HEADER HYDROLASE 07-NOV-07 3BA6
TITLE STRUCTURE OF THE CA2E1P PHOSPHOENZYME INTERMEDIATE OF THE SERCA CA2+-
TITLE 2 ATPASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CALCIUM PUMP 1, SERCA1, SR CA2+, -ATPASE 1, CALCIUM-
COMPND 5 TRANSPORTING ATPASE SARCOPLASMIC RETICULUM TYPE, FAST TWITCH SKELETAL
COMPND 6 MUSCLE ISOFORM, ENDOPLASMIC RETICULUM CLASS 1/2 CA2+, ATPASE;
COMPND 7 EC: 3.6.3.8
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;
SOURCE 3 ORGANISM_COMMON: RABBIT;
SOURCE 4 ORGANISM_TAXID: 9986;
SOURCE 5 TISSUE: FAST TWITCH SKELETAL MUSCLE
KEYWDS MEMBRANE PROTEIN, P-TYPE ATPASE, PHOSPHOENZYME, ASPARTYL-
KEYWDS 2 PHOSPHOANHYDRIDE, ALTERNATIVE SPLICING, ATP-BINDING, CALCIUM,
KEYWDS 3 CALCIUM TRANSPORT, ENDOPLASMIC RETICULUM, HYDROLASE, ION TRANSPORT,
KEYWDS 4 MAGNESIUM, METAL-BINDING, NUCLEOTIDE-BINDING, PHOSPHORYLATION,
KEYWDS 5 SARCOPLASMIC RETICULUM, TRANSMEMBRANE, TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR M.PICARD,A.M.L.WINTHER,C.OLESEN,C.GYRUP,J.P.MORTH,C.OXVIG,J.V.MOLLER,
AUTHOR 2 P.NISSEN
REVDAT 4 01-NOV-23 3BA6 1 REMARK LINK
REVDAT 3 25-OCT-17 3BA6 1 REMARK
REVDAT 2 24-FEB-09 3BA6 1 VERSN
REVDAT 1 18-DEC-07 3BA6 0
JRNL AUTH C.OLESEN,M.PICARD,A.M.WINTHER,C.GYRUP,J.P.MORTH,C.OXVIG,
JRNL AUTH 2 J.V.MOLLER,P.NISSEN
JRNL TITL THE STRUCTURAL BASIS OF CALCIUM TRANSPORT BY THE CALCIUM
JRNL TITL 2 PUMP.
JRNL REF NATURE V. 450 1036 2007
JRNL REFN ISSN 0028-0836
JRNL PMID 18075584
JRNL DOI 10.1038/NATURE06418
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.0
REMARK 3 NUMBER OF REFLECTIONS : 40204
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.288
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.940
REMARK 3 FREE R VALUE TEST SET COUNT : 1180
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 2.9200 - 2.8000 0.73 0 75 0.3175 0.3571
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 74.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 74.36
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -6.31000
REMARK 3 B22 (A**2) : 48.45000
REMARK 3 B33 (A**2) : -46.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.05000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.009 NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : 19.792 NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: B-FACTOR REFINEMENT WAS RESTRAINED AS
REMARK 3 IMPLEMENTED IN PHENIX
REMARK 4
REMARK 4 3BA6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-NOV-07.
REMARK 100 THE DEPOSITION ID IS D_1000045271.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-SEP-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0723
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : PT COATED SI MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41562
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.8
REMARK 200 DATA REDUNDANCY : 5.700
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : 0.07000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 71.7
REMARK 200 DATA REDUNDANCY IN SHELL : 5.10
REMARK 200 R MERGE FOR SHELL (I) : 0.50900
REMARK 200 R SYM FOR SHELL (I) : 0.50900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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 1T5S
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 6% PEG6000, 200MM SODIUM ACETATE, 15%
REMARK 280 GLYCEROL, 4% TERT-BUTANOL, 5MM B-MERCAPTOETHANOL, PH 6.8, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 292K
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 81.25500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.98350
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 81.25500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 37.98350
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 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 PRO A 803 C - N - CA ANGL. DEV. = -9.8 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 PRO A 26 -31.17 -34.82
REMARK 500 PRO A 42 -74.46 -54.02
REMARK 500 ALA A 43 -138.35 18.10
REMARK 500 GLU A 44 -6.98 75.44
REMARK 500 SER A 48 124.37 -172.49
REMARK 500 GLU A 55 43.03 -58.80
REMARK 500 GLU A 58 -13.83 71.60
REMARK 500 ASP A 59 -163.50 -73.73
REMARK 500 LEU A 60 -82.81 -81.11
REMARK 500 LEU A 61 12.51 -69.61
REMARK 500 THR A 84 44.90 -82.42
REMARK 500 ILE A 85 -38.78 -143.79
REMARK 500 GLU A 121 22.98 -65.93
REMARK 500 VAL A 155 118.21 -33.51
REMARK 500 LEU A 180 -95.91 -102.28
REMARK 500 ASP A 196 98.00 -61.58
REMARK 500 PRO A 197 0.64 -64.53
REMARK 500 LYS A 205 24.67 -73.57
REMARK 500 SER A 229 12.06 -58.32
REMARK 500 GLN A 238 109.64 -59.57
REMARK 500 MET A 239 -150.64 -7.01
REMARK 500 ALA A 240 108.12 77.86
REMARK 500 ALA A 241 48.65 -72.14
REMARK 500 THR A 242 -1.05 -57.75
REMARK 500 GLN A 244 -157.70 -38.46
REMARK 500 ASP A 245 -141.36 -113.88
REMARK 500 CYS A 268 -73.09 -72.71
REMARK 500 VAL A 269 -36.21 -38.81
REMARK 500 ASN A 275 -121.02 -110.34
REMARK 500 ILE A 276 -8.47 58.72
REMARK 500 ASP A 281 147.13 -38.78
REMARK 500 HIS A 284 31.06 -88.02
REMARK 500 SER A 287 157.04 -48.12
REMARK 500 ILE A 289 -39.56 -153.32
REMARK 500 ARG A 290 2.92 -65.21
REMARK 500 THR A 316 -45.85 -28.33
REMARK 500 LEU A 319 -71.23 -56.84
REMARK 500 CYS A 344 52.95 -92.30
REMARK 500 LYS A 352 -72.00 -90.26
REMARK 500 THR A 353 107.16 -57.14
REMARK 500 THR A 355 -77.18 -97.19
REMARK 500 ASP A 370 -74.03 -101.79
REMARK 500 PRO A 391 41.64 -79.19
REMARK 500 ASN A 421 114.12 -165.62
REMARK 500 ASN A 453 71.19 38.78
REMARK 500 ASN A 456 56.17 32.22
REMARK 500 ASN A 461 40.19 -102.11
REMARK 500 ALA A 501 -92.86 -60.67
REMARK 500 LYS A 502 -8.81 -48.59
REMARK 500 VAL A 508 1.26 -67.94
REMARK 500
REMARK 500 THIS ENTRY HAS 87 RAMACHANDRAN OUTLIERS.
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 A1003 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL A 304 O
REMARK 620 2 ALA A 305 O 78.6
REMARK 620 3 ILE A 307 O 87.2 114.5
REMARK 620 4 GLU A 309 OE2 80.7 151.5 83.5
REMARK 620 5 ASN A 796 OD1 66.6 66.5 153.4 87.4
REMARK 620 6 ASP A 800 OD2 119.7 59.1 146.9 117.4 58.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1005 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHD A 351 OD2
REMARK 620 2 PHD A 351 OP1 62.1
REMARK 620 3 THR A 353 O 77.2 113.4
REMARK 620 4 ASP A 703 OD2 71.2 118.4 91.4
REMARK 620 5 HOH A1008 O 175.4 113.4 105.4 112.2
REMARK 620 6 HOH A1042 O 75.2 66.0 148.2 65.0 103.2
REMARK 620 7 HOH A1044 O 114.5 56.8 106.9 161.6 61.3 98.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1004 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 768 OD1
REMARK 620 2 GLU A 771 OE2 105.1
REMARK 620 3 THR A 799 OG1 157.9 92.5
REMARK 620 4 ASP A 800 OD2 80.2 116.4 104.0
REMARK 620 5 GLU A 908 OE2 117.1 81.3 51.8 152.4
REMARK 620 N 1 2 3 4
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 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 1006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AN2 A 1001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1T5S RELATED DB: PDB
REMARK 900 AMPPCP COMPLEX, PRESTATE OF PHOSPHORYLATION
REMARK 900 RELATED ID: 1T5T RELATED DB: PDB
REMARK 900 ADP:ALF4- COMPLEX, TRANSITION STATE OF PHOSPHORYLATION
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THIS SEQUENCE IS ISOFORM SERCA1A.
DBREF 3BA6 A 1 994 UNP P04191 AT2A1_RABIT 1 994
SEQRES 1 A 994 MET GLU ALA ALA HIS SER LYS SER THR GLU GLU CYS LEU
SEQRES 2 A 994 ALA TYR PHE GLY VAL SER GLU THR THR GLY LEU THR PRO
SEQRES 3 A 994 ASP GLN VAL LYS ARG HIS LEU GLU LYS TYR GLY HIS ASN
SEQRES 4 A 994 GLU LEU PRO ALA GLU GLU GLY LYS SER LEU TRP GLU LEU
SEQRES 5 A 994 VAL ILE GLU GLN PHE GLU ASP LEU LEU VAL ARG ILE LEU
SEQRES 6 A 994 LEU LEU ALA ALA CYS ILE SER PHE VAL LEU ALA TRP PHE
SEQRES 7 A 994 GLU GLU GLY GLU GLU THR ILE THR ALA PHE VAL GLU PRO
SEQRES 8 A 994 PHE VAL ILE LEU LEU ILE LEU ILE ALA ASN ALA ILE VAL
SEQRES 9 A 994 GLY VAL TRP GLN GLU ARG ASN ALA GLU ASN ALA ILE GLU
SEQRES 10 A 994 ALA LEU LYS GLU TYR GLU PRO GLU MET GLY LYS VAL TYR
SEQRES 11 A 994 ARG ALA ASP ARG LYS SER VAL GLN ARG ILE LYS ALA ARG
SEQRES 12 A 994 ASP ILE VAL PRO GLY ASP ILE VAL GLU VAL ALA VAL GLY
SEQRES 13 A 994 ASP LYS VAL PRO ALA ASP ILE ARG ILE LEU SER ILE LYS
SEQRES 14 A 994 SER THR THR LEU ARG VAL ASP GLN SER ILE LEU THR GLY
SEQRES 15 A 994 GLU SER VAL SER VAL ILE LYS HIS THR GLU PRO VAL PRO
SEQRES 16 A 994 ASP PRO ARG ALA VAL ASN GLN ASP LYS LYS ASN MET LEU
SEQRES 17 A 994 PHE SER GLY THR ASN ILE ALA ALA GLY LYS ALA LEU GLY
SEQRES 18 A 994 ILE VAL ALA THR THR GLY VAL SER THR GLU ILE GLY LYS
SEQRES 19 A 994 ILE ARG ASP GLN MET ALA ALA THR GLU GLN ASP LYS THR
SEQRES 20 A 994 PRO LEU GLN GLN LYS LEU ASP GLU PHE GLY GLU GLN LEU
SEQRES 21 A 994 SER LYS VAL ILE SER LEU ILE CYS VAL ALA VAL TRP LEU
SEQRES 22 A 994 ILE ASN ILE GLY HIS PHE ASN ASP PRO VAL HIS GLY GLY
SEQRES 23 A 994 SER TRP ILE ARG GLY ALA ILE TYR TYR PHE LYS ILE ALA
SEQRES 24 A 994 VAL ALA LEU ALA VAL ALA ALA ILE PRO GLU GLY LEU PRO
SEQRES 25 A 994 ALA VAL ILE THR THR CYS LEU ALA LEU GLY THR ARG ARG
SEQRES 26 A 994 MET ALA LYS LYS ASN ALA ILE VAL ARG SER LEU PRO SER
SEQRES 27 A 994 VAL GLU THR LEU GLY CYS THR SER VAL ILE CYS SER PHD
SEQRES 28 A 994 LYS THR GLY THR LEU THR THR ASN GLN MET SER VAL CYS
SEQRES 29 A 994 LYS MET PHE ILE ILE ASP LYS VAL ASP GLY ASP PHE CYS
SEQRES 30 A 994 SER LEU ASN GLU PHE SER ILE THR GLY SER THR TYR ALA
SEQRES 31 A 994 PRO GLU GLY GLU VAL LEU LYS ASN ASP LYS PRO ILE ARG
SEQRES 32 A 994 SER GLY GLN PHE ASP GLY LEU VAL GLU LEU ALA THR ILE
SEQRES 33 A 994 CYS ALA LEU CYS ASN ASP SER SER LEU ASP PHE ASN GLU
SEQRES 34 A 994 THR LYS GLY VAL TYR GLU LYS VAL GLY GLU ALA THR GLU
SEQRES 35 A 994 THR ALA LEU THR THR LEU VAL GLU LYS MET ASN VAL PHE
SEQRES 36 A 994 ASN THR GLU VAL ARG ASN LEU SER LYS VAL GLU ARG ALA
SEQRES 37 A 994 ASN ALA CYS ASN SER VAL ILE ARG GLN LEU MET LYS LYS
SEQRES 38 A 994 GLU PHE THR LEU GLU PHE SER ARG ASP ARG LYS SER MET
SEQRES 39 A 994 SER VAL TYR CYS SER PRO ALA LYS SER SER ARG ALA ALA
SEQRES 40 A 994 VAL GLY ASN LYS MET PHE VAL LYS GLY ALA PRO GLU GLY
SEQRES 41 A 994 VAL ILE ASP ARG CYS ASN TYR VAL ARG VAL GLY THR THR
SEQRES 42 A 994 ARG VAL PRO MET THR GLY PRO VAL LYS GLU LYS ILE LEU
SEQRES 43 A 994 SER VAL ILE LYS GLU TRP GLY THR GLY ARG ASP THR LEU
SEQRES 44 A 994 ARG CYS LEU ALA LEU ALA THR ARG ASP THR PRO PRO LYS
SEQRES 45 A 994 ARG GLU GLU MET VAL LEU ASP ASP SER SER ARG PHE MET
SEQRES 46 A 994 GLU TYR GLU THR ASP LEU THR PHE VAL GLY VAL VAL GLY
SEQRES 47 A 994 MET LEU ASP PRO PRO ARG LYS GLU VAL MET GLY SER ILE
SEQRES 48 A 994 GLN LEU CYS ARG ASP ALA GLY ILE ARG VAL ILE MET ILE
SEQRES 49 A 994 THR GLY ASP ASN LYS GLY THR ALA ILE ALA ILE CYS ARG
SEQRES 50 A 994 ARG ILE GLY ILE PHE GLY GLU ASN GLU GLU VAL ALA ASP
SEQRES 51 A 994 ARG ALA TYR THR GLY ARG GLU PHE ASP ASP LEU PRO LEU
SEQRES 52 A 994 ALA GLU GLN ARG GLU ALA CYS ARG ARG ALA CYS CYS PHE
SEQRES 53 A 994 ALA ARG VAL GLU PRO SER HIS LYS SER LYS ILE VAL GLU
SEQRES 54 A 994 TYR LEU GLN SER TYR ASP GLU ILE THR ALA MET THR GLY
SEQRES 55 A 994 ASP GLY VAL ASN ASP ALA PRO ALA LEU LYS LYS ALA GLU
SEQRES 56 A 994 ILE GLY ILE ALA MET GLY SER GLY THR ALA VAL ALA LYS
SEQRES 57 A 994 THR ALA SER GLU MET VAL LEU ALA ASP ASP ASN PHE SER
SEQRES 58 A 994 THR ILE VAL ALA ALA VAL GLU GLU GLY ARG ALA ILE TYR
SEQRES 59 A 994 ASN ASN MET LYS GLN PHE ILE ARG TYR LEU ILE SER SER
SEQRES 60 A 994 ASN VAL GLY GLU VAL VAL CYS ILE PHE LEU THR ALA ALA
SEQRES 61 A 994 LEU GLY LEU PRO GLU ALA LEU ILE PRO VAL GLN LEU LEU
SEQRES 62 A 994 TRP VAL ASN LEU VAL THR ASP GLY LEU PRO ALA THR ALA
SEQRES 63 A 994 LEU GLY PHE ASN PRO PRO ASP LEU ASP ILE MET ASP ARG
SEQRES 64 A 994 PRO PRO ARG SER PRO LYS GLU PRO LEU ILE SER GLY TRP
SEQRES 65 A 994 LEU PHE PHE ARG TYR MET ALA ILE GLY GLY TYR VAL GLY
SEQRES 66 A 994 ALA ALA THR VAL GLY ALA ALA ALA TRP TRP PHE MET TYR
SEQRES 67 A 994 ALA GLU ASP GLY PRO GLY VAL THR TYR HIS GLN LEU THR
SEQRES 68 A 994 HIS PHE MET GLN CYS THR GLU ASP HIS PRO HIS PHE GLU
SEQRES 69 A 994 GLY LEU ASP CYS GLU ILE PHE GLU ALA PRO GLU PRO MET
SEQRES 70 A 994 THR MET ALA LEU SER VAL LEU VAL THR ILE GLU MET CYS
SEQRES 71 A 994 ASN ALA LEU ASN SER LEU SER GLU ASN GLN SER LEU MET
SEQRES 72 A 994 ARG MET PRO PRO TRP VAL ASN ILE TRP LEU LEU GLY SER
SEQRES 73 A 994 ILE CYS LEU SER MET SER LEU HIS PHE LEU ILE LEU TYR
SEQRES 74 A 994 VAL ASP PRO LEU PRO MET ILE PHE LYS LEU LYS ALA LEU
SEQRES 75 A 994 ASP LEU THR GLN TRP LEU MET VAL LEU LYS ILE SER LEU
SEQRES 76 A 994 PRO VAL ILE GLY LEU ASP GLU ILE LEU LYS PHE ILE ALA
SEQRES 77 A 994 ARG ASN TYR LEU GLU GLY
MODRES 3BA6 PHD A 351 ASP ASPARTYL PHOSPHATE
HET PHD A 351 12
HET CA A1003 1
HET CA A1004 1
HET CA A1005 1
HET K A1006 1
HET AN2 A1001 27
HETNAM PHD ASPARTYL PHOSPHATE
HETNAM CA CALCIUM ION
HETNAM K POTASSIUM ION
HETNAM AN2 AMP PHOSPHORAMIDATE
FORMUL 1 PHD C4 H8 N O7 P
FORMUL 2 CA 3(CA 2+)
FORMUL 5 K K 1+
FORMUL 6 AN2 C10 H16 N6 O9 P2
FORMUL 7 HOH *9(H2 O)
HELIX 1 1 SER A 8 GLY A 17 1 10
HELIX 2 2 THR A 25 GLY A 37 1 13
HELIX 3 3 LEU A 49 GLU A 55 1 7
HELIX 4 4 ASP A 59 LEU A 75 1 17
HELIX 5 5 ILE A 85 GLU A 121 1 37
HELIX 6 6 ARG A 143 ILE A 145 5 3
HELIX 7 7 VAL A 200 LYS A 204 5 5
HELIX 8 8 THR A 226 SER A 229 5 4
HELIX 9 9 THR A 230 ILE A 235 1 6
HELIX 10 10 THR A 247 ASN A 275 1 29
HELIX 11 11 ILE A 276 ASN A 280 5 5
HELIX 12 12 ASP A 281 GLY A 285 5 5
HELIX 13 13 GLY A 291 ILE A 307 1 17
HELIX 14 14 GLY A 310 LYS A 329 1 20
HELIX 15 15 PRO A 337 CYS A 344 1 8
HELIX 16 16 ARG A 403 GLN A 406 5 4
HELIX 17 17 PHE A 407 CYS A 420 1 14
HELIX 18 18 GLU A 439 ASN A 453 1 15
HELIX 19 19 VAL A 465 ALA A 468 5 4
HELIX 20 20 ASN A 469 LEU A 478 1 10
HELIX 21 21 ALA A 517 ARG A 524 1 8
HELIX 22 22 THR A 538 GLY A 555 1 18
HELIX 23 23 LYS A 572 MET A 576 5 5
HELIX 24 24 ASP A 580 SER A 582 5 3
HELIX 25 25 ARG A 583 GLU A 588 1 6
HELIX 26 26 GLU A 606 ALA A 617 1 12
HELIX 27 27 ASN A 628 GLY A 640 1 13
HELIX 28 28 GLY A 655 LEU A 661 1 7
HELIX 29 29 PRO A 662 ALA A 673 1 12
HELIX 30 30 GLU A 680 SER A 693 1 14
HELIX 31 31 ASP A 707 ALA A 714 1 8
HELIX 32 32 THR A 724 ALA A 730 1 7
HELIX 33 33 PHE A 740 GLY A 782 1 43
HELIX 34 34 ILE A 788 ASP A 800 1 13
HELIX 35 35 GLY A 801 GLY A 808 1 8
HELIX 36 36 ASP A 815 ARG A 819 5 5
HELIX 37 37 SER A 830 THR A 848 1 19
HELIX 38 38 THR A 848 MET A 857 1 10
HELIX 39 39 THR A 866 THR A 871 5 6
HELIX 40 40 ASP A 879 PHE A 883 5 5
HELIX 41 41 ALA A 893 ALA A 912 1 20
HELIX 42 42 PRO A 926 VAL A 929 5 4
HELIX 43 43 ASN A 930 VAL A 950 1 21
HELIX 44 44 ASP A 951 PHE A 957 1 7
HELIX 45 45 THR A 965 LEU A 975 1 11
HELIX 46 46 LEU A 975 ALA A 988 1 14
SHEET 1 A 6 GLN A 138 LYS A 141 0
SHEET 2 A 6 MET A 126 TYR A 130 -1 N VAL A 129 O GLN A 138
SHEET 3 A 6 ILE A 150 ALA A 154 -1 O GLU A 152 N LYS A 128
SHEET 4 A 6 LYS A 218 THR A 225 -1 O ALA A 219 N VAL A 153
SHEET 5 A 6 ASP A 162 ILE A 168 -1 N ARG A 164 O ILE A 222
SHEET 6 A 6 MET A 207 LEU A 208 -1 O LEU A 208 N ILE A 163
SHEET 1 B 3 VAL A 187 ILE A 188 0
SHEET 2 B 3 ARG A 174 ASP A 176 -1 N VAL A 175 O VAL A 187
SHEET 3 B 3 ASN A 213 ALA A 216 -1 O ASN A 213 N ASP A 176
SHEET 1 C 8 ALA A 331 VAL A 333 0
SHEET 2 C 8 MET A 733 LEU A 735 -1 O VAL A 734 N ILE A 332
SHEET 3 C 8 ILE A 716 MET A 720 1 N ALA A 719 O MET A 733
SHEET 4 C 8 THR A 698 GLY A 702 1 N MET A 700 O ILE A 718
SHEET 5 C 8 VAL A 347 SER A 350 1 N CYS A 349 O ALA A 699
SHEET 6 C 8 ARG A 620 ILE A 624 1 O ARG A 620 N ILE A 348
SHEET 7 C 8 CYS A 675 ALA A 677 1 O PHE A 676 N MET A 623
SHEET 8 C 8 ALA A 652 THR A 654 1 N TYR A 653 O ALA A 677
SHEET 1 D 9 LYS A 400 PRO A 401 0
SHEET 2 D 9 VAL A 395 LYS A 397 -1 N LYS A 397 O LYS A 400
SHEET 3 D 9 PHE A 376 ILE A 384 -1 N SER A 383 O LEU A 396
SHEET 4 D 9 SER A 362 ASP A 373 -1 N ASP A 370 O SER A 378
SHEET 5 D 9 LEU A 591 LEU A 600 -1 O GLY A 598 N LYS A 365
SHEET 6 D 9 ARG A 560 ARG A 567 -1 N ARG A 560 O MET A 599
SHEET 7 D 9 LYS A 511 GLY A 516 -1 N VAL A 514 O ALA A 565
SHEET 8 D 9 SER A 493 PRO A 500 -1 N CYS A 498 O LYS A 511
SHEET 9 D 9 MET A 479 SER A 488 -1 N LYS A 480 O SER A 499
SHEET 1 E 7 LYS A 400 PRO A 401 0
SHEET 2 E 7 VAL A 395 LYS A 397 -1 N LYS A 397 O LYS A 400
SHEET 3 E 7 PHE A 376 ILE A 384 -1 N SER A 383 O LEU A 396
SHEET 4 E 7 SER A 362 ASP A 373 -1 N ASP A 370 O SER A 378
SHEET 5 E 7 LEU A 591 LEU A 600 -1 O GLY A 598 N LYS A 365
SHEET 6 E 7 CYS A 525 VAL A 530 1 N TYR A 527 O PHE A 593
SHEET 7 E 7 THR A 533 PRO A 536 -1 O THR A 533 N VAL A 530
SHEET 1 F 2 SER A 424 ASN A 428 0
SHEET 2 F 2 VAL A 433 VAL A 437 -1 O GLU A 435 N ASP A 426
LINK C SER A 350 N PHD A 351 1555 1555 1.33
LINK C PHD A 351 N LYS A 352 1555 1555 1.34
LINK O VAL A 304 CA CA A1003 1555 1555 2.78
LINK O ALA A 305 CA CA A1003 1555 1555 2.69
LINK O ILE A 307 CA CA A1003 1555 1555 2.66
LINK OE2 GLU A 309 CA CA A1003 1555 1555 2.75
LINK OD2 PHD A 351 CA CA A1005 1555 1555 2.48
LINK OP1 PHD A 351 CA CA A1005 1555 1555 2.71
LINK O THR A 353 CA CA A1005 1555 1555 2.35
LINK OD2 ASP A 703 CA CA A1005 1555 1555 2.47
LINK OD1 ASN A 768 CA CA A1004 1555 1555 2.48
LINK OE2 GLU A 771 CA CA A1004 1555 1555 2.70
LINK OD1 ASN A 796 CA CA A1003 1555 1555 2.76
LINK OG1 THR A 799 CA CA A1004 1555 1555 2.72
LINK OD2 ASP A 800 CA CA A1003 1555 1555 2.86
LINK OD2 ASP A 800 CA CA A1004 1555 1555 2.84
LINK OE2 GLU A 908 CA CA A1004 1555 1555 2.87
LINK CA CA A1005 O HOH A1008 1555 1555 2.75
LINK CA CA A1005 O HOH A1042 1555 1555 2.51
LINK CA CA A1005 O HOH A1044 1555 1555 3.00
SITE 1 AC1 6 VAL A 304 ALA A 305 ILE A 307 GLU A 309
SITE 2 AC1 6 ASN A 796 ASP A 800
SITE 1 AC2 5 ASN A 768 GLU A 771 THR A 799 ASP A 800
SITE 2 AC2 5 GLU A 908
SITE 1 AC3 6 PHD A 351 THR A 353 ASP A 703 HOH A1008
SITE 2 AC3 6 HOH A1042 HOH A1044
SITE 1 AC4 4 LEU A 711 LYS A 712 ALA A 714 GLU A 732
SITE 1 AC5 19 PHD A 351 THR A 353 GLU A 442 PHE A 487
SITE 2 AC5 19 ARG A 489 MET A 494 LYS A 515 GLY A 516
SITE 3 AC5 19 ALA A 517 ARG A 560 LEU A 562 THR A 625
SITE 4 AC5 19 GLY A 626 ASP A 627 ARG A 678 HOH A1044
SITE 5 AC5 19 HOH A1047 HOH A1049 HOH A1050
CRYST1 162.510 75.967 152.407 90.00 109.01 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 0.006153 0.000000 0.002120 0.00000
SCALE2 0.000000 0.013164 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006940 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
