HEADER METAL BINDING PROTEIN 06-DEC-06 2O60
TITLE CALMODULIN BOUND TO PEPTIDE FROM NEURONAL NITRIC OXIDE SYNTHASE
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: PEPTIDE CORRESPONDING TO CALMODULIN BINDING DOMAIN OF
COMPND 8 NEURONAL NITRIC OXIDE SYNTHASE;
COMPND 9 CHAIN: B;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 GENE: CALM;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
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: PET 15B;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THIS SEQUENCE
SOURCE 14 OCCURS NATURALLY IN MICE. PEPTIDE IS ACETYLATED AT N-TERMINUS AND
SOURCE 15 AMIDATED AT C-TERMINUS.
KEYWDS PROTEIN-PEPTIDE COMPLEX, METAL BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR H.L.NG,T.ALBER,A.J.WAND
REVDAT 5 27-DEC-23 2O60 1 REMARK LINK
REVDAT 4 18-OCT-17 2O60 1 REMARK
REVDAT 3 13-JUL-11 2O60 1 VERSN
REVDAT 2 24-FEB-09 2O60 1 VERSN
REVDAT 1 25-DEC-07 2O60 0
JRNL AUTH K.G.VALENTINE,H.L.NG,L.SCHNEEWEIS,J.K.KRANZ,K.K.FREDERICK,
JRNL AUTH 2 T.ALBER,A.J.WAND
JRNL TITL CRYSTAL STRUCTURE OF CALMODULIN-NEURONAL NITRIC OXIDE
JRNL TITL 2 SYNTHASE COMPLEX
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
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) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 74.54
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 22393
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) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1208
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) : 1.55
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.59
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1673
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.89
REMARK 3 BIN R VALUE (WORKING SET) : 0.2050
REMARK 3 BIN FREE R VALUE SET COUNT : 80
REMARK 3 BIN FREE R VALUE : 0.2730
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1316
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 165
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.63
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.03000
REMARK 3 B22 (A**2) : 0.30000
REMARK 3 B33 (A**2) : -0.33000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.47000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.097
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.100
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.061
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.231
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.928
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1357 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 922 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1812 ; 1.656 ; 1.974
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2279 ; 1.505 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 166 ; 6.118 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 73 ;28.061 ;26.575
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 275 ;15.569 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 6 ;15.492 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 199 ; 0.095 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1506 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 248 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 377 ; 0.249 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 971 ; 0.179 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 701 ; 0.187 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 642 ; 0.090 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 111 ; 0.205 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 13 ; 0.120 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 14 ; 0.180 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 40 ; 0.227 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 30 ; 0.184 ; 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): 870 ; 1.190 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 345 ; 0.376 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1332 ; 1.659 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 549 ; 2.462 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 480 ; 3.473 ; 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 : 6
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 1 A 14
REMARK 3 ORIGIN FOR THE GROUP (A): 37.8605 27.5462 3.8680
REMARK 3 T TENSOR
REMARK 3 T11: -0.2411 T22: -0.2256
REMARK 3 T33: -0.1152 T12: -0.0021
REMARK 3 T13: 0.0124 T23: -0.0500
REMARK 3 L TENSOR
REMARK 3 L11: 12.8686 L22: 14.5695
REMARK 3 L33: 8.0821 L12: 8.0799
REMARK 3 L13: -5.2600 L23: -6.3935
REMARK 3 S TENSOR
REMARK 3 S11: 0.2016 S12: 0.0898 S13: 0.4498
REMARK 3 S21: -0.1786 S22: 0.0832 S23: 0.3548
REMARK 3 S31: -0.2114 S32: -0.1296 S33: -0.2848
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 15 A 74
REMARK 3 RESIDUE RANGE : A 402 A 403
REMARK 3 ORIGIN FOR THE GROUP (A): 22.9667 14.9514 7.7495
REMARK 3 T TENSOR
REMARK 3 T11: -0.2202 T22: -0.2354
REMARK 3 T33: -0.2127 T12: -0.0281
REMARK 3 T13: 0.0034 T23: 0.0054
REMARK 3 L TENSOR
REMARK 3 L11: 4.5354 L22: 1.5874
REMARK 3 L33: 2.7173 L12: 0.8993
REMARK 3 L13: -0.4872 L23: -0.4774
REMARK 3 S TENSOR
REMARK 3 S11: 0.0779 S12: -0.3399 S13: -0.1187
REMARK 3 S21: 0.1246 S22: -0.0891 S23: 0.0039
REMARK 3 S31: 0.0355 S32: 0.0010 S33: 0.0112
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 87 A 113
REMARK 3 RESIDUE RANGE : A 404 A 404
REMARK 3 ORIGIN FOR THE GROUP (A): 25.5459 23.9108 28.5946
REMARK 3 T TENSOR
REMARK 3 T11: -0.0884 T22: 0.0647
REMARK 3 T33: -0.1699 T12: -0.0480
REMARK 3 T13: 0.0144 T23: -0.0340
REMARK 3 L TENSOR
REMARK 3 L11: 1.3376 L22: 6.2374
REMARK 3 L33: 9.4696 L12: -1.4801
REMARK 3 L13: 0.7177 L23: 4.8429
REMARK 3 S TENSOR
REMARK 3 S11: -0.0284 S12: -0.3325 S13: -0.3957
REMARK 3 S21: 0.0669 S22: -0.2693 S23: 0.2535
REMARK 3 S31: 0.1900 S32: -0.8038 S33: 0.2977
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 114 A 148
REMARK 3 RESIDUE RANGE : A 401 A 401
REMARK 3 ORIGIN FOR THE GROUP (A): 33.8942 30.0739 25.8521
REMARK 3 T TENSOR
REMARK 3 T11: -0.0073 T22: 0.0310
REMARK 3 T33: -0.1920 T12: -0.0541
REMARK 3 T13: 0.0065 T23: 0.0134
REMARK 3 L TENSOR
REMARK 3 L11: 2.7054 L22: 4.1956
REMARK 3 L33: 8.4771 L12: 0.7019
REMARK 3 L13: 1.7822 L23: 2.4534
REMARK 3 S TENSOR
REMARK 3 S11: -0.0811 S12: -0.0398 S13: -0.0107
REMARK 3 S21: -0.4631 S22: 0.0496 S23: -0.2544
REMARK 3 S31: -0.5391 S32: 0.2320 S33: 0.0316
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 4 B 18
REMARK 3 ORIGIN FOR THE GROUP (A): 28.0780 25.8618 16.2411
REMARK 3 T TENSOR
REMARK 3 T11: -0.1412 T22: -0.1187
REMARK 3 T33: -0.1764 T12: -0.0463
REMARK 3 T13: 0.0187 T23: -0.0359
REMARK 3 L TENSOR
REMARK 3 L11: 13.9203 L22: 6.1158
REMARK 3 L33: 10.7720 L12: 3.5856
REMARK 3 L13: 8.9398 L23: 1.5948
REMARK 3 S TENSOR
REMARK 3 S11: -0.1140 S12: 0.5108 S13: 0.1643
REMARK 3 S21: -0.1650 S22: -0.0512 S23: -0.3938
REMARK 3 S31: -0.2475 S32: 0.8270 S33: 0.1651
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 19 B 23
REMARK 3 ORIGIN FOR THE GROUP (A): 14.8376 23.9608 12.8067
REMARK 3 T TENSOR
REMARK 3 T11: -0.0856 T22: -0.1145
REMARK 3 T33: -0.1097 T12: 0.0031
REMARK 3 T13: -0.0206 T23: -0.0858
REMARK 3 L TENSOR
REMARK 3 L11: 23.9457 L22: 18.5589
REMARK 3 L33: 12.8341 L12: 8.9513
REMARK 3 L13: -3.8996 L23: -7.2871
REMARK 3 S TENSOR
REMARK 3 S11: -0.2377 S12: -0.5891 S13: 0.7842
REMARK 3 S21: 1.1991 S22: -0.0952 S23: 1.7203
REMARK 3 S31: -0.6701 S32: -0.7266 S33: 0.3329
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 : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2O60 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-DEC-06.
REMARK 100 THE DEPOSITION ID IS D_1000040730.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-OCT-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23547
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
REMARK 200 RESOLUTION RANGE LOW (A) : 74.536
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.03900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.25400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: EPMR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 4000, 0.2 M SODIUM ACETATE,
REMARK 280 0.1 M SODIUM CITRATE PH 5.6, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298K
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 33.56300
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 16.46500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 33.56300
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 16.46500
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 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 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 LYS B 1
REMARK 465 ARG B 2
REMARK 465 ARG B 3
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 7 O HOH A 557 1.47
REMARK 500 NZ LYS A 13 O HOH A 457 1.86
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 72 CG - SD - CE ANGL. DEV. = -10.2 DEGREES
REMARK 500 GLN B 23 CA - C - N ANGL. DEV. = -16.6 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 ASP A 2 -58.76 -24.83
REMARK 500 MET A 76 -99.21 -86.11
REMARK 500 LYS A 77 -130.32 51.57
REMARK 500 ASP A 78 -125.77 -149.18
REMARK 500 THR A 79 -162.96 57.02
REMARK 500 ASP A 80 96.38 37.64
REMARK 500 SER A 81 -73.29 79.97
REMARK 500 GLU A 82 -159.18 55.01
REMARK 500
REMARK 500 REMARK: NULL
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 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 404
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2O5G RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 PEPTIDE IN CHAIN B IS ACETYLATED AT N-TERMINUS AND
REMARK 999 AMIDATED AT C-TERMINUS. ACE GROUP WAS NOT MODELED DUE
REMARK 999 TO LACK OF ELECTRON DENSITY.
DBREF 2O60 A 1 148 UNP P62149 CALM_CHICK 1 148
DBREF 2O60 B 1 23 UNP Q9Z0J4 NOS1_MOUSE 725 747
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 ARG ARG ALA ILE GLY PHE LYS LYS LEU ALA GLU ALA
SEQRES 2 B 24 VAL LYS PHE SER ALA LYS LEU MET GLY GLN NH2
HET NH2 B 24 1
HET CA A 401 1
HET CA A 402 1
HET CA A 403 1
HET CA A 404 1
HETNAM NH2 AMINO GROUP
HETNAM CA CALCIUM ION
FORMUL 2 NH2 H2 N
FORMUL 3 CA 4(CA 2+)
FORMUL 7 HOH *165(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 ASP A 56 1 13
HELIX 4 4 ASP A 64 MET A 76 1 13
HELIX 5 5 GLU A 84 ASP A 93 1 10
HELIX 6 6 SER A 101 LEU A 112 1 12
HELIX 7 7 THR A 117 ARG A 126 1 10
HELIX 8 8 TYR A 138 ALA A 147 1 10
HELIX 9 9 GLY B 6 MET B 21 1 16
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 C GLN B 23 N NH2 B 24 1555 1555 1.34
SITE 1 AC1 6 ASP A 129 ASP A 131 ASP A 133 GLN A 135
SITE 2 AC1 6 GLU A 140 HOH A 432
SITE 1 AC2 6 ASP A 56 ASP A 58 ASN A 60 THR A 62
SITE 2 AC2 6 GLU A 67 HOH A 410
SITE 1 AC3 6 ASP A 20 ASP A 22 ASP A 24 THR A 26
SITE 2 AC3 6 GLU A 31 HOH A 419
SITE 1 AC4 6 ASP A 93 ASP A 95 ASN A 97 TYR A 99
SITE 2 AC4 6 GLU A 104 HOH A 476
CRYST1 67.126 32.930 73.830 90.00 93.30 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 0.014897 0.000000 0.000859 0.00000
SCALE2 0.000000 0.030367 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013567 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
