HEADER PROTEIN BINDING 24-SEP-14 4RF0
TITLE CRYSTAL STRUCTURE OF THE MIDDLE-EAST RESPIRATORY SYNDROME CORONAVIRUS
TITLE 2 PAPAIN-LIKE PROTEASE IN COMPLEX WITH UBIQUITIN (SPACE GROUP P6522)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ORF1AB PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 1480-1803;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: UBIQUITIN-60S RIBOSOMAL PROTEIN L40;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: UNP RESIDUES 1-75;
COMPND 10 SYNONYM: CEP52, UBIQUITIN A-52 RESIDUE RIBOSOMAL PROTEIN FUSION
COMPND 11 PRODUCT 1, UBIQUITIN, 60S RIBOSOMAL PROTEIN L40;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN BETACORONAVIRUS 2C JORDAN-N3/2012;
SOURCE 3 ORGANISM_TAXID: 1306931;
SOURCE 4 GENE: ORF1AB;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 GENE: UBA52, UBCEP2;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ZINC RIBBON, DEUBIQUITINASE, PAPAIN-LIKE PROTEASE, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR B.A.BAILEY-ELKIN,G.G.JOHNSON,B.L.MARK
REVDAT 3 14-JAN-15 4RF0 1 JRNL
REVDAT 2 29-OCT-14 4RF0 1 JRNL
REVDAT 1 22-OCT-14 4RF0 0
JRNL AUTH B.A.BAILEY-ELKIN,R.C.KNAAP,G.G.JOHNSON,T.J.DALEBOUT,
JRNL AUTH 2 D.K.NINABER,P.B.VAN KASTEREN,P.J.BREDENBEEK,E.J.SNIJDER,
JRNL AUTH 3 M.KIKKERT,B.L.MARK
JRNL TITL CRYSTAL STRUCTURE OF THE MIDDLE EAST RESPIRATORY SYNDROME
JRNL TITL 2 CORONAVIRUS (MERS-COV) PAPAIN-LIKE PROTEASE BOUND TO
JRNL TITL 3 UBIQUITIN FACILITATES TARGETED DISRUPTION OF
JRNL TITL 4 DEUBIQUITINATING ACTIVITY TO DEMONSTRATE ITS ROLE IN INNATE
JRNL TITL 5 IMMUNE SUPPRESSION.
JRNL REF J.BIOL.CHEM. V. 289 34667 2014
JRNL REFN ISSN 0021-9258
JRNL PMID 25320088
JRNL DOI 10.1074/JBC.M114.609644
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.9_1692)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : 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) : 44.24
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 19690
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.243
REMARK 3 R VALUE (WORKING SET) : 0.240
REMARK 3 FREE R VALUE : 0.281
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.170
REMARK 3 FREE R VALUE TEST SET COUNT : 1609
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 44.2485 - 6.2219 1.00 1796 160 0.2187 0.2291
REMARK 3 2 6.2219 - 4.9407 1.00 1679 150 0.2194 0.2585
REMARK 3 3 4.9407 - 4.3167 1.00 1657 146 0.2023 0.2397
REMARK 3 4 4.3167 - 3.9223 1.00 1638 147 0.2372 0.3022
REMARK 3 5 3.9223 - 3.6413 1.00 1636 145 0.2455 0.2487
REMARK 3 6 3.6413 - 3.4267 1.00 1628 145 0.2737 0.3417
REMARK 3 7 3.4267 - 3.2552 1.00 1610 144 0.2913 0.3600
REMARK 3 8 3.2552 - 3.1135 1.00 1618 144 0.2997 0.3598
REMARK 3 9 3.1135 - 2.9937 1.00 1617 143 0.2877 0.3832
REMARK 3 10 2.9937 - 2.8904 1.00 1600 142 0.2989 0.3763
REMARK 3 11 2.8904 - 2.8000 1.00 1602 143 0.3158 0.3717
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) : 0.360
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.780
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 : 0.002 3123
REMARK 3 ANGLE : 0.539 4238
REMARK 3 CHIRALITY : 0.021 491
REMARK 3 PLANARITY : 0.003 531
REMARK 3 DIHEDRAL : 12.410 1101
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 4RF0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-SEP-14.
REMARK 100 THE RCSB ID CODE IS RCSB087263.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
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 : CLSI
REMARK 200 BEAMLINE : 08B1-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.28219
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24473
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 44.240
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 71.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.80 M AMMONIUM SULPHATE, PH 8.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 56.36600
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 28.18300
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 42.27450
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 14.09150
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 70.45750
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 56.36600
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 28.18300
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 14.09150
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 42.27450
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 70.45750
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
REMARK 350 TOTAL BURIED SURFACE AREA: 4220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -153.0 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A2026 LIES ON A SPECIAL POSITION.
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 THR A 1480
REMARK 465 GLN A 1481
REMARK 465 GLN A 1482
REMARK 465 LEU A 1483
REMARK 465 CYS A 1802
REMARK 465 ASN A 1803
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 ILE A1485 CG1 CG2 CD1
REMARK 470 VAL A1487 CG1 CG2
REMARK 470 LEU A1501 CG CD1 CD2
REMARK 470 LYS A1504 CG CD CE NZ
REMARK 470 ASN A1505 OD1 ND2
REMARK 470 ARG A1508 CG CD NE CZ NH1 NH2
REMARK 470 GLN A1510 CG CD OE1 NE2
REMARK 470 ASN A1517 CG OD1 ND2
REMARK 470 LYS A1575 CG CD CE NZ
REMARK 470 ASP A1580 CG OD1 OD2
REMARK 470 LYS A1605 CG CD CE NZ
REMARK 470 LYS A1608 CG CD CE NZ
REMARK 470 ASP A1743 CG OD1 OD2
REMARK 470 LYS A1797 CG CD CE NZ
REMARK 470 SER A1799 OG
REMARK 470 SER A1800 OG
REMARK 470 ASP A1801 CG OD1 OD2
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 VAL A1494 -57.19 -127.70
REMARK 500 ASP A1523 15.31 -142.04
REMARK 500 ASP A1527 -145.94 -115.20
REMARK 500 HIS A1533 -168.60 -102.15
REMARK 500 ASP A1580 72.13 55.06
REMARK 500 LYS A1581 22.55 45.58
REMARK 500 SER A1588 133.74 -170.97
REMARK 500 THR A1740 74.11 55.56
REMARK 500 PRO A1742 179.16 -59.55
REMARK 500 ALA A1756 -154.60 -107.31
REMARK 500 ASP A1774 68.90 -108.96
REMARK 500 THR A1789 -77.09 -121.25
REMARK 500 PRO A1794 -169.09 -71.53
REMARK 500 SER A1800 32.27 -87.33
REMARK 500 GLN B 62 -169.72 -101.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2017 DISTANCE = 5.08 ANGSTROMS
REMARK 525 HOH A2026 DISTANCE = 5.76 ANGSTROMS
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 ZN A1901 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1675 SG
REMARK 620 2 CYS A1672 SG 112.0
REMARK 620 3 CYS A1709 SG 98.6 125.7
REMARK 620 4 CYS A1707 SG 98.0 120.5 96.7
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1905
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1906
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1907
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1908
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3CN B 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 103
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4REZ RELATED DB: PDB
REMARK 900 RELATED ID: 4RF1 RELATED DB: PDB
DBREF 4RF0 A 1480 1803 UNP M4STU1 M4STU1_9BETC 1480 1803
DBREF 4RF0 B 1 75 UNP P62987 RL40_HUMAN 1 75
SEQRES 1 A 324 THR GLN GLN LEU THR ILE GLU VAL LEU VAL THR VAL ASP
SEQRES 2 A 324 GLY VAL ASN PHE ARG THR VAL VAL LEU ASN ASN LYS ASN
SEQRES 3 A 324 THR TYR ARG SER GLN LEU GLY CYS VAL PHE PHE ASN GLY
SEQRES 4 A 324 ALA ASP ILE SER ASP THR ILE PRO ASP GLU LYS GLN ASN
SEQRES 5 A 324 GLY HIS SER LEU TYR LEU ALA ASP ASN LEU THR ALA ASP
SEQRES 6 A 324 GLU THR LYS ALA LEU LYS GLU LEU TYR GLY PRO VAL ASP
SEQRES 7 A 324 PRO THR PHE LEU HIS ARG PHE TYR SER LEU LYS ALA ALA
SEQRES 8 A 324 VAL HIS GLY TRP LYS MET VAL VAL CYS ASP LYS VAL ARG
SEQRES 9 A 324 SER LEU LYS LEU SER ASP ASN ASN CYS TYR LEU ASN ALA
SEQRES 10 A 324 VAL ILE MET THR LEU ASP LEU LEU LYS ASP ILE LYS PHE
SEQRES 11 A 324 VAL ILE PRO ALA LEU GLN HIS ALA PHE MET LYS HIS LYS
SEQRES 12 A 324 GLY GLY ASP SER THR ASP PHE ILE ALA LEU ILE MET ALA
SEQRES 13 A 324 TYR GLY ASN CYS THR PHE GLY ALA PRO ASP ASP ALA SER
SEQRES 14 A 324 ARG LEU LEU HIS THR VAL LEU ALA LYS ALA GLU LEU CYS
SEQRES 15 A 324 CYS SER ALA ARG MET VAL TRP ARG GLU TRP CYS ASN VAL
SEQRES 16 A 324 CYS GLY ILE LYS ASP VAL VAL LEU GLN GLY LEU LYS ALA
SEQRES 17 A 324 CYS CYS TYR VAL GLY VAL GLN THR VAL GLU ASP LEU ARG
SEQRES 18 A 324 ALA ARG MET THR TYR VAL CYS GLN CYS GLY GLY GLU ARG
SEQRES 19 A 324 HIS ARG GLN LEU VAL GLU HIS THR THR PRO TRP LEU LEU
SEQRES 20 A 324 LEU SER GLY THR PRO ASN GLU LYS LEU VAL THR THR SER
SEQRES 21 A 324 THR ALA PRO ASP PHE VAL ALA PHE ASN VAL PHE GLN GLY
SEQRES 22 A 324 ILE GLU THR ALA VAL GLY HIS TYR VAL HIS ALA ARG LEU
SEQRES 23 A 324 LYS GLY GLY LEU ILE LEU LYS PHE ASP SER GLY THR VAL
SEQRES 24 A 324 SER LYS THR SER ASP TRP LYS CYS LYS VAL THR ASP VAL
SEQRES 25 A 324 LEU PHE PRO GLY GLN LYS TYR SER SER ASP CYS ASN
SEQRES 1 B 75 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 2 B 75 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES 3 B 75 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 4 B 75 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP
SEQRES 5 B 75 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 6 B 75 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY
HET ZN A1901 1
HET SO4 A1902 5
HET SO4 A1903 5
HET SO4 A1904 5
HET SO4 A1905 5
HET SO4 A1906 5
HET SO4 A1907 5
HET SO4 A1908 5
HET 3CN B 101 4
HET SO4 B 102 5
HET SO4 B 103 5
HETNAM ZN ZINC ION
HETNAM SO4 SULFATE ION
HETNAM 3CN 3-AMINOPROPANE
FORMUL 3 ZN ZN 2+
FORMUL 4 SO4 9(O4 S 2-)
FORMUL 11 3CN C3 H9 N
FORMUL 14 HOH *55(H2 O)
HELIX 1 1 THR A 1506 LEU A 1511 1 6
HELIX 2 2 THR A 1542 GLY A 1554 1 13
HELIX 3 3 THR A 1559 VAL A 1571 1 13
HELIX 4 4 HIS A 1572 TRP A 1574 5 3
HELIX 5 5 ASN A 1591 ASP A 1602 1 12
HELIX 6 6 ILE A 1611 LYS A 1622 1 12
HELIX 7 7 SER A 1626 GLY A 1637 1 12
HELIX 8 8 ASP A 1646 ALA A 1656 1 11
HELIX 9 9 LEU A 1685 ALA A 1687 5 3
HELIX 10 10 THR A 1695 ALA A 1701 1 7
HELIX 11 11 THR B 22 GLY B 35 1 14
HELIX 12 12 PRO B 37 ASP B 39 5 3
SHEET 1 A 3 ARG A1497 LEU A1501 0
SHEET 2 A 3 ILE A1485 THR A1490 -1 N VAL A1487 O VAL A1499
SHEET 3 A 3 SER A1534 TYR A1536 1 O LEU A1535 N LEU A1488
SHEET 1 B 2 MET A1576 VAL A1578 0
SHEET 2 B 2 ARG A1583 LEU A1585 -1 O SER A1584 N VAL A1577
SHEET 1 C 2 ILE A1607 PHE A1609 0
SHEET 2 C 2 ALA A1658 LEU A1660 -1 O GLU A1659 N LYS A1608
SHEET 1 D 4 GLY A1676 GLN A1683 0
SHEET 2 D 4 ARG A1665 CYS A1672 -1 N GLU A1670 O LYS A1678
SHEET 3 D 4 GLU A1712 THR A1722 -1 O GLU A1719 N VAL A1667
SHEET 4 D 4 MET A1703 VAL A1706 -1 N MET A1703 O ARG A1715
SHEET 1 E 4 GLY A1676 GLN A1683 0
SHEET 2 E 4 ARG A1665 CYS A1672 -1 N GLU A1670 O LYS A1678
SHEET 3 E 4 GLU A1712 THR A1722 -1 O GLU A1719 N VAL A1667
SHEET 4 E 4 GLN A1796 SER A1799 -1 O GLN A1796 N THR A1722
SHEET 1 F 7 CYS A1689 VAL A1691 0
SHEET 2 F 7 LEU A1725 THR A1737 1 O LEU A1726 N TYR A1690
SHEET 3 F 7 ASP A1783 PHE A1793 -1 O VAL A1791 N LEU A1727
SHEET 4 F 7 ALA A1746 GLN A1751 -1 N ASN A1748 O THR A1789
SHEET 5 F 7 HIS A1759 LYS A1766 -1 O HIS A1759 N GLN A1751
SHEET 6 F 7 LEU A1769 PHE A1773 -1 O PHE A1773 N HIS A1762
SHEET 7 F 7 VAL A1778 SER A1779 -1 O SER A1779 N LYS A1772
SHEET 1 G 5 THR B 12 GLU B 16 0
SHEET 2 G 5 GLN B 2 LYS B 6 -1 N ILE B 3 O LEU B 15
SHEET 3 G 5 SER B 65 LEU B 71 1 O LEU B 67 N PHE B 4
SHEET 4 G 5 GLN B 41 PHE B 45 -1 N ARG B 42 O VAL B 70
SHEET 5 G 5 LYS B 48 GLN B 49 -1 O LYS B 48 N PHE B 45
LINK SG CYS A1675 ZN ZN A1901 1555 1555 2.31
LINK SG CYS A1672 ZN ZN A1901 1555 1555 2.31
LINK SG CYS A1709 ZN ZN A1901 1555 1555 2.31
LINK SG CYS A1707 ZN ZN A1901 1555 1555 2.31
LINK SG CYS A1592 CA 3CN B 101 1555 1555 1.45
LINK C GLY B 75 ND 3CN B 101 1555 1555 1.45
SITE 1 AC1 4 CYS A1672 CYS A1675 CYS A1707 CYS A1709
SITE 1 AC2 3 ASN A1673 HIS A1714 HIS A1759
SITE 1 AC3 3 GLN A1751 GLY A1752 LYS A1787
SITE 1 AC4 5 GLU A1659 LEU A1660 GLY A1684 LEU A1685
SITE 2 AC4 5 LYS A1686
SITE 1 AC5 4 TRP A1668 GLU A1670 ARG A1715 ALA B 46
SITE 1 AC6 7 HIS A1652 LEU A1655 ALA A1656 LYS A1686
SITE 2 AC6 7 CYS A1689 HOH A2002 LYS B 48
SITE 1 AC7 3 VAL A1582 ASP A1602 ARG A1764
SITE 1 AC8 3 PHE A1515 TYR A1565 LYS A1568
SITE 1 AC9 6 ASN A1590 CYS A1592 ASN A1673 GLY A1758
SITE 2 AC9 6 HIS A1759 GLY B 75
SITE 1 BC1 4 TYR A1705 ARG A1715 THR B 66 HIS B 68
SITE 1 BC2 4 GLN B 31 ASP B 39 ARG B 72 ARG B 74
CRYST1 176.972 176.972 84.549 90.00 90.00 120.00 P 65 2 2 12
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 0.005651 0.003262 0.000000 0.00000
SCALE2 0.000000 0.006525 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011827 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
