HEADER HYDROLASE 16-SEP-11 4A1N
TITLE HUMAN MITOCHONDRIAL ENDO-EXONUCLEASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NUCLEASE EXOG, MITOCHONDRIAL;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 42-368;
COMPND 5 SYNONYM: ENDONUCLEASE G-LIKE 1, ENDO G-LIKE 1, ENDO-EXO NUCLEASE;
COMPND 6 EC: 3.1.30.-;
COMPND 7 ENGINEERED: YES;
COMPND 8 OTHER_DETAILS: CLONING ARTIFACT GLU330VAL
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: R3 PRARE;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC-CH2
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.WELIN,M.MOCHE,C.H.ARROWSMITH,H.BERGLUND,C.BOUNTRA,R.COLLINS,
AUTHOR 2 A.M.EDWARDS,S.FLODIN,S.GRASLUND,M.HAMMARSTROM,I.JOHANSSON,
AUTHOR 3 T.KARLBERG,T.KOTENYOVA,T.NYMAN,C.PERSSON,H.SCHULER,A.G.THORSELL,
AUTHOR 4 L.TRESAUGUES,J.WEIGELT,P.NORDLUND
REVDAT 2 20-DEC-23 4A1N 1 REMARK LINK
REVDAT 1 29-FEB-12 4A1N 0
JRNL AUTH M.WELIN,M.MOCHE,C.H.ARROWSMITH,H.BERGLUND,C.BOUNTRA,
JRNL AUTH 2 R.COLLINS,A.M.EDWARDS,S.FLODIN,S.GRASLUND,M.HAMMARSTROM,
JRNL AUTH 3 I.JOHANSSON,T.KARLBERG,T.KOTENYOVA,T.NYMAN,C.PERSSON,
JRNL AUTH 4 H.SCHULER,A.G.THORSELL,L.TRESAUGUES,J.WEIGELT,P.NORDLUND
JRNL TITL HUMAN MITOCHONDRIAL ENDO-EXONUCLEASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.1
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.68
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 13052
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) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 653
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 7
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.02
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2661
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.1954
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2528
REMARK 3 BIN R VALUE (WORKING SET) : 0.1927
REMARK 3 BIN FREE R VALUE : 0.2439
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 133
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2299
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 67
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 51.36
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.17
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.28680
REMARK 3 B22 (A**2) : 0.28680
REMARK 3 B33 (A**2) : -0.57370
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.283
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.411
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.266
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.401
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.268
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.928
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.895
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2364 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 3207 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1083 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 59 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 343 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2364 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 1 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 303 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 2745 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.14
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.45
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 3.10
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: IDEAL-DIST CONTACT TERM CONTACT SETUP.
REMARK 3 RESIDUE TYPES WITHOUT CCP4 ATOM TYPE IN LIBRARY=MG CL NA. NUMBER
REMARK 3 OF ATOMS WITH PROPER CCP4 ATOM TYPE=2375. NUMBER WITH APPROX
REMARK 3 DEFAULT CCP4 ATOM TYPE=2. NUMBER TREATED BY BAD NON-BONDED
REMARK 3 CONTACTS=2.
REMARK 4
REMARK 4 4A1N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-SEP-11.
REMARK 100 THE DEPOSITION ID IS D_1290049673.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-AUG-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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) : 0.91841
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 : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13052
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 44.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 11.00
REMARK 200 R MERGE (I) : 0.16000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.8000
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 11.20
REMARK 200 R MERGE FOR SHELL (I) : 0.69000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.800
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 3ISM
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 27.96333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 55.92667
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 55.92667
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 27.96333
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -109.9 KCAL/MOL
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 350 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 -0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 27.96333
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 41
REMARK 465 GLN A 42
REMARK 465 GLY A 43
REMARK 465 ALA A 44
REMARK 465 GLU A 45
REMARK 465 GLY A 46
REMARK 465 ALA A 47
REMARK 465 LEU A 48
REMARK 465 THR A 49
REMARK 465 GLY A 50
REMARK 465 LYS A 51
REMARK 465 GLN A 52
REMARK 465 PRO A 53
REMARK 465 ASP A 54
REMARK 465 GLY A 55
REMARK 465 SER A 56
REMARK 465 ALA A 57
REMARK 465 GLU A 58
REMARK 465 ALA A 319
REMARK 465 ARG A 320
REMARK 465 ALA A 335
REMARK 465 GLU A 352
REMARK 465 GLU A 353
REMARK 465 LEU A 354
REMARK 465 LYS A 355
REMARK 465 ALA A 356
REMARK 465 LYS A 357
REMARK 465 GLU A 358
REMARK 465 GLN A 359
REMARK 465 SER A 360
REMARK 465 GLY A 361
REMARK 465 THR A 362
REMARK 465 GLN A 363
REMARK 465 ILE A 364
REMARK 465 ARG A 365
REMARK 465 LYS A 366
REMARK 465 PRO A 367
REMARK 465 SER A 368
REMARK 465 ALA A 369
REMARK 465 HIS A 370
REMARK 465 HIS A 371
REMARK 465 HIS A 372
REMARK 465 HIS A 373
REMARK 465 HIS A 374
REMARK 465 HIS A 375
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLN A 86 CG CD OE1 NE2
REMARK 470 LYS A 110 CG CD CE NZ
REMARK 470 LYS A 327 CG CD CE NZ
REMARK 470 VAL A 330 CG1 CG2
REMARK 470 LYS A 333 CG CD CE NZ
REMARK 470 GLU A 338 CG CD OE1 OE2
REMARK 470 ASP A 341 CG OD1 OD2
REMARK 470 LYS A 349 CG CD CE NZ
REMARK 470 LYS A 350 CG CD CE NZ
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 LEU A 160 -8.49 -57.97
REMARK 500 PHE A 281 66.80 38.81
REMARK 500 GLU A 317 -47.43 174.54
REMARK 500 VAL A 322 -175.49 62.14
REMARK 500 LEU A 323 52.54 -109.69
REMARK 500 ILE A 337 -101.68 -75.68
REMARK 500 GLU A 338 -1.00 72.68
REMARK 500 PRO A 339 -127.10 -86.17
REMARK 500 ASP A 340 131.25 70.91
REMARK 500 TYR A 347 37.37 -90.06
REMARK 500 GLU A 348 -43.96 -154.01
REMARK 500 LYS A 350 -64.49 -100.04
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 MG A1352 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 171 OD1
REMARK 620 2 HOH A2024 O 94.3
REMARK 620 3 HOH A2031 O 77.1 95.3
REMARK 620 4 HOH A2032 O 73.4 166.6 87.1
REMARK 620 5 HOH A2034 O 146.6 118.3 91.7 74.7
REMARK 620 6 HOH A2040 O 85.0 94.3 160.3 79.8 98.9
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 MG A 1352
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1353
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1354
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 1355
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THERE IS A GLU330VAL MUTATION IN THE PROTEIN SEQUENCE. THE
REMARK 999 SIDE CHAIN WAS NOT VISIBLE IN THE ELECTRON DENSITY. WE
REMARK 999 BELIEVE THIS IS A CLONING ARTIFACT.
DBREF 4A1N A 42 368 UNP Q9Y2C4 EXOG_HUMAN 42 368
SEQADV 4A1N MET A 41 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 4A1N VAL A 330 UNP Q9Y2C4 GLU 330 CLONING ARTIFACT
SEQADV 4A1N ALA A 369 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 4A1N HIS A 370 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 4A1N HIS A 371 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 4A1N HIS A 372 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 4A1N HIS A 373 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 4A1N HIS A 374 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 4A1N HIS A 375 UNP Q9Y2C4 EXPRESSION TAG
SEQRES 1 A 335 MET GLN GLY ALA GLU GLY ALA LEU THR GLY LYS GLN PRO
SEQRES 2 A 335 ASP GLY SER ALA GLU LYS ALA VAL LEU GLU GLN PHE GLY
SEQRES 3 A 335 PHE PRO LEU THR GLY THR GLU ALA ARG CYS TYR THR ASN
SEQRES 4 A 335 HIS ALA LEU SER TYR ASP GLN ALA LYS ARG VAL PRO ARG
SEQRES 5 A 335 TRP VAL LEU GLU HIS ILE SER LYS SER LYS ILE MET GLY
SEQRES 6 A 335 ASP ALA ASP ARG LYS HIS CYS LYS PHE LYS PRO ASP PRO
SEQRES 7 A 335 ASN ILE PRO PRO THR PHE SER ALA PHE ASN GLU ASP TYR
SEQRES 8 A 335 VAL GLY SER GLY TRP SER ARG GLY HIS MET ALA PRO ALA
SEQRES 9 A 335 GLY ASN ASN LYS PHE SER SER LYS ALA MET ALA GLU THR
SEQRES 10 A 335 PHE TYR LEU SER ASN ILE VAL PRO GLN ASP PHE ASP ASN
SEQRES 11 A 335 ASN SER GLY TYR TRP ASN ARG ILE GLU MET TYR CYS ARG
SEQRES 12 A 335 GLU LEU THR GLU ARG PHE GLU ASP VAL TRP VAL VAL SER
SEQRES 13 A 335 GLY PRO LEU THR LEU PRO GLN THR ARG GLY ASP GLY LYS
SEQRES 14 A 335 LYS ILE VAL SER TYR GLN VAL ILE GLY GLU ASP ASN VAL
SEQRES 15 A 335 ALA VAL PRO SER HIS LEU TYR LYS VAL ILE LEU ALA ARG
SEQRES 16 A 335 ARG SER SER VAL SER THR GLU PRO LEU ALA LEU GLY ALA
SEQRES 17 A 335 PHE VAL VAL PRO ASN GLU ALA ILE GLY PHE GLN PRO GLN
SEQRES 18 A 335 LEU THR GLU PHE GLN VAL SER LEU GLN ASP LEU GLU LYS
SEQRES 19 A 335 LEU SER GLY LEU VAL PHE PHE PRO HIS LEU ASP ARG THR
SEQRES 20 A 335 SER ASP ILE ARG ASN ILE CYS SER VAL ASP THR CYS LYS
SEQRES 21 A 335 LEU LEU ASP PHE GLN GLU PHE THR LEU TYR LEU SER THR
SEQRES 22 A 335 ARG LYS ILE GLU GLY ALA ARG SER VAL LEU ARG LEU GLU
SEQRES 23 A 335 LYS ILE MET VAL ASN LEU LYS ASN ALA GLU ILE GLU PRO
SEQRES 24 A 335 ASP ASP TYR PHE MET SER ARG TYR GLU LYS LYS LEU GLU
SEQRES 25 A 335 GLU LEU LYS ALA LYS GLU GLN SER GLY THR GLN ILE ARG
SEQRES 26 A 335 LYS PRO SER ALA HIS HIS HIS HIS HIS HIS
HET MG A1352 1
HET CL A1353 1
HET CL A1354 1
HET NA A1355 1
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
HETNAM NA SODIUM ION
FORMUL 2 MG MG 2+
FORMUL 3 CL 2(CL 1-)
FORMUL 5 NA NA 1+
FORMUL 6 HOH *67(H2 O)
HELIX 1 1 ASP A 108 CYS A 112 5 5
HELIX 2 2 PHE A 127 VAL A 132 1 6
HELIX 3 3 PRO A 143 ASN A 147 5 5
HELIX 4 4 SER A 150 THR A 157 1 8
HELIX 5 5 ASP A 167 GLY A 173 1 7
HELIX 6 6 GLY A 173 LEU A 185 1 13
HELIX 7 7 THR A 186 ARG A 188 5 3
HELIX 8 8 GLN A 261 GLU A 264 5 4
HELIX 9 9 SER A 268 GLY A 277 1 10
HELIX 10 10 CYS A 294 VAL A 296 5 3
HELIX 11 11 ASP A 303 ILE A 316 1 14
HELIX 12 12 ARG A 324 ASN A 334 1 11
HELIX 13 13 ASP A 340 SER A 345 1 6
SHEET 1 AA 7 ALA A 74 CYS A 76 0
SHEET 2 AA 7 HIS A 80 ASP A 85 -1 O LEU A 82 N ARG A 75
SHEET 3 AA 7 VAL A 90 ILE A 98 -1 O VAL A 90 N ASP A 85
SHEET 4 AA 7 ASP A 191 LEU A 199 -1 O VAL A 192 N ILE A 98
SHEET 5 AA 7 HIS A 227 ARG A 235 -1 O HIS A 227 N LEU A 199
SHEET 6 AA 7 LEU A 244 PRO A 252 -1 O ALA A 245 N ALA A 234
SHEET 7 AA 7 GLN A 266 VAL A 267 1 O VAL A 267 N ALA A 248
SHEET 1 AB 7 ALA A 74 CYS A 76 0
SHEET 2 AB 7 HIS A 80 ASP A 85 -1 O LEU A 82 N ARG A 75
SHEET 3 AB 7 VAL A 90 ILE A 98 -1 O VAL A 90 N ASP A 85
SHEET 4 AB 7 ASP A 191 LEU A 199 -1 O VAL A 192 N ILE A 98
SHEET 5 AB 7 HIS A 227 ARG A 235 -1 O HIS A 227 N LEU A 199
SHEET 6 AB 7 LEU A 244 PRO A 252 -1 O ALA A 245 N ALA A 234
SHEET 7 AB 7 ILE A 290 ASN A 292 1 O ARG A 291 N LEU A 246
SHEET 1 AC 2 GLN A 266 VAL A 267 0
SHEET 2 AC 2 LEU A 244 PRO A 252 1 O ALA A 248 N VAL A 267
SHEET 1 AD 2 SER A 137 HIS A 140 0
SHEET 2 AD 2 ILE A 163 GLN A 166 -1 O VAL A 164 N GLY A 139
SHEET 1 AE 2 GLN A 203 THR A 204 0
SHEET 2 AE 2 LYS A 210 ILE A 211 -1 O ILE A 211 N GLN A 203
SHEET 1 AF 2 VAL A 216 ILE A 217 0
SHEET 2 AF 2 VAL A 222 ALA A 223 -1 O VAL A 222 N ILE A 217
LINK OD1 ASN A 171 MG MG A1352 1555 1555 2.19
LINK MG MG A1352 O HOH A2024 1555 1555 2.33
LINK MG MG A1352 O HOH A2031 1555 1555 2.24
LINK MG MG A1352 O HOH A2032 1555 1555 2.24
LINK MG MG A1352 O HOH A2034 1555 1555 2.00
LINK MG MG A1352 O HOH A2040 1555 1555 1.93
SITE 1 AC1 6 ASN A 171 HOH A2024 HOH A2031 HOH A2032
SITE 2 AC1 6 HOH A2034 HOH A2040
SITE 1 AC2 4 ASP A 169 TYR A 174 ILE A 256 GLY A 257
SITE 1 AC3 1 ARG A 138
SITE 1 AC4 2 GLU A 129 ASP A 130
CRYST1 103.180 103.180 83.890 90.00 90.00 120.00 P 31 2 1 6
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 0.009692 0.005596 0.000000 0.00000
SCALE2 0.000000 0.011191 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011920 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
