HEADER LIGASE 28-JAN-14 4ONM
TITLE CRYSTAL STRUCTURE OF HUMAN MMS2/UBC13 - NSC697923
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN-CONJUGATING ENZYME E2 VARIANT 2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DDVIT 1, ENTEROCYTE DIFFERENTIATION-ASSOCIATED FACTOR 1,
COMPND 5 EDAF-1, ENTEROCYTE DIFFERENTIATION-PROMOTING FACTOR 1, EDPF-1, MMS2
COMPND 6 HOMOLOG, VITAMIN D3-INDUCIBLE PROTEIN;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: UBIQUITIN-CONJUGATING ENZYME E2 N;
COMPND 10 CHAIN: B;
COMPND 11 SYNONYM: BENDLESS-LIKE UBIQUITIN-CONJUGATING ENZYME, UBC13, UBCH13,
COMPND 12 UBIQUITIN CARRIER PROTEIN N, UBIQUITIN-PROTEIN LIGASE N;
COMPND 13 EC: 6.3.2.19;
COMPND 14 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: MMS2, UBE2V2, UEV2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX6P1;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: BLU, UBE2N;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PGEX6P1
KEYWDS E2 UBIQUITIN CONJUGATING ENZYME, E1, E3, UBIQUITIN, COVALENT ADDUCT,
KEYWDS 2 LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.D.HODGE,R.A.EDWARDS,J.N.M.GLOVER
REVDAT 3 22-NOV-17 4ONM 1 REMARK
REVDAT 2 05-AUG-15 4ONM 1 JRNL
REVDAT 1 06-MAY-15 4ONM 0
JRNL AUTH C.D.HODGE,R.A.EDWARDS,C.J.MARKIN,D.MCDONALD,M.PULVINO,
JRNL AUTH 2 M.S.HUEN,J.ZHAO,L.SPYRACOPOULOS,M.J.HENDZEL,J.N.GLOVER
JRNL TITL COVALENT INHIBITION OF UBC13 AFFECTS UBIQUITIN SIGNALING AND
JRNL TITL 2 REVEALS ACTIVE SITE ELEMENTS IMPORTANT FOR TARGETING.
JRNL REF ACS CHEM.BIOL. V. 10 1718 2015
JRNL REFN ISSN 1554-8929
JRNL PMID 25909880
JRNL DOI 10.1021/ACSCHEMBIO.5B00222
REMARK 2
REMARK 2 RESOLUTION. 1.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.3_1479
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) : 1.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.27
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 67463
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.161
REMARK 3 R VALUE (WORKING SET) : 0.159
REMARK 3 FREE R VALUE : 0.192
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.310
REMARK 3 FREE R VALUE TEST SET COUNT : 3585
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 24.2710 - 3.9928 1.00 2681 133 0.1682 0.1513
REMARK 3 2 3.9928 - 3.1715 1.00 2560 130 0.1671 0.2119
REMARK 3 3 3.1715 - 2.7712 1.00 2525 137 0.1827 0.2225
REMARK 3 4 2.7712 - 2.5181 1.00 2500 154 0.1803 0.2174
REMARK 3 5 2.5181 - 2.3378 1.00 2478 142 0.1643 0.2093
REMARK 3 6 2.3378 - 2.2001 1.00 2475 158 0.1530 0.1828
REMARK 3 7 2.2001 - 2.0899 1.00 2491 125 0.1515 0.2004
REMARK 3 8 2.0899 - 1.9990 1.00 2475 133 0.1372 0.1687
REMARK 3 9 1.9990 - 1.9221 1.00 2463 137 0.1403 0.1900
REMARK 3 10 1.9221 - 1.8558 1.00 2451 124 0.1307 0.1765
REMARK 3 11 1.8558 - 1.7978 1.00 2472 151 0.1313 0.1881
REMARK 3 12 1.7978 - 1.7464 1.00 2463 133 0.1260 0.1973
REMARK 3 13 1.7464 - 1.7004 1.00 2412 150 0.1241 0.1485
REMARK 3 14 1.7004 - 1.6590 1.00 2442 151 0.1233 0.1758
REMARK 3 15 1.6590 - 1.6213 0.99 2441 143 0.1218 0.1718
REMARK 3 16 1.6213 - 1.5868 0.99 2425 139 0.1261 0.1749
REMARK 3 17 1.5868 - 1.5550 0.99 2445 126 0.1318 0.2060
REMARK 3 18 1.5550 - 1.5257 0.99 2413 144 0.1361 0.1788
REMARK 3 19 1.5257 - 1.4984 0.99 2436 114 0.1452 0.1843
REMARK 3 20 1.4984 - 1.4731 0.99 2398 151 0.1496 0.1943
REMARK 3 21 1.4731 - 1.4493 0.99 2445 120 0.1524 0.1945
REMARK 3 22 1.4493 - 1.4270 0.99 2418 149 0.1655 0.2297
REMARK 3 23 1.4270 - 1.4060 0.99 2406 128 0.1734 0.2116
REMARK 3 24 1.4060 - 1.3862 0.99 2402 135 0.1945 0.2514
REMARK 3 25 1.3862 - 1.3675 0.99 2441 134 0.2164 0.2645
REMARK 3 26 1.3675 - 1.3500 0.97 2320 144 0.2441 0.2864
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) : 0.140
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.300
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.79
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.06
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 : 0.013 2475
REMARK 3 ANGLE : 1.440 3377
REMARK 3 CHIRALITY : 0.095 359
REMARK 3 PLANARITY : 0.008 450
REMARK 3 DIHEDRAL : 13.111 973
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4ONM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-FEB-14.
REMARK 100 THE DEPOSITION ID IS D_1000084719.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-AUG-12
REMARK 200 TEMPERATURE (KELVIN) : 105
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CLSI
REMARK 200 BEAMLINE : 08B1-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.03321
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX300HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 67525
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.350
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 (%) : 99.5
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : 0.03900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.37
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.67900
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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.27
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM CITRATE, 15% PEG 8000,
REMARK 280 PH 7.4, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 22.26900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.66250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.42750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 45.66250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.26900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.42750
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1720 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 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 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 -7
REMARK 465 PRO A -6
REMARK 465 LEU A -5
REMARK 465 GLY A -4
REMARK 465 SER A -3
REMARK 465 PRO A -2
REMARK 465 GLU A -1
REMARK 465 PHE A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 VAL A 3
REMARK 465 SER A 4
REMARK 465 THR A 5
REMARK 465 GLY B -7
REMARK 465 PRO B -6
REMARK 465 LEU B -5
REMARK 465 GLY B -4
REMARK 465 SER B -3
REMARK 465 PRO B -2
REMARK 465 GLU B -1
REMARK 465 PHE B 0
REMARK 465 MET B 1
REMARK 465 ASN B 151
REMARK 465 ILE B 152
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 B 92 -108.53 -132.51
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 THE COMPOUND N2F LOSES THE 4-METHYLBENZENE-SULFINIC ACID GROUP ON
REMARK 600 INERACTING WITH UBC13 AND THE REMAINING PART OF N2F FORMS A
REMARK 600 COVALENT BOND WITH THE SG ATOM OF CYS B87
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE N2F B 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4ONL RELATED DB: PDB
REMARK 900 RELATED ID: 4ONN RELATED DB: PDB
DBREF 4ONM A 1 145 UNP Q15819 UB2V2_HUMAN 1 145
DBREF 4ONM B 1 152 UNP P61088 UBE2N_HUMAN 1 152
SEQADV 4ONM GLY A -7 UNP Q15819 EXPRESSION TAG
SEQADV 4ONM PRO A -6 UNP Q15819 EXPRESSION TAG
SEQADV 4ONM LEU A -5 UNP Q15819 EXPRESSION TAG
SEQADV 4ONM GLY A -4 UNP Q15819 EXPRESSION TAG
SEQADV 4ONM SER A -3 UNP Q15819 EXPRESSION TAG
SEQADV 4ONM PRO A -2 UNP Q15819 EXPRESSION TAG
SEQADV 4ONM GLU A -1 UNP Q15819 EXPRESSION TAG
SEQADV 4ONM PHE A 0 UNP Q15819 EXPRESSION TAG
SEQADV 4ONM GLY B -7 UNP P61088 EXPRESSION TAG
SEQADV 4ONM PRO B -6 UNP P61088 EXPRESSION TAG
SEQADV 4ONM LEU B -5 UNP P61088 EXPRESSION TAG
SEQADV 4ONM GLY B -4 UNP P61088 EXPRESSION TAG
SEQADV 4ONM SER B -3 UNP P61088 EXPRESSION TAG
SEQADV 4ONM PRO B -2 UNP P61088 EXPRESSION TAG
SEQADV 4ONM GLU B -1 UNP P61088 EXPRESSION TAG
SEQADV 4ONM PHE B 0 UNP P61088 EXPRESSION TAG
SEQRES 1 A 153 GLY PRO LEU GLY SER PRO GLU PHE MET ALA VAL SER THR
SEQRES 2 A 153 GLY VAL LYS VAL PRO ARG ASN PHE ARG LEU LEU GLU GLU
SEQRES 3 A 153 LEU GLU GLU GLY GLN LYS GLY VAL GLY ASP GLY THR VAL
SEQRES 4 A 153 SER TRP GLY LEU GLU ASP ASP GLU ASP MET THR LEU THR
SEQRES 5 A 153 ARG TRP THR GLY MET ILE ILE GLY PRO PRO ARG THR ASN
SEQRES 6 A 153 TYR GLU ASN ARG ILE TYR SER LEU LYS VAL GLU CYS GLY
SEQRES 7 A 153 PRO LYS TYR PRO GLU ALA PRO PRO SER VAL ARG PHE VAL
SEQRES 8 A 153 THR LYS ILE ASN MET ASN GLY ILE ASN ASN SER SER GLY
SEQRES 9 A 153 MET VAL ASP ALA ARG SER ILE PRO VAL LEU ALA LYS TRP
SEQRES 10 A 153 GLN ASN SER TYR SER ILE LYS VAL VAL LEU GLN GLU LEU
SEQRES 11 A 153 ARG ARG LEU MET MET SER LYS GLU ASN MET LYS LEU PRO
SEQRES 12 A 153 GLN PRO PRO GLU GLY GLN THR TYR ASN ASN
SEQRES 1 B 160 GLY PRO LEU GLY SER PRO GLU PHE MET ALA GLY LEU PRO
SEQRES 2 B 160 ARG ARG ILE ILE LYS GLU THR GLN ARG LEU LEU ALA GLU
SEQRES 3 B 160 PRO VAL PRO GLY ILE LYS ALA GLU PRO ASP GLU SER ASN
SEQRES 4 B 160 ALA ARG TYR PHE HIS VAL VAL ILE ALA GLY PRO GLN ASP
SEQRES 5 B 160 SER PRO PHE GLU GLY GLY THR PHE LYS LEU GLU LEU PHE
SEQRES 6 B 160 LEU PRO GLU GLU TYR PRO MET ALA ALA PRO LYS VAL ARG
SEQRES 7 B 160 PHE MET THR LYS ILE TYR HIS PRO ASN VAL ASP LYS LEU
SEQRES 8 B 160 GLY ARG ILE CYS LEU ASP ILE LEU LYS ASP LYS TRP SER
SEQRES 9 B 160 PRO ALA LEU GLN ILE ARG THR VAL LEU LEU SER ILE GLN
SEQRES 10 B 160 ALA LEU LEU SER ALA PRO ASN PRO ASP ASP PRO LEU ALA
SEQRES 11 B 160 ASN ASP VAL ALA GLU GLN TRP LYS THR ASN GLU ALA GLN
SEQRES 12 B 160 ALA ILE GLU THR ALA ARG ALA TRP THR ARG LEU TYR ALA
SEQRES 13 B 160 MET ASN ASN ILE
HET GOL A 201 6
HET N2F B 201 10
HETNAM GOL GLYCEROL
HETNAM N2F 2-[(4-METHYLPHENYL)SULFONYL]-5-NITROFURAN
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN N2F NSC697923
FORMUL 3 GOL C3 H8 O3
FORMUL 4 N2F C11 H9 N O5 S
FORMUL 5 HOH *212(H2 O)
HELIX 1 1 PRO A 10 GLY A 25 1 16
HELIX 2 2 ASP A 99 SER A 102 5 4
HELIX 3 3 ILE A 103 LYS A 108 1 6
HELIX 4 4 SER A 114 MET A 127 1 14
HELIX 5 5 PRO B 5 GLU B 18 1 14
HELIX 6 6 LEU B 88 LYS B 92 5 5
HELIX 7 7 GLN B 100 ALA B 114 1 15
HELIX 8 8 VAL B 125 ASN B 132 1 8
HELIX 9 9 ASN B 132 ALA B 148 1 17
SHEET 1 A 4 VAL A 31 LEU A 35 0
SHEET 2 A 4 ARG A 45 ILE A 51 -1 O THR A 47 N GLY A 34
SHEET 3 A 4 ILE A 62 GLU A 68 -1 O TYR A 63 N ILE A 50
SHEET 4 A 4 SER A 79 PHE A 82 -1 O SER A 79 N GLU A 68
SHEET 1 B 4 ILE B 23 PRO B 27 0
SHEET 2 B 4 TYR B 34 ALA B 40 -1 O HIS B 36 N GLU B 26
SHEET 3 B 4 THR B 51 PHE B 57 -1 O LEU B 56 N PHE B 35
SHEET 4 B 4 LYS B 68 PHE B 71 -1 O ARG B 70 N GLU B 55
LINK SG CYS B 87 C5 N2F B 201 1555 1555 1.75
CISPEP 1 TYR A 73 PRO A 74 0 1.02
CISPEP 2 TYR B 62 PRO B 63 0 6.67
SITE 1 AC1 8 ASN A 60 ILE A 62 GLY A 90 ILE A 91
SITE 2 AC1 8 ASN A 92 ASN A 93 HOH A 379 HOH A 399
SITE 1 AC2 11 PRO B 78 ASN B 79 VAL B 80 ASP B 81
SITE 2 AC2 11 ARG B 85 ILE B 86 CYS B 87 LEU B 121
SITE 3 AC2 11 ALA B 122 ASN B 123 HOH B 305
CRYST1 44.538 74.855 91.325 90.00 90.00 90.00 P 21 21 21 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 0.022453 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013359 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010950 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
