU THR LEU LYS
SEQRES 14 B 415 LEU ILE CYS THR THR GLY LYS LEU PRO VAL PRO TRP PRO
SEQRES 15 B 415 THR LEU VAL THR THR LEU CR2 LEU LYS CYS PHE ALA ARG
SEQRES 16 B 415 TYR PRO ASP HIS MET LYS GLN HIS ASP PHE PHE LYS SER
SEQRES 17 B 415 ALA MET PRO GLU GLY TYR VAL GLN GLU ARG THR ILE PHE
SEQRES 18 B 415 PHE LYS ASP ASP GLY ASN TYR LYS THR ARG ALA GLU VAL
SEQRES 19 B 415 LYS PHE GLU GLY ASP THR LEU VAL ASN ARG ILE GLU LEU
SEQRES 20 B 415 LYS GLY ILE GLY PHE LYS GLU ASP GLY ASN ILE LEU GLY
SEQRES 21 B 415 HIS LYS LEU GLU TYR ASN THR ARG ASP GLN LEU THR GLU
SEQRES 22 B 415 GLU GLN ILE ALA GLU PHE LYS GLU ALA PHE SER LEU PHE
SEQRES 23 B 415 ASP LYS ASP GLY ASP GLY THR ILE THR THR LYS GLU LEU
SEQRES 24 B 415 GLY THR VAL MET ARG SER LEU GLY GLN ASN PRO THR GLU
SEQRES 25 B 415 ALA GLU LEU GLN ASP MET ILE ASN GLU VAL ASP ALA ASP
SEQRES 26 B 415 GLY ASN GLY THR ILE ASP PHE PRO GLU PHE LEU THR MET
SEQRES 27 B 415 MET ALA ARG LYS MET LYS ASP THR ASP SER GLU GLU GLU
SEQRES 28 B 415 ILE ARG GLU ALA PHE ARG VAL PHE ASP LYS ASP GLY ASN
SEQRES 29 B 415 GLY TYR ILE SER ALA ALA GLU LEU ARG HIS VAL MET THR
SEQRES 30 B 415 ASN LEU GLY GLU LYS LEU THR ASP GLU GLU VAL ASP GLU
SEQRES 31 B 415 MET ILE ARG GLU ALA ASP ILE ASP GLY ASP GLY GLN VAL
SEQRES 32 B 415 ASN TYR GLU GLU PHE VAL GLN MET MET THR ALA LYS
MODRES 3O78 CR2 A 190 SER CHROMOPHORE
MODRES 3O78 CR2 B 190 SER CHROMOPHORE
HET CR2 A 190 19
HET CR2 B 190 19
HET CA A 501 1
HET CA A 502 1
HET CA A 503 1
HET CA A 504 1
HET CA B 501 1
HET CA B 502 1
HET CA B 503 1
HET CA B 504 1
HETNAM CR2 {(4Z)-2-(AMINOMETHYL)-4-[(4-HYDROXYPHENYL)METHYLIDENE]-
HETNAM 2 CR2 5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC ACID
HETNAM CA CALCIUM ION
HETSYN CR2 CHROMOPHORE (GLY-TYR-GLY)
FORMUL 1 CR2 2(C13 H13 N3 O4)
FORMUL 3 CA 8(CA 2+)
FORMUL 11 HOH *77(H2 O)
HELIX 1 1 SER A 4 SER A 23 1 20
HELIX 2 2 LYS A 34 ASN A 37 5 4
HELIX 3 3 LYS A 127 PHE A 132 5 6
HELIX 4 4 ALA A 161 TYR A 163 5 3
HELIX 5 5 PRO A 180 VAL A 185 5 6
HELIX 6 6 LEU A 192 ALA A 196 5 5
HELIX 7 7 PRO A 199 LYS A 203 5 5
HELIX 8 8 ASP A 206 ALA A 211 1 6
HELIX 9 9 THR A 274 ASP A 289 1 16
HELIX 10 10 THR A 297 GLY A 309 1 13
HELIX 11 11 THR A 313 GLU A 323 1 11
HELIX 12 12 PHE A 334 ARG A 343 1 10
HELIX 13 13 LYS A 346 ASP A 362 1 17
HELIX 14 14 SER A 370 LEU A 381 1 12
HELIX 15 15 THR A 386 ASP A 398 1 13
HELIX 16 16 ASN A 406 THR A 415 1 10
HELIX 17 17 ARG B 7 SER B 23 1 17
HELIX 18 18 LYS B 34 ASN B 37 5 4
HELIX 19 19 LYS B 127 THR B 133 5 7
HELIX 20 20 ALA B 161 TYR B 163 5 3
HELIX 21 21 PRO B 180 VAL B 185 5 6
HELIX 22 22 LEU B 192 ALA B 196 5 5
HELIX 23 23 PRO B 199 LYS B 203 5 5
HELIX 24 24 ASP B 206 ALA B 211 1 6
HELIX 25 25 THR B 274 ASP B 289 1 16
HELIX 26 26 THR B 297 GLY B 309 1 13
HELIX 27 27 THR B 313 GLU B 323 1 11
HELIX 28 28 PHE B 334 ARG B 343 1 10
HELIX 29 29 LYS B 346 ASP B 362 1 17
HELIX 30 30 SER B 370 LEU B 381 1 12
HELIX 31 31 THR B 386 ASP B 398 1 13
HELIX 32 32 ASN B 406 THR B 415 1 10
SHEET 1 A12 VAL A 28 ASP A 33 0
SHEET 2 A12 GLY A 38 ASN A 48 -1 O GLY A 38 N ASP A 33
SHEET 3 A12 VAL A 54 PRO A 65 -1 O GLN A 55 N HIS A 47
SHEET 4 A12 TYR A 216 PHE A 224 -1 O VAL A 217 N THR A 64
SHEET 5 A12 ASN A 229 GLU A 239 -1 O VAL A 236 N TYR A 216
SHEET 6 A12 THR A 242 ILE A 252 -1 O VAL A 244 N LYS A 237
SHEET 7 A12 VAL A 136 VAL A 146 1 N ASP A 143 O LEU A 249
SHEET 8 A12 HIS A 149 ASP A 160 -1 O GLY A 157 N ILE A 138
SHEET 9 A12 LYS A 165 CYS A 172 -1 O ILE A 171 N SER A 154
SHEET 10 A12 HIS A 95 ALA A 105 -1 N MET A 96 O LEU A 170
SHEET 11 A12 HIS A 77 SER A 86 -1 N TYR A 78 O ALA A 105
SHEET 12 A12 VAL A 28 ASP A 33 -1 N ILE A 30 O HIS A 77
SHEET 1 B 2 THR A 295 ILE A 296 0
SHEET 2 B 2 ILE A 332 ASP A 333 -1 O ILE A 332 N ILE A 296
SHEET 1 C12 VAL B 28 ASP B 33 0
SHEET 2 C12 GLY B 38 ASN B 48 -1 O GLY B 38 N ASP B 33
SHEET 3 C12 VAL B 54 PRO B 65 -1 O GLN B 55 N HIS B 47
SHEET 4 C12 TYR B 216 PHE B 224 -1 O VAL B 217 N THR B 64
SHEET 5 C12 ASN B 229 GLU B 239 -1 O TYR B 230 N ILE B 222
SHEET 6 C12 THR B 242 ILE B 252 -1 O ILE B 252 N ASN B 229
SHEET 7 C12 VAL B 136 VAL B 146 1 N ASP B 143 O LEU B 249
SHEET 8 C12 HIS B 149 ASP B 160 -1 O GLY B 157 N ILE B 138
SHEET 9 C12 LYS B 165 ILE B 171 -1 O ILE B 171 N SER B 154
SHEET 10 C12 HIS B 95 ALA B 105 -1 N LEU B 98 O LEU B 168
SHEET 11 C12 HIS B 77 SER B 86 -1 N TYR B 78 O ALA B 105
SHEET 12 C12 VAL B 28 ASP B 33 -1 N ILE B 30 O HIS B 77
SHEET 1 D 2 THR B 295 ILE B 296 0
SHEET 2 D 2 ILE B 332 ASP B 333 -1 O ILE B 332 N ILE B 296
LINK C LEU A 188 N1 CR2 A 190 1555 1555 1.45
LINK C3 CR2 A 190 N LEU A 192 1555 1555 1.36
LINK C LEU B 188 N1 CR2 B 190 1555 1555 1.20
LINK C3 CR2 B 190 N LEU B 192 1555 1555 1.37
LINK OD1 ASP A 289 CA CA A 501 1555 1555 2.50
LINK OD1 ASP A 291 CA CA A 501 1555 1555 2.32
LINK OD1 ASP A 293 CA CA A 501 1555 1555 2.29
LINK O THR A 295 CA CA A 501 1555 1555 2.90
LINK OE1 GLU A 300 CA CA A 501 1555 1555 2.24
LINK OE2 GLU A 300 CA CA A 501 1555 1555 2.81
LINK OD2 ASP A 325 CA CA A 502 1555 1555 2.25
LINK OD1 ASP A 327 CA CA A 502 1555 1555 2.77
LINK OD1 ASN A 329 CA CA A 502 1555 1555 2.44
LINK O THR A 331 CA CA A 502 1555 1555 2.32
LINK OE1 GLU A 336 CA CA A 502 1555 1555 2.65
LINK OE2 GLU A 336 CA CA A 502 1555 1555 2.70
LINK OD2 ASP A 362 CA CA A 503 1555 1555 2.55
LINK OD2 ASP A 364 CA CA A 503 1555 1555 2.21
LINK OD1 ASN A 366 CA CA A 503 1555 1555 2.18
LINK O TYR A 368 CA CA A 503 1555 1555 2.14
LINK OE2 GLU A 373 CA CA A 503 1555 1555 2.55
LINK OE1 GLU A 373 CA CA A 503 1555 1555 2.67
LINK OD1 ASP A 398 CA CA A 504 1555 1555 2.12
LINK OD2 ASP A 400 CA CA A 504 1555 1555 2.74
LINK OD1 ASP A 402 CA CA A 504 1555 1555 2.53
LINK O GLN A 404 CA CA A 504 1555 1555 2.23
LINK OE2 GLU A 409 CA CA A 504 1555 1555 2.60
LINK OE1 GLU A 409 CA CA A 504 1555 1555 2.90
LINK O HOH A 448 CA CA A 504 1555 1555 2.54
LINK OD1 ASP B 289 CA CA B 501 1555 1555 2.29
LINK OD1 ASP B 291 CA CA B 501 1555 1555 2.39
LINK OD1 ASP B 293 CA CA B 501 1555 1555 2.42
LINK O THR B 295 CA CA B 501 1555 1555 2.58
LINK OE1 GLU B 300 CA CA B 501 1555 1555 2.08
LINK OE2 GLU B 300 CA CA B 501 1555 1555 2.61
LINK OD2 ASP B 325 CA CA B 502 1555 1555 2.15
LINK OD1 ASP B 327 CA CA B 502 1555 1555 2.70
LINK OD1 ASN B 329 CA CA B 502 1555 1555 2.66
LINK O THR B 331 CA CA B 502 1555 1555 2.35
LINK OE1 GLU B 336 CA CA B 502 1555 1555 2.35
LINK OE2 GLU B 336 CA CA B 502 1555 1555 2.39
LINK OD2 ASP B 362 CA CA B 503 1555 1555 2.50
LINK OD2 ASP B 364 CA CA B 503 1555 1555 2.33
LINK OD1 ASN B 366 CA CA B 503 1555 1555 2.66
LINK O TYR B 368 CA CA B 503 1555 1555 2.19
LINK OE1 GLU B 373 CA CA B 503 1555 1555 2.20
LINK OE2 GLU B 373 CA CA B 503 1555 1555 2.24
LINK OD1 ASP B 398 CA CA B 504 1555 1555 2.30
LINK OD2 ASP B 400 CA CA B 504 1555 1555 2.29
LINK OD1 ASP B 402 CA CA B 504 1555 1555 2.56
LINK O GLN B 404 CA CA B 504 1555 1555 2.41
LINK OE2 GLU B 409 CA CA B 504 1555 1555 2.47
LINK OE1 GLU B 409 CA CA B 504 1555 1555 2.58
SITE 1 AC1 5 ASP A 289 ASP A 291 ASP A 293 THR A 295
SITE 2 AC1 5 GLU A 300
SITE 1 AC2 5 ASP A 325 ASP A 327 ASN A 329 THR A 331
SITE 2 AC2 5 GLU A 336
SITE 1 AC3 5 ASP A 362 ASP A 364 ASN A 366 TYR A 368
SITE 2 AC3 5 GLU A 373
SITE 1 AC4 6 ASP A 398 ASP A 400 ASP A 402 GLN A 404
SITE 2 AC4 6 GLU A 409 HOH A 448
SITE 1 AC5 5 ASP B 289 ASP B 291 ASP B 293 THR B 295
SITE 2 AC5 5 GLU B 300
SITE 1 AC6 5 ASP B 325 ASP B 327 ASN B 329 THR B 331
SITE 2 AC6 5 GLU B 336
SITE 1 AC7 5 ASP B 362 ASP B 364 ASN B 366 TYR B 368
SITE 2 AC7 5 GLU B 373
SITE 1 AC8 5 ASP B 398 ASP B 400 ASP B 402 GLN B 404
SITE 2 AC8 5 GLU B 409
CRYST1 46.374 101.635 82.211 90.00 91.45 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 0.021564 0.000000 0.000547 0.00000
SCALE2 0.000000 0.009839 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012168 0.00000
(ATOM LINES ARE NOT SHOWN.)
END