HEADER PEPTIDE BINDING PROTEIN 30-SEP-10 3P1R
TITLE CRYSTAL STRUCTURE OF HUMAN 14-3-3 SIGMA C38V/N166H IN COMPLEX WITH
TITLE 2 TASK-3 PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 14-3-3 PROTEIN SIGMA;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: STRATIFIN, EPITHELIAL CELL MARKER PROTEIN 1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: 6-MER PEPTIDE FROM POTASSIUM CHANNEL SUBFAMILY K MEMBER 9;
COMPND 9 CHAIN: P;
COMPND 10 SYNONYM: TASK-3 PEPTIDE;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: SFN;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA DE3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPROEX HTB;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS.
KEYWDS HELICAL PROTEIN, PHOSPHOPROTEIN, ADAPTER PROTEIN, PEPTIDE BINDING
KEYWDS 2 PROTEIN, NUCLEUS
EXPDTA X-RAY DIFFRACTION
AUTHOR C.ANDERS,Y.HIGUCHI,B.SCHUMACHER,P.THIEL,N.KATO,C.OTTMANN
REVDAT 4 01-NOV-23 3P1R 1 REMARK SEQADV LINK
REVDAT 3 08-NOV-17 3P1R 1 REMARK
REVDAT 2 07-JUN-17 3P1R 1 JRNL
REVDAT 1 12-OCT-11 3P1R 0
JRNL AUTH C.ANDERS,Y.HIGUCHI,K.KOSCHINSKY,M.BARTEL,B.SCHUMACHER,
JRNL AUTH 2 P.THIEL,H.NITTA,R.PREISIG-MULLER,G.SCHLICHTHORL,V.RENIGUNTA,
JRNL AUTH 3 J.OHKANDA,J.DAUT,N.KATO,C.OTTMANN
JRNL TITL A SEMISYNTHETIC FUSICOCCANE STABILIZES A PROTEIN-PROTEIN
JRNL TITL 2 INTERACTION AND ENHANCES THE EXPRESSION OF K+ CHANNELS AT
JRNL TITL 3 THE CELL SURFACE
JRNL REF CHEM. BIOL. V. 20 583 2013
JRNL REFN ISSN 1879-1301
JRNL PMID 23601647
JRNL DOI 10.1016/J.CHEMBIOL.2013.03.015
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.58
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 30261
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) : 0.153
REMARK 3 R VALUE (WORKING SET) : 0.151
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 : 1593
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2148
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.1800
REMARK 3 BIN FREE R VALUE SET COUNT : 113
REMARK 3 BIN FREE R VALUE : 0.2330
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1907
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 9
REMARK 3 SOLVENT ATOMS : 366
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.49
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.48
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.17000
REMARK 3 B22 (A**2) : -0.03000
REMARK 3 B33 (A**2) : -0.14000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.096
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.052
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.550
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.941
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2180 ; 0.028 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2993 ; 2.204 ; 1.992
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 309 ; 5.011 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 106 ;37.456 ;24.811
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 446 ;13.806 ;15.034
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;12.814 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 335 ; 0.175 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1666 ; 0.012 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 1320 ; 1.270 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2160 ; 2.028 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 860 ; 3.245 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 793 ; 5.211 ; 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 : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 3P1R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-OCT-10.
REMARK 100 THE DEPOSITION ID IS D_1000061848.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-MAY-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.4
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 : BRUKER AXS MICROSTAR
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
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 : 31854
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 19.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 3.950
REMARK 200 R MERGE (I) : 0.09600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.91
REMARK 200 R MERGE FOR SHELL (I) : 0.31500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.370
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: PDB ENTRY 3LW1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.095M HEPES NA-SALT, 25.6% PEG 400,
REMARK 280 0.19M CACL2, 5% GLYCEROL, PH 7.4, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 31.34500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 31.34500
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 41.16000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 56.14500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 41.16000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 56.14500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 31.34500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 41.16000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 56.14500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 31.34500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 41.16000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 56.14500
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, P
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 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
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 GLN A 67 CD OE1 NE2
REMARK 470 GLU A 72 CB CG CD OE1 OE2
REMARK 470 LYS A 214 CD CE NZ
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 A 364 O HOH A 365 2.03
REMARK 500 O HOH A 350 O HOH A 469 2.13
REMARK 500 NZ LYS A 195 O HOH A 322 2.15
REMARK 500 OD1 ASP A 138 O HOH A 288 2.16
REMARK 500 O HOH A 350 O HOH A 543 2.17
REMARK 500 O HOH A 306 O HOH A 353 2.18
REMARK 500 CB ASN A 50 O HOH A 598 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 OD2 ASP A 145 O HOH A 467 6545 1.72
REMARK 500 NE2 GLN A 8 O HOH A 302 6544 1.73
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 GLU A 182 CB GLU A 182 CG -0.139
REMARK 500 ARG P 370 CG ARG P 370 CD 0.191
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 3 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG A 85 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ASP A 104 CB - CG - OD1 ANGL. DEV. = 15.1 DEGREES
REMARK 500 ASP A 104 CB - CG - OD2 ANGL. DEV. = -10.9 DEGREES
REMARK 500 ASP A 139 CB - CG - OD1 ANGL. DEV. = 12.2 DEGREES
REMARK 500 ASP A 139 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ARG A 148 NE - CZ - NH2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 ARG A 148 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ASP A 204 CB - CG - OD2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 ARG P 370 CG - CD - NE ANGL. DEV. = -14.1 DEGREES
REMARK 500 ARG P 370 CD - NE - CZ ANGL. DEV. = 13.0 DEGREES
REMARK 500 ARG P 370 NE - CZ - NH1 ANGL. DEV. = 8.7 DEGREES
REMARK 500 ARG P 370 NE - CZ - NH2 ANGL. DEV. = -10.8 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 ARG A 18 75.66 -108.86
REMARK 500 HIS A 106 39.84 -144.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG P 370 0.09 SIDE CHAIN
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 MG A 250 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 2 OE1
REMARK 620 2 HOH A 283 O 81.9
REMARK 620 3 HOH A 364 O 89.1 62.0
REMARK 620 4 HOH A 365 O 88.1 110.3 49.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 257 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 8 OE1
REMARK 620 2 HOH A 538 O 97.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 249 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 75 OE1
REMARK 620 2 HOH A 309 O 73.8
REMARK 620 3 HOH A 536 O 121.2 69.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 256 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 188 OE2
REMARK 620 2 HOH A 483 O 72.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 251 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 215 O
REMARK 620 2 HOH A 300 O 111.3
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 249
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 250
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 251
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 252
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 253
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 254
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 255
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 256
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 257
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2O98 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE 14-3-3 / H+-ATPASE PLANT COMPLEX
REMARK 900 RELATED ID: 3LW1 RELATED DB: PDB
REMARK 900 BINARY COMPLEX OF 14-3-3 SIGMA AND P53 PT387-PEPTIDE
REMARK 900 RELATED ID: 3IQU RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN 14-3-3 SIGMA IN COMPLEX WITH RAF1
REMARK 900 PEPTIDE (6MER)
REMARK 900 RELATED ID: 3P1N RELATED DB: PDB
REMARK 900 RELATED ID: 3P1O RELATED DB: PDB
REMARK 900 RELATED ID: 3P1P RELATED DB: PDB
REMARK 900 RELATED ID: 3P1Q RELATED DB: PDB
REMARK 900 RELATED ID: 3P1S RELATED DB: PDB
DBREF 3P1R A 1 231 UNP P31947 1433S_HUMAN 1 231
DBREF 3P1R P 369 374 UNP Q9NPC2 KCNK9_HUMAN 369 374
SEQADV 3P1R GLY A -4 UNP P31947 EXPRESSION TAG
SEQADV 3P1R ALA A -3 UNP P31947 EXPRESSION TAG
SEQADV 3P1R MET A -2 UNP P31947 EXPRESSION TAG
SEQADV 3P1R GLY A -1 UNP P31947 EXPRESSION TAG
SEQADV 3P1R SER A 0 UNP P31947 EXPRESSION TAG
SEQADV 3P1R VAL A 38 UNP P31947 CYS 38 ENGINEERED MUTATION
SEQADV 3P1R HIS A 166 UNP P31947 ASN 166 ENGINEERED MUTATION
SEQRES 1 A 236 GLY ALA MET GLY SER MET GLU ARG ALA SER LEU ILE GLN
SEQRES 2 A 236 LYS ALA LYS LEU ALA GLU GLN ALA GLU ARG TYR GLU ASP
SEQRES 3 A 236 MET ALA ALA PHE MET LYS GLY ALA VAL GLU LYS GLY GLU
SEQRES 4 A 236 GLU LEU SER VAL GLU GLU ARG ASN LEU LEU SER VAL ALA
SEQRES 5 A 236 TYR LYS ASN VAL VAL GLY GLY GLN ARG ALA ALA TRP ARG
SEQRES 6 A 236 VAL LEU SER SER ILE GLU GLN LYS SER ASN GLU GLU GLY
SEQRES 7 A 236 SER GLU GLU LYS GLY PRO GLU VAL ARG GLU TYR ARG GLU
SEQRES 8 A 236 LYS VAL GLU THR GLU LEU GLN GLY VAL CYS ASP THR VAL
SEQRES 9 A 236 LEU GLY LEU LEU ASP SER HIS LEU ILE LYS GLU ALA GLY
SEQRES 10 A 236 ASP ALA GLU SER ARG VAL PHE TYR LEU LYS MET LYS GLY
SEQRES 11 A 236 ASP TYR TYR ARG TYR LEU ALA GLU VAL ALA THR GLY ASP
SEQRES 12 A 236 ASP LYS LYS ARG ILE ILE ASP SER ALA ARG SER ALA TYR
SEQRES 13 A 236 GLN GLU ALA MET ASP ILE SER LYS LYS GLU MET PRO PRO
SEQRES 14 A 236 THR HIS PRO ILE ARG LEU GLY LEU ALA LEU ASN PHE SER
SEQRES 15 A 236 VAL PHE HIS TYR GLU ILE ALA ASN SER PRO GLU GLU ALA
SEQRES 16 A 236 ILE SER LEU ALA LYS THR THR PHE ASP GLU ALA MET ALA
SEQRES 17 A 236 ASP LEU HIS THR LEU SER GLU ASP SER TYR LYS ASP SER
SEQRES 18 A 236 THR LEU ILE MET GLN LEU LEU ARG ASP ASN LEU THR LEU
SEQRES 19 A 236 TRP THR
SEQRES 1 P 6 LYS ARG ARG LYS SEP VAL
MODRES 3P1R SEP P 373 SER PHOSPHOSERINE
HET SEP P 373 10
HET MG A 249 1
HET MG A 250 1
HET MG A 251 1
HET CL A 252 1
HET CL A 253 1
HET CL A 254 1
HET CL A 255 1
HET CA A 256 1
HET MG A 257 1
HETNAM SEP PHOSPHOSERINE
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
HETNAM CA CALCIUM ION
HETSYN SEP PHOSPHONOSERINE
FORMUL 2 SEP C3 H8 N O6 P
FORMUL 3 MG 4(MG 2+)
FORMUL 6 CL 4(CL 1-)
FORMUL 10 CA CA 2+
FORMUL 12 HOH *366(H2 O)
HELIX 1 1 GLU A 2 ALA A 16 1 15
HELIX 2 2 ARG A 18 LYS A 32 1 15
HELIX 3 3 SER A 37 ASN A 70 1 34
HELIX 4 4 PRO A 79 SER A 105 1 27
HELIX 5 5 HIS A 106 ALA A 111 1 6
HELIX 6 6 ASP A 113 ALA A 135 1 23
HELIX 7 7 ASP A 139 MET A 162 1 24
HELIX 8 8 HIS A 166 ILE A 183 1 18
HELIX 9 9 SER A 186 ALA A 203 1 18
HELIX 10 10 ASP A 204 LEU A 208 5 5
HELIX 11 11 SER A 209 THR A 231 1 23
LINK C LYS P 372 N SEP P 373 1555 1555 1.35
LINK C SEP P 373 N VAL P 374 1555 1555 1.34
LINK OE1 GLU A 2 MG MG A 250 1555 1555 2.31
LINK OE1BGLN A 8 MG MG A 257 1555 1555 2.45
LINK OE1 GLU A 75 MG MG A 249 1555 1555 2.26
LINK OE2 GLU A 188 CA CA A 256 1555 1555 2.36
LINK O ASP A 215 MG MG A 251 1555 1555 2.84
LINK MG MG A 249 O HOH A 309 1555 1555 2.54
LINK MG MG A 249 O HOH A 536 1555 1555 2.38
LINK MG MG A 250 O HOH A 283 1555 1555 2.57
LINK MG MG A 250 O HOH A 364 1555 1555 2.19
LINK MG MG A 250 O HOH A 365 1555 1555 2.61
LINK MG MG A 251 O HOH A 300 1555 1555 2.71
LINK CA CA A 256 O HOH A 483 1555 1555 2.32
LINK MG MG A 257 O HOH A 538 1555 1555 2.41
CISPEP 1 SER A 105 HIS A 106 0 10.62
SITE 1 AC1 5 GLU A 75 GLU A 161 HOH A 309 HOH A 498
SITE 2 AC1 5 HOH A 536
SITE 1 AC2 4 GLU A 2 HOH A 283 HOH A 364 HOH A 365
SITE 1 AC3 5 ASP A 215 LEU A 218 ILE A 219 HOH A 300
SITE 2 AC3 5 HOH A 496
SITE 1 AC4 4 LYS A 9 LYS A 87 HOH A 456 HOH A 478
SITE 1 AC5 4 LYS A 124 ALA A 150 GLU A 153 HOH A 409
SITE 1 AC6 4 TYR A 19 GLU A 20 HOH A 367 HOH A 499
SITE 1 AC7 4 THR A 228 THR A 231 HOH A 277 HOH A 291
SITE 1 AC8 6 GLU A 35 GLU A 110 GLU A 188 HOH A 444
SITE 2 AC8 6 HOH A 457 HOH A 483
SITE 1 AC9 6 GLN A 8 LYS A 77 GLU A 80 HOH A 438
SITE 2 AC9 6 HOH A 538 HOH A 590
CRYST1 82.320 112.290 62.690 90.00 90.00 90.00 C 2 2 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 0.012148 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008906 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015952 0.00000
(ATOM LINES ARE NOT SHOWN.)
END