HEADER LIGASE 06-DEC-04 1Y6L
TITLE HUMAN UBIQUITIN CONJUGATING ENZYME E2E2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN-CONJUGATING ENZYME E2E2;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: RESIDUES 55-201;
COMPND 5 SYNONYM: UBIQUITIN-PROTEIN LIGASE E2, UBIQUITIN CARRIER PROTEIN E2,
COMPND 6 UBCH8;
COMPND 7 EC: 6.3.2.19;
COMPND 8 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: UBE2E2, UBCH8;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS STRUCTURAL GENOMICS CONSORTIUM, UBIQUITIN, UBIQUITIN-CONJUGATING
KEYWDS 2 ENZYME, LIGASE, SGC
EXPDTA X-RAY DIFFRACTION
AUTHOR J.R.WALKER,G.V.AVVAKUMOV,E.M.NEWMAN,F.MACKENZIE,I.KOZIERADZKI,
AUTHOR 2 A.BOCHKAREV,M.SUNDSTROM,C.ARROWSMITH,A.EDWARDS,S.DHE-PAGANON,
AUTHOR 3 STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 6 23-AUG-23 1Y6L 1 SEQADV
REVDAT 5 28-NOV-12 1Y6L 1 JRNL VERSN
REVDAT 4 24-FEB-09 1Y6L 1 VERSN
REVDAT 3 10-OCT-06 1Y6L 1 AUTHOR KEYWDS DBREF SEQADV
REVDAT 2 24-JAN-06 1Y6L 1 JRNL
REVDAT 1 11-JAN-05 1Y6L 0
JRNL AUTH Y.SHENG,J.H.HONG,R.DOHERTY,T.SRIKUMAR,J.SHLOUSH,
JRNL AUTH 2 G.V.AVVAKUMOV,J.R.WALKER,S.XUE,D.NECULAI,J.W.WAN,S.K.KIM,
JRNL AUTH 3 C.H.ARROWSMITH,B.RAUGHT,S.DHE-PAGANON
JRNL TITL A HUMAN UBIQUITIN CONJUGATING ENZYME (E2)-HECT E3 LIGASE
JRNL TITL 2 STRUCTURE-FUNCTION SCREEN.
JRNL REF MOL CELL PROTEOMICS V. 11 329 2012
JRNL REFN ISSN 1535-9476
JRNL PMID 22496338
JRNL DOI 10.1074/MCP.O111.013706
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.5
REMARK 3 NUMBER OF REFLECTIONS : 37014
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) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1995
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2773
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.43
REMARK 3 BIN R VALUE (WORKING SET) : 0.2770
REMARK 3 BIN FREE R VALUE SET COUNT : 130
REMARK 3 BIN FREE R VALUE : 0.3590
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3486
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 369
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.99
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.34000
REMARK 3 B22 (A**2) : 2.13000
REMARK 3 B33 (A**2) : -0.74000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.13000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.158
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.154
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.100
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.315
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3579 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4881 ; 1.588 ; 1.969
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 441 ; 5.673 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 147 ;35.318 ;23.469
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 585 ;15.655 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;14.507 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 546 ; 0.117 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2715 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1797 ; 0.204 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2473 ; 0.315 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 302 ; 0.179 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 80 ; 0.185 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 27 ; 0.163 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2300 ; 1.058 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3651 ; 1.723 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1485 ; 2.762 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1230 ; 4.285 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 1Y6L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-DEC-04.
REMARK 100 THE DEPOSITION ID IS D_1000031180.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-NOV-04
REMARK 200 TEMPERATURE (KELVIN) : 298.0
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39009
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 19.260
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.5
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.04400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.2800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.92
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.9
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1QCQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M (NH4)2SO4, 0.1M TRIS, PH 8.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 54.05450
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 18.05500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 54.05450
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 18.05500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 300 REMARK: THE BIOLOGICAL UNIT IS EXPECTED TO BE A MONOMER.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 B 193 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 GLY A -1
REMARK 465 GLY B -1
REMARK 465 GLY C -1
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 180 O HOH C 254 2.07
REMARK 500 NH2 ARG A 5 O PRO A 95 2.15
REMARK 500 NH2 ARG B 5 O LEU B 97 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 5 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LYS A 90 -103.03 -132.33
REMARK 500 LYS B 90 -120.72 -129.98
REMARK 500 ASN B 130 63.52 -151.49
REMARK 500 LYS C 90 -117.61 -131.34
REMARK 500 ASN C 130 67.46 -152.57
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1Y6L A 1 147 UNP Q96LR5 UB2E2_HUMAN 55 201
DBREF 1Y6L B 1 147 UNP Q96LR5 UB2E2_HUMAN 55 201
DBREF 1Y6L C 1 147 UNP Q96LR5 UB2E2_HUMAN 55 201
SEQADV 1Y6L GLY A -1 UNP Q96LR5 CLONING ARTIFACT
SEQADV 1Y6L SER A 0 UNP Q96LR5 CLONING ARTIFACT
SEQADV 1Y6L GLY B -1 UNP Q96LR5 CLONING ARTIFACT
SEQADV 1Y6L SER B 0 UNP Q96LR5 CLONING ARTIFACT
SEQADV 1Y6L GLY C -1 UNP Q96LR5 CLONING ARTIFACT
SEQADV 1Y6L SER C 0 UNP Q96LR5 CLONING ARTIFACT
SEQRES 1 A 149 GLY SER THR SER ALA LYS ARG ILE GLN LYS GLU LEU ALA
SEQRES 2 A 149 GLU ILE THR LEU ASP PRO PRO PRO ASN CYS SER ALA GLY
SEQRES 3 A 149 PRO LYS GLY ASP ASN ILE TYR GLU TRP ARG SER THR ILE
SEQRES 4 A 149 LEU GLY PRO PRO GLY SER VAL TYR GLU GLY GLY VAL PHE
SEQRES 5 A 149 PHE LEU ASP ILE THR PHE SER PRO ASP TYR PRO PHE LYS
SEQRES 6 A 149 PRO PRO LYS VAL THR PHE ARG THR ARG ILE TYR HIS CYS
SEQRES 7 A 149 ASN ILE ASN SER GLN GLY VAL ILE CYS LEU ASP ILE LEU
SEQRES 8 A 149 LYS ASP ASN TRP SER PRO ALA LEU THR ILE SER LYS VAL
SEQRES 9 A 149 LEU LEU SER ILE CYS SER LEU LEU THR ASP CYS ASN PRO
SEQRES 10 A 149 ALA ASP PRO LEU VAL GLY SER ILE ALA THR GLN TYR MET
SEQRES 11 A 149 THR ASN ARG ALA GLU HIS ASP ARG MET ALA ARG GLN TRP
SEQRES 12 A 149 THR LYS ARG TYR ALA THR
SEQRES 1 B 149 GLY SER THR SER ALA LYS ARG ILE GLN LYS GLU LEU ALA
SEQRES 2 B 149 GLU ILE THR LEU ASP PRO PRO PRO ASN CYS SER ALA GLY
SEQRES 3 B 149 PRO LYS GLY ASP ASN ILE TYR GLU TRP ARG SER THR ILE
SEQRES 4 B 149 LEU GLY PRO PRO GLY SER VAL TYR GLU GLY GLY VAL PHE
SEQRES 5 B 149 PHE LEU ASP ILE THR PHE SER PRO ASP TYR PRO PHE LYS
SEQRES 6 B 149 PRO PRO LYS VAL THR PHE ARG THR ARG ILE TYR HIS CYS
SEQRES 7 B 149 ASN ILE ASN SER GLN GLY VAL ILE CYS LEU ASP ILE LEU
SEQRES 8 B 149 LYS ASP ASN TRP SER PRO ALA LEU THR ILE SER LYS VAL
SEQRES 9 B 149 LEU LEU SER ILE CYS SER LEU LEU THR ASP CYS ASN PRO
SEQRES 10 B 149 ALA ASP PRO LEU VAL GLY SER ILE ALA THR GLN TYR MET
SEQRES 11 B 149 THR ASN ARG ALA GLU HIS ASP ARG MET ALA ARG GLN TRP
SEQRES 12 B 149 THR LYS ARG TYR ALA THR
SEQRES 1 C 149 GLY SER THR SER ALA LYS ARG ILE GLN LYS GLU LEU ALA
SEQRES 2 C 149 GLU ILE THR LEU ASP PRO PRO PRO ASN CYS SER ALA GLY
SEQRES 3 C 149 PRO LYS GLY ASP ASN ILE TYR GLU TRP ARG SER THR ILE
SEQRES 4 C 149 LEU GLY PRO PRO GLY SER VAL TYR GLU GLY GLY VAL PHE
SEQRES 5 C 149 PHE LEU ASP ILE THR PHE SER PRO ASP TYR PRO PHE LYS
SEQRES 6 C 149 PRO PRO LYS VAL THR PHE ARG THR ARG ILE TYR HIS CYS
SEQRES 7 C 149 ASN ILE ASN SER GLN GLY VAL ILE CYS LEU ASP ILE LEU
SEQRES 8 C 149 LYS ASP ASN TRP SER PRO ALA LEU THR ILE SER LYS VAL
SEQRES 9 C 149 LEU LEU SER ILE CYS SER LEU LEU THR ASP CYS ASN PRO
SEQRES 10 C 149 ALA ASP PRO LEU VAL GLY SER ILE ALA THR GLN TYR MET
SEQRES 11 C 149 THR ASN ARG ALA GLU HIS ASP ARG MET ALA ARG GLN TRP
SEQRES 12 C 149 THR LYS ARG TYR ALA THR
FORMUL 4 HOH *369(H2 O)
HELIX 1 1 THR A 1 ASP A 16 1 16
HELIX 2 2 LEU A 86 LYS A 90 5 5
HELIX 3 3 THR A 98 ASP A 112 1 15
HELIX 4 4 VAL A 120 ASN A 130 1 11
HELIX 5 5 ASN A 130 ALA A 146 1 17
HELIX 6 6 THR B 1 ASP B 16 1 16
HELIX 7 7 LEU B 86 LYS B 90 5 5
HELIX 8 8 THR B 98 ASP B 112 1 15
HELIX 9 9 VAL B 120 ASN B 130 1 11
HELIX 10 10 ASN B 130 ALA B 146 1 17
HELIX 11 11 THR C 1 ASP C 16 1 16
HELIX 12 12 LEU C 86 LYS C 90 5 5
HELIX 13 13 THR C 98 ASP C 112 1 15
HELIX 14 14 VAL C 120 ASN C 130 1 11
HELIX 15 15 ASN C 130 ALA C 146 1 17
SHEET 1 A 4 CYS A 21 PRO A 25 0
SHEET 2 A 4 GLU A 32 LEU A 38 -1 O ARG A 34 N GLY A 24
SHEET 3 A 4 VAL A 49 THR A 55 -1 O PHE A 50 N ILE A 37
SHEET 4 A 4 LYS A 66 PHE A 69 -1 O LYS A 66 N THR A 55
SHEET 1 B 4 CYS B 21 PRO B 25 0
SHEET 2 B 4 GLU B 32 LEU B 38 -1 O ARG B 34 N GLY B 24
SHEET 3 B 4 VAL B 49 THR B 55 -1 O PHE B 50 N ILE B 37
SHEET 4 B 4 LYS B 66 PHE B 69 -1 O LYS B 66 N THR B 55
SHEET 1 C 4 CYS C 21 PRO C 25 0
SHEET 2 C 4 GLU C 32 LEU C 38 -1 O ARG C 34 N GLY C 24
SHEET 3 C 4 VAL C 49 THR C 55 -1 O PHE C 50 N ILE C 37
SHEET 4 C 4 LYS C 66 PHE C 69 -1 O LYS C 66 N THR C 55
CISPEP 1 TYR A 60 PRO A 61 0 8.31
CISPEP 2 TYR B 60 PRO B 61 0 9.06
CISPEP 3 TYR C 60 PRO C 61 0 8.23
CRYST1 108.109 36.110 130.568 90.00 99.92 90.00 C 1 2 1 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 0.009250 0.000000 0.001618 0.00000
SCALE2 0.000000 0.027693 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007775 0.00000
(ATOM LINES ARE NOT SHOWN.)
END