HEADER TRANSCRIPTION 26-OCT-15 5EG0
TITLE HOXB13-MEIS1 HETERODIMER BOUND TO DNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HOMEOBOX PROTEIN MEIS2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 284-338;
COMPND 5 SYNONYM: MEIS1-RELATED PROTEIN 1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: DNA (5'-
COMPND 9 D(P*GP*TP*TP*GP*AP*CP*AP*GP*TP*TP*TP*TP*AP*CP*GP*AP*GP*G)-3');
COMPND 10 CHAIN: D;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: DNA (5'-
COMPND 14 D(*CP*CP*TP*CP*GP*TP*AP*AP*AP*AP*CP*TP*GP*TP*CP*AP*AP*C)-3');
COMPND 15 CHAIN: E;
COMPND 16 ENGINEERED: YES;
COMPND 17 MOL_ID: 4;
COMPND 18 MOLECULE: HOMEOBOX PROTEIN HOX-B13;
COMPND 19 CHAIN: B;
COMPND 20 FRAGMENT: UNP RESIDUES 217-277;
COMPND 21 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: MEIS2, MRG1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: ROSETTA;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PETG20A;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 14 ORGANISM_TAXID: 32630;
SOURCE 15 MOL_ID: 3;
SOURCE 16 SYNTHETIC: YES;
SOURCE 17 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 18 ORGANISM_TAXID: 32630;
SOURCE 19 MOL_ID: 4;
SOURCE 20 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 21 ORGANISM_COMMON: HUMAN;
SOURCE 22 ORGANISM_TAXID: 9606;
SOURCE 23 GENE: HOXB13;
SOURCE 24 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 25 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 26 EXPRESSION_SYSTEM_VARIANT: ROSETTA;
SOURCE 27 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 28 EXPRESSION_SYSTEM_PLASMID: PETG20A
KEYWDS TRANSCRIPTION FACTOR, HETERODIMER, COMPLEX, BOUND TO DNA,
KEYWDS 2 TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR E.MORGUNOVA,Y.YIN,A.JOLMA,A.POPOV,J.TAIPALE
REVDAT 1 09-NOV-16 5EG0 0
JRNL AUTH E.MORGUNOVA,Y.YIN,A.JOLMA,A.POPOV,J.TAIPALE
JRNL TITL MOLECULAR BASIS OF RECOGNITION OF TWO DISTINCT DNA SEQUENCES
JRNL TITL 2 BY A SINGLE TRANSCRIPTION FACTOR
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 3.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.95
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 9326
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.288
REMARK 3 R VALUE (WORKING SET) : 0.286
REMARK 3 FREE R VALUE : 0.322
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 485
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 19.9462 - 4.4606 0.99 2992 155 0.2119 0.2660
REMARK 3 2 4.4606 - 3.5470 0.99 2925 180 0.3341 0.3583
REMARK 3 3 3.5470 - 3.1005 0.97 2924 150 0.3906 0.3882
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) : 0.380
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 37.340
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 : 0.005 1813
REMARK 3 ANGLE : 0.827 2593
REMARK 3 CHIRALITY : 0.036 288
REMARK 3 PLANARITY : 0.004 203
REMARK 3 DIHEDRAL : 26.294 746
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 279 THROUGH 334 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.0795 -12.1021 -20.6674
REMARK 3 T TENSOR
REMARK 3 T11: 0.3858 T22: 0.5089
REMARK 3 T33: 0.3786 T12: -0.0544
REMARK 3 T13: -0.0267 T23: 0.1471
REMARK 3 L TENSOR
REMARK 3 L11: 0.0763 L22: 0.0638
REMARK 3 L33: 0.0238 L12: 0.0049
REMARK 3 L13: -0.0068 L23: 0.0109
REMARK 3 S TENSOR
REMARK 3 S11: -0.0770 S12: 0.1860 S13: 0.0979
REMARK 3 S21: -0.0347 S22: 0.1778 S23: 0.1987
REMARK 3 S31: 0.0569 S32: -0.1805 S33: 0.0319
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 20 THROUGH 37)
REMARK 3 ORIGIN FOR THE GROUP (A): 7.6850 -0.9248 -33.0833
REMARK 3 T TENSOR
REMARK 3 T11: 0.6637 T22: 1.2857
REMARK 3 T33: 0.3175 T12: 0.2181
REMARK 3 T13: 0.0106 T23: -0.0201
REMARK 3 L TENSOR
REMARK 3 L11: 0.2160 L22: 1.0897
REMARK 3 L33: 0.3355 L12: 0.4887
REMARK 3 L13: -0.1665 L23: -0.4175
REMARK 3 S TENSOR
REMARK 3 S11: -0.2497 S12: 0.1379 S13: 0.3671
REMARK 3 S21: -0.0643 S22: 0.6856 S23: -0.0754
REMARK 3 S31: -0.0145 S32: -0.2310 S33: 0.2253
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 1 THROUGH 18)
REMARK 3 ORIGIN FOR THE GROUP (A): 7.2367 1.4291 -32.5406
REMARK 3 T TENSOR
REMARK 3 T11: 1.1000 T22: 0.8026
REMARK 3 T33: 0.2824 T12: -0.0763
REMARK 3 T13: 0.0322 T23: 0.1670
REMARK 3 L TENSOR
REMARK 3 L11: 0.1429 L22: 0.0787
REMARK 3 L33: 0.0806 L12: -0.1180
REMARK 3 L13: 0.0169 L23: -0.0176
REMARK 3 S TENSOR
REMARK 3 S11: -0.0880 S12: 0.0615 S13: 0.2450
REMARK 3 S21: -0.5436 S22: 0.5549 S23: 0.0087
REMARK 3 S31: -0.5145 S32: -0.9147 S33: 0.0977
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 217 THROUGH 277 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.2611 -0.8486 -46.5463
REMARK 3 T TENSOR
REMARK 3 T11: 0.2204 T22: 0.5277
REMARK 3 T33: 0.3567 T12: -0.2602
REMARK 3 T13: 0.0666 T23: -0.1125
REMARK 3 L TENSOR
REMARK 3 L11: 0.2484 L22: 0.1916
REMARK 3 L33: 1.2619 L12: 0.2190
REMARK 3 L13: 0.0746 L23: 0.1256
REMARK 3 S TENSOR
REMARK 3 S11: -0.0953 S12: 0.0858 S13: 0.0938
REMARK 3 S21: -0.1269 S22: 0.3442 S23: -0.2372
REMARK 3 S31: 0.3513 S32: 0.1313 S33: 0.2357
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 5EG0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-OCT-15.
REMARK 100 THE DEPOSITION ID IS D_1000214842.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-NOV-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.972390
REMARK 200 MONOCHROMATOR : SI(111) AND SI (311)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 6006
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.970
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 4.900
REMARK 200 R MERGE (I) : 0.28000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 3.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.97
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.13
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.2
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 2.77000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.400
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: 4XRM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 5000, POTASSIUM CHLORIDE,
REMARK 280 MAGNESIUM CHLORIDE, PENTANOL, PH 8, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 293K
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 20.86300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 57.57600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.16600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 57.57600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.86300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 28.16600
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D, E, 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 ALA A 278
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 TYR B 223 CG CD1 CD2 CE1 CE2 CZ OH
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 C2 DA E 7 NH2 ARG B 220 1.85
REMARK 500 NH1 ARG B 220 O HOH B 301 1.97
REMARK 500 O THR B 261 O HOH B 302 2.03
REMARK 500 O4' DC E 2 O HOH E 101 2.17
REMARK 500 O2 DC E 1 O HOH E 101 2.18
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 DT D 21 O4' - C1' - N1 ANGL. DEV. = 1.8 DEGREES
REMARK 500 DT D 22 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DG D 36 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DC E 1 O4' - C1' - N1 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DT E 3 O4' - C1' - N1 ANGL. DEV. = 1.8 DEGREES
REMARK 500 DA E 10 O4' - C1' - N9 ANGL. DEV. = 2.1 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 281 -60.83 -103.16
REMARK 500 THR A 312 -58.09 -144.81
REMARK 500 ILE A 330 -61.15 -129.12
REMARK 500 GLU B 232 -18.06 77.09
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5EG0 A 280 334 UNP O14770 MEIS2_HUMAN 284 338
DBREF 5EG0 D 20 37 PDB 5EG0 5EG0 20 37
DBREF 5EG0 E 1 18 PDB 5EG0 5EG0 1 18
DBREF 5EG0 B 217 277 UNP Q92826 HXB13_HUMAN 217 277
SEQADV 5EG0 ALA A 278 UNP O14770 EXPRESSION TAG
SEQADV 5EG0 ALA A 279 UNP O14770 EXPRESSION TAG
SEQRES 1 A 57 ALA ALA PRO LYS VAL ALA THR ASN ILE MET ARG ALA TRP
SEQRES 2 A 57 LEU PHE GLN HIS LEU THR HIS PRO TYR PRO SER GLU GLU
SEQRES 3 A 57 GLN LYS LYS GLN LEU ALA GLN ASP THR GLY LEU THR ILE
SEQRES 4 A 57 LEU GLN VAL ASN ASN TRP PHE ILE ASN ALA ARG ARG ARG
SEQRES 5 A 57 ILE VAL GLN PRO MET
SEQRES 1 D 18 DG DT DT DG DA DC DA DG DT DT DT DT DA
SEQRES 2 D 18 DC DG DA DG DG
SEQRES 1 E 18 DC DC DT DC DG DT DA DA DA DA DC DT DG
SEQRES 2 E 18 DT DC DA DA DC
SEQRES 1 B 61 ARG LYS LYS ARG ILE PRO TYR SER LYS GLY GLN LEU ARG
SEQRES 2 B 61 GLU LEU GLU ARG GLU TYR ALA ALA ASN LYS PHE ILE THR
SEQRES 3 B 61 LYS ASP LYS ARG ARG LYS ILE SER ALA ALA THR SER LEU
SEQRES 4 B 61 SER GLU ARG GLN ILE THR ILE TRP PHE GLN ASN ARG ARG
SEQRES 5 B 61 VAL LYS GLU LYS LYS VAL LEU ALA LYS
FORMUL 5 HOH *29(H2 O)
HELIX 1 AA1 LYS A 281 HIS A 294 1 14
HELIX 2 AA2 SER A 301 ASP A 311 1 11
HELIX 3 AA3 THR A 315 ILE A 330 1 16
HELIX 4 AA4 GLY B 226 LEU B 231 1 6
HELIX 5 AA5 ARG B 233 ASN B 238 1 6
HELIX 6 AA6 ASP B 244 SER B 254 1 11
HELIX 7 AA7 SER B 256 VAL B 274 1 19
CISPEP 1 ALA A 279 PRO A 280 0 -4.81
CISPEP 2 ALA B 276 LYS B 277 0 -17.23
CRYST1 41.726 56.332 115.152 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 0.023966 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017752 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008684 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
