HEADER PROTEIN BINDING/INHIBITOR 25-JUN-12 4FQO
TITLE CRYSTAL STRUCTURE OF CALCIUM-LOADED S100B BOUND TO SBI4211
CAVEAT 4FQO SOME CLOSE CONTACTS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN S100-B;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: S-100 PROTEIN BETA CHAIN, S-100 PROTEIN SUBUNIT BETA, S100
COMPND 5 CALCIUM-BINDING PROTEIN B
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: BOVINE;
SOURCE 4 ORGANISM_TAXID: 9913
KEYWDS PROTEIN-INHIBITOR COMPLEX, EF-HAND PROTEIN, CALCIUM BINDING PROTEIN,
KEYWDS 2 PROTEIN BINDING-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR L.E.MCKNIGHT,E.P.RAMAN,P.BEZAWADA,S.KUDRIMOTI,P.T.WILDER,K.G.HARTMAN,
AUTHOR 2 E.A.TOTH,A.COOP,A.D.MACKERRELL,D.J.WEBER
REVDAT 5 13-MAR-24 4FQO 1 COMPND SOURCE
REVDAT 4 28-FEB-24 4FQO 1 REMARK LINK
REVDAT 3 15-NOV-17 4FQO 1 REMARK
REVDAT 2 16-JAN-13 4FQO 1 JRNL
REVDAT 1 17-OCT-12 4FQO 0
JRNL AUTH L.E.MCKNIGHT,E.P.RAMAN,P.BEZAWADA,S.KUDRIMOTI,P.T.WILDER,
JRNL AUTH 2 K.G.HARTMAN,R.GODOY-RUIZ,E.A.TOTH,A.COOP,A.D.MACKERELL,
JRNL AUTH 3 D.J.WEBER
JRNL TITL STRUCTURE-BASED DISCOVERY OF A NOVEL PENTAMIDINE-RELATED
JRNL TITL 2 INHIBITOR OF THE CALCIUM-BINDING PROTEIN S100B.
JRNL REF ACS MED CHEM LETT V. 3 975 2012
JRNL REFN ISSN 1948-5875
JRNL PMID 23264854
JRNL DOI 10.1021/ML300166S
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC REFMAC_5.5.0102
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) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.60
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 12291
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) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 590
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) : 1.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.70
REMARK 3 REFLECTION IN BIN (WORKING SET) : 832
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.89
REMARK 3 BIN R VALUE (WORKING SET) : 0.2130
REMARK 3 BIN FREE R VALUE SET COUNT : 48
REMARK 3 BIN FREE R VALUE : 0.2500
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 712
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 29
REMARK 3 SOLVENT ATOMS : 89
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.35
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.54000
REMARK 3 B22 (A**2) : -0.54000
REMARK 3 B33 (A**2) : 1.07000
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): 0.106
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.097
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.068
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.353
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.959
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 767 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1027 ; 1.434 ; 1.996
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 94 ; 5.261 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 38 ;34.464 ;26.579
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 150 ;13.700 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 1 ;25.469 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 110 ; 0.102 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 571 ; 0.006 ; 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): 449 ; 0.873 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 723 ; 1.526 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 318 ; 2.444 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 301 ; 4.005 ; 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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 4
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 88
REMARK 3 RESIDUE RANGE : A 101 A 102
REMARK 3 RESIDUE RANGE : A 103 A 103
REMARK 3 RESIDUE RANGE : A 201 A 289
REMARK 3 ORIGIN FOR THE GROUP (A): 13.9566 1.0265 9.6102
REMARK 3 T TENSOR
REMARK 3 T11: 0.0811 T22: 0.0415
REMARK 3 T33: 0.0662 T12: 0.0023
REMARK 3 T13: -0.0222 T23: 0.0291
REMARK 3 L TENSOR
REMARK 3 L11: 3.8548 L22: 2.0414
REMARK 3 L33: 2.3793 L12: 0.3375
REMARK 3 L13: -1.6180 L23: -0.2767
REMARK 3 S TENSOR
REMARK 3 S11: 0.0696 S12: -0.0380 S13: 0.2210
REMARK 3 S21: 0.1986 S22: -0.0533 S23: -0.2576
REMARK 3 S31: -0.1904 S32: 0.0698 S33: -0.0163
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 U VALUES : RESIDUAL ONLY
REMARK 4
REMARK 4 4FQO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JUN-12.
REMARK 100 THE DEPOSITION ID IS D_1000073234.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-JUL-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.21
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 MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12333
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 13.50
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.68
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 13.50
REMARK 200 R MERGE FOR SHELL (I) : 0.65100
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, SODIUM CACODYLATE, CALCIUM
REMARK 280 CHLORIDE, PH 7.21, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
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 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 24.49900
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 31.53950
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 31.53950
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 12.24950
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 31.53950
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 31.53950
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 36.74850
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 31.53950
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 31.53950
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 12.24950
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 31.53950
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 31.53950
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 36.74850
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 24.49900
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: 3130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -82.0 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 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 24.49900
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 PHE A 88 CG CD1 CD2 CE1 CE2 CZ
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 H LYS A 48 O HOH A 242 1.58
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 HE1 HIS A 15 HE1 HIS A 85 8555 0.52
REMARK 500 HH22 ARG A 20 O HOH A 232 7555 1.58
REMARK 500 HE1 HIS A 15 CE1 HIS A 85 8555 1.59
REMARK 500 CE1 HIS A 15 HE1 HIS A 85 8555 1.60
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 20 NE - CZ - NH1 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 PHE A 87 67.55 30.47
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 101 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 18 O
REMARK 620 2 GLU A 21 O 102.0
REMARK 620 3 ASP A 23 O 83.4 86.1
REMARK 620 4 LYS A 26 O 90.3 162.6 83.0
REMARK 620 5 GLU A 31 OE1 103.3 113.1 157.2 75.3
REMARK 620 6 GLU A 31 OE2 77.0 75.7 149.7 119.6 52.1
REMARK 620 7 HOH A 206 O 171.2 82.0 89.0 84.3 82.1 111.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 102 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 61 OD1
REMARK 620 2 ASP A 63 OD1 83.5
REMARK 620 3 ASP A 65 OD1 85.9 85.4
REMARK 620 4 GLU A 67 O 87.0 161.5 78.1
REMARK 620 5 GLU A 72 OE1 113.9 123.2 145.5 75.2
REMARK 620 6 GLU A 72 OE2 87.4 78.3 163.0 117.2 51.1
REMARK 620 7 HOH A 212 O 163.0 87.1 79.2 97.9 83.1 104.5
REMARK 620 N 1 2 3 4 5 6
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 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZ3 A 103
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3CR4 RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF BOVINE S100B-CA2+-PNT
DBREF 4FQO A 0 88 UNP P02638 S100B_BOVIN 1 89
SEQRES 1 A 89 MET SER GLU LEU GLU LYS ALA VAL VAL ALA LEU ILE ASP
SEQRES 2 A 89 VAL PHE HIS GLN TYR SER GLY ARG GLU GLY ASP LYS HIS
SEQRES 3 A 89 LYS LEU LYS LYS SER GLU LEU LYS GLU LEU ILE ASN ASN
SEQRES 4 A 89 GLU LEU SER HIS PHE LEU GLU GLU ILE LYS GLU GLN GLU
SEQRES 5 A 89 VAL VAL ASP LYS VAL MET GLU THR LEU ASP SER ASP GLY
SEQRES 6 A 89 ASP GLY GLU CYS ASP PHE GLN GLU PHE MET ALA PHE VAL
SEQRES 7 A 89 ALA MET ILE THR THR ALA CYS HIS GLU PHE PHE
HET CA A 101 1
HET CA A 102 1
HET AZ3 A 103 27
HETNAM CA CALCIUM ION
HETNAM AZ3 4,4'-[HEPTANE-1,7-DIYLBIS(OXY)]DIBENZENECARBOXIMIDAMIDE
FORMUL 2 CA 2(CA 2+)
FORMUL 4 AZ3 C21 H28 N4 O2
FORMUL 5 HOH *89(H2 O)
HELIX 1 1 SER A 1 GLY A 19 1 19
HELIX 2 2 LYS A 28 LEU A 40 1 13
HELIX 3 3 GLU A 49 ASP A 61 1 13
HELIX 4 4 ASP A 69 GLU A 86 1 18
LINK O SER A 18 CA CA A 101 1555 1555 2.31
LINK O GLU A 21 CA CA A 101 1555 1555 2.43
LINK O ASP A 23 CA CA A 101 1555 1555 2.36
LINK O LYS A 26 CA CA A 101 1555 1555 2.38
LINK OE1 GLU A 31 CA CA A 101 1555 1555 2.43
LINK OE2 GLU A 31 CA CA A 101 1555 1555 2.45
LINK OD1 ASP A 61 CA CA A 102 1555 1555 2.26
LINK OD1 ASP A 63 CA CA A 102 1555 1555 2.33
LINK OD1 ASP A 65 CA CA A 102 1555 1555 2.41
LINK O GLU A 67 CA CA A 102 1555 1555 2.38
LINK OE1 GLU A 72 CA CA A 102 1555 1555 2.48
LINK OE2 GLU A 72 CA CA A 102 1555 1555 2.62
LINK CA CA A 101 O HOH A 206 1555 1555 2.40
LINK CA CA A 102 O HOH A 212 1555 1555 2.26
SITE 1 AC1 6 SER A 18 GLU A 21 ASP A 23 LYS A 26
SITE 2 AC1 6 GLU A 31 HOH A 206
SITE 1 AC2 6 ASP A 61 ASP A 63 ASP A 65 GLU A 67
SITE 2 AC2 6 GLU A 72 HOH A 212
SITE 1 AC3 12 MET A 0 VAL A 8 ILE A 11 ASP A 12
SITE 2 AC3 12 HIS A 42 PHE A 43 CYS A 84 HIS A 85
SITE 3 AC3 12 PHE A 87 PHE A 88 HOH A 274 HOH A 288
CRYST1 63.079 63.079 48.998 90.00 90.00 90.00 P 41 21 2 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 0.015853 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015853 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020409 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
