HEADER HYDROLASE 12-MAR-08 3CJA
TITLE STRUCTURE OF RATTUS NORVEGICUS NTPDASE2 IN COMPLEX WITH
TITLE 2 CALCIUM AND AMPPNP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ECTONUCLEOSIDE TRIPHOSPHATE DIPHOSPHOHYDROLASE 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ECTODOMAIN, EXTRACELLULAR DOMAIN, UNP RESIDUES
COMPND 5 29-461;
COMPND 6 SYNONYM: NTPDASE 2, ECTO-ATPASE, CD39 ANTIGEN-LIKE 1;
COMPND 7 EC: 3.6.1.5;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: ENTPD2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ER2566;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET45B(+)
KEYWDS HYDROLASE, ALPHA/BETA PROTEIN, ACTIN-LIKE FOLD, ALTERNATIVE
KEYWDS 2 SPLICING, CALCIUM, GLYCOPROTEIN, MAGNESIUM, MEMBRANE,
KEYWDS 3 TRANSMEMBRANE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.ZEBISCH,N.STRATER
REVDAT 3 24-FEB-09 3CJA 1 VERSN
REVDAT 2 27-MAY-08 3CJA 1 JRNL
REVDAT 1 29-APR-08 3CJA 0
JRNL AUTH M.ZEBISCH,N.STRATER
JRNL TITL STRUCTURAL INSIGHT INTO SIGNAL CONVERSION AND
JRNL TITL 2 INACTIVATION BY NTPDASE2 IN PURINERGIC SIGNALING
JRNL REF PROC.NATL.ACAD.SCI.USA V. 105 6882 2008
JRNL REFN ISSN 0027-8424
JRNL PMID 18458329
JRNL DOI 10.1073/PNAS.0802535105
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.34
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 3 NUMBER OF REFLECTIONS : 25565
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) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1082
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1622
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 82.54
REMARK 3 BIN R VALUE (WORKING SET) : 0.2020
REMARK 3 BIN FREE R VALUE SET COUNT : 66
REMARK 3 BIN FREE R VALUE : 0.2730
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3271
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 337
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.66
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.34000
REMARK 3 B22 (A**2) : 0.73000
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): 0.205
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.171
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.115
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.844
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.932
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3391 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4619 ; 1.391 ; 1.958
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 417 ; 6.060 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 151 ;35.668 ;23.046
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 527 ;13.413 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;14.480 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 506 ; 0.093 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2586 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1523 ; 0.196 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2320 ; 0.301 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 295 ; 0.127 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 3 ; 0.100 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 49 ; 0.159 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 22 ; 0.142 ; 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): 2140 ; 0.807 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3340 ; 1.243 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1452 ; 2.040 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1279 ; 3.184 ; 4.500
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 : 1.20
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
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 3CJA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-MAR-08.
REMARK 100 THE RCSB ID CODE IS RCSB046843.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-NOV-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9184
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26670
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 26.670
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : 0.11800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.21
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.42600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM NAHEPES, 2% PEG 6000, PH 7.2,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 20.45000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 81.86000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.43500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 81.86000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.45000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.43500
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 MET A 6
REMARK 465 ALA A 7
REMARK 465 HIS A 8
REMARK 465 HIS A 9
REMARK 465 HIS A 10
REMARK 465 HIS A 11
REMARK 465 HIS A 12
REMARK 465 HIS A 13
REMARK 465 VAL A 14
REMARK 465 GLY A 15
REMARK 465 THR A 16
REMARK 465 GLY A 17
REMARK 465 SER A 18
REMARK 465 ASN A 19
REMARK 465 ASP A 20
REMARK 465 ASP A 21
REMARK 465 ASP A 22
REMARK 465 ASP A 23
REMARK 465 LYS A 24
REMARK 465 SER A 25
REMARK 465 PRO A 26
REMARK 465 ASP A 27
REMARK 465 PRO A 28
REMARK 465 THR A 29
REMARK 465 GLN A 30
REMARK 465 ASP A 31
REMARK 465 VAL A 32
REMARK 465 ARG A 33
REMARK 465 GLU A 34
REMARK 465 PRO A 35
REMARK 465 ARG A 289
REMARK 465 PRO A 290
REMARK 465 ARG A 291
REMARK 465 ALA A 292
REMARK 465 PHE A 293
REMARK 465 ASN A 294
REMARK 465 GLY A 295
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 O HOH A 509 O HOH A 714 2.18
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 THR A 122 -135.69 -113.80
REMARK 500 ARG A 188 72.81 -152.87
REMARK 500 ARG A 193 150.03 -46.82
REMARK 500 ARG A 261 18.66 59.52
REMARK 500 SER A 329 -89.48 -76.99
REMARK 500 PHE A 345 -157.98 -118.30
REMARK 500 SER A 346 -131.60 47.85
REMARK 500 ARG A 394 -15.51 79.14
REMARK 500 ASP A 431 18.14 54.91
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 502 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 505 O
REMARK 620 2 HOH A 508 O 92.2
REMARK 620 3 HOH A 507 O 92.6 84.8
REMARK 620 4 ANP A 501 O3G 84.5 93.2 176.5
REMARK 620 5 HOH A 506 O 85.0 169.3 85.0 96.7
REMARK 620 6 ANP A 501 O2B 169.4 88.3 98.0 84.8 96.4
REMARK 620 N 1 2 3 4 5
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 502
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP A 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3CJ1 RELATED DB: PDB
REMARK 900 APO FORM
REMARK 900 RELATED ID: 3CJ7 RELATED DB: PDB
REMARK 900 AMP COMPLEX
REMARK 900 RELATED ID: 3CJ9 RELATED DB: PDB
REMARK 900 CA2+XAMPXPI COMPLEX
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE IS BASED ON REFERENCE 2 IN THE DATABASE,
REMARK 999 ENTP2_RAT.
DBREF 3CJA A 29 461 UNP O35795 ENTP2_RAT 29 461
SEQADV 3CJA MET A 6 UNP O35795 INITIATING METHIONINE
SEQADV 3CJA ALA A 7 UNP O35795 EXPRESSION TAG
SEQADV 3CJA HIS A 8 UNP O35795 EXPRESSION TAG
SEQADV 3CJA HIS A 9 UNP O35795 EXPRESSION TAG
SEQADV 3CJA HIS A 10 UNP O35795 EXPRESSION TAG
SEQADV 3CJA HIS A 11 UNP O35795 EXPRESSION TAG
SEQADV 3CJA HIS A 12 UNP O35795 EXPRESSION TAG
SEQADV 3CJA HIS A 13 UNP O35795 EXPRESSION TAG
SEQADV 3CJA VAL A 14 UNP O35795 EXPRESSION TAG
SEQADV 3CJA GLY A 15 UNP O35795 EXPRESSION TAG
SEQADV 3CJA THR A 16 UNP O35795 EXPRESSION TAG
SEQADV 3CJA GLY A 17 UNP O35795 EXPRESSION TAG
SEQADV 3CJA SER A 18 UNP O35795 EXPRESSION TAG
SEQADV 3CJA ASN A 19 UNP O35795 EXPRESSION TAG
SEQADV 3CJA ASP A 20 UNP O35795 EXPRESSION TAG
SEQADV 3CJA ASP A 21 UNP O35795 EXPRESSION TAG
SEQADV 3CJA ASP A 22 UNP O35795 EXPRESSION TAG
SEQADV 3CJA ASP A 23 UNP O35795 EXPRESSION TAG
SEQADV 3CJA LYS A 24 UNP O35795 EXPRESSION TAG
SEQADV 3CJA SER A 25 UNP O35795 EXPRESSION TAG
SEQADV 3CJA PRO A 26 UNP O35795 EXPRESSION TAG
SEQADV 3CJA ASP A 27 UNP O35795 EXPRESSION TAG
SEQADV 3CJA PRO A 28 UNP O35795 EXPRESSION TAG
SEQRES 1 A 456 MET ALA HIS HIS HIS HIS HIS HIS VAL GLY THR GLY SER
SEQRES 2 A 456 ASN ASP ASP ASP ASP LYS SER PRO ASP PRO THR GLN ASP
SEQRES 3 A 456 VAL ARG GLU PRO PRO ALA LEU LYS TYR GLY ILE VAL LEU
SEQRES 4 A 456 ASP ALA GLY SER SER HIS THR SER MET PHE VAL TYR LYS
SEQRES 5 A 456 TRP PRO ALA ASP LYS GLU ASN ASP THR GLY ILE VAL GLY
SEQRES 6 A 456 GLN HIS SER SER CYS ASP VAL GLN GLY GLY GLY ILE SER
SEQRES 7 A 456 SER TYR ALA ASN ASP PRO SER LYS ALA GLY GLN SER LEU
SEQRES 8 A 456 VAL ARG CYS LEU GLU GLN ALA LEU ARG ASP VAL PRO ARG
SEQRES 9 A 456 ASP ARG HIS ALA SER THR PRO LEU TYR LEU GLY ALA THR
SEQRES 10 A 456 ALA GLY MET ARG LEU LEU ASN LEU THR SER PRO GLU ALA
SEQRES 11 A 456 THR ALA ARG VAL LEU GLU ALA VAL THR GLN THR LEU THR
SEQRES 12 A 456 GLN TYR PRO PHE ASP PHE ARG GLY ALA ARG ILE LEU SER
SEQRES 13 A 456 GLY GLN ASP GLU GLY VAL PHE GLY TRP VAL THR ALA ASN
SEQRES 14 A 456 TYR LEU LEU GLU ASN PHE ILE LYS TYR GLY TRP VAL GLY
SEQRES 15 A 456 ARG TRP ILE ARG PRO ARG LYS GLY THR LEU GLY ALA MET
SEQRES 16 A 456 ASP LEU GLY GLY ALA SER THR GLN ILE THR PHE GLU THR
SEQRES 17 A 456 THR SER PRO SER GLU ASP PRO GLY ASN GLU VAL HIS LEU
SEQRES 18 A 456 ARG LEU TYR GLY GLN HIS TYR ARG VAL TYR THR HIS SER
SEQRES 19 A 456 PHE LEU CYS TYR GLY ARG ASP GLN ILE LEU LEU ARG LEU
SEQRES 20 A 456 LEU ALA SER ALA LEU GLN ILE HIS ARG PHE HIS PRO CYS
SEQRES 21 A 456 TRP PRO LYS GLY TYR SER THR GLN VAL LEU LEU GLN GLU
SEQRES 22 A 456 VAL TYR GLN SER PRO CYS THR MET GLY GLN ARG PRO ARG
SEQRES 23 A 456 ALA PHE ASN GLY SER ALA ILE VAL SER LEU SER GLY THR
SEQRES 24 A 456 SER ASN ALA THR LEU CYS ARG ASP LEU VAL SER ARG LEU
SEQRES 25 A 456 PHE ASN ILE SER SER CYS PRO PHE SER GLN CYS SER PHE
SEQRES 26 A 456 ASN GLY VAL PHE GLN PRO PRO VAL ALA GLY ASN PHE ILE
SEQRES 27 A 456 ALA PHE SER ALA PHE TYR TYR THR VAL ASP PHE LEU THR
SEQRES 28 A 456 THR VAL MET GLY LEU PRO VAL GLY THR LEU LYS GLN LEU
SEQRES 29 A 456 GLU GLU ALA THR GLU ILE THR CYS ASN GLN THR TRP THR
SEQRES 30 A 456 GLU LEU GLN ALA ARG VAL PRO GLY GLN LYS THR ARG LEU
SEQRES 31 A 456 ALA ASP TYR CYS ALA VAL ALA MET PHE ILE HIS GLN LEU
SEQRES 32 A 456 LEU SER ARG GLY TYR HIS PHE ASP GLU ARG SER PHE ARG
SEQRES 33 A 456 GLU VAL VAL PHE GLN LYS LYS ALA ALA ASP THR ALA VAL
SEQRES 34 A 456 GLY TRP ALA LEU GLY TYR MET LEU ASN LEU THR ASN LEU
SEQRES 35 A 456 ILE PRO ALA ASP LEU PRO GLY LEU ARG LYS GLY THR HIS
SEQRES 36 A 456 PHE
HET CA A 502 1
HET ANP A 501 31
HETNAM CA CALCIUM ION
HETNAM ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
FORMUL 2 CA CA 2+
FORMUL 3 ANP C10 H17 N6 O12 P3
FORMUL 4 HOH *337(H2 O)
HELIX 1 1 GLY A 81 ALA A 86 5 6
HELIX 2 2 PRO A 89 SER A 95 1 7
HELIX 3 3 LEU A 96 VAL A 107 1 12
HELIX 4 4 PRO A 108 SER A 114 5 7
HELIX 5 5 THR A 122 SER A 132 1 11
HELIX 6 6 SER A 132 THR A 148 1 17
HELIX 7 7 SER A 161 LEU A 177 1 17
HELIX 8 8 ASP A 219 GLY A 221 5 3
HELIX 9 9 GLY A 244 HIS A 260 1 17
HELIX 10 10 LEU A 276 GLN A 281 1 6
HELIX 11 11 ASN A 306 ARG A 316 1 11
HELIX 12 12 ALA A 347 VAL A 358 1 12
HELIX 13 13 THR A 365 GLN A 379 1 15
HELIX 14 14 THR A 380 ALA A 386 1 7
HELIX 15 15 ARG A 394 ALA A 396 5 3
HELIX 16 16 ASP A 397 ARG A 411 1 15
HELIX 17 17 ASP A 416 ARG A 421 1 6
HELIX 18 18 TRP A 436 THR A 445 1 10
HELIX 19 19 LEU A 452 THR A 459 5 8
SHEET 1 A 5 GLY A 70 ASP A 76 0
SHEET 2 A 5 THR A 51 PRO A 59 -1 N MET A 53 O CYS A 75
SHEET 3 A 5 LEU A 38 ALA A 46 -1 N GLY A 41 O TYR A 56
SHEET 4 A 5 PRO A 116 ALA A 121 1 O TYR A 118 N LEU A 44
SHEET 5 A 5 ASP A 153 ILE A 159 1 O ARG A 155 N LEU A 117
SHEET 1 B 2 GLY A 184 TRP A 185 0
SHEET 2 B 2 ARG A 188 TRP A 189 -1 O ARG A 188 N TRP A 185
SHEET 1 C 6 GLU A 223 LEU A 228 0
SHEET 2 C 6 GLN A 231 LEU A 241 -1 O VAL A 235 N VAL A 224
SHEET 3 C 6 SER A 206 GLU A 212 -1 N THR A 207 O PHE A 240
SHEET 4 C 6 GLY A 198 LEU A 202 -1 N ALA A 199 O THR A 210
SHEET 5 C 6 PHE A 342 SER A 346 1 O ILE A 343 N GLY A 198
SHEET 6 C 6 VAL A 423 PHE A 425 1 O VAL A 424 N PHE A 342
SHEET 1 D 2 SER A 271 LEU A 275 0
SHEET 2 D 2 ILE A 298 SER A 302 -1 O VAL A 299 N VAL A 274
SHEET 1 E 2 LYS A 428 ALA A 429 0
SHEET 2 E 2 THR A 432 ALA A 433 -1 O THR A 432 N ALA A 429
SSBOND 1 CYS A 75 CYS A 99 1555 1555 2.05
SSBOND 2 CYS A 242 CYS A 284 1555 1555 2.05
SSBOND 3 CYS A 265 CYS A 310 1555 1555 2.09
SSBOND 4 CYS A 323 CYS A 328 1555 1555 2.04
SSBOND 5 CYS A 377 CYS A 399 1555 1555 2.03
LINK CA CA A 502 O HOH A 505 1555 1555 2.44
LINK CA CA A 502 O HOH A 508 1555 1555 2.43
LINK CA CA A 502 O HOH A 507 1555 1555 2.43
LINK CA CA A 502 O3G ANP A 501 1555 1555 2.30
LINK CA CA A 502 O HOH A 506 1555 1555 2.40
LINK CA CA A 502 O2B ANP A 501 1555 1555 2.30
CISPEP 1 ARG A 191 PRO A 192 0 -7.95
SITE 1 AC1 4 HOH A 505 HOH A 506 HOH A 507 HOH A 508
SITE 1 AC2 25 GLY A 47 SER A 48 SER A 49 HIS A 50
SITE 2 AC2 25 THR A 122 ALA A 123 GLU A 165 LEU A 202
SITE 3 AC2 25 GLY A 203 GLY A 204 ALA A 205 SER A 206
SITE 4 AC2 25 ARG A 245 ASP A 246 SER A 346 ALA A 347
SITE 5 AC2 25 TYR A 350 ARG A 394 HOH A 503 HOH A 504
SITE 6 AC2 25 HOH A 506 HOH A 510 HOH A 624 HOH A 718
SITE 7 AC2 25 HOH A 777
CRYST1 40.900 68.870 163.720 90.00 90.00 90.00 P 21 21 21 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 0.024450 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014520 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006108 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
