HEADER CELL CYCLE 09-JUN-16 5L95
TITLE CRYSTAL STRUCTURE OF HUMAN UBA5 IN COMPLEX WITH UFM1 AND AMP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN-LIKE MODIFIER-ACTIVATING ENZYME 5;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: UBIQUITIN-ACTIVATING ENZYME 5,THIFP1,UFM1-ACTIVATING ENZYME,
COMPND 5 UBIQUITIN-ACTIVATING ENZYME E1 DOMAIN-CONTAINING PROTEIN 1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: UBIQUITIN-FOLD MODIFIER 1;
COMPND 9 CHAIN: C, D;
COMPND 10 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: UBA5, UBE1DC1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: UFM1, C13ORF20, BM-002;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS UBIQUITIN LIKE PROTEIN E1, UBL, CELL CYCLE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.OWEIS,P.PADALA,R.WIENER
REVDAT 3 10-JAN-24 5L95 1 REMARK
REVDAT 2 05-OCT-16 5L95 1 JRNL
REVDAT 1 21-SEP-16 5L95 0
JRNL AUTH W.OWEIS,P.PADALA,F.HASSOUNA,E.COHEN-KFIR,D.R.GIBBS,E.A.TODD,
JRNL AUTH 2 C.E.BERNDSEN,R.WIENER
JRNL TITL TRANS-BINDING MECHANISM OF UBIQUITIN-LIKE PROTEIN ACTIVATION
JRNL TITL 2 REVEALED BY A UBA5-UFM1 COMPLEX.
JRNL REF CELL REP V. 16 3113 2016
JRNL REFN ESSN 2211-1247
JRNL PMID 27653677
JRNL DOI 10.1016/J.CELREP.2016.08.067
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10_2142: ???)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 77.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 65664
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 3326
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 77.0508 - 6.0566 1.00 2755 148 0.1865 0.2292
REMARK 3 2 6.0566 - 4.8075 1.00 2659 146 0.1932 0.2104
REMARK 3 3 4.8075 - 4.1999 1.00 2652 129 0.1532 0.1854
REMARK 3 4 4.1999 - 3.8159 1.00 2614 145 0.1646 0.1810
REMARK 3 5 3.8159 - 3.5424 1.00 2628 147 0.1711 0.2017
REMARK 3 6 3.5424 - 3.3335 1.00 2577 152 0.1726 0.1958
REMARK 3 7 3.3335 - 3.1666 1.00 2607 140 0.1657 0.1719
REMARK 3 8 3.1666 - 3.0287 1.00 2617 125 0.1767 0.1856
REMARK 3 9 3.0287 - 2.9121 0.99 2587 125 0.1838 0.2130
REMARK 3 10 2.9121 - 2.8116 1.00 2609 148 0.1909 0.2006
REMARK 3 11 2.8116 - 2.7237 1.00 2585 128 0.1880 0.2102
REMARK 3 12 2.7237 - 2.6459 1.00 2586 126 0.1996 0.2012
REMARK 3 13 2.6459 - 2.5762 1.00 2596 153 0.2039 0.2168
REMARK 3 14 2.5762 - 2.5133 1.00 2595 127 0.2189 0.2090
REMARK 3 15 2.5133 - 2.4562 1.00 2547 149 0.2182 0.2569
REMARK 3 16 2.4562 - 2.4039 1.00 2602 123 0.2361 0.2344
REMARK 3 17 2.4039 - 2.3558 1.00 2571 129 0.2431 0.2845
REMARK 3 18 2.3558 - 2.3114 1.00 2596 129 0.2456 0.2568
REMARK 3 19 2.3114 - 2.2701 1.00 2610 110 0.2596 0.2943
REMARK 3 20 2.2701 - 2.2316 0.99 2502 159 0.3126 0.3709
REMARK 3 21 2.2316 - 2.1956 0.99 2575 162 0.2843 0.3178
REMARK 3 22 2.1956 - 2.1618 0.99 2571 122 0.2954 0.3436
REMARK 3 23 2.1618 - 2.1300 1.00 2541 149 0.3124 0.3279
REMARK 3 24 2.1300 - 2.1000 0.99 2556 155 0.3110 0.3083
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.770
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 : 0.006 5160
REMARK 3 ANGLE : 0.884 7002
REMARK 3 CHIRALITY : 0.053 809
REMARK 3 PLANARITY : 0.006 908
REMARK 3 DIHEDRAL : 13.775 3093
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESSEQ 68:346)
REMARK 3 ORIGIN FOR THE GROUP (A): 53.8654 -42.2456 15.8417
REMARK 3 T TENSOR
REMARK 3 T11: 0.1534 T22: 0.1340
REMARK 3 T33: 0.1710 T12: -0.0695
REMARK 3 T13: 0.0104 T23: 0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 1.5644 L22: 1.5198
REMARK 3 L33: 2.0580 L12: 0.1549
REMARK 3 L13: 0.2820 L23: -0.4911
REMARK 3 S TENSOR
REMARK 3 S11: 0.0752 S12: -0.1151 S13: -0.0314
REMARK 3 S21: 0.1523 S22: 0.0092 S23: 0.1360
REMARK 3 S31: -0.2093 S32: -0.0562 S33: 0.0490
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN B AND RESSEQ 68:346)
REMARK 3 ORIGIN FOR THE GROUP (A): 28.7106 -58.3952 9.1767
REMARK 3 T TENSOR
REMARK 3 T11: 0.2071 T22: 0.2634
REMARK 3 T33: 0.2777 T12: -0.1271
REMARK 3 T13: 0.0314 T23: 0.0297
REMARK 3 L TENSOR
REMARK 3 L11: 1.9335 L22: 1.9410
REMARK 3 L33: 1.7619 L12: 0.9304
REMARK 3 L13: -0.2972 L23: 0.2277
REMARK 3 S TENSOR
REMARK 3 S11: -0.0459 S12: -0.0136 S13: 0.2839
REMARK 3 S21: 0.1809 S22: 0.0417 S23: 0.4713
REMARK 3 S31: 0.1444 S32: -0.3538 S33: -0.1149
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN C AND RESSEQ 4:83)
REMARK 3 ORIGIN FOR THE GROUP (A): 51.7109 -31.3142 -7.6828
REMARK 3 T TENSOR
REMARK 3 T11: 0.3730 T22: 0.2809
REMARK 3 T33: 0.2858 T12: -0.1240
REMARK 3 T13: -0.0281 T23: -0.0059
REMARK 3 L TENSOR
REMARK 3 L11: 0.3446 L22: 0.6765
REMARK 3 L33: 0.8934 L12: -0.1834
REMARK 3 L13: 0.2031 L23: -0.1866
REMARK 3 S TENSOR
REMARK 3 S11: -0.1936 S12: 0.0436 S13: 0.0295
REMARK 3 S21: -0.3237 S22: 0.2713 S23: 0.1790
REMARK 3 S31: -0.2235 S32: -0.2308 S33: 0.0375
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN D AND RESSEQ 4:83)
REMARK 3 ORIGIN FOR THE GROUP (A): 43.6643 -74.2674 -4.2265
REMARK 3 T TENSOR
REMARK 3 T11: 0.4053 T22: 0.3667
REMARK 3 T33: 0.2773 T12: -0.1143
REMARK 3 T13: 0.0214 T23: -0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 0.5474 L22: 0.4895
REMARK 3 L33: 0.6310 L12: 0.0662
REMARK 3 L13: -0.2415 L23: 0.3220
REMARK 3 S TENSOR
REMARK 3 S11: -0.1959 S12: 0.0419 S13: -0.2235
REMARK 3 S21: 0.1060 S22: 0.1968 S23: -0.0988
REMARK 3 S31: 0.4276 S32: 0.2226 S33: 0.0193
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 5L95 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-JUN-16.
REMARK 100 THE DEPOSITION ID IS D_1200000357.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-SEP-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979490
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 65695
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 77.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 8.700
REMARK 200 R MERGE (I) : 0.15500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 5IAA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH7.5, 10% PEG 6000 AND 5%
REMARK 280 2-METHYL-2,4-PENTANEDIOL (MPD), VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
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 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 66.49467
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 33.24733
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 33.24733
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 66.49467
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11060 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -60.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 ALA A 111
REMARK 465 ASN A 112
REMARK 465 MET A 113
REMARK 465 ASN A 114
REMARK 465 ARG A 115
REMARK 465 LEU A 116
REMARK 465 LEU A 244
REMARK 465 LYS A 245
REMARK 465 ARG A 246
REMARK 465 GLU A 247
REMARK 465 GLY A 248
REMARK 465 VAL A 249
REMARK 465 CYS A 250
REMARK 465 ALA A 251
REMARK 465 ALA A 252
REMARK 465 LYS A 324
REMARK 465 GLN A 325
REMARK 465 GLU A 326
REMARK 465 VAL A 327
REMARK 465 ILE A 328
REMARK 465 GLN A 329
REMARK 465 GLU A 330
REMARK 465 GLU A 331
REMARK 465 GLU A 332
REMARK 465 LYS B 107
REMARK 465 VAL B 108
REMARK 465 GLU B 109
REMARK 465 LEU B 110
REMARK 465 ALA B 111
REMARK 465 ASN B 112
REMARK 465 MET B 113
REMARK 465 ASN B 114
REMARK 465 ARG B 115
REMARK 465 LEU B 116
REMARK 465 PHE B 117
REMARK 465 PHE B 118
REMARK 465 GLN B 119
REMARK 465 PRO B 120
REMARK 465 HIS B 121
REMARK 465 GLN B 122
REMARK 465 ALA B 123
REMARK 465 THR B 243
REMARK 465 LEU B 244
REMARK 465 LYS B 245
REMARK 465 ARG B 246
REMARK 465 GLU B 247
REMARK 465 GLY B 248
REMARK 465 VAL B 249
REMARK 465 CYS B 250
REMARK 465 ALA B 251
REMARK 465 ALA B 252
REMARK 465 PRO B 323
REMARK 465 LYS B 324
REMARK 465 GLN B 325
REMARK 465 GLU B 326
REMARK 465 VAL B 327
REMARK 465 ILE B 328
REMARK 465 GLN B 329
REMARK 465 GLU B 330
REMARK 465 GLU B 331
REMARK 465 GLU B 332
REMARK 465 GLU B 333
REMARK 465 ILE B 334
REMARK 465 ILE B 335
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 OE1 GLU A 209 O HOH A 501 2.08
REMARK 500 NE2 HIS B 336 OE1 GLU C 39 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU B 340 CD GLU B 340 OE1 -0.126
REMARK 500 GLU B 340 CD GLU B 340 OE2 -0.100
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 GLU A 69 1.42 -68.60
REMARK 500 VAL A 81 55.22 -116.21
REMARK 500 GLU A 241 80.14 -57.07
REMARK 500 LEU A 322 -179.11 -68.22
REMARK 500 GLU A 337 84.36 -54.95
REMARK 500 ASP A 338 159.51 87.51
REMARK 500 ASN A 339 82.68 -172.02
REMARK 500 VAL B 81 52.26 -115.37
REMARK 500 GLU B 241 2.94 -58.69
REMARK 500 ASN B 339 89.36 -167.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LEU A 322 PRO A 323 -145.42
REMARK 500 ALA B 321 LEU B 322 141.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 226 SG
REMARK 620 2 CYS A 229 SG 113.7
REMARK 620 3 CYS A 303 SG 104.7 115.8
REMARK 620 4 CYS A 308 SG 104.7 103.0 114.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 226 SG
REMARK 620 2 CYS B 229 SG 114.1
REMARK 620 3 CYS B 303 SG 107.4 110.3
REMARK 620 4 CYS B 308 SG 105.1 103.2 116.9
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 AMP A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 401
DBREF 5L95 A 68 346 UNP Q9GZZ9 UBA5_HUMAN 68 346
DBREF 5L95 B 68 346 UNP Q9GZZ9 UBA5_HUMAN 68 346
DBREF 5L95 C 4 83 UNP P61960 UFM1_HUMAN 4 83
DBREF 5L95 D 4 83 UNP P61960 UFM1_HUMAN 4 83
SEQRES 1 A 279 TYR GLU LYS ILE ARG THR PHE ALA VAL ALA ILE VAL GLY
SEQRES 2 A 279 VAL GLY GLY VAL GLY SER VAL THR ALA GLU MET LEU THR
SEQRES 3 A 279 ARG CYS GLY ILE GLY LYS LEU LEU LEU PHE ASP TYR ASP
SEQRES 4 A 279 LYS VAL GLU LEU ALA ASN MET ASN ARG LEU PHE PHE GLN
SEQRES 5 A 279 PRO HIS GLN ALA GLY LEU SER LYS VAL GLN ALA ALA GLU
SEQRES 6 A 279 HIS THR LEU ARG ASN ILE ASN PRO ASP VAL LEU PHE GLU
SEQRES 7 A 279 VAL HIS ASN TYR ASN ILE THR THR VAL GLU ASN PHE GLN
SEQRES 8 A 279 HIS PHE MET ASP ARG ILE SER ASN GLY GLY LEU GLU GLU
SEQRES 9 A 279 GLY LYS PRO VAL ASP LEU VAL LEU SER CYS VAL ASP ASN
SEQRES 10 A 279 PHE GLU ALA ARG MET THR ILE ASN THR ALA CYS ASN GLU
SEQRES 11 A 279 LEU GLY GLN THR TRP MET GLU SER GLY VAL SER GLU ASN
SEQRES 12 A 279 ALA VAL SER GLY HIS ILE GLN LEU ILE ILE PRO GLY GLU
SEQRES 13 A 279 SER ALA CYS PHE ALA CYS ALA PRO PRO LEU VAL VAL ALA
SEQRES 14 A 279 ALA ASN ILE ASP GLU LYS THR LEU LYS ARG GLU GLY VAL
SEQRES 15 A 279 CYS ALA ALA SER LEU PRO THR THR MET GLY VAL VAL ALA
SEQRES 16 A 279 GLY ILE LEU VAL GLN ASN VAL LEU LYS PHE LEU LEU ASN
SEQRES 17 A 279 PHE GLY THR VAL SER PHE TYR LEU GLY TYR ASN ALA MET
SEQRES 18 A 279 GLN ASP PHE PHE PRO THR MET SER MET LYS PRO ASN PRO
SEQRES 19 A 279 GLN CYS ASP ASP ARG ASN CYS ARG LYS GLN GLN GLU GLU
SEQRES 20 A 279 TYR LYS LYS LYS VAL ALA ALA LEU PRO LYS GLN GLU VAL
SEQRES 21 A 279 ILE GLN GLU GLU GLU GLU ILE ILE HIS GLU ASP ASN GLU
SEQRES 22 A 279 TRP GLY ILE GLU LEU VAL
SEQRES 1 B 279 TYR GLU LYS ILE ARG THR PHE ALA VAL ALA ILE VAL GLY
SEQRES 2 B 279 VAL GLY GLY VAL GLY SER VAL THR ALA GLU MET LEU THR
SEQRES 3 B 279 ARG CYS GLY ILE GLY LYS LEU LEU LEU PHE ASP TYR ASP
SEQRES 4 B 279 LYS VAL GLU LEU ALA ASN MET ASN ARG LEU PHE PHE GLN
SEQRES 5 B 279 PRO HIS GLN ALA GLY LEU SER LYS VAL GLN ALA ALA GLU
SEQRES 6 B 279 HIS THR LEU ARG ASN ILE ASN PRO ASP VAL LEU PHE GLU
SEQRES 7 B 279 VAL HIS ASN TYR ASN ILE THR THR VAL GLU ASN PHE GLN
SEQRES 8 B 279 HIS PHE MET ASP ARG ILE SER ASN GLY GLY LEU GLU GLU
SEQRES 9 B 279 GLY LYS PRO VAL ASP LEU VAL LEU SER CYS VAL ASP ASN
SEQRES 10 B 279 PHE GLU ALA ARG MET THR ILE ASN THR ALA CYS ASN GLU
SEQRES 11 B 279 LEU GLY GLN THR TRP MET GLU SER GLY VAL SER GLU ASN
SEQRES 12 B 279 ALA VAL SER GLY HIS ILE GLN LEU ILE ILE PRO GLY GLU
SEQRES 13 B 279 SER ALA CYS PHE ALA CYS ALA PRO PRO LEU VAL VAL ALA
SEQRES 14 B 279 ALA ASN ILE ASP GLU LYS THR LEU LYS ARG GLU GLY VAL
SEQRES 15 B 279 CYS ALA ALA SER LEU PRO THR THR MET GLY VAL VAL ALA
SEQRES 16 B 279 GLY ILE LEU VAL GLN ASN VAL LEU LYS PHE LEU LEU ASN
SEQRES 17 B 279 PHE GLY THR VAL SER PHE TYR LEU GLY TYR ASN ALA MET
SEQRES 18 B 279 GLN ASP PHE PHE PRO THR MET SER MET LYS PRO ASN PRO
SEQRES 19 B 279 GLN CYS ASP ASP ARG ASN CYS ARG LYS GLN GLN GLU GLU
SEQRES 20 B 279 TYR LYS LYS LYS VAL ALA ALA LEU PRO LYS GLN GLU VAL
SEQRES 21 B 279 ILE GLN GLU GLU GLU GLU ILE ILE HIS GLU ASP ASN GLU
SEQRES 22 B 279 TRP GLY ILE GLU LEU VAL
SEQRES 1 C 80 VAL SER PHE LYS ILE THR LEU THR SER ASP PRO ARG LEU
SEQRES 2 C 80 PRO TYR LYS VAL LEU SER VAL PRO GLU SER THR PRO PHE
SEQRES 3 C 80 THR ALA VAL LEU LYS PHE ALA ALA GLU GLU PHE LYS VAL
SEQRES 4 C 80 PRO ALA ALA THR SER ALA ILE ILE THR ASN ASP GLY ILE
SEQRES 5 C 80 GLY ILE ASN PRO ALA GLN THR ALA GLY ASN VAL PHE LEU
SEQRES 6 C 80 LYS HIS GLY SER GLU LEU ARG ILE ILE PRO ARG ASP ARG
SEQRES 7 C 80 VAL GLY
SEQRES 1 D 80 VAL SER PHE LYS ILE THR LEU THR SER ASP PRO ARG LEU
SEQRES 2 D 80 PRO TYR LYS VAL LEU SER VAL PRO GLU SER THR PRO PHE
SEQRES 3 D 80 THR ALA VAL LEU LYS PHE ALA ALA GLU GLU PHE LYS VAL
SEQRES 4 D 80 PRO ALA ALA THR SER ALA ILE ILE THR ASN ASP GLY ILE
SEQRES 5 D 80 GLY ILE ASN PRO ALA GLN THR ALA GLY ASN VAL PHE LEU
SEQRES 6 D 80 LYS HIS GLY SER GLU LEU ARG ILE ILE PRO ARG ASP ARG
SEQRES 7 D 80 VAL GLY
HET AMP A 401 23
HET ZN A 402 1
HET ZN B 401 1
HETNAM AMP ADENOSINE MONOPHOSPHATE
HETNAM ZN ZINC ION
FORMUL 5 AMP C10 H14 N5 O7 P
FORMUL 6 ZN 2(ZN 2+)
FORMUL 8 HOH *193(H2 O)
HELIX 1 AA1 TYR A 68 THR A 73 5 6
HELIX 2 AA2 GLY A 82 GLY A 96 1 15
HELIX 3 AA3 GLN A 119 ALA A 123 5 5
HELIX 4 AA4 SER A 126 ASN A 139 1 14
HELIX 5 AA5 THR A 153 GLY A 167 1 15
HELIX 6 AA6 ASN A 184 GLY A 199 1 16
HELIX 7 AA7 PRO A 232 ALA A 237 1 6
HELIX 8 AA8 LEU A 254 ASN A 275 1 22
HELIX 9 AA9 ASP A 305 ALA A 321 1 17
HELIX 10 AB1 TYR B 68 THR B 73 5 6
HELIX 11 AB2 GLY B 82 GLY B 96 1 15
HELIX 12 AB3 SER B 126 ASN B 139 1 14
HELIX 13 AB4 THR B 153 GLY B 167 1 15
HELIX 14 AB5 ASN B 184 GLY B 199 1 16
HELIX 15 AB6 PRO B 232 ALA B 237 1 6
HELIX 16 AB7 LEU B 254 ASN B 275 1 22
HELIX 17 AB8 ASP B 305 ALA B 321 1 17
HELIX 18 AB9 PRO C 28 LYS C 41 1 14
HELIX 19 AC1 THR C 62 GLY C 71 1 10
HELIX 20 AC2 PRO D 28 LYS D 41 1 14
HELIX 21 AC3 THR D 62 GLY D 71 1 10
SHEET 1 AA1 7 LEU A 143 HIS A 147 0
SHEET 2 AA1 7 LYS A 99 PHE A 103 1 N LEU A 100 O LEU A 143
SHEET 3 AA1 7 ALA A 75 VAL A 79 1 N ILE A 78 O LEU A 101
SHEET 4 AA1 7 LEU A 177 SER A 180 1 O LEU A 179 N VAL A 79
SHEET 5 AA1 7 TRP A 202 VAL A 207 1 O MET A 203 N SER A 180
SHEET 6 AA1 7 SER A 213 ILE A 219 -1 O ILE A 219 N TRP A 202
SHEET 7 AA1 7 TYR A 282 ASN A 286 -1 O TYR A 285 N GLY A 214
SHEET 1 AA2 6 GLU A 344 LEU A 345 0
SHEET 2 AA2 6 TYR D 18 SER D 22 -1 O SER D 22 N GLU A 344
SHEET 3 AA2 6 SER D 5 LEU D 10 -1 N ILE D 8 O LYS D 19
SHEET 4 AA2 6 GLU D 73 PRO D 78 1 O ILE D 76 N THR D 9
SHEET 5 AA2 6 SER D 47 THR D 51 -1 N ILE D 50 O ARG D 75
SHEET 6 AA2 6 GLY D 56 ILE D 57 -1 O ILE D 57 N ILE D 49
SHEET 1 AA3 8 LEU B 143 ASN B 148 0
SHEET 2 AA3 8 LYS B 99 ASP B 104 1 N LEU B 100 O LEU B 143
SHEET 3 AA3 8 ALA B 75 VAL B 79 1 N ILE B 78 O LEU B 101
SHEET 4 AA3 8 LEU B 177 SER B 180 1 O LEU B 179 N VAL B 79
SHEET 5 AA3 8 TRP B 202 VAL B 207 1 O MET B 203 N SER B 180
SHEET 6 AA3 8 SER B 213 ILE B 219 -1 O ILE B 219 N TRP B 202
SHEET 7 AA3 8 TYR B 282 ASN B 286 -1 O TYR B 285 N GLY B 214
SHEET 8 AA3 8 THR B 294 MET B 295 -1 O MET B 295 N TYR B 282
SHEET 1 AA4 6 GLU B 344 VAL B 346 0
SHEET 2 AA4 6 TYR C 18 SER C 22 -1 O SER C 22 N GLU B 344
SHEET 3 AA4 6 SER C 5 LEU C 10 -1 N ILE C 8 O LYS C 19
SHEET 4 AA4 6 GLU C 73 PRO C 78 1 O ILE C 76 N THR C 9
SHEET 5 AA4 6 SER C 47 THR C 51 -1 N ILE C 50 O ARG C 75
SHEET 6 AA4 6 GLY C 56 ILE C 57 -1 O ILE C 57 N ILE C 49
LINK SG CYS A 226 ZN ZN A 402 1555 1555 2.26
LINK SG CYS A 229 ZN ZN A 402 1555 1555 2.26
LINK SG CYS A 303 ZN ZN A 402 1555 1555 2.27
LINK SG CYS A 308 ZN ZN A 402 1555 1555 2.33
LINK SG CYS B 226 ZN ZN B 401 1555 1555 2.35
LINK SG CYS B 229 ZN ZN B 401 1555 1555 2.32
LINK SG CYS B 303 ZN ZN B 401 1555 1555 2.31
LINK SG CYS B 308 ZN ZN B 401 1555 1555 2.37
SITE 1 AC1 21 GLY A 80 GLY A 82 GLY A 83 ASP A 104
SITE 2 AC1 21 TYR A 105 ASP A 106 LYS A 127 TYR A 149
SITE 3 AC1 21 ASN A 150 ILE A 151 THR A 152 CYS A 181
SITE 4 AC1 21 VAL A 182 ASP A 183 ASN A 184 ALA A 187
SITE 5 AC1 21 HOH A 529 HOH A 534 HOH A 566 VAL C 82
SITE 6 AC1 21 GLY C 83
SITE 1 AC2 4 CYS A 226 CYS A 229 CYS A 303 CYS A 308
SITE 1 AC3 4 CYS B 226 CYS B 229 CYS B 303 CYS B 308
CRYST1 139.875 139.875 99.742 90.00 90.00 120.00 P 32 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 0.007149 0.004128 0.000000 0.00000
SCALE2 0.000000 0.008255 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010026 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
