HEADER PROTEIN BINDING/INHIBITOR 20-JUL-11 3T0M
TITLE SMALL-MOLECULE INHIBITORS OF 14-3-3 PROTEIN-PROTEIN INTERACTIONS FROM
TITLE 2 VIRTUAL SCREENING
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 14-3-3 PROTEIN SIGMA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 1-231;
COMPND 5 SYNONYM: EPITHELIAL CELL MARKER PROTEIN 1, STRATIFIN;
COMPND 6 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: HME1, SFN;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPROEX HTB
KEYWDS HELICAL PROTEIN, ADAPTER PROTEIN, PROTEIN-PROTEIN INTERACTION,
KEYWDS 2 PROTEIN BINDING-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR P.THIEL,C.OTTMANN
REVDAT 3 28-FEB-24 3T0M 1 REMARK SEQADV LINK
REVDAT 2 04-SEP-13 3T0M 1 JRNL
REVDAT 1 26-DEC-12 3T0M 0
JRNL AUTH P.THIEL,L.ROGLIN,N.MEISSNER,S.HENNIG,O.KOHLBACHER,C.OTTMANN
JRNL TITL VIRTUAL SCREENING AND EXPERIMENTAL VALIDATION REVEAL NOVEL
JRNL TITL 2 SMALL-MOLECULE INHIBITORS OF 14-3-3 PROTEIN-PROTEIN
JRNL TITL 3 INTERACTIONS.
JRNL REF CHEM.COMMUN.(CAMB.) V. 49 8468 2013
JRNL REFN ISSN 1359-7345
JRNL PMID 23939230
JRNL DOI 10.1039/C3CC44612C
REMARK 2
REMARK 2 RESOLUTION. 1.62 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 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.62
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.42
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 34642
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) : 0.157
REMARK 3 R VALUE (WORKING SET) : 0.155
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1824
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) : 1.62
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.66
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2489
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.1950
REMARK 3 BIN FREE R VALUE SET COUNT : 131
REMARK 3 BIN FREE R VALUE : 0.2480
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1807
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 42
REMARK 3 SOLVENT ATOMS : 333
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.42
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.17
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.87000
REMARK 3 B22 (A**2) : -0.38000
REMARK 3 B33 (A**2) : -0.49000
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): 0.087
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.052
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.468
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2187 ; 0.026 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3013 ; 2.223 ; 2.011
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 313 ; 5.656 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 107 ;40.176 ;24.673
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 439 ;13.707 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;15.429 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 331 ; 0.164 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1695 ; 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): 1290 ; 1.405 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2125 ; 2.306 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 897 ; 3.665 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 841 ; 5.875 ; 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: U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 3T0M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUL-11.
REMARK 100 THE DEPOSITION ID IS D_1000066886.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-MAY-11; 14-APR-11
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; N
REMARK 200 RADIATION SOURCE : SLS; ROTATING ANODE
REMARK 200 BEAMLINE : X10SA; NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL; RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9778; 1.5418
REMARK 200 MONOCHROMATOR : SI(111) MONOCHROMATOR
REMARK 200 (HORIZONTAL), DYNAMICALLY
REMARK 200 BENDABLE MIRROR (VERTICAL); NULL
REMARK 200 OPTICS : NULL; MULTILAYER MIRRORS
REMARK 200 (VARIMAX)
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL; IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M; MAR SCANNER
REMARK 200 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE, XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36467
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.620
REMARK 200 RESOLUTION RANGE LOW (A) : 45.420
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 6.730
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.8700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.62
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.38800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.040
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.2.1
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.095M HEPES NA SALT, 0.19M CALCIUM
REMARK 280 CHLORIDE, 5% GLYCEROL, 25.6% PEG 400, PH 7.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, 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 31.18500
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 31.18500
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 41.04500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 56.15000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 41.04500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 56.15000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 31.18500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 41.04500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 56.15000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 31.18500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 41.04500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 56.15000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.0 KCAL/MOL
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 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 503 LIES ON A SPECIAL POSITION.
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 GLU A 71
REMARK 465 GLU A 72
REMARK 465 GLY A 73
REMARK 465 SER A 74
REMARK 465 GLU A 75
REMARK 465 GLU A 76
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 OD1 ASP A 145 O HOH A 472 2.05
REMARK 500 OE1 GLU A 86 O HOH A 377 2.15
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 O HOH A 430 O HOH A 461 3555 2.16
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 CYS A 96 CB CYS A 96 SG -0.097
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 - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG A 3 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 85 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 85 NE - CZ - NH2 ANGL. DEV. = -3.1 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 -2 8.09 -63.74
REMARK 500 ARG A 18 79.17 -107.90
REMARK 500 HIS A 106 38.17 -146.30
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 ALA A -3 MET A -2 142.20
REMARK 500 ASP A 138 ASP A 139 135.33
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 238 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 2 OE1
REMARK 620 2 HOH A 334 O 137.1
REMARK 620 3 HOH A 334 O 173.5 49.2
REMARK 620 4 HOH A 338 O 70.3 66.9 115.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 239 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 35 OE1
REMARK 620 2 GLU A 35 OE2 50.6
REMARK 620 3 GLU A 110 O 87.6 87.2
REMARK 620 4 HOH A 279 O 162.1 142.4 103.4
REMARK 620 5 HOH A 337 O 82.8 87.0 170.4 85.7
REMARK 620 6 HOH A 520 O 79.6 130.1 87.5 86.9 90.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 237 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 228 O
REMARK 620 2 THR A 231 OXT 87.8
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 2CT A 232
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 233
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 234
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 235
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 236
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 237
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 238
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 239
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3LW1 RELATED DB: PDB
REMARK 900 RELATED ID: 3MHR RELATED DB: PDB
REMARK 900 RELATED ID: 3T0L RELATED DB: PDB
REMARK 900 RELATED ID: 3U9X RELATED DB: PDB
REMARK 900 RELATED ID: 4DHM RELATED DB: PDB
REMARK 900 RELATED ID: 4DHN RELATED DB: PDB
REMARK 900 RELATED ID: 4DHO RELATED DB: PDB
REMARK 900 RELATED ID: 4DHP RELATED DB: PDB
REMARK 900 RELATED ID: 4DHQ RELATED DB: PDB
REMARK 900 RELATED ID: 4DHR RELATED DB: PDB
REMARK 900 RELATED ID: 4DHS RELATED DB: PDB
REMARK 900 RELATED ID: 4DHT RELATED DB: PDB
REMARK 900 RELATED ID: 4DHU RELATED DB: PDB
DBREF 3T0M A 1 231 UNP P31947 1433S_HUMAN 1 231
SEQADV 3T0M ALA A -3 UNP P31947 EXPRESSION TAG
SEQADV 3T0M MET A -2 UNP P31947 EXPRESSION TAG
SEQADV 3T0M GLY A -1 UNP P31947 EXPRESSION TAG
SEQADV 3T0M SER A 0 UNP P31947 EXPRESSION TAG
SEQRES 1 A 235 ALA MET GLY SER MET GLU ARG ALA SER LEU ILE GLN LYS
SEQRES 2 A 235 ALA LYS LEU ALA GLU GLN ALA GLU ARG TYR GLU ASP MET
SEQRES 3 A 235 ALA ALA PHE MET LYS GLY ALA VAL GLU LYS GLY GLU GLU
SEQRES 4 A 235 LEU SER CYS GLU GLU ARG ASN LEU LEU SER VAL ALA TYR
SEQRES 5 A 235 LYS ASN VAL VAL GLY GLY GLN ARG ALA ALA TRP ARG VAL
SEQRES 6 A 235 LEU SER SER ILE GLU GLN LYS SER ASN GLU GLU GLY SER
SEQRES 7 A 235 GLU GLU LYS GLY PRO GLU VAL ARG GLU TYR ARG GLU LYS
SEQRES 8 A 235 VAL GLU THR GLU LEU GLN GLY VAL CYS ASP THR VAL LEU
SEQRES 9 A 235 GLY LEU LEU ASP SER HIS LEU ILE LYS GLU ALA GLY ASP
SEQRES 10 A 235 ALA GLU SER ARG VAL PHE TYR LEU LYS MET LYS GLY ASP
SEQRES 11 A 235 TYR TYR ARG TYR LEU ALA GLU VAL ALA THR GLY ASP ASP
SEQRES 12 A 235 LYS LYS ARG ILE ILE ASP SER ALA ARG SER ALA TYR GLN
SEQRES 13 A 235 GLU ALA MET ASP ILE SER LYS LYS GLU MET PRO PRO THR
SEQRES 14 A 235 ASN PRO ILE ARG LEU GLY LEU ALA LEU ASN PHE SER VAL
SEQRES 15 A 235 PHE HIS TYR GLU ILE ALA ASN SER PRO GLU GLU ALA ILE
SEQRES 16 A 235 SER LEU ALA LYS THR THR PHE ASP GLU ALA MET ALA ASP
SEQRES 17 A 235 LEU HIS THR LEU SER GLU ASP SER TYR LYS ASP SER THR
SEQRES 18 A 235 LEU ILE MET GLN LEU LEU ARG ASP ASN LEU THR LEU TRP
SEQRES 19 A 235 THR
HET 2CT A 232 38
HET GOL A 233 6
HET GOL A 234 6
HET CL A 235 1
HET CL A 236 1
HET MG A 237 1
HET MG A 238 1
HET MG A 239 1
HETNAM 2CT (2-{2-[(2,5-DIMETHOXYPHENYL)AMINO]-2-OXOETHOXY}PHENYL)
HETNAM 2 2CT PHOSPHONIC ACID
HETNAM GOL GLYCEROL
HETNAM CL CHLORIDE ION
HETNAM MG MAGNESIUM ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 2CT C16 H18 N O7 P
FORMUL 3 GOL 2(C3 H8 O3)
FORMUL 5 CL 2(CL 1-)
FORMUL 7 MG 3(MG 2+)
FORMUL 10 HOH *333(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 SER A 69 1 33
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 ASN 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 OE1 GLU A 2 MG MG A 238 1555 1555 2.69
LINK OE1 GLU A 35 MG MG A 239 1555 1555 2.11
LINK OE2 GLU A 35 MG MG A 239 1555 1555 2.73
LINK O GLU A 110 MG MG A 239 1555 1555 2.22
LINK O THR A 228 MG MG A 237 1555 1555 2.52
LINK OXT THR A 231 MG MG A 237 1555 1555 2.62
LINK MG MG A 238 O BHOH A 334 1555 1555 2.10
LINK MG MG A 238 O AHOH A 334 1555 1555 2.44
LINK MG MG A 238 O HOH A 338 1555 1555 2.69
LINK MG MG A 239 O HOH A 279 1555 1555 2.46
LINK MG MG A 239 O HOH A 337 1555 1555 2.39
LINK MG MG A 239 O HOH A 520 1555 1555 2.24
CISPEP 1 SER A 105 HIS A 106 0 9.48
SITE 1 AC1 18 LYS A 49 GLY A 53 ARG A 56 ALA A 57
SITE 2 AC1 18 ARG A 60 ARG A 129 TYR A 130 ASN A 175
SITE 3 AC1 18 HOH A 269 HOH A 293 HOH A 310 HOH A 319
SITE 4 AC1 18 HOH A 321 HOH A 324 HOH A 440 HOH A 479
SITE 5 AC1 18 HOH A 523 HOH A 541
SITE 1 AC2 6 GLU A 110 MET A 202 LEU A 205 THR A 217
SITE 2 AC2 6 ARG A 224 HOH A 333
SITE 1 AC3 10 GLU A 17 ARG A 18 TYR A 19 GLU A 20
SITE 2 AC3 10 ASP A 21 HOH A 275 HOH A 296 HOH A 367
SITE 3 AC3 10 HOH A 380 HOH A 559
SITE 1 AC4 3 LYS A 9 HOH A 253 HOH A 418
SITE 1 AC5 1 LYS A 109
SITE 1 AC6 2 THR A 228 THR A 231
SITE 1 AC7 3 GLU A 2 HOH A 334 HOH A 338
SITE 1 AC8 6 GLU A 35 GLU A 110 GLU A 188 HOH A 279
SITE 2 AC8 6 HOH A 337 HOH A 520
CRYST1 82.090 112.300 62.370 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 0.012182 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008905 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016033 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
