HEADER PROTEIN BINDING/SIGNALING PROTEIN 01-OCT-14 4WJP
TITLE CRYSTAL STRUCTURE OF SUMO1 IN COMPLEX WITH PHOSPHORYLATED DAXX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SMALL UBIQUITIN-RELATED MODIFIER 1;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: UNP RESIDUES 17-97;
COMPND 5 SYNONYM: SUMO-1,GAP-MODIFYING PROTEIN 1,GMP1,SMT3 HOMOLOG 3,SENTRIN,
COMPND 6 UBIQUITIN-HOMOLOGY DOMAIN PROTEIN PIC1,UBIQUITIN-LIKE PROTEIN SMT3C,
COMPND 7 SMT3C,UBIQUITIN-LIKE PROTEIN UBL1;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: DAXX;
COMPND 12 CHAIN: B, D;
COMPND 13 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: SUMO1, SMT3C, SMT3H3, UBL1, OK/SW-CL.43;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: TOPP2;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX2T;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_TAXID: 9606
KEYWDS SUMO1, DAXX, SUMO INTERACTION MOTIF, PHOSPHOSIM, PROTEIN BINDING-
KEYWDS 2 SIGNALING PROTEIN COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR L.CAPPADOCIA,X.H.MASCLE,V.BOURDEAU,S.TREMBLAY-BELZILE,M.CHAKER-
AUTHOR 2 MARGOT,M.LUSSIER-PRICE,J.WADA,K.SAKAGUCHI,M.AUBRY,G.FERBEYRE,
AUTHOR 3 J.G.OMICHINSKI
REVDAT 4 27-SEP-23 4WJP 1 REMARK
REVDAT 3 22-NOV-17 4WJP 1 SOURCE KEYWDS JRNL REMARK
REVDAT 2 14-JAN-15 4WJP 1 JRNL
REVDAT 1 31-DEC-14 4WJP 0
JRNL AUTH L.CAPPADOCIA,X.H.MASCLE,V.BOURDEAU,S.TREMBLAY-BELZILE,
JRNL AUTH 2 M.CHAKER-MARGOT,M.LUSSIER-PRICE,J.WADA,K.SAKAGUCHI,M.AUBRY,
JRNL AUTH 3 G.FERBEYRE,J.G.OMICHINSKI
JRNL TITL STRUCTURAL AND FUNCTIONAL CHARACTERIZATION OF THE
JRNL TITL 2 PHOSPHORYLATION-DEPENDENT INTERACTION BETWEEN PML AND SUMO1.
JRNL REF STRUCTURE V. 23 126 2015
JRNL REFN ISSN 0969-2126
JRNL PMID 25497731
JRNL DOI 10.1016/J.STR.2014.10.015
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: DEV_1555)
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.71
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 20821
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.195
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 1051
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 33.7197 - 3.3990 1.00 2541 135 0.1350 0.1651
REMARK 3 2 3.3990 - 2.6983 1.00 2479 131 0.1692 0.2013
REMARK 3 3 2.6983 - 2.3573 1.00 2504 131 0.1695 0.2062
REMARK 3 4 2.3573 - 2.1418 1.00 2436 134 0.1656 0.2030
REMARK 3 5 2.1418 - 1.9883 1.00 2464 135 0.1737 0.1939
REMARK 3 6 1.9883 - 1.8711 1.00 2485 123 0.1846 0.2231
REMARK 3 7 1.8711 - 1.7774 1.00 2428 133 0.2067 0.2168
REMARK 3 8 1.7774 - 1.7000 1.00 2433 129 0.2525 0.2942
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) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.250
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.04
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.91
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 : 0.012 1496
REMARK 3 ANGLE : 1.253 2007
REMARK 3 CHIRALITY : 0.055 216
REMARK 3 PLANARITY : 0.006 260
REMARK 3 DIHEDRAL : 16.926 592
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ( CHAIN A AND RESID 19:97 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.4062 -0.9761 31.9142
REMARK 3 T TENSOR
REMARK 3 T11: 0.1195 T22: 0.1336
REMARK 3 T33: 0.1682 T12: -0.0027
REMARK 3 T13: 0.0089 T23: -0.0079
REMARK 3 L TENSOR
REMARK 3 L11: 2.3930 L22: 3.7675
REMARK 3 L33: 2.4078 L12: -0.6240
REMARK 3 L13: 0.5230 L23: 0.1860
REMARK 3 S TENSOR
REMARK 3 S11: 0.0383 S12: 0.1220 S13: 0.0358
REMARK 3 S21: -0.0556 S22: -0.0675 S23: -0.0846
REMARK 3 S31: 0.0135 S32: 0.1079 S33: 0.0485
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: ( CHAIN B AND RESID 6:10 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.1987 4.6577 33.4392
REMARK 3 T TENSOR
REMARK 3 T11: 0.2751 T22: 0.1876
REMARK 3 T33: 0.2725 T12: -0.0351
REMARK 3 T13: -0.0188 T23: -0.0026
REMARK 3 L TENSOR
REMARK 3 L11: 6.4292 L22: 4.1568
REMARK 3 L33: 3.8328 L12: 1.4281
REMARK 3 L13: 0.3502 L23: -0.2586
REMARK 3 S TENSOR
REMARK 3 S11: 0.4856 S12: 0.0371 S13: -0.3186
REMARK 3 S21: 0.0324 S22: -0.1729 S23: -0.0504
REMARK 3 S31: 0.4696 S32: -0.6389 S33: -0.3862
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: ( CHAIN B AND ( RESID 11:14 OR RESID 15:15 ) )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.5883 9.6019 26.1435
REMARK 3 T TENSOR
REMARK 3 T11: 0.2530 T22: 0.2332
REMARK 3 T33: 0.3760 T12: -0.0589
REMARK 3 T13: 0.0534 T23: 0.0646
REMARK 3 L TENSOR
REMARK 3 L11: 4.7896 L22: 4.9792
REMARK 3 L33: 2.8782 L12: -0.7403
REMARK 3 L13: 2.2278 L23: 1.9478
REMARK 3 S TENSOR
REMARK 3 S11: -0.2572 S12: 0.4588 S13: 0.7236
REMARK 3 S21: -0.4607 S22: -0.1457 S23: -0.8832
REMARK 3 S31: -0.7272 S32: 0.5316 S33: 0.3892
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: ( CHAIN C AND RESID 18:94 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.7812 -5.9101 7.9500
REMARK 3 T TENSOR
REMARK 3 T11: 0.1969 T22: 0.2095
REMARK 3 T33: 0.1530 T12: 0.0033
REMARK 3 T13: -0.0156 T23: -0.0027
REMARK 3 L TENSOR
REMARK 3 L11: 2.1707 L22: 3.0832
REMARK 3 L33: 2.6101 L12: -0.3824
REMARK 3 L13: 0.5443 L23: 1.0122
REMARK 3 S TENSOR
REMARK 3 S11: 0.0186 S12: -0.0177 S13: 0.0071
REMARK 3 S21: 0.0166 S22: 0.0087 S23: -0.0142
REMARK 3 S31: 0.1023 S32: -0.1181 S33: -0.0186
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: ( CHAIN D AND RESID 7:14 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.7415 -13.1960 1.7673
REMARK 3 T TENSOR
REMARK 3 T11: 0.3412 T22: 0.4172
REMARK 3 T33: 0.3131 T12: 0.0083
REMARK 3 T13: -0.0233 T23: 0.0218
REMARK 3 L TENSOR
REMARK 3 L11: 5.1161 L22: 5.8137
REMARK 3 L33: 9.7398 L12: -0.6599
REMARK 3 L13: 1.1115 L23: 0.4564
REMARK 3 S TENSOR
REMARK 3 S11: 0.0314 S12: 0.3757 S13: -0.5656
REMARK 3 S21: -0.4561 S22: -0.1819 S23: 0.3395
REMARK 3 S31: -0.3165 S32: -0.4652 S33: 0.5421
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: ( CHAIN D AND RESID 15:18 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.5052 -17.1139 18.6843
REMARK 3 T TENSOR
REMARK 3 T11: 1.0735 T22: 1.5726
REMARK 3 T33: 0.9082 T12: -0.0717
REMARK 3 T13: -0.1901 T23: 0.5818
REMARK 3 L TENSOR
REMARK 3 L11: 2.1000 L22: 0.1264
REMARK 3 L33: 3.7884 L12: -0.4895
REMARK 3 L13: 2.7836 L23: -0.6837
REMARK 3 S TENSOR
REMARK 3 S11: 0.1777 S12: -0.1884 S13: 0.1903
REMARK 3 S21: -0.1910 S22: -0.2170 S23: -0.0593
REMARK 3 S31: -0.1633 S32: -0.1201 S33: 0.0677
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 4WJP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-OCT-14.
REMARK 100 THE DEPOSITION ID IS D_1000202246.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-FEB-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X25
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.10
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS, SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20835
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.04200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.41200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: PDB ENTRY 2UYZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM SODIUM CACODYLATE, 26% PEG3350,
REMARK 280 10MM CACL2, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 19.03450
REMARK 290 SMTRY3 2 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 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 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 GLY A 15
REMARK 465 SER A 16
REMARK 465 LYS A 17
REMARK 465 GLU A 18
REMARK 465 GLY B 3
REMARK 465 SER B 4
REMARK 465 GLY B 5
REMARK 465 SEP B 17
REMARK 465 ASP B 18
REMARK 465 TYR B 19
REMARK 465 GLY C 15
REMARK 465 SER C 16
REMARK 465 LYS C 17
REMARK 465 THR C 95
REMARK 465 GLY C 96
REMARK 465 GLY C 97
REMARK 465 GLY D 3
REMARK 465 SER D 4
REMARK 465 GLY D 5
REMARK 465 GLU D 6
REMARK 465 TYR D 19
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 OE2 GLU A 20 O HOH A 101 2.12
REMARK 500 O HOH C 156 O HOH C 157 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 A 120 O HOH A 137 2556 2.19
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 SER A 31 2.70 80.72
REMARK 500 GLU A 85 -1.71 83.67
REMARK 500 SEP B 15 -179.62 -62.44
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4WJN RELATED DB: PDB
REMARK 900 RELATED ID: 4WJO RELATED DB: PDB
REMARK 900 RELATED ID: 4WJQ RELATED DB: PDB
DBREF 4WJP A 17 97 UNP P63165 SUMO1_HUMAN 17 97
DBREF 4WJP B 3 19 PDB 4WJP 4WJP 3 19
DBREF 4WJP C 17 97 UNP P63165 SUMO1_HUMAN 17 97
DBREF 4WJP D 3 19 PDB 4WJP 4WJP 3 19
SEQADV 4WJP GLY A 15 UNP P63165 EXPRESSION TAG
SEQADV 4WJP SER A 16 UNP P63165 EXPRESSION TAG
SEQADV 4WJP ALA A 52 UNP P63165 CYS 52 ENGINEERED MUTATION
SEQADV 4WJP GLY C 15 UNP P63165 EXPRESSION TAG
SEQADV 4WJP SER C 16 UNP P63165 EXPRESSION TAG
SEQADV 4WJP ALA C 52 UNP P63165 CYS 52 ENGINEERED MUTATION
SEQRES 1 A 83 GLY SER LYS GLU GLY GLU TYR ILE LYS LEU LYS VAL ILE
SEQRES 2 A 83 GLY GLN ASP SER SER GLU ILE HIS PHE LYS VAL LYS MET
SEQRES 3 A 83 THR THR HIS LEU LYS LYS LEU LYS GLU SER TYR ALA GLN
SEQRES 4 A 83 ARG GLN GLY VAL PRO MET ASN SER LEU ARG PHE LEU PHE
SEQRES 5 A 83 GLU GLY GLN ARG ILE ALA ASP ASN HIS THR PRO LYS GLU
SEQRES 6 A 83 LEU GLY MET GLU GLU GLU ASP VAL ILE GLU VAL TYR GLN
SEQRES 7 A 83 GLU GLN THR GLY GLY
SEQRES 1 B 17 GLY SER GLY GLU ALA GLU GLU ARG ILE ILE VAL LEU SEP
SEQRES 2 B 17 ASP SEP ASP TYR
SEQRES 1 C 83 GLY SER LYS GLU GLY GLU TYR ILE LYS LEU LYS VAL ILE
SEQRES 2 C 83 GLY GLN ASP SER SER GLU ILE HIS PHE LYS VAL LYS MET
SEQRES 3 C 83 THR THR HIS LEU LYS LYS LEU LYS GLU SER TYR ALA GLN
SEQRES 4 C 83 ARG GLN GLY VAL PRO MET ASN SER LEU ARG PHE LEU PHE
SEQRES 5 C 83 GLU GLY GLN ARG ILE ALA ASP ASN HIS THR PRO LYS GLU
SEQRES 6 C 83 LEU GLY MET GLU GLU GLU ASP VAL ILE GLU VAL TYR GLN
SEQRES 7 C 83 GLU GLN THR GLY GLY
SEQRES 1 D 17 GLY SER GLY GLU ALA GLU GLU ARG ILE ILE VAL LEU SEP
SEQRES 2 D 17 ASP SEP ASP TYR
HET SEP B 15 14
HET SEP D 15 13
HET SEP D 17 13
HETNAM SEP PHOSPHOSERINE
HETSYN SEP PHOSPHONOSERINE
FORMUL 2 SEP 3(C3 H8 N O6 P)
FORMUL 5 HOH *177(H2 O)
HELIX 1 AA1 LEU A 44 GLY A 56 1 13
HELIX 2 AA2 PRO A 58 ASN A 60 5 3
HELIX 3 AA3 THR A 76 GLY A 81 1 6
HELIX 4 AA4 LEU C 44 GLY C 56 1 13
HELIX 5 AA5 PRO C 58 ASN C 60 5 3
HELIX 6 AA6 THR C 76 GLY C 81 1 6
SHEET 1 AA1 6 GLN A 69 ARG A 70 0
SHEET 2 AA1 6 LEU A 62 PHE A 66 -1 N PHE A 66 O GLN A 69
SHEET 3 AA1 6 VAL A 87 GLN A 92 -1 O GLU A 89 N LEU A 65
SHEET 4 AA1 6 TYR A 21 ILE A 27 1 N LYS A 25 O ILE A 88
SHEET 5 AA1 6 GLU A 33 LYS A 39 -1 O VAL A 38 N ILE A 22
SHEET 6 AA1 6 ILE B 11 VAL B 13 1 O ILE B 12 N HIS A 35
SHEET 1 AA2 6 GLN C 69 ARG C 70 0
SHEET 2 AA2 6 LEU C 62 PHE C 66 -1 N PHE C 66 O GLN C 69
SHEET 3 AA2 6 VAL C 87 GLN C 92 -1 O GLU C 89 N LEU C 65
SHEET 4 AA2 6 TYR C 21 ILE C 27 1 N LYS C 25 O ILE C 88
SHEET 5 AA2 6 GLU C 33 LYS C 39 -1 O VAL C 38 N ILE C 22
SHEET 6 AA2 6 ILE D 11 VAL D 13 1 O ILE D 12 N HIS C 35
LINK C LEU B 14 N SEP B 15 1555 1555 1.33
LINK C SEP B 15 N ASP B 16 1555 1555 1.33
LINK C LEU D 14 N SEP D 15 1555 1555 1.33
LINK C SEP D 15 N ASP D 16 1555 1555 1.33
LINK C ASP D 16 N SEP D 17 1555 1555 1.33
LINK C SEP D 17 N ASP D 18 1555 1555 1.33
CISPEP 1 GLN A 94 THR A 95 0 22.56
CRYST1 34.266 38.069 73.950 90.00 101.04 90.00 P 1 21 1 4
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 0.029183 0.000000 0.005695 0.00000
SCALE2 0.000000 0.026268 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013778 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
