HEADER METAL BINDING PROTEIN 05-DEC-06 2O5G
TITLE CALMODULIN-SMOOTH MUSCLE LIGHT CHAIN KINASE PEPTIDE 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: SMOOTH MUSCLE MYOSIN LIGHT CHAIN KINASE PEPTIDE;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: CALMODULIN BINDING DOMAIN;
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, MODIFIED;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE
SOURCE 14 CAN BE NATURALLY FOUND IN GALLUS GALLUS (CHICKEN)
KEYWDS PROTEIN-PEPTIDE COMPLEX, METAL BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR K.G.VALENTINE,H.L.NG,J.K.SCHNEEWEIS,J.K.KRANZ,K.K.FREDERICK,T.ALBER,
AUTHOR 2 A.J.WAND
REVDAT 5 27-DEC-23 2O5G 1 REMARK LINK
REVDAT 4 18-OCT-17 2O5G 1 REMARK
REVDAT 3 13-JUL-11 2O5G 1 VERSN
REVDAT 2 24-FEB-09 2O5G 1 VERSN
REVDAT 1 25-DEC-07 2O5G 0
JRNL AUTH K.G.VALENTINE,H.L.NG,J.K.SCHNEEWEIS,J.K.KRANZ,K.K.FREDERICK,
JRNL AUTH 2 T.ALBER,A.J.WAND
JRNL TITL ULTRAHIGH RESOLUTION CRYSTAL STRUCTURE OF CALMODULIN-SMOOTH
JRNL TITL 2 MUSCLE LIGHT KINASE PEPTIDE COMPLEX
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.08 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) : 1.08
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 57946
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) : 0.144
REMARK 3 R VALUE (WORKING SET) : 0.142
REMARK 3 FREE R VALUE : 0.165
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3092
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) : 1.08
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.11
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4192
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2120
REMARK 3 BIN FREE R VALUE SET COUNT : 188
REMARK 3 BIN FREE R VALUE : 0.2400
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1314
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 9
REMARK 3 SOLVENT ATOMS : 246
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 7.93
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 11.05
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.06000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : -0.03000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.35000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.030
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.030
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.021
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.438
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.976
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.970
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1380 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1237 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1847 ; 1.799 ; 1.962
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2901 ; 1.001 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 164 ; 5.340 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 200 ; 0.118 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1523 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 263 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 378 ; 0.247 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1474 ; 0.242 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 767 ; 0.089 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 136 ; 0.123 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 19 ; 0.095 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 22 ; 0.215 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 86 ; 0.289 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 49 ; 0.122 ; 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): 827 ; 1.650 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1335 ; 2.462 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 553 ; 3.315 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 512 ; 4.963 ; 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): 1380 ; 1.482 ; 2.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 250 ;12.227 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 1367 ; 5.138 ; 5.000
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 : 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 2O5G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-DEC-06.
REMARK 100 THE DEPOSITION ID IS D_1000040710.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-JUN-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
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) : 1.008
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 : 61087
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.080
REMARK 200 RESOLUTION RANGE LOW (A) : 56.796
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.08
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.14
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 1.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.22700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
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 (%): 36.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 400, 0.2 M SODIUM ACETATE, 0.1
REMARK 280 M TRIS PH 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 28.44700
REMARK 290 SMTRY3 2 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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 3660 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -84.0 KCAL/MOL
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 A 148
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 ASP A 78 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
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 1 ASP A 2 148.93
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 403 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 20 OD1
REMARK 620 2 ASP A 22 OD1 82.3
REMARK 620 3 ASP A 24 OD1 87.1 79.9
REMARK 620 4 THR A 26 O 85.2 157.1 80.4
REMARK 620 5 GLU A 31 OE1 107.2 127.3 150.0 74.8
REMARK 620 6 GLU A 31 OE2 94.8 75.5 154.9 124.7 52.4
REMARK 620 7 HOH A 503 O 162.8 80.7 87.6 110.0 85.3 83.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 404 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 56 OD1
REMARK 620 2 ASP A 58 OD1 80.5
REMARK 620 3 ASN A 60 OD1 87.9 78.4
REMARK 620 4 THR A 62 O 91.0 154.8 77.6
REMARK 620 5 GLU A 67 OE1 104.4 126.0 153.7 79.1
REMARK 620 6 GLU A 67 OE2 91.4 74.5 152.6 129.8 51.9
REMARK 620 7 HOH A 550 O 165.3 84.9 89.3 102.4 84.1 84.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 402 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 93 OD1
REMARK 620 2 ASP A 95 OD1 81.9
REMARK 620 3 ASN A 97 OD1 84.3 79.1
REMARK 620 4 TYR A 99 O 85.9 156.4 79.6
REMARK 620 5 GLU A 104 OE1 114.8 128.5 146.6 75.0
REMARK 620 6 GLU A 104 OE2 99.4 78.5 156.5 123.7 51.7
REMARK 620 7 HOH A 511 O 160.9 80.2 85.6 108.2 82.0 83.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 129 OD1
REMARK 620 2 ASP A 131 OD1 83.4
REMARK 620 3 ASP A 133 OD1 86.1 77.6
REMARK 620 4 GLN A 135 O 79.8 154.1 81.6
REMARK 620 5 GLU A 140 OE1 115.9 122.9 150.0 82.5
REMARK 620 6 GLU A 140 OE2 88.2 76.6 154.1 122.1 52.9
REMARK 620 7 HOH A 536 O 162.3 85.6 78.1 105.2 81.7 102.6
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 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 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 501
DBREF 2O5G A 1 148 UNP P62149 CALM_CHICK 1 148
DBREF 2O5G B 1 19 UNP P11799 MYLK_CHICK 1730 1748
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 21 ACE ALA ARG ARG LYS TRP GLN LYS THR GLY HIS ALA VAL
SEQRES 2 B 21 ARG ALA ILE GLY ARG LEU SER NH2
HET ACE B 0 3
HET NH2 B 20 1
HET CA A 401 1
HET CA A 402 1
HET CA A 403 1
HET CA A 404 1
HET SO4 A 501 5
HETNAM ACE ACETYL GROUP
HETNAM NH2 AMINO GROUP
HETNAM CA CALCIUM ION
HETNAM SO4 SULFATE ION
FORMUL 2 ACE C2 H4 O
FORMUL 2 NH2 H2 N
FORMUL 3 CA 4(CA 2+)
FORMUL 7 SO4 O4 S 2-
FORMUL 8 HOH *246(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 PHE A 65 ARG A 74 1 10
HELIX 5 5 ASP A 80 ASP A 93 1 14
HELIX 6 6 SER A 101 LEU A 112 1 12
HELIX 7 7 THR A 117 ASP A 129 1 13
HELIX 8 8 TYR A 138 MET A 145 1 8
HELIX 9 9 ALA B 1 SER B 19 1 19
SHEET 1 A 2 THR A 26 ILE A 27 0
SHEET 2 A 2 ILE A 63 ASP A 64 -1 O ILE A 63 N ILE A 27
SHEET 1 B 2 TYR A 99 ILE A 100 0
SHEET 2 B 2 VAL A 136 ASN A 137 -1 O VAL A 136 N ILE A 100
LINK C ACE B 0 N ALA B 1 1555 1555 1.31
LINK C SER B 19 N NH2 B 20 1555 1555 1.32
LINK OD1 ASP A 20 CA CA A 403 1555 1555 2.27
LINK OD1 ASP A 22 CA CA A 403 1555 1555 2.39
LINK OD1 ASP A 24 CA CA A 403 1555 1555 2.37
LINK O THR A 26 CA CA A 403 1555 1555 2.35
LINK OE1 GLU A 31 CA CA A 403 1555 1555 2.44
LINK OE2 GLU A 31 CA CA A 403 1555 1555 2.51
LINK OD1 ASP A 56 CA CA A 404 1555 1555 2.29
LINK OD1 ASP A 58 CA CA A 404 1555 1555 2.38
LINK OD1 ASN A 60 CA CA A 404 1555 1555 2.38
LINK O THR A 62 CA CA A 404 1555 1555 2.36
LINK OE1 GLU A 67 CA CA A 404 1555 1555 2.46
LINK OE2 GLU A 67 CA CA A 404 1555 1555 2.57
LINK OD1 ASP A 93 CA CA A 402 1555 1555 2.27
LINK OD1 ASP A 95 CA CA A 402 1555 1555 2.36
LINK OD1 ASN A 97 CA CA A 402 1555 1555 2.43
LINK O TYR A 99 CA CA A 402 1555 1555 2.29
LINK OE1 GLU A 104 CA CA A 402 1555 1555 2.44
LINK OE2 GLU A 104 CA CA A 402 1555 1555 2.55
LINK OD1 ASP A 129 CA CA A 401 1555 1555 2.29
LINK OD1 ASP A 131 CA CA A 401 1555 1555 2.37
LINK OD1 ASP A 133 CA CA A 401 1555 1555 2.44
LINK O GLN A 135 CA CA A 401 1555 1555 2.21
LINK OE1 GLU A 140 CA CA A 401 1555 1555 2.41
LINK OE2 GLU A 140 CA CA A 401 1555 1555 2.49
LINK CA CA A 401 O HOH A 536 1555 1555 2.41
LINK CA CA A 402 O HOH A 511 1555 1555 2.40
LINK CA CA A 403 O HOH A 503 1555 1555 2.42
LINK CA CA A 404 O HOH A 550 1555 1555 2.34
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 536
SITE 1 AC2 6 ASP A 93 ASP A 95 ASN A 97 TYR A 99
SITE 2 AC2 6 GLU A 104 HOH A 511
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 503
SITE 1 AC4 6 ASP A 56 ASP A 58 ASN A 60 THR A 62
SITE 2 AC4 6 GLU A 67 HOH A 550
SITE 1 AC5 4 ARG A 90 ARG A 126 HOH A 555 HOH A 610
CRYST1 28.861 56.894 44.760 90.00 97.45 90.00 P 1 21 1 2
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 0.034649 0.000000 0.004531 0.00000
SCALE2 0.000000 0.017577 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022532 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
