HEADER TRANSFERASE 13-JUL-15 5CIU
TITLE STRUCTURAL BASIS OF THE RECOGNITION OF H3K36ME3 BY DNMT3B PWWP DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA (CYTOSINE-5)-METHYLTRANSFERASE 3B;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: DNMT3B,DNA METHYLTRANSFERASE HSAIIIB,M.HSAIIIB;
COMPND 5 EC: 2.1.1.37;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: HISTONE H3.2;
COMPND 9 CHAIN: C, D;
COMPND 10 SYNONYM: HISTONE H3/M,HISTONE H3/O;
COMPND 11 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: DNMT3B;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28-MHL;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606
KEYWDS PROTEIN-PEPTIDE COMPLEX, DNMT3B, PWWP DOMAIN, HISTONE BINDING,
KEYWDS 2 H3K36ME3, METHYLTRANSFERASE 3 BETA, S-ADENOSYL-L-METHIONINE,
KEYWDS 3 TRANSFERASE, ZINC-FINGER
EXPDTA X-RAY DIFFRACTION
AUTHOR G.RONDELET,T.DAL MASO,L.WILLEMS,J.WOUTERS
REVDAT 4 10-JAN-24 5CIU 1 REMARK
REVDAT 3 12-JUN-19 5CIU 1 AUTHOR REMARK ATOM
REVDAT 2 04-MAY-16 5CIU 1 JRNL
REVDAT 1 30-MAR-16 5CIU 0
JRNL AUTH G.RONDELET,T.DAL MASO,L.WILLEMS,J.WOUTERS
JRNL TITL STRUCTURAL BASIS FOR RECOGNITION OF HISTONE H3K36ME3
JRNL TITL 2 NUCLEOSOME BY HUMAN DE NOVO DNA METHYLTRANSFERASES 3A AND
JRNL TITL 3 3B.
JRNL REF J.STRUCT.BIOL. V. 194 357 2016
JRNL REFN ESSN 1095-8657
JRNL PMID 26993463
JRNL DOI 10.1016/J.JSB.2016.03.013
REMARK 2
REMARK 2 RESOLUTION. 2.24 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 2.24
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.72
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 24436
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.227
REMARK 3 R VALUE (WORKING SET) : 0.224
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1905
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 36.7234 - 5.3935 0.97 1694 148 0.2347 0.2472
REMARK 3 2 5.3935 - 4.2831 1.00 1653 141 0.1836 0.2014
REMARK 3 3 4.2831 - 3.7423 1.00 1632 133 0.1904 0.1851
REMARK 3 4 3.7423 - 3.4004 1.00 1633 136 0.1978 0.2501
REMARK 3 5 3.4004 - 3.1568 1.00 1616 132 0.2253 0.2806
REMARK 3 6 3.1568 - 2.9708 1.00 1606 132 0.2465 0.3166
REMARK 3 7 2.9708 - 2.8220 1.00 1571 135 0.2481 0.3184
REMARK 3 8 2.8220 - 2.6992 1.00 1612 140 0.2564 0.3434
REMARK 3 9 2.6992 - 2.5954 1.00 1596 135 0.2609 0.3185
REMARK 3 10 2.5954 - 2.5058 1.00 1584 134 0.2736 0.3266
REMARK 3 11 2.5058 - 2.4275 1.00 1582 136 0.2885 0.3455
REMARK 3 12 2.4275 - 2.3581 1.00 1580 134 0.2788 0.3145
REMARK 3 13 2.3581 - 2.2960 1.00 1568 133 0.2992 0.3533
REMARK 3 14 2.2960 - 2.2400 1.00 1604 136 0.3168 0.3815
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) : 0.330
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.700
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 49.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.45
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 : 0.009 2162
REMARK 3 ANGLE : 1.204 2898
REMARK 3 CHIRALITY : 0.087 282
REMARK 3 PLANARITY : 0.005 354
REMARK 3 DIHEDRAL : 13.937 774
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 5CIU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-JUL-15.
REMARK 100 THE DEPOSITION ID IS D_1000211709.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-JUN-14
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 : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9801
REMARK 200 MONOCHROMATOR : CRYOGENICALLY COOLED CHANNEL-CUT
REMARK 200 SI[111]
REMARK 200 OPTICS : X-RAY FLUORESCCENCE DETECTOR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24436
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.240
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.4400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.24
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.37
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.63300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.950
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.2
REMARK 200 STARTING MODEL: 3QKJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M SODIUM CITRATE TRIBASIC, PH 6.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
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 105.46667
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 52.73333
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 52.73333
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 105.46667
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 950 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7750 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 910 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 A 416 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 GLU A 206
REMARK 465 ALA A 207
REMARK 465 ASP A 208
REMARK 465 SER A 209
REMARK 465 GLY A 210
REMARK 465 ASP A 211
REMARK 465 GLY A 212
REMARK 465 ASP A 213
REMARK 465 SER A 214
REMARK 465 SER A 215
REMARK 465 PRO A 318
REMARK 465 SER A 319
REMARK 465 SER A 320
REMARK 465 PRO A 321
REMARK 465 GLY A 322
REMARK 465 ASP A 323
REMARK 465 SER A 324
REMARK 465 LEU A 325
REMARK 465 GLU A 326
REMARK 465 ASN A 352
REMARK 465 THR A 353
REMARK 465 GLN A 354
REMARK 465 PRO A 355
REMARK 465 GLU B 206
REMARK 465 ALA B 207
REMARK 465 ASP B 208
REMARK 465 SER B 209
REMARK 465 GLY B 210
REMARK 465 ASP B 211
REMARK 465 GLY B 212
REMARK 465 ASP B 213
REMARK 465 SER B 214
REMARK 465 SER B 215
REMARK 465 ALA B 290
REMARK 465 THR B 291
REMARK 465 THR B 316
REMARK 465 PHE B 317
REMARK 465 PRO B 318
REMARK 465 SER B 319
REMARK 465 SER B 320
REMARK 465 PRO B 321
REMARK 465 GLY B 322
REMARK 465 ASP B 323
REMARK 465 SER B 324
REMARK 465 LEU B 325
REMARK 465 GLU B 326
REMARK 465 ASP B 327
REMARK 465 GLN B 328
REMARK 465 ASN B 352
REMARK 465 THR B 353
REMARK 465 GLN B 354
REMARK 465 PRO B 355
REMARK 465 SER C 28
REMARK 465 ALA C 29
REMARK 465 PRO C 30
REMARK 465 ALA C 31
REMARK 465 HIS C 39
REMARK 465 ARG C 40
REMARK 465 TYR C 41
REMARK 465 ARG C 42
REMARK 465 SER D 28
REMARK 465 ALA D 29
REMARK 465 PRO D 30
REMARK 465 ALA D 31
REMARK 465 HIS D 39
REMARK 465 ARG D 40
REMARK 465 TYR D 41
REMARK 465 ARG D 42
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 234 CG CD CE NZ
REMARK 480 LYS B 234 CB CG CD CE NZ
REMARK 480 LYS B 330 CB CG CD CE NZ
REMARK 480 GLU B 334 CB CG CD OE1 OE2
REMARK 480 LYS B 341 CB CG CD CE NZ
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 NZ LYS A 232 O PHE A 236 2.04
REMARK 500 O PRO A 342 O HOH A 401 2.13
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 PHE A 223 138.10 79.94
REMARK 500 LYS A 251 -98.58 -117.30
REMARK 500 THR A 316 -63.14 -109.18
REMARK 500 TYR B 217 19.15 81.94
REMARK 500 LYS B 251 -95.83 -108.55
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 A 496 DISTANCE = 6.80 ANGSTROMS
REMARK 525 HOH A 497 DISTANCE = 7.83 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 401
DBREF 5CIU A 206 355 UNP Q9UBC3 DNM3B_HUMAN 206 355
DBREF 5CIU B 206 355 UNP Q9UBC3 DNM3B_HUMAN 206 355
DBREF 5CIU C 28 42 PDB 5CIU 5CIU 28 42
DBREF 5CIU D 28 42 PDB 5CIU 5CIU 28 42
SEQRES 1 A 150 GLU ALA ASP SER GLY ASP GLY ASP SER SER GLU TYR GLN
SEQRES 2 A 150 ASP GLY LYS GLU PHE GLY ILE GLY ASP LEU VAL TRP GLY
SEQRES 3 A 150 LYS ILE LYS GLY PHE SER TRP TRP PRO ALA MET VAL VAL
SEQRES 4 A 150 SER TRP LYS ALA THR SER LYS ARG GLN ALA MET SER GLY
SEQRES 5 A 150 MET ARG TRP VAL GLN TRP PHE GLY ASP GLY LYS PHE SER
SEQRES 6 A 150 GLU VAL SER ALA ASP LYS LEU VAL ALA LEU GLY LEU PHE
SEQRES 7 A 150 SER GLN HIS PHE ASN LEU ALA THR PHE ASN LYS LEU VAL
SEQRES 8 A 150 SER TYR ARG LYS ALA MET TYR HIS ALA LEU GLU LYS ALA
SEQRES 9 A 150 ARG VAL ARG ALA GLY LYS THR PHE PRO SER SER PRO GLY
SEQRES 10 A 150 ASP SER LEU GLU ASP GLN LEU LYS PRO MET LEU GLU TRP
SEQRES 11 A 150 ALA HIS GLY GLY PHE LYS PRO THR GLY ILE GLU GLY LEU
SEQRES 12 A 150 LYS PRO ASN ASN THR GLN PRO
SEQRES 1 B 150 GLU ALA ASP SER GLY ASP GLY ASP SER SER GLU TYR GLN
SEQRES 2 B 150 ASP GLY LYS GLU PHE GLY ILE GLY ASP LEU VAL TRP GLY
SEQRES 3 B 150 LYS ILE LYS GLY PHE SER TRP TRP PRO ALA MET VAL VAL
SEQRES 4 B 150 SER TRP LYS ALA THR SER LYS ARG GLN ALA MET SER GLY
SEQRES 5 B 150 MET ARG TRP VAL GLN TRP PHE GLY ASP GLY LYS PHE SER
SEQRES 6 B 150 GLU VAL SER ALA ASP LYS LEU VAL ALA LEU GLY LEU PHE
SEQRES 7 B 150 SER GLN HIS PHE ASN LEU ALA THR PHE ASN LYS LEU VAL
SEQRES 8 B 150 SER TYR ARG LYS ALA MET TYR HIS ALA LEU GLU LYS ALA
SEQRES 9 B 150 ARG VAL ARG ALA GLY LYS THR PHE PRO SER SER PRO GLY
SEQRES 10 B 150 ASP SER LEU GLU ASP GLN LEU LYS PRO MET LEU GLU TRP
SEQRES 11 B 150 ALA HIS GLY GLY PHE LYS PRO THR GLY ILE GLU GLY LEU
SEQRES 12 B 150 LYS PRO ASN ASN THR GLN PRO
SEQRES 1 C 15 SER ALA PRO ALA THR GLY GLY VAL M3L LYS PRO HIS ARG
SEQRES 2 C 15 TYR ARG
SEQRES 1 D 15 SER ALA PRO ALA THR GLY GLY VAL M3L LYS PRO HIS ARG
SEQRES 2 D 15 TYR ARG
MODRES 5CIU M3L C 36 LYS MODIFIED RESIDUE
MODRES 5CIU M3L D 36 LYS MODIFIED RESIDUE
HET M3L C 36 12
HET M3L D 36 12
HET GOL B 401 6
HETNAM M3L N-TRIMETHYLLYSINE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 M3L 2(C9 H21 N2 O2 1+)
FORMUL 5 GOL C3 H8 O3
FORMUL 6 HOH *163(H2 O)
HELIX 1 AA1 SER A 245 THR A 249 5 5
HELIX 2 AA2 ASN A 288 LEU A 295 1 8
HELIX 3 AA3 LEU A 295 GLY A 314 1 20
HELIX 4 AA4 GLN A 328 GLY A 338 1 11
HELIX 5 AA5 GLY A 344 LYS A 349 5 6
HELIX 6 AA6 SER B 245 THR B 249 5 5
HELIX 7 AA7 ASP B 275 LEU B 277 5 3
HELIX 8 AA8 LEU B 282 PHE B 287 1 6
HELIX 9 AA9 LEU B 295 GLY B 314 1 20
HELIX 10 AB1 LYS B 330 GLY B 338 1 9
HELIX 11 AB2 GLY B 344 LEU B 348 5 5
SHEET 1 AA1 5 PHE A 269 SER A 273 0
SHEET 2 AA1 5 MET A 258 TRP A 263 -1 N ARG A 259 O VAL A 272
SHEET 3 AA1 5 TRP A 239 VAL A 244 -1 N MET A 242 O GLN A 262
SHEET 4 AA1 5 LEU A 228 GLY A 231 -1 N VAL A 229 O ALA A 241
SHEET 5 AA1 5 LEU A 277 ALA A 279 -1 O VAL A 278 N TRP A 230
SHEET 1 AA2 5 PHE B 269 SER B 273 0
SHEET 2 AA2 5 MET B 258 TRP B 263 -1 N ARG B 259 O VAL B 272
SHEET 3 AA2 5 TRP B 239 VAL B 244 -1 N MET B 242 O GLN B 262
SHEET 4 AA2 5 LEU B 228 GLY B 231 -1 N VAL B 229 O ALA B 241
SHEET 5 AA2 5 VAL B 278 ALA B 279 -1 O VAL B 278 N TRP B 230
LINK C VAL C 35 N M3L C 36 1555 1555 1.33
LINK C M3L C 36 N LYS C 37 1555 1555 1.33
LINK C VAL D 35 N M3L D 36 1555 1555 1.34
LINK C M3L D 36 N LYS D 37 1555 1555 1.33
CISPEP 1 LYS A 341 PRO A 342 0 9.11
CISPEP 2 ASP B 219 GLY B 220 0 -3.61
CISPEP 3 LYS B 341 PRO B 342 0 5.53
SITE 1 AC1 2 ARG B 252 VAL C 35
CRYST1 73.437 73.437 158.200 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 0.013617 0.007862 0.000000 0.00000
SCALE2 0.000000 0.015724 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006321 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
