HEADER HYDROLASE/RNA/DNA 24-MAR-18 5ZKJ
TITLE HUMAN EXOG-H140A IN COMPLEX WITH RNA/DNA HYBRID DUPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NUCLEASE EXOG, MITOCHONDRIAL;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ENDONUCLEASE G-LIKE 1,ENDO G-LIKE 1;
COMPND 5 EC: 3.1.30.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: RNA (5'-R(P*CP*GP*GP*GP*AP*UP*GP*UP*CP*AP*CP*G)-3');
COMPND 10 CHAIN: C, E;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: DNA (5'-D(*CP*GP*TP*GP*AP*CP*AP*TP*CP*CP*CP*G)-3');
COMPND 14 CHAIN: D, F;
COMPND 15 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: EXOG, ENDOGL1, ENDOGL2, ENGL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA 2 (DE3) PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 14 ORGANISM_TAXID: 32630;
SOURCE 15 MOL_ID: 3;
SOURCE 16 SYNTHETIC: YES;
SOURCE 17 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 18 ORGANISM_TAXID: 32630
KEYWDS ENZYME-SUBSTRATE COMPLEX, MITOCHONDRIAL EXONUCLEASE, HYDROLASE-RNA-
KEYWDS 2 DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.C.WU,J.L.J.LIN,H.S.YUAN
REVDAT 4 22-NOV-23 5ZKJ 1 LINK
REVDAT 3 19-JUN-19 5ZKJ 1 JRNL
REVDAT 2 17-APR-19 5ZKJ 1 JRNL
REVDAT 1 03-APR-19 5ZKJ 0
JRNL AUTH C.C.WU,J.L.J.LIN,H.F.YANG-YEN,H.S.YUAN
JRNL TITL A UNIQUE EXONUCLEASE EXOG CLEAVES BETWEEN RNA AND DNA IN
JRNL TITL 2 MITOCHONDRIAL DNA REPLICATION.
JRNL REF NUCLEIC ACIDS RES. V. 47 5405 2019
JRNL REFN ESSN 1362-4962
JRNL PMID 30949702
JRNL DOI 10.1093/NAR/GKZ241
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.43
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.980
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.4
REMARK 3 NUMBER OF REFLECTIONS : 25986
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.160
REMARK 3 FREE R VALUE TEST SET COUNT : 1340
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 28.4353 - 6.0106 0.89 2311 122 0.1584 0.1714
REMARK 3 2 6.0106 - 4.7782 0.93 2415 129 0.1566 0.2142
REMARK 3 3 4.7782 - 4.1763 0.93 2409 134 0.1497 0.2123
REMARK 3 4 4.1763 - 3.7954 0.95 2397 187 0.1716 0.2384
REMARK 3 5 3.7954 - 3.5239 0.97 2518 119 0.1927 0.2353
REMARK 3 6 3.5239 - 3.3165 0.97 2520 114 0.2088 0.2421
REMARK 3 7 3.3165 - 3.1506 0.98 2550 129 0.2241 0.2928
REMARK 3 8 3.1506 - 3.0136 0.99 2572 131 0.2363 0.3251
REMARK 3 9 3.0136 - 2.8977 0.98 2550 126 0.2635 0.3099
REMARK 3 10 2.8977 - 2.7978 0.94 2404 149 0.2894 0.3274
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.390
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.100
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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 : 0.003 6059
REMARK 3 ANGLE : 0.487 8419
REMARK 3 CHIRALITY : 0.040 935
REMARK 3 PLANARITY : 0.003 921
REMARK 3 DIHEDRAL : 13.770 3523
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: NULL
REMARK 4
REMARK 4 5ZKJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-MAR-18.
REMARK 100 THE DEPOSITION ID IS D_1300007178.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-SEP-17
REMARK 200 TEMPERATURE (KELVIN) : 80
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSRRC
REMARK 200 BEAMLINE : TPS 05A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : LN2-COOLED, FIXED-EXIT DOUBLE
REMARK 200 CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX300HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25994
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.798
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 200 DATA REDUNDANCY : 1.900
REMARK 200 R MERGE (I) : 0.04900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.6000
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) : 2.88
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.7
REMARK 200 DATA REDUNDANCY IN SHELL : 1.80
REMARK 200 R MERGE FOR SHELL (I) : 0.46800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.747
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: 5T4I
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6.0, 22% PEG 400, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 0.00000
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 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 83.78800
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 48.37502
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 35.14600
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 83.78800
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 48.37502
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 35.14600
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 83.78800
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 48.37502
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 35.14600
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 96.75005
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 70.29200
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 96.75005
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 70.29200
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 96.75005
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 70.29200
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -122.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
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 21
REMARK 465 GLY A 22
REMARK 465 SER A 23
REMARK 465 SER A 24
REMARK 465 HIS A 25
REMARK 465 HIS A 26
REMARK 465 HIS A 27
REMARK 465 HIS A 28
REMARK 465 HIS A 29
REMARK 465 HIS A 30
REMARK 465 SER A 31
REMARK 465 SER A 32
REMARK 465 GLY A 33
REMARK 465 LEU A 34
REMARK 465 VAL A 35
REMARK 465 PRO A 36
REMARK 465 ARG A 37
REMARK 465 GLY A 38
REMARK 465 SER A 39
REMARK 465 HIS A 40
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 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 MET B 21
REMARK 465 GLY B 22
REMARK 465 SER B 23
REMARK 465 SER B 24
REMARK 465 HIS B 25
REMARK 465 HIS B 26
REMARK 465 HIS B 27
REMARK 465 HIS B 28
REMARK 465 HIS B 29
REMARK 465 HIS B 30
REMARK 465 SER B 31
REMARK 465 SER B 32
REMARK 465 GLY B 33
REMARK 465 LEU B 34
REMARK 465 VAL B 35
REMARK 465 PRO B 36
REMARK 465 ARG B 37
REMARK 465 GLY B 38
REMARK 465 SER B 39
REMARK 465 HIS B 40
REMARK 465 MET B 41
REMARK 465 GLN B 42
REMARK 465 GLY B 43
REMARK 465 ALA B 44
REMARK 465 GLU B 45
REMARK 465 GLY B 46
REMARK 465 ALA B 47
REMARK 465 LEU B 48
REMARK 465 THR B 49
REMARK 465 GLY B 50
REMARK 465 LYS B 51
REMARK 465 GLN B 52
REMARK 465 PRO B 53
REMARK 465 ASP B 54
REMARK 465 GLY B 55
REMARK 465 GLN B 359
REMARK 465 SER B 360
REMARK 465 GLY B 361
REMARK 465 THR B 362
REMARK 465 GLN B 363
REMARK 465 ILE B 364
REMARK 465 ARG B 365
REMARK 465 LYS B 366
REMARK 465 PRO B 367
REMARK 465 SER B 368
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 C C 1 P C C 1 OP3 -0.127
REMARK 500 C E 1 P C E 1 OP3 -0.127
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 ASN A 79 29.59 -154.32
REMARK 500 HIS A 80 144.91 -173.49
REMARK 500 ILE A 256 -59.41 -127.00
REMARK 500 PHE A 281 74.09 47.16
REMARK 500 SER A 288 177.00 -58.75
REMARK 500 GLU A 336 -5.07 78.87
REMARK 500 PHE B 281 73.37 52.04
REMARK 500 SER B 288 -170.05 -69.49
REMARK 500 ASP B 297 -159.15 -112.19
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 A 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 171 OD1
REMARK 620 2 HOH A 507 O 168.2
REMARK 620 3 HOH A 508 O 101.1 90.5
REMARK 620 4 G E 2 O3' 78.8 91.1 159.7
REMARK 620 5 G E 3 OP1 72.9 107.2 100.9 59.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 101 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 171 OD1
REMARK 620 2 HOH B 508 O 78.3
REMARK 620 3 HOH B 513 O 173.8 95.5
REMARK 620 4 HOH B 522 O 101.4 98.1 80.3
REMARK 620 5 G C 2 O3' 84.1 99.2 96.0 162.6
REMARK 620 6 G C 3 OP1 94.5 159.9 90.9 101.7 61.2
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 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 101
DBREF 5ZKJ A 42 368 UNP Q9Y2C4 EXOG_HUMAN 42 368
DBREF 5ZKJ B 42 368 UNP Q9Y2C4 EXOG_HUMAN 42 368
DBREF 5ZKJ C 1 12 PDB 5ZKJ 5ZKJ 1 12
DBREF 5ZKJ D 1 12 PDB 5ZKJ 5ZKJ 1 12
DBREF 5ZKJ E 1 12 PDB 5ZKJ 5ZKJ 1 12
DBREF 5ZKJ F 1 12 PDB 5ZKJ 5ZKJ 1 12
SEQADV 5ZKJ MET A 21 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 5ZKJ GLY A 22 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 5ZKJ SER A 23 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 5ZKJ SER A 24 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 5ZKJ HIS A 25 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 5ZKJ HIS A 26 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 5ZKJ HIS A 27 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 5ZKJ HIS A 28 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 5ZKJ HIS A 29 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 5ZKJ HIS A 30 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 5ZKJ SER A 31 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 5ZKJ SER A 32 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 5ZKJ GLY A 33 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 5ZKJ LEU A 34 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 5ZKJ VAL A 35 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 5ZKJ PRO A 36 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 5ZKJ ARG A 37 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 5ZKJ GLY A 38 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 5ZKJ SER A 39 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 5ZKJ HIS A 40 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 5ZKJ MET A 41 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 5ZKJ ALA A 140 UNP Q9Y2C4 HIS 140 ENGINEERED MUTATION
SEQADV 5ZKJ MET B 21 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 5ZKJ GLY B 22 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 5ZKJ SER B 23 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 5ZKJ SER B 24 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 5ZKJ HIS B 25 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 5ZKJ HIS B 26 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 5ZKJ HIS B 27 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 5ZKJ HIS B 28 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 5ZKJ HIS B 29 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 5ZKJ HIS B 30 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 5ZKJ SER B 31 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 5ZKJ SER B 32 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 5ZKJ GLY B 33 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 5ZKJ LEU B 34 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 5ZKJ VAL B 35 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 5ZKJ PRO B 36 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 5ZKJ ARG B 37 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 5ZKJ GLY B 38 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 5ZKJ SER B 39 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 5ZKJ HIS B 40 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 5ZKJ MET B 41 UNP Q9Y2C4 EXPRESSION TAG
SEQADV 5ZKJ ALA B 140 UNP Q9Y2C4 HIS 140 ENGINEERED MUTATION
SEQRES 1 A 348 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 348 LEU VAL PRO ARG GLY SER HIS MET GLN GLY ALA GLU GLY
SEQRES 3 A 348 ALA LEU THR GLY LYS GLN PRO ASP GLY SER ALA GLU LYS
SEQRES 4 A 348 ALA VAL LEU GLU GLN PHE GLY PHE PRO LEU THR GLY THR
SEQRES 5 A 348 GLU ALA ARG CYS TYR THR ASN HIS ALA LEU SER TYR ASP
SEQRES 6 A 348 GLN ALA LYS ARG VAL PRO ARG TRP VAL LEU GLU HIS ILE
SEQRES 7 A 348 SER LYS SER LYS ILE MET GLY ASP ALA ASP ARG LYS HIS
SEQRES 8 A 348 CYS LYS PHE LYS PRO ASP PRO ASN ILE PRO PRO THR PHE
SEQRES 9 A 348 SER ALA PHE ASN GLU ASP TYR VAL GLY SER GLY TRP SER
SEQRES 10 A 348 ARG GLY ALA MET ALA PRO ALA GLY ASN ASN LYS PHE SER
SEQRES 11 A 348 SER LYS ALA MET ALA GLU THR PHE TYR LEU SER ASN ILE
SEQRES 12 A 348 VAL PRO GLN ASP PHE ASP ASN ASN SER GLY TYR TRP ASN
SEQRES 13 A 348 ARG ILE GLU MET TYR CYS ARG GLU LEU THR GLU ARG PHE
SEQRES 14 A 348 GLU ASP VAL TRP VAL VAL SER GLY PRO LEU THR LEU PRO
SEQRES 15 A 348 GLN THR ARG GLY ASP GLY LYS LYS ILE VAL SER TYR GLN
SEQRES 16 A 348 VAL ILE GLY GLU ASP ASN VAL ALA VAL PRO SER HIS LEU
SEQRES 17 A 348 TYR LYS VAL ILE LEU ALA ARG ARG SER SER VAL SER THR
SEQRES 18 A 348 GLU PRO LEU ALA LEU GLY ALA PHE VAL VAL PRO ASN GLU
SEQRES 19 A 348 ALA ILE GLY PHE GLN PRO GLN LEU THR GLU PHE GLN VAL
SEQRES 20 A 348 SER LEU GLN ASP LEU GLU LYS LEU SER GLY LEU VAL PHE
SEQRES 21 A 348 PHE PRO HIS LEU ASP ARG THR SER ASP ILE ARG ASN ILE
SEQRES 22 A 348 CYS SER VAL ASP THR CYS LYS LEU LEU ASP PHE GLN GLU
SEQRES 23 A 348 PHE THR LEU TYR LEU SER THR ARG LYS ILE GLU GLY ALA
SEQRES 24 A 348 ARG SER VAL LEU ARG LEU GLU LYS ILE MET GLU ASN LEU
SEQRES 25 A 348 LYS ASN ALA GLU ILE GLU PRO ASP ASP TYR PHE MET SER
SEQRES 26 A 348 ARG TYR GLU LYS LYS LEU GLU GLU LEU LYS ALA LYS GLU
SEQRES 27 A 348 GLN SER GLY THR GLN ILE ARG LYS PRO SER
SEQRES 1 B 348 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 348 LEU VAL PRO ARG GLY SER HIS MET GLN GLY ALA GLU GLY
SEQRES 3 B 348 ALA LEU THR GLY LYS GLN PRO ASP GLY SER ALA GLU LYS
SEQRES 4 B 348 ALA VAL LEU GLU GLN PHE GLY PHE PRO LEU THR GLY THR
SEQRES 5 B 348 GLU ALA ARG CYS TYR THR ASN HIS ALA LEU SER TYR ASP
SEQRES 6 B 348 GLN ALA LYS ARG VAL PRO ARG TRP VAL LEU GLU HIS ILE
SEQRES 7 B 348 SER LYS SER LYS ILE MET GLY ASP ALA ASP ARG LYS HIS
SEQRES 8 B 348 CYS LYS PHE LYS PRO ASP PRO ASN ILE PRO PRO THR PHE
SEQRES 9 B 348 SER ALA PHE ASN GLU ASP TYR VAL GLY SER GLY TRP SER
SEQRES 10 B 348 ARG GLY ALA MET ALA PRO ALA GLY ASN ASN LYS PHE SER
SEQRES 11 B 348 SER LYS ALA MET ALA GLU THR PHE TYR LEU SER ASN ILE
SEQRES 12 B 348 VAL PRO GLN ASP PHE ASP ASN ASN SER GLY TYR TRP ASN
SEQRES 13 B 348 ARG ILE GLU MET TYR CYS ARG GLU LEU THR GLU ARG PHE
SEQRES 14 B 348 GLU ASP VAL TRP VAL VAL SER GLY PRO LEU THR LEU PRO
SEQRES 15 B 348 GLN THR ARG GLY ASP GLY LYS LYS ILE VAL SER TYR GLN
SEQRES 16 B 348 VAL ILE GLY GLU ASP ASN VAL ALA VAL PRO SER HIS LEU
SEQRES 17 B 348 TYR LYS VAL ILE LEU ALA ARG ARG SER SER VAL SER THR
SEQRES 18 B 348 GLU PRO LEU ALA LEU GLY ALA PHE VAL VAL PRO ASN GLU
SEQRES 19 B 348 ALA ILE GLY PHE GLN PRO GLN LEU THR GLU PHE GLN VAL
SEQRES 20 B 348 SER LEU GLN ASP LEU GLU LYS LEU SER GLY LEU VAL PHE
SEQRES 21 B 348 PHE PRO HIS LEU ASP ARG THR SER ASP ILE ARG ASN ILE
SEQRES 22 B 348 CYS SER VAL ASP THR CYS LYS LEU LEU ASP PHE GLN GLU
SEQRES 23 B 348 PHE THR LEU TYR LEU SER THR ARG LYS ILE GLU GLY ALA
SEQRES 24 B 348 ARG SER VAL LEU ARG LEU GLU LYS ILE MET GLU ASN LEU
SEQRES 25 B 348 LYS ASN ALA GLU ILE GLU PRO ASP ASP TYR PHE MET SER
SEQRES 26 B 348 ARG TYR GLU LYS LYS LEU GLU GLU LEU LYS ALA LYS GLU
SEQRES 27 B 348 GLN SER GLY THR GLN ILE ARG LYS PRO SER
SEQRES 1 C 12 C G G G A U G U C A C G
SEQRES 1 D 12 DC DG DT DG DA DC DA DT DC DC DC DG
SEQRES 1 E 12 C G G G A U G U C A C G
SEQRES 1 F 12 DC DG DT DG DA DC DA DT DC DC DC DG
HET MG A 401 1
HET CL B 401 1
HET MG C 101 1
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
FORMUL 7 MG 2(MG 2+)
FORMUL 8 CL CL 1-
FORMUL 10 HOH *50(H2 O)
HELIX 1 AA1 SER A 56 GLU A 63 1 8
HELIX 2 AA2 PHE A 127 VAL A 132 1 6
HELIX 3 AA3 PRO A 143 LYS A 148 5 6
HELIX 4 AA4 SER A 150 PHE A 158 1 9
HELIX 5 AA5 TYR A 159 SER A 161 5 3
HELIX 6 AA6 ASP A 167 GLY A 173 1 7
HELIX 7 AA7 GLY A 173 THR A 186 1 14
HELIX 8 AA8 GLN A 261 GLU A 264 5 4
HELIX 9 AA9 SER A 268 GLY A 277 1 10
HELIX 10 AB1 ASP A 303 GLY A 318 1 16
HELIX 11 AB2 SER A 321 ALA A 335 1 15
HELIX 12 AB3 ASP A 340 LYS A 349 1 10
HELIX 13 AB4 ALA B 57 VAL B 61 1 5
HELIX 14 AB5 LEU B 62 GLY B 66 5 5
HELIX 15 AB6 ASP B 108 CYS B 112 5 5
HELIX 16 AB7 PRO B 121 SER B 125 5 5
HELIX 17 AB8 PHE B 127 VAL B 132 1 6
HELIX 18 AB9 PRO B 143 LYS B 148 5 6
HELIX 19 AC1 SER B 150 THR B 157 1 8
HELIX 20 AC2 PHE B 158 SER B 161 5 4
HELIX 21 AC3 ASP B 167 GLY B 173 1 7
HELIX 22 AC4 GLY B 173 THR B 186 1 14
HELIX 23 AC5 GLN B 261 GLU B 264 5 4
HELIX 24 AC6 SER B 268 GLY B 277 1 10
HELIX 25 AC7 ILE B 293 ASP B 297 1 5
HELIX 26 AC8 ASP B 303 ALA B 319 1 17
HELIX 27 AC9 SER B 321 ALA B 335 1 15
HELIX 28 AD1 ASP B 340 GLU B 358 1 19
SHEET 1 AA1 7 ALA A 74 CYS A 76 0
SHEET 2 AA1 7 ALA A 81 ASP A 85 -1 O LEU A 82 N ARG A 75
SHEET 3 AA1 7 VAL A 90 ILE A 98 -1 O ARG A 92 N SER A 83
SHEET 4 AA1 7 ASP A 191 LEU A 199 -1 O VAL A 192 N ILE A 98
SHEET 5 AA1 7 HIS A 227 ARG A 235 -1 O LEU A 233 N TRP A 193
SHEET 6 AA1 7 LEU A 244 PRO A 252 -1 O GLY A 247 N ILE A 232
SHEET 7 AA1 7 GLN A 266 VAL A 267 -1 O VAL A 267 N ALA A 248
SHEET 1 AA2 7 ALA A 74 CYS A 76 0
SHEET 2 AA2 7 ALA A 81 ASP A 85 -1 O LEU A 82 N ARG A 75
SHEET 3 AA2 7 VAL A 90 ILE A 98 -1 O ARG A 92 N SER A 83
SHEET 4 AA2 7 ASP A 191 LEU A 199 -1 O VAL A 192 N ILE A 98
SHEET 5 AA2 7 HIS A 227 ARG A 235 -1 O LEU A 233 N TRP A 193
SHEET 6 AA2 7 LEU A 244 PRO A 252 -1 O GLY A 247 N ILE A 232
SHEET 7 AA2 7 ILE A 290 ASN A 292 1 O ARG A 291 N LEU A 244
SHEET 1 AA3 2 SER A 137 ALA A 140 0
SHEET 2 AA3 2 ILE A 163 GLN A 166 -1 O VAL A 164 N GLY A 139
SHEET 1 AA4 4 PRO A 202 THR A 204 0
SHEET 2 AA4 4 LYS A 210 ILE A 217 -1 O ILE A 211 N GLN A 203
SHEET 3 AA4 4 LYS B 210 ILE B 217 -1 O VAL B 212 N TYR A 214
SHEET 4 AA4 4 PRO B 202 THR B 204 -1 N GLN B 203 O ILE B 211
SHEET 1 AA5 4 VAL A 222 ALA A 223 0
SHEET 2 AA5 4 LYS A 210 ILE A 217 -1 N ILE A 217 O VAL A 222
SHEET 3 AA5 4 LYS B 210 ILE B 217 -1 O VAL B 212 N TYR A 214
SHEET 4 AA5 4 VAL B 222 ALA B 223 -1 O VAL B 222 N ILE B 217
SHEET 1 AA6 7 ALA B 74 CYS B 76 0
SHEET 2 AA6 7 HIS B 80 ASP B 85 -1 O LEU B 82 N ARG B 75
SHEET 3 AA6 7 VAL B 90 ILE B 98 -1 O ARG B 92 N SER B 83
SHEET 4 AA6 7 ASP B 191 LEU B 199 -1 O VAL B 194 N GLU B 96
SHEET 5 AA6 7 HIS B 227 ARG B 235 -1 O LEU B 233 N TRP B 193
SHEET 6 AA6 7 LEU B 244 PRO B 252 -1 O GLY B 247 N ILE B 232
SHEET 7 AA6 7 GLN B 266 VAL B 267 -1 O VAL B 267 N ALA B 248
SHEET 1 AA7 7 ALA B 74 CYS B 76 0
SHEET 2 AA7 7 HIS B 80 ASP B 85 -1 O LEU B 82 N ARG B 75
SHEET 3 AA7 7 VAL B 90 ILE B 98 -1 O ARG B 92 N SER B 83
SHEET 4 AA7 7 ASP B 191 LEU B 199 -1 O VAL B 194 N GLU B 96
SHEET 5 AA7 7 HIS B 227 ARG B 235 -1 O LEU B 233 N TRP B 193
SHEET 6 AA7 7 LEU B 244 PRO B 252 -1 O GLY B 247 N ILE B 232
SHEET 7 AA7 7 ILE B 290 ASN B 292 1 O ARG B 291 N LEU B 244
SHEET 1 AA8 2 SER B 137 ALA B 140 0
SHEET 2 AA8 2 ILE B 163 GLN B 166 -1 O GLN B 166 N SER B 137
SSBOND 1 CYS A 294 CYS A 299 1555 1555 2.03
SSBOND 2 CYS B 294 CYS B 299 1555 1555 2.03
LINK OD1 ASN A 171 MG MG A 401 1555 1555 2.44
LINK MG MG A 401 O HOH A 507 1555 1555 2.08
LINK MG MG A 401 O HOH A 508 1555 1555 2.09
LINK MG MG A 401 O3' G E 2 1555 1555 2.45
LINK MG MG A 401 OP1 G E 3 1555 1555 2.56
LINK OD1 ASN B 171 MG MG C 101 1555 1555 2.24
LINK O HOH B 508 MG MG C 101 1555 1555 2.08
LINK O HOH B 513 MG MG C 101 1555 1555 2.08
LINK O HOH B 522 MG MG C 101 1555 1555 2.07
LINK O3' G C 2 MG MG C 101 1555 1555 2.34
LINK OP1 G C 3 MG MG C 101 1555 1555 2.56
SITE 1 AC1 6 ASN A 171 GLU A 179 HOH A 507 HOH A 508
SITE 2 AC1 6 G E 2 G E 3
SITE 1 AC2 1 GLY B 133
SITE 1 AC3 6 ASN B 171 HOH B 508 HOH B 513 HOH B 522
SITE 2 AC3 6 G C 2 G C 3
CRYST1 167.576 167.576 105.438 90.00 90.00 120.00 H 3 18
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 0.005967 0.003445 0.000000 0.00000
SCALE2 0.000000 0.006891 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009484 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
