HEADER METAL BINDING PROTEIN 15-JAN-08 3BYA
TITLE STRUCTURE OF A CALMODULIN COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALMODULIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CAM;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: GLUTAMATE [NMDA] RECEPTOR SUBUNIT ZETA-1 PEPTIDE;
COMPND 8 CHAIN: B;
COMPND 9 SYNONYM: N-METHYL-D-ASPARTATE RECEPTOR SUBUNIT NR1;
COMPND 10 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: CALM1, CALM, CAM, CAM1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: C41;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PTYB12;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 OTHER_DETAILS: SYNTHETIC PEPTIDE. THE SEQUENCE IS NATURALLY FOUND IN
SOURCE 14 HUMAN (HOMO SAPIENS).
KEYWDS CALMODULIN, EF HAND MOTIF, NR1, N-METHYL-D-ASPARTATE RECEPTOR,
KEYWDS 2 GLUTAMATE, CENTRAL NERVOUS SYSTEM, NEURONAL CHANNEL, CALCIUM
KEYWDS 3 CHANNEL, METHYLATION, PHOSPHOPROTEIN, CELL JUNCTION, GLYCOPROTEIN,
KEYWDS 4 ION TRANSPORT, IONIC CHANNEL, MAGNESIUM, MEMBRANE, POSTSYNAPTIC CELL
KEYWDS 5 MEMBRANE, SYNAPSE, TRANSMEMBRANE, TRANSPORT, METAL BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR G.BIRRANE,A.SONI,J.A.A.LADIAS
REVDAT 3 30-AUG-23 3BYA 1 REMARK
REVDAT 2 13-JUL-11 3BYA 1 VERSN
REVDAT 1 20-JAN-09 3BYA 0
JRNL AUTH G.BIRRANE,A.SONI,J.A.A.LADIAS
JRNL TITL STRUCTURE OF A CALMODULIN COMPLEX
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.74
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 13948
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) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 735
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) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1005
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.98
REMARK 3 BIN R VALUE (WORKING SET) : 0.1990
REMARK 3 BIN FREE R VALUE SET COUNT : 62
REMARK 3 BIN FREE R VALUE : 0.2850
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1239
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 79
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 25.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.06000
REMARK 3 B22 (A**2) : 0.01000
REMARK 3 B33 (A**2) : -0.05000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.04000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.136
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.136
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.096
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.438
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.930
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1288 ; 0.020 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 879 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1733 ; 1.682 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2156 ; 0.998 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 166 ; 5.330 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 70 ;35.591 ;25.857
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 251 ;15.499 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;21.340 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 192 ; 0.107 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1454 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 250 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 409 ; 0.241 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 937 ; 0.193 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 660 ; 0.187 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 649 ; 0.089 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 63 ; 0.195 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 16 ; 0.166 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 10 ; 0.139 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 30 ; 0.279 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 11 ; 0.167 ; 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): 832 ; 1.244 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 327 ; 0.320 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1276 ; 1.810 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 520 ; 3.013 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 451 ; 4.485 ; 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 : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 3 A 73
REMARK 3 ORIGIN FOR THE GROUP (A): 23.4130 -4.0310 17.9680
REMARK 3 T TENSOR
REMARK 3 T11: 0.1144 T22: 0.4711
REMARK 3 T33: -0.0416 T12: 0.0949
REMARK 3 T13: -0.0227 T23: -0.0909
REMARK 3 L TENSOR
REMARK 3 L11: 9.8289 L22: 1.8661
REMARK 3 L33: 3.4434 L12: -3.0475
REMARK 3 L13: -1.9108 L23: -0.7020
REMARK 3 S TENSOR
REMARK 3 S11: -0.1775 S12: -2.2159 S13: 0.4514
REMARK 3 S21: 0.3666 S22: 0.6046 S23: -0.1247
REMARK 3 S31: -0.4048 S32: -0.1021 S33: -0.4272
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 81 A 95
REMARK 3 ORIGIN FOR THE GROUP (A): 17.1900 8.6950 3.0140
REMARK 3 T TENSOR
REMARK 3 T11: -0.1420 T22: -0.1470
REMARK 3 T33: 0.0023 T12: 0.0009
REMARK 3 T13: -0.0237 T23: -0.0166
REMARK 3 L TENSOR
REMARK 3 L11: 6.8019 L22: 5.2158
REMARK 3 L33: 7.4175 L12: 0.1178
REMARK 3 L13: 2.9855 L23: 2.1627
REMARK 3 S TENSOR
REMARK 3 S11: 0.1415 S12: 0.0340 S13: -0.1205
REMARK 3 S21: -0.0512 S22: 0.0399 S23: -0.6263
REMARK 3 S31: -0.2629 S32: 0.5229 S33: -0.1814
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 96 A 146
REMARK 3 ORIGIN FOR THE GROUP (A): 6.5270 2.2890 7.0410
REMARK 3 T TENSOR
REMARK 3 T11: -0.1014 T22: -0.1434
REMARK 3 T33: -0.0208 T12: 0.0250
REMARK 3 T13: 0.0029 T23: 0.0858
REMARK 3 L TENSOR
REMARK 3 L11: 6.3081 L22: 2.3269
REMARK 3 L33: 1.8259 L12: -3.2728
REMARK 3 L13: -0.2863 L23: 0.9149
REMARK 3 S TENSOR
REMARK 3 S11: -0.2787 S12: -0.6455 S13: -0.8690
REMARK 3 S21: 0.1819 S22: 0.2580 S23: 0.3541
REMARK 3 S31: 0.1946 S32: 0.1136 S33: 0.0206
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 875 B 894
REMARK 3 ORIGIN FOR THE GROUP (A): 18.8740 3.7530 11.9340
REMARK 3 T TENSOR
REMARK 3 T11: 0.0403 T22: -0.0773
REMARK 3 T33: -0.0075 T12: 0.1197
REMARK 3 T13: -0.0322 T23: -0.0151
REMARK 3 L TENSOR
REMARK 3 L11: 16.4895 L22: 6.0209
REMARK 3 L33: 4.0023 L12: -0.7201
REMARK 3 L13: -2.9325 L23: 1.0760
REMARK 3 S TENSOR
REMARK 3 S11: -0.1725 S12: -0.7766 S13: 0.7098
REMARK 3 S21: 0.6035 S22: 0.3925 S23: -0.6681
REMARK 3 S31: -0.4301 S32: -0.1298 S33: -0.2200
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 3BYA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JAN-08.
REMARK 100 THE DEPOSITION ID IS D_1000046107.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-SEP-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X12B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14639
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.04000
REMARK 200 R SYM (I) : 0.04300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 28.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.92
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.29800
REMARK 200 R SYM FOR SHELL (I) : 0.33200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.600
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 1IWQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 17-19% PEG 3350, 0.120MM AMMONIUM
REMARK 280 PHOSPHATE, 15% ETHYLENE GLYCOL, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K, PH 7
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 33.88400
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 21.36850
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 33.88400
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 21.36850
REMARK 290 SMTRY3 4 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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS THE MONOMER CONTAINED IN THE
REMARK 300 ASYMMETRIC UNIT
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: 3080 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 153 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 223 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 ALA A 1
REMARK 465 ASP A 2
REMARK 465 ARG A 74
REMARK 465 LYS A 75
REMARK 465 MET A 76
REMARK 465 LYS A 77
REMARK 465 ASP A 78
REMARK 465 THR A 79
REMARK 465 ASP A 80
REMARK 465 ALA A 147
REMARK 465 LYS A 148
REMARK 465 ARG B 895
REMARK 465 SER B 896
REMARK 465 SER B 897
REMARK 465 LYS B 898
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 OE1 GLU A 45 O HOH A 220 2.12
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 45 CD GLU A 45 OE2 0.070
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 MET A 36 CG - SD - CE ANGL. DEV. = -9.9 DEGREES
REMARK 500 ARG A 106 NE - CZ - NH1 ANGL. DEV. = 3.7 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 B 876 23.25 -67.51
REMARK 500 ARG B 893 35.70 -94.58
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 152 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 20 OD1
REMARK 620 2 ASP A 22 OD1 87.6
REMARK 620 3 ASP A 24 OD1 90.5 80.0
REMARK 620 4 THR A 26 O 79.6 159.0 83.5
REMARK 620 5 GLU A 31 OE1 106.2 128.0 146.9 72.1
REMARK 620 6 GLU A 31 OE2 95.1 78.4 157.4 119.1 51.1
REMARK 620 7 HOH A 176 O 164.9 77.9 82.9 112.9 86.3 86.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 151 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 56 OD1
REMARK 620 2 ASP A 58 OD1 83.0
REMARK 620 3 ASN A 60 OD1 87.1 76.0
REMARK 620 4 THR A 62 O 75.1 150.8 83.8
REMARK 620 5 GLU A 67 OE1 71.6 118.6 151.4 72.6
REMARK 620 6 GLU A 67 OE2 85.3 76.5 152.2 119.8 47.2
REMARK 620 7 HOH A 226 O 167.5 85.2 86.0 114.3 118.2 96.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 150 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 93 OD1
REMARK 620 2 ASP A 95 OD1 85.6
REMARK 620 3 ASN A 97 OD1 86.6 77.7
REMARK 620 4 TYR A 99 O 85.9 154.2 77.5
REMARK 620 5 GLU A 104 OE1 105.8 127.9 151.5 77.9
REMARK 620 6 GLU A 104 OE2 100.3 74.6 150.8 131.0 53.4
REMARK 620 7 HOH A 157 O 164.2 79.5 85.4 105.5 87.5 80.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 149 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 129 OD1
REMARK 620 2 ASP A 131 OD1 82.9
REMARK 620 3 ASP A 133 OD1 96.9 79.4
REMARK 620 4 GLN A 135 O 86.4 156.4 81.1
REMARK 620 5 GLU A 140 OE1 107.2 124.4 147.3 78.9
REMARK 620 6 GLU A 140 OE2 82.8 77.7 156.9 121.8 51.1
REMARK 620 7 HOH A 156 O 166.1 83.6 77.5 105.0 83.1 97.3
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 149
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 150
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 151
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 152
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2HQW RELATED DB: PDB
REMARK 900 A STRUCTURE OF THE SAME COMPLEX IN A DIFFERENCE SPACE GROUP
REMARK 900 RELATED ID: 1EXR RELATED DB: PDB
REMARK 900 A HIGH RESOLUTION STRUCTURE OF CALMODULIN
DBREF 3BYA A 1 148 UNP P62158 CALM_HUMAN 2 149
DBREF 3BYA B 875 898 UNP Q05586 NMDZ1_HUMAN 875 898
SEQRES 1 A 148 ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS
SEQRES 2 A 148 GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR
SEQRES 3 A 148 ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU
SEQRES 4 A 148 GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE
SEQRES 5 A 148 ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE
SEQRES 6 A 148 PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP
SEQRES 7 A 148 THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL
SEQRES 8 A 148 PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA GLU
SEQRES 9 A 148 LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR
SEQRES 10 A 148 ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE
SEQRES 11 A 148 ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL GLN
SEQRES 12 A 148 MET MET THR ALA LYS
SEQRES 1 B 24 LYS LYS LYS ALA THR PHE ARG ALA ILE THR SER THR LEU
SEQRES 2 B 24 ALA SER SER PHE LYS ARG ARG ARG SER SER LYS
HET CA A 149 1
HET CA A 150 1
HET CA A 151 1
HET CA A 152 1
HETNAM CA CALCIUM ION
FORMUL 3 CA 4(CA 2+)
FORMUL 7 HOH *79(H2 O)
HELIX 1 1 THR A 5 ASP A 20 1 16
HELIX 2 2 THR A 28 LEU A 39 1 12
HELIX 3 3 THR A 44 GLU A 54 1 11
HELIX 4 4 ASP A 64 MET A 72 1 9
HELIX 5 5 SER A 81 ASP A 93 1 13
HELIX 6 6 SER A 101 GLY A 113 1 13
HELIX 7 7 THR A 117 ASP A 129 1 13
HELIX 8 8 TYR A 138 THR A 146 1 9
HELIX 9 9 LYS B 876 ARG B 893 1 18
SHEET 1 A 2 TYR A 99 ILE A 100 0
SHEET 2 A 2 VAL A 136 ASN A 137 -1 O VAL A 136 N ILE A 100
LINK OD1 ASP A 20 CA CA A 152 1555 1555 2.07
LINK OD1 ASP A 22 CA CA A 152 1555 1555 2.15
LINK OD1 ASP A 24 CA CA A 152 1555 1555 2.44
LINK O THR A 26 CA CA A 152 1555 1555 2.17
LINK OE1 GLU A 31 CA CA A 152 1555 1555 2.53
LINK OE2 GLU A 31 CA CA A 152 1555 1555 2.51
LINK OD1 ASP A 56 CA CA A 151 1555 1555 2.40
LINK OD1 ASP A 58 CA CA A 151 1555 1555 2.34
LINK OD1 ASN A 60 CA CA A 151 1555 1555 2.11
LINK O THR A 62 CA CA A 151 1555 1555 2.37
LINK OE1 GLU A 67 CA CA A 151 1555 1555 2.84
LINK OE2 GLU A 67 CA CA A 151 1555 1555 2.63
LINK OD1 ASP A 93 CA CA A 150 1555 1555 2.30
LINK OD1 ASP A 95 CA CA A 150 1555 1555 2.33
LINK OD1 ASN A 97 CA CA A 150 1555 1555 2.40
LINK O TYR A 99 CA CA A 150 1555 1555 2.35
LINK OE1 GLU A 104 CA CA A 150 1555 1555 2.43
LINK OE2 GLU A 104 CA CA A 150 1555 1555 2.50
LINK OD1 ASP A 129 CA CA A 149 1555 1555 2.31
LINK OD1 ASP A 131 CA CA A 149 1555 1555 2.37
LINK OD1 ASP A 133 CA CA A 149 1555 1555 2.34
LINK O GLN A 135 CA CA A 149 1555 1555 2.28
LINK OE1 GLU A 140 CA CA A 149 1555 1555 2.46
LINK OE2 GLU A 140 CA CA A 149 1555 1555 2.60
LINK CA CA A 149 O HOH A 156 1555 1555 2.38
LINK CA CA A 150 O HOH A 157 1555 1555 2.43
LINK CA CA A 151 O HOH A 226 1555 1555 2.97
LINK CA CA A 152 O HOH A 176 1555 1555 2.43
SITE 1 AC1 5 ASP A 129 ASP A 131 ASP A 133 GLN A 135
SITE 2 AC1 5 GLU A 140
SITE 1 AC2 5 ASP A 93 ASP A 95 ASN A 97 TYR A 99
SITE 2 AC2 5 GLU A 104
SITE 1 AC3 5 ASP A 56 ASP A 58 ASN A 60 THR A 62
SITE 2 AC3 5 GLU A 67
SITE 1 AC4 5 ASP A 20 ASP A 22 ASP A 24 THR A 26
SITE 2 AC4 5 GLU A 31
CRYST1 67.768 42.737 62.012 90.00 106.92 90.00 C 1 2 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 0.014756 0.000000 0.004489 0.00000
SCALE2 0.000000 0.023399 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016855 0.00000
(ATOM LINES ARE NOT SHOWN.)
END