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HEADER HYDROLASE 03-SEP-04 1XD3
TITLE CRYSTAL STRUCTURE OF UCHL3-UBVME COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN CARBOXYL-TERMINAL ESTERASE L3;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: UCH-L3, UBIQUITIN THIOLESTERASE, UBIQUITIN C-
COMPND 5 TERMINAL HYDROLASE;
COMPND 6 EC: 3.4.19.12;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: UBC PROTEIN;
COMPND 10 CHAIN: B, D;
COMPND 11 SYNONYM: UBIQUITIN FUSED TO VINYL METHYLESTER, UBVME;
COMPND 12 ENGINEERED: YES
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 BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PRSET;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PTYB
KEYWDS ENZYME-LIGAND COMPLEX, ACTIVE SITE CROSSOVER LOOP, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.MISAGHI,P.J.GALARDY,W.J.N.MEESTER,H.OVAA,H.L.PLOEGH,
AUTHOR 2 R.GAUDET
REVDAT 3 24-FEB-09 1XD3 1 VERSN
REVDAT 2 25-JAN-05 1XD3 1 JRNL
REVDAT 1 23-NOV-04 1XD3 0
JRNL AUTH S.MISAGHI,P.J.GALARDY,W.J.N.MEESTER,H.OVAA,
JRNL AUTH 2 H.L.PLOEGH,R.GAUDET
JRNL TITL STRUCTURE OF THE UBIQUITIN HYDROLASE UCH-L3
JRNL TITL 2 COMPLEXED WITH A SUICIDE SUBSTRATE
JRNL REF J.BIOL.CHEM. V. 280 1512 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 15531586
JRNL DOI 10.1074/JBC.M410770200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.BORODOVSKY,H.OVAA,N.KOLLI,T.GAN-ERDENE,
REMARK 1 AUTH 2 K.D.WILKINSON,H.L.PLOEGH,B.M.KESSLER
REMARK 1 TITL CHEMISTRY-BASED FUNCTIONAL PROTEOMICS REVEALS
REMARK 1 TITL 2 NOVEL MEMBERS OF THE DEUBIQUITINATING ENZYME FAMILY
REMARK 1 REF CHEM.BIOL. V. 9 1149 2002
REMARK 1 REFN ISSN 1074-5521
REMARK 1 PMID 12401499
REMARK 1 DOI 10.1016/S1074-5521(02)00248-X
REMARK 1 REFERENCE 2
REMARK 1 AUTH A.BORODOVSKY,B.M.KESSLER,R.CASAGRANDE,
REMARK 1 AUTH 2 H.S.OVERKLEEFT,K.D.WILKINSON,H.L.PLOEGH
REMARK 1 TITL A NOVEL ACTIVE SITE-DIRECTED PROBE SPECIFIC FOR
REMARK 1 TITL 2 DEUBIQUITINATING ENZYMES REVEALS PROTEASOME
REMARK 1 TITL 3 ASSOCIATION OF USP14
REMARK 1 REF EMBO J. V. 20 5187 2001
REMARK 1 REFN ISSN 0261-4189
REMARK 1 PMID 11566882
REMARK 1 DOI 10.1093/EMBOJ/20.18.5187
REMARK 1 REFERENCE 3
REMARK 1 AUTH S.C.JOHNSTON,C.N.LARSEN,W.J.COOK,K.D.WILKINSON,
REMARK 1 AUTH 2 C.P.HILL
REMARK 1 TITL CRYSTAL STRUCTURE OF A DEUBIQUITINATING ENZYME
REMARK 1 TITL 2 (HUMAN UCH-L3) AT 1.8 A RESOLUTION
REMARK 1 REF EMBO J. V. 16 3787 1997
REMARK 1 REFN ISSN 0261-4189
REMARK 1 PMID 9233788
REMARK 1 DOI 10.1093/EMBOJ/16.13.3787
REMARK 1 REFERENCE 4
REMARK 1 AUTH S.C.JOHNSTON,S.M.RIDDLE,R.E.COHEN,C.P.HILL
REMARK 1 TITL STRUCTURAL BASIS FOR THE SPECIFICITY OF UBIQUITIN
REMARK 1 TITL 2 C-TERMINAL HYDROLASES
REMARK 1 REF EMBO J. V. 18 3877 1999
REMARK 1 REFN ISSN 0261-4189
REMARK 1 PMID 10406793
REMARK 1 DOI 10.1093/EMBOJ/18.14.3877
REMARK 2
REMARK 2 RESOLUTION. 1.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.76
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 91.8
REMARK 3 NUMBER OF REFLECTIONS : 91094
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 SET) : 0.166
REMARK 3 FREE R VALUE : 0.192
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2756
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.45
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.52
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 79.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 9595
REMARK 3 BIN R VALUE (WORKING SET) : 0.2730
REMARK 3 BIN FREE R VALUE : 0.3120
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 2.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 283
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.019
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5083
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 42
REMARK 3 SOLVENT ATOMS : 1057
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.32
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.27000
REMARK 3 B22 (A**2) : 2.09000
REMARK 3 B33 (A**2) : -2.36000
REMARK 3 B12 (A**2) : 3.26000
REMARK 3 B13 (A**2) : 0.66000
REMARK 3 B23 (A**2) : -0.07000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.14
REMARK 3 ESD FROM SIGMAA (A) : 0.17
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.16
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.21
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.40
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ANISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : CNS BULK SOLVENT MODEL USED
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 50.67
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : GVE.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : GVE.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1XD3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-NOV-04.
REMARK 100 THE RCSB ID CODE IS RCSB030223.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-JUN-04
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 8-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9779
REMARK 200 MONOCHROMATOR : SI III MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : ADSC
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 93859
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450
REMARK 200 RESOLUTION RANGE LOW (A) : 23.760
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 5.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 27.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.46700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1UCH, PDB ENTRY 1UBQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, MAGNESIUM CHLORIDE, TRIS,
REMARK 280 PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 2910 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 3100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 1
REMARK 465 MET C 1
REMARK 465 GLU C 2
REMARK 465 GLY C 3
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 GLU A 158 CG CD OE1 OE2
REMARK 470 ARG C 136 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 24 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH C 2072 O HOH C 2425 2.08
REMARK 500 OE1 GLU A 60 O HOH A 2399 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH C 2065 O HOH C 2425 1455 2.17
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 27 24.37 -78.06
REMARK 500 PRO C 27 51.03 -69.96
REMARK 500 ASP C 216 59.52 -142.05
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 B1249 DISTANCE = 5.62 ANGSTROMS
REMARK 525 HOH C2084 DISTANCE = 7.44 ANGSTROMS
REMARK 525 HOH A2151 DISTANCE = 5.39 ANGSTROMS
REMARK 525 HOH C2355 DISTANCE = 7.51 ANGSTROMS
REMARK 525 HOH A2360 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH A2368 DISTANCE = 7.54 ANGSTROMS
REMARK 525 HOH A2370 DISTANCE = 5.07 ANGSTROMS
REMARK 525 HOH A2376 DISTANCE = 5.39 ANGSTROMS
REMARK 525 HOH C2383 DISTANCE = 5.30 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 MG A2006 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 109 OD1
REMARK 620 2 HOH A2346 O 147.5
REMARK 620 3 HOH B1243 O 94.1 113.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A2009 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A2264 O
REMARK 620 2 HOH A2305 O 105.8
REMARK 620 3 HOH D2344 O 169.1 81.1
REMARK 620 4 HOH D2347 O 90.5 155.8 80.5
REMARK 620 5 HOH D2354 O 93.4 82.0 78.9 79.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A2010 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 114 OE2
REMARK 620 2 HOH A2317 O 65.8
REMARK 620 3 LYS A 21 O 124.7 99.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C2001 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C2193 O
REMARK 620 2 HOH C2366 O 89.0
REMARK 620 3 HOH C2129 O 166.0 77.0
REMARK 620 4 ASP C 163 OD2 92.5 113.8 94.3
REMARK 620 5 HOH A2246 O 84.8 75.2 90.4 170.5
REMARK 620 6 HOH A2190 O 86.5 169.8 107.1 75.5 95.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C2002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C2194 O
REMARK 620 2 HOH C2150 O 95.3
REMARK 620 3 HOH C2281 O 91.8 93.2
REMARK 620 4 HOH A2123 O 84.9 85.6 176.4
REMARK 620 5 HOH A2227 O 92.9 169.9 92.5 89.2
REMARK 620 6 HOH A2191 O 170.3 75.0 88.9 94.1 96.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C2003 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 179 NE2
REMARK 620 2 HOH C2185 O 98.0
REMARK 620 3 HOH C2191 O 90.5 87.1
REMARK 620 4 HOH C2270 O 89.4 172.4 91.2
REMARK 620 5 HOH C2374 O 82.1 88.6 170.9 94.0
REMARK 620 6 HOH C2184 O 172.7 88.0 94.0 84.7 93.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C2004 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C2249 O
REMARK 620 2 HOH C2397 O 88.4
REMARK 620 3 HOH C2169 O 99.6 168.6
REMARK 620 4 HOH C2425 O 138.6 97.4 71.1
REMARK 620 5 HOH C2072 O 83.3 81.3 91.6 57.6
REMARK 620 6 HOH C2190 O 86.4 88.5 100.0 134.4 165.7
REMARK 620 7 HOH C2065 O 160.5 83.1 91.6 60.3 112.6 75.8
REMARK 620 8 MG C2005 MG 73.9 132.6 58.2 125.0 137.0 47.7 99.1
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C2005 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C2181 O
REMARK 620 2 ASP C 79 N 129.1
REMARK 620 3 ASP C 79 N 129.1 0.6
REMARK 620 4 HOH C2190 O 92.2 125.8 126.2
REMARK 620 5 ASP C 79 OD1 71.4 62.3 62.1 159.2
REMARK 620 6 HOH C2249 O 58.9 150.6 150.0 76.8 103.9
REMARK 620 7 HOH C2169 O 123.1 82.3 81.9 104.9 95.0 72.7
REMARK 620 8 MG C2004 MG 100.4 125.4 125.1 63.0 131.2 42.6 48.2
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C2007 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C2069 O
REMARK 620 2 HOH C2433 O 105.5
REMARK 620 3 GLU C 149 OE1 60.5 140.2
REMARK 620 4 HOH C2078 O 136.7 114.4 95.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C2008 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR C 181 OH
REMARK 620 2 ASP C 79 OD2 122.8
REMARK 620 3 ASP C 79 OD2 158.5 53.0
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 2001
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 2002
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 2003
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 2004
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 2005
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 2006
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 2007
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 2008
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 2009
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 2010
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GVE B 1176
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GVE D 2276
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CMX RELATED DB: PDB
REMARK 900 YEAST HOMOLOGUE YUH1 IN COMPLEX WITH UBIQUITIN ALDEHYDE
REMARK 900 RELATED ID: 1UBQ RELATED DB: PDB
REMARK 900 HUMAN UBIQUITIN
REMARK 900 RELATED ID: 1UCH RELATED DB: PDB
REMARK 900 HUMAN UCH-L3 (SAME PROTEIN) UNLIGANDED
DBREF 1XD3 A 1 230 UNP P15374 UCHL3_HUMAN 1 230
DBREF 1XD3 B 1 75 UNP P62988 UBIQ_HUMAN 229 303
DBREF 1XD3 C 1 230 UNP P15374 UCHL3_HUMAN 1 230
DBREF 1XD3 D 1 75 UNP P62988 UBIQ_HUMAN 229 303
SEQRES 1 A 230 MET GLU GLY GLN ARG TRP LEU PRO LEU GLU ALA ASN PRO
SEQRES 2 A 230 GLU VAL THR ASN GLN PHE LEU LYS GLN LEU GLY LEU HIS
SEQRES 3 A 230 PRO ASN TRP GLN PHE VAL ASP VAL TYR GLY MET ASP PRO
SEQRES 4 A 230 GLU LEU LEU SER MET VAL PRO ARG PRO VAL CYS ALA VAL
SEQRES 5 A 230 LEU LEU LEU PHE PRO ILE THR GLU LYS TYR GLU VAL PHE
SEQRES 6 A 230 ARG THR GLU GLU GLU GLU LYS ILE LYS SER GLN GLY GLN
SEQRES 7 A 230 ASP VAL THR SER SER VAL TYR PHE MET LYS GLN THR ILE
SEQRES 8 A 230 SER ASN ALA CYS GLY THR ILE GLY LEU ILE HIS ALA ILE
SEQRES 9 A 230 ALA ASN ASN LYS ASP LYS MET HIS PHE GLU SER GLY SER
SEQRES 10 A 230 THR LEU LYS LYS PHE LEU GLU GLU SER VAL SER MET SER
SEQRES 11 A 230 PRO GLU GLU ARG ALA ARG TYR LEU GLU ASN TYR ASP ALA
SEQRES 12 A 230 ILE ARG VAL THR HIS GLU THR SER ALA HIS GLU GLY GLN
SEQRES 13 A 230 THR GLU ALA PRO SER ILE ASP GLU LYS VAL ASP LEU HIS
SEQRES 14 A 230 PHE ILE ALA LEU VAL HIS VAL ASP GLY HIS LEU TYR GLU
SEQRES 15 A 230 LEU ASP GLY ARG LYS PRO PHE PRO ILE ASN HIS GLY GLU
SEQRES 16 A 230 THR SER ASP GLU THR LEU LEU GLU ASP ALA ILE GLU VAL
SEQRES 17 A 230 CYS LYS LYS PHE MET GLU ARG ASP PRO ASP GLU LEU ARG
SEQRES 18 A 230 PHE ASN ALA ILE ALA LEU SER ALA ALA
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
SEQRES 1 C 230 MET GLU GLY GLN ARG TRP LEU PRO LEU GLU ALA ASN PRO
SEQRES 2 C 230 GLU VAL THR ASN GLN PHE LEU LYS GLN LEU GLY LEU HIS
SEQRES 3 C 230 PRO ASN TRP GLN PHE VAL ASP VAL TYR GLY MET ASP PRO
SEQRES 4 C 230 GLU LEU LEU SER MET VAL PRO ARG PRO VAL CYS ALA VAL
SEQRES 5 C 230 LEU LEU LEU PHE PRO ILE THR GLU LYS TYR GLU VAL PHE
SEQRES 6 C 230 ARG THR GLU GLU GLU GLU LYS ILE LYS SER GLN GLY GLN
SEQRES 7 C 230 ASP VAL THR SER SER VAL TYR PHE MET LYS GLN THR ILE
SEQRES 8 C 230 SER ASN ALA CYS GLY THR ILE GLY LEU ILE HIS ALA ILE
SEQRES 9 C 230 ALA ASN ASN LYS ASP LYS MET HIS PHE GLU SER GLY SER
SEQRES 10 C 230 THR LEU LYS LYS PHE LEU GLU GLU SER VAL SER MET SER
SEQRES 11 C 230 PRO GLU GLU ARG ALA ARG TYR LEU GLU ASN TYR ASP ALA
SEQRES 12 C 230 ILE ARG VAL THR HIS GLU THR SER ALA HIS GLU GLY GLN
SEQRES 13 C 230 THR GLU ALA PRO SER ILE ASP GLU LYS VAL ASP LEU HIS
SEQRES 14 C 230 PHE ILE ALA LEU VAL HIS VAL ASP GLY HIS LEU TYR GLU
SEQRES 15 C 230 LEU ASP GLY ARG LYS PRO PHE PRO ILE ASN HIS GLY GLU
SEQRES 16 C 230 THR SER ASP GLU THR LEU LEU GLU ASP ALA ILE GLU VAL
SEQRES 17 C 230 CYS LYS LYS PHE MET GLU ARG ASP PRO ASP GLU LEU ARG
SEQRES 18 C 230 PHE ASN ALA ILE ALA LEU SER ALA ALA
SEQRES 1 D 75 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 2 D 75 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES 3 D 75 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 4 D 75 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP
SEQRES 5 D 75 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 6 D 75 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY
HET MG C2001 1
HET MG C2002 1
HET MG C2003 1
HET MG C2004 1
HET MG C2005 1
HET MG A2006 1
HET MG C2007 1
HET MG C2008 1
HET MG A2009 1
HET MG A2010 1
HET GVE B1176 16
HET GVE D2276 16
HETNAM MG MAGNESIUM ION
HETNAM GVE METHYL 4-AMINOBUTANOATE
FORMUL 5 MG 10(MG 2+)
FORMUL 15 GVE 2(C5 H11 N O2)
FORMUL 17 HOH *1057(H2 O)
HELIX 1 1 ASN A 12 LEU A 23 1 12
HELIX 2 2 ASP A 38 SER A 43 1 6
HELIX 3 3 THR A 59 GLY A 77 1 19
HELIX 4 4 ALA A 94 ASN A 106 1 13
HELIX 5 5 ASN A 107 MET A 111 5 5
HELIX 6 6 SER A 117 VAL A 127 1 11
HELIX 7 7 SER A 130 ASN A 140 1 11
HELIX 8 8 TYR A 141 HIS A 153 1 13
HELIX 9 9 THR A 200 ASP A 216 1 17
HELIX 10 10 THR B 22 GLY B 35 1 14
HELIX 11 11 PRO B 37 ASP B 39 5 3
HELIX 12 12 ASN C 12 LEU C 23 1 12
HELIX 13 13 ASP C 38 SER C 43 1 6
HELIX 14 14 THR C 59 GLY C 77 1 19
HELIX 15 15 ALA C 94 ASN C 106 1 13
HELIX 16 16 ASN C 107 MET C 111 5 5
HELIX 17 17 SER C 117 VAL C 127 1 11
HELIX 18 18 SER C 130 ASN C 140 1 11
HELIX 19 19 TYR C 141 HIS C 153 1 13
HELIX 20 20 THR C 200 ARG C 215 1 16
HELIX 21 21 THR D 22 GLY D 35 1 14
HELIX 22 22 PRO D 37 ASP D 39 5 3
HELIX 23 23 LEU D 56 ASN D 60 5 5
SHEET 1 A 2 LEU A 9 GLU A 10 0
SHEET 2 A 2 ARG B 74 GLY B 75 -1 O GLY B 75 N LEU A 9
SHEET 1 B 6 TRP A 29 ASP A 33 0
SHEET 2 B 6 ASN A 223 ALA A 229 -1 O SER A 228 N GLN A 30
SHEET 3 B 6 VAL A 49 PRO A 57 -1 N LEU A 55 O ASN A 223
SHEET 4 B 6 LEU A 168 VAL A 176 -1 O HIS A 169 N PHE A 56
SHEET 5 B 6 HIS A 179 LEU A 183 -1 O LEU A 183 N ALA A 172
SHEET 6 B 6 ILE A 191 GLU A 195 -1 O HIS A 193 N LEU A 180
SHEET 1 C 5 THR B 12 GLU B 16 0
SHEET 2 C 5 GLN B 2 THR B 7 -1 N VAL B 5 O ILE B 13
SHEET 3 C 5 THR B 66 LEU B 71 1 O LEU B 67 N PHE B 4
SHEET 4 C 5 GLN B 41 PHE B 45 -1 N ARG B 42 O VAL B 70
SHEET 5 C 5 LYS B 48 GLN B 49 -1 O LYS B 48 N PHE B 45
SHEET 1 D 2 LEU C 9 GLU C 10 0
SHEET 2 D 2 ARG D 74 GLY D 75 -1 O GLY D 75 N LEU C 9
SHEET 1 E 6 TRP C 29 ASP C 33 0
SHEET 2 E 6 ASN C 223 ALA C 229 -1 O SER C 228 N GLN C 30
SHEET 3 E 6 VAL C 49 PRO C 57 -1 N LEU C 55 O ASN C 223
SHEET 4 E 6 LEU C 168 VAL C 176 -1 O HIS C 169 N PHE C 56
SHEET 5 E 6 HIS C 179 LEU C 183 -1 O LEU C 183 N ALA C 172
SHEET 6 E 6 ILE C 191 GLU C 195 -1 O HIS C 193 N LEU C 180
SHEET 1 F 5 THR D 12 GLU D 16 0
SHEET 2 F 5 GLN D 2 LYS D 6 -1 N VAL D 5 O ILE D 13
SHEET 3 F 5 THR D 66 LEU D 71 1 O LEU D 69 N LYS D 6
SHEET 4 F 5 GLN D 41 PHE D 45 -1 N ARG D 42 O VAL D 70
SHEET 5 F 5 LYS D 48 GLN D 49 -1 O LYS D 48 N PHE D 45
LINK C GLY B 75 N AGVE B1176 1555 1555 1.33
LINK C GLY D 75 N AGVE D2276 1555 1555 1.33
LINK C GLY B 75 N BGVE B1176 1555 1555 1.33
LINK C GLY D 75 N BGVE D2276 1555 1555 1.33
LINK SG CYS C 95 CB BGVE D2276 1555 1555 1.79
LINK SG CYS A 95 CB BGVE B1176 1555 1555 1.81
LINK SG CYS A 95 CB AGVE B1176 1555 1555 1.82
LINK SG CYS C 95 CB AGVE D2276 1555 1555 1.87
LINK MG MG A2006 OD1 ASP A 109 1555 1555 1.94
LINK MG MG A2006 O HOH A2346 1555 1555 2.05
LINK MG MG A2009 O HOH A2264 1555 1555 2.17
LINK MG MG A2009 O HOH A2305 1555 1555 2.19
LINK MG MG A2010 OE2 GLU A 114 1555 1555 2.07
LINK MG MG A2010 O HOH A2317 1555 1555 3.12
LINK MG MG A2010 O LYS A 21 1555 1555 2.84
LINK MG MG C2001 O HOH C2193 1555 1555 2.24
LINK MG MG C2001 O HOH C2366 1555 1555 2.61
LINK MG MG C2001 O HOH C2129 1555 1555 2.10
LINK MG MG C2001 OD2 ASP C 163 1555 1555 2.06
LINK MG MG C2002 O HOH C2194 1555 1555 2.13
LINK MG MG C2002 O HOH C2150 1555 1555 2.19
LINK MG MG C2002 O HOH C2281 1555 1555 2.03
LINK MG MG C2003 NE2 HIS C 179 1555 1555 2.09
LINK MG MG C2003 O HOH C2185 1555 1555 2.12
LINK MG MG C2003 O HOH C2191 1555 1555 2.09
LINK MG MG C2004 O HOH C2249 1555 1555 2.03
LINK MG MG C2004 O HOH C2397 1555 1555 2.15
LINK MG MG C2004 O HOH C2169 1555 1555 2.08
LINK MG MG C2004 O HOH C2425 1555 1555 2.20
LINK MG MG C2004 O HOH C2072 1555 1555 2.12
LINK MG MG C2005 O HOH C2181 1555 1555 2.69
LINK MG MG C2005 N AASP C 79 1555 1555 3.01
LINK MG MG C2005 N BASP C 79 1555 1555 3.01
LINK MG MG C2005 O HOH C2190 1555 1555 2.12
LINK MG MG C2005 OD1BASP C 79 1555 1555 1.94
LINK MG MG C2007 O HOH C2069 1555 1555 2.92
LINK MG MG C2007 O HOH C2433 1555 1555 2.95
LINK MG MG C2007 OE1 GLU C 149 1555 1555 2.03
LINK MG MG C2007 O HOH C2078 1555 1555 3.04
LINK MG MG C2008 OH TYR C 181 1555 1555 2.81
LINK MG MG C2008 OD2BASP C 79 1555 1555 2.84
LINK MG MG C2008 OD2AASP C 79 1555 1555 1.87
LINK MG MG A2006 O HOH B1243 1555 1645 2.66
LINK MG MG A2009 O HOH D2344 1555 1455 2.33
LINK MG MG A2009 O HOH D2347 1555 1455 2.17
LINK MG MG A2009 O HOH D2354 1555 1455 2.23
LINK MG MG C2001 O HOH A2246 1555 1664 2.06
LINK MG MG C2001 O HOH A2190 1555 1664 3.13
LINK MG MG C2002 O HOH A2123 1555 1565 2.22
LINK MG MG C2002 O HOH A2227 1555 1565 2.08
LINK MG MG C2002 O HOH A2191 1555 1565 2.31
LINK MG MG C2003 O HOH C2270 1555 1455 2.18
LINK MG MG C2003 O HOH C2374 1555 1455 2.20
LINK MG MG C2003 O HOH C2184 1555 1455 1.97
LINK MG MG C2004 O HOH C2190 1555 1655 2.56
LINK MG MG C2004 O HOH C2065 1555 1655 2.11
LINK MG MG C2004 MG MG C2005 1555 1655 2.68
LINK MG MG C2005 O HOH C2249 1555 1455 2.88
LINK MG MG C2005 O HOH C2169 1555 1455 2.38
LINK MG MG C2005 MG MG C2004 1555 1455 2.68
CISPEP 1 ARG A 47 PRO A 48 0 -0.40
CISPEP 2 ARG C 47 PRO C 48 0 -0.36
SITE 1 AC1 5 HOH A2246 ASP C 163 HOH C2129 HOH C2193
SITE 2 AC1 5 HOH C2366
SITE 1 AC2 6 HOH A2123 HOH A2191 HOH A2227 HOH C2150
SITE 2 AC2 6 HOH C2194 HOH C2281
SITE 1 AC3 6 HIS C 179 HOH C2184 HOH C2185 HOH C2191
SITE 2 AC3 6 HOH C2270 HOH C2374
SITE 1 AC4 8 MG C2005 HOH C2065 HOH C2072 HOH C2169
SITE 2 AC4 8 HOH C2190 HOH C2249 HOH C2397 HOH C2425
SITE 1 AC5 7 GLN C 78 ASP C 79 MG C2004 HOH C2169
SITE 2 AC5 7 HOH C2181 HOH C2190 HOH C2249
SITE 1 AC6 4 LYS A 108 ASP A 109 HOH A2346 HOH B1243
SITE 1 AC7 4 GLU C 149 HOH C2069 HOH C2078 HOH C2433
SITE 1 AC8 3 ASP C 79 THR C 81 TYR C 181
SITE 1 AC9 5 HOH A2264 HOH A2305 HOH D2344 HOH D2347
SITE 2 AC9 5 HOH D2354
SITE 1 BC1 4 LYS A 21 GLY A 24 LEU A 25 GLU A 114
SITE 1 BC2 8 ILE A 58 GLN A 89 ASN A 93 CYS A 95
SITE 2 BC2 8 VAL A 166 LEU A 168 HIS A 169 GLY B 75
SITE 1 BC3 8 GLN C 89 ASN C 93 CYS C 95 VAL C 166
SITE 2 BC3 8 LEU C 168 HIS C 169 HOH C2432 GLY D 75
CRYST1 46.110 49.290 67.620 86.12 75.03 76.78 P 1 2
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 0.021687 -0.005095 -0.005753 0.00000
SCALE2 0.000000 0.020840 -0.000190 0.00000
SCALE3 0.000000 0.000000 0.015309 0.00000
ATOM 1 N GLU A 2 39.210 43.308 59.499 1.00 53.33 N
ATOM 2 CA GLU A 2 40.438 44.160 59.479 1.00 50.81 C
ATOM 3 C GLU A 2 40.041 45.592 59.867 1.00 49.68 C
ATOM 4 O GLU A 2 40.863 46.513 59.859 1.00 52.12 O
ATOM 5 CB GLU A 2 41.074 44.114 58.083 1.00 51.48 C
ATOM 6 CG GLU A 2 42.527 44.575 58.052 1.00 55.24 C
ATOM 7 CD GLU A 2 43.047 44.730 56.638 1.00 56.89 C
ATOM 8 OE1 GLU A 2 42.212 44.897 55.726 1.00 61.52 O
ATOM 9 OE2 GLU A 2 44.280 44.706 56.435 1.00 59.16 O
ATOM 10 N GLY A 3 38.767 45.743 60.225 1.00 46.68 N
ATOM 11 CA GLY A 3 38.234 47.019 60.659 1.00 40.20 C
ATOM 12 C GLY A 3 38.007 48.099 59.616 1.00 38.25 C
ATOM 13 O GLY A 3 37.690 49.237 59.973 1.00 34.54 O
ATOM 14 N GLN A 4 38.145 47.778 58.333 1.00 33.53 N
ATOM 15 CA GLN A 4 37.947 48.809 57.325 1.00 28.87 C
ATOM 16 C GLN A 4 36.508 49.284 57.193 1.00 24.56 C
ATOM 17 O GLN A 4 35.552 48.603 57.586 1.00 22.86 O
ATOM 18 CB GLN A 4 38.502 48.367 55.956 1.00 33.73 C
ATOM 19 CG GLN A 4 38.202 46.958 55.498 1.00 31.98 C
ATOM 20 CD GLN A 4 39.005 46.570 54.251 1.00 32.23 C
ATOM 21 OE1 GLN A 4 38.797 47.104 53.158 1.00 25.71 O
ATOM 22 NE2 GLN A 4 39.927 45.642 54.420 1.00 27.07 N
ATOM 23 N ARG A 5 36.377 50.493 56.664 1.00 24.44 N
ATOM 24 CA ARG A 5 35.086 51.122 56.446 1.00 25.69 C
ATOM 25 C ARG A 5 35.088 51.575 55.001 1.00 23.95 C
ATOM 26 O ARG A 5 36.076 52.128 54.514 1.00 25.27 O
ATOM 27 CB ARG A 5 34.921 52.356 57.334 1.00 27.49 C
ATOM 28 CG ARG A 5 35.040 52.121 58.829 1.00 29.91 C
ATOM 29 CD ARG A 5 35.027 53.465 59.547 1.00 36.10 C
ATOM 30 NE ARG A 5 36.151 54.293 59.114 1.00 35.74 N
ATOM 31 CZ ARG A 5 36.228 55.613 59.267 1.00 32.49 C
ATOM 32 NH1 ARG A 5 35.241 56.284 59.847 1.00 26.87 N
ATOM 33 NH2 ARG A 5 37.300 56.264 58.834 1.00 32.31 N
ATOM 34 N TRP A 6 33.977 51.343 54.322 1.00 18.68 N
ATOM 35 CA TRP A 6 33.834 51.734 52.929 1.00 17.18 C
ATOM 36 C TRP A 6 32.723 52.762 52.848 1.00 18.52 C
ATOM 37 O TRP A 6 32.136 53.123 53.862 1.00 20.56 O
ATOM 38 CB TRP A 6 33.454 50.523 52.089 1.00 15.31 C
ATOM 39 CG TRP A 6 34.534 49.502 51.921 1.00 11.81 C
ATOM 40 CD1 TRP A 6 35.755 49.461 52.544 1.00 13.15 C
ATOM 41 CD2 TRP A 6 34.475 48.350 51.075 1.00 11.58 C
ATOM 42 NE1 TRP A 6 36.455 48.349 52.132 1.00 12.65 N
ATOM 43 CE2 TRP A 6 35.691 47.651 51.230 1.00 13.06 C
ATOM 44 CE3 TRP A 6 33.507 47.839 50.193 1.00 11.17 C
ATOM 45 CZ2 TRP A 6 35.970 46.466 50.544 1.00 13.22 C
ATOM 46 CZ3 TRP A 6 33.783 46.658 49.508 1.00 13.70 C
ATOM 47 CH2 TRP A 6 35.006 45.984 49.688 1.00 12.84 C
ATOM 48 N LEU A 7 32.443 53.243 51.642 1.00 15.47 N
ATOM 49 CA LEU A 7 31.375 54.214 51.446 1.00 15.31 C
ATOM 50 C LEU A 7 30.119 53.505 50.978 1.00 15.12 C
ATOM 51 O LEU A 7 30.202 52.514 50.274 1.00 15.75 O
ATOM 52 CB LEU A 7 31.765 55.230 50.376 1.00 16.56 C
ATOM 53 CG LEU A 7 32.874 56.218 50.713 1.00 20.71 C
ATOM 54 CD1 LEU A 7 33.274 56.948 49.447 1.00 20.31 C
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