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HEADER SIGNALING PROTEIN 16-JUL-07 2QMQ
TITLE CRYSTAL STRUCTURE OF N-MYC DOWNSTREAM REGULATED 2
TITLE 2 (15277975) FROM MUS MUSCULUS AT 1.70 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN NDRG2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 40-313;
COMPND 5 SYNONYM: PROTEIN NDR2;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 GENE: 15277975, NDRG2, KIAA1248, NDR2;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: HK100;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: SPEEDET
KEYWDS 15277975, NDR FAMILY, N-MYC DOWNSTREAM REGULATED 2,
KEYWDS 2 STRUCTURAL GENOMICS, JOINT CENTER FOR STRUCTURAL GENOMICS,
KEYWDS 3 JCSG, PROTEIN STRUCTURE INITIATIVE, PSI-2, ALTERNATIVE
KEYWDS 4 SPLICING, CYTOPLASM, DEVELOPMENTAL PROTEIN, DIFFERENTIATION,
KEYWDS 5 NEUROGENESIS, PHOSPHORYLATION, REGULATORY PROTEIN,
KEYWDS 6 SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 1 04-SEP-07 2QMQ 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF N-MYC DOWNSTREAM REGULATED 2
JRNL TITL 2 (15277975) FROM MUS MUSCULUS AT 1.70 A RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.35
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 28649
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.147
REMARK 3 R VALUE (WORKING SET) : 0.145
REMARK 3 FREE R VALUE : 0.183
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1449
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1302
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.1890
REMARK 3 BIN FREE R VALUE SET COUNT : 69
REMARK 3 BIN FREE R VALUE : 0.2430
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 2551
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.36
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.35000
REMARK 3 B22 (A**2) : 0.35000
REMARK 3 B33 (A**2) : -0.53000
REMARK 3 B12 (A**2) : 0.18000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.098
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.097
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.059
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.438
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.957
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2304 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1525 ; 0.008 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3151 ; 1.561 ; 1.968
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3758 ; 0.953 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 301 ; 6.579 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 104 ;32.568 ;25.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 363 ;11.741 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;21.224 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 346 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2603 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 445 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 469 ; 0.223 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1583 ; 0.193 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1128 ; 0.188 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1160 ; 0.087 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 223 ; 0.165 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 1 ; 0.047 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 13 ; 0.150 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 40 ; 0.254 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 31 ; 0.169 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1522 ; 1.454 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 572 ; 0.402 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2313 ; 1.977 ; 3.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 964 ; 2.751 ; 4.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 826 ; 3.742 ; 5.000
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 0
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A -2 A 313
REMARK 3 ORIGIN FOR THE GROUP (A): 3.7832 34.5458 16.8449
REMARK 3 T TENSOR
REMARK 3 T11: -0.0432 T22: -0.0141
REMARK 3 T33: -0.0311 T12: -0.0243
REMARK 3 T13: -0.0040 T23: 0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 0.7468 L22: 0.5567
REMARK 3 L33: 0.6603 L12: 0.2506
REMARK 3 L13: 0.1012 L23: 0.1081
REMARK 3 S TENSOR
REMARK 3 S11: 0.0130 S12: -0.1019 S13: -0.0032
REMARK 3 S21: 0.0357 S22: -0.0449 S23: -0.0177
REMARK 3 S31: 0.0360 S32: 0.0075 S33: 0.0319
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 1. HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. 2. ATOM RECORD CONTAINS RESIDUAL B FACTORS
REMARK 3 ONLY. 3. MG AND PEG 400 (2PE) ARE PRESENT IN THE
REMARK 3 CRYSTALLIZATION CONDITIONS. 4. THE BENZOIC ACID (BEZ) MOLECULE
REMARK 3 IS ASSIGNED BASED ON THE ELECTRON DENSITY AND ITS INTERACTION
REMARK 3 WITH THE PROTEIN. IT COULD BE SOME RELATED COMPOUND WITH A
REMARK 3 SIMILAR STRUCTURE.
REMARK 4
REMARK 4 2QMQ COMPLIES WITH FORMAT V. 3.1, 1-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE RCSB ID CODE IS RCSB043792.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-OCT-2005
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.019976
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28650
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 29.348
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.9
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : 0.05000
REMARK 200 FOR THE DATA SET : 11.7000
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) : 1.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 61.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.60
REMARK 200 R MERGE FOR SHELL (I) : 0.40500
REMARK 200 R SYM FOR SHELL (I) : 0.40500
REMARK 200 FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1U2E
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NANODROP, 20.0% PEG 400, 0.2M
REMARK 280 MGCL2, 0.1M HEPES PH 7.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K, PH 7.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,1/3+Z
REMARK 290 3555 -X+Y,-X,2/3+Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,2/3-Z
REMARK 290 6555 -X,-X+Y,1/3-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 -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 71.58300
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 143.16600
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 143.16600
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 71.58300
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND 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 300 SIZE EXCLUSION CHROMATOGRAPHY WITH STATIC LIGHT
REMARK 300 SCATTERING SUPPORTS THE ASSIGNMENT OF A MONOMER AS A
REMARK 300 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE.
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: MONOMER
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMER
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSEQI
REMARK 465 MET A -11
REMARK 465 GLY A -10
REMARK 465 SER A -9
REMARK 465 ASP A -8
REMARK 465 LYS A -7
REMARK 465 ILE A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
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 HIS A -3 CG ND1 CD2 CE1 NE2
REMARK 470 HIS A -2 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 61 CB CG CD CE NZ
REMARK 470 TRP A 178 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 178 CZ3 CH2
REMARK 470 GLU A 212 CG CD OE1 OE2
REMARK 470 ARG A 247 CZ NH1 NH2
REMARK 470 GLU A 250 CD OE1 OE2
REMARK 470 LYS A 254 CD CE NZ
REMARK 470 GLU A 305 CD OE1 OE2
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 2PE A 4
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 MG A 2 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 244 OD1
REMARK 620 2 HOH A 441 O 92.7
REMARK 620 3 HOH A 486 O 86.9 99.3
REMARK 620 4 HOH A 421 O 92.6 166.8 93.0
REMARK 620 5 HOH A 429 O 178.5 85.8 93.4 88.8
REMARK 620 6 HOH A 418 O 84.9 80.0 171.7 88.5 94.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 1 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 377 O
REMARK 620 2 HOH A 397 O 85.3
REMARK 620 3 HOH A 392 O 85.2 170.1
REMARK 620 4 HOH A 344 O 89.1 86.9 90.1
REMARK 620 5 HOH A 385 O 175.0 91.1 98.2 87.3
REMARK 620 6 HOH A 358 O 92.0 101.3 81.8 171.7 92.0
REMARK 620 N 1 2 3 4 5
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 358981 RELATED DB: TARGETDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CONSTRUCT CONSISTS OF RESIDUES 40-313 OF THE
REMARK 999 FULL LENGTH PROTEIN. IT WAS EXPRESSED WITH A
REMARK 999 PURIFICATION TAG MGSDKIHHHHHH.
DBREF 2QMQ A 40 313 UNP Q9QYG0 NDRG2_MOUSE 40 313
SEQADV 2QMQ MET A -11 UNP Q9QYG0 LEADER SEQUENCE
SEQADV 2QMQ GLY A -10 UNP Q9QYG0 LEADER SEQUENCE
SEQADV 2QMQ SER A -9 UNP Q9QYG0 LEADER SEQUENCE
SEQADV 2QMQ ASP A -8 UNP Q9QYG0 LEADER SEQUENCE
SEQADV 2QMQ LYS A -7 UNP Q9QYG0 LEADER SEQUENCE
SEQADV 2QMQ ILE A -6 UNP Q9QYG0 LEADER SEQUENCE
SEQADV 2QMQ HIS A -5 UNP Q9QYG0 LEADER SEQUENCE
SEQADV 2QMQ HIS A -4 UNP Q9QYG0 LEADER SEQUENCE
SEQADV 2QMQ HIS A -3 UNP Q9QYG0 LEADER SEQUENCE
SEQADV 2QMQ HIS A -2 UNP Q9QYG0 LEADER SEQUENCE
SEQADV 2QMQ HIS A -1 UNP Q9QYG0 LEADER SEQUENCE
SEQADV 2QMQ HIS A 0 UNP Q9QYG0 LEADER SEQUENCE
SEQRES 1 A 286 MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS THR
SEQRES 2 A 286 HIS SER VAL GLU THR PRO TYR GLY SER VAL THR PHE THR
SEQRES 3 A 286 VAL TYR GLY THR PRO LYS PRO LYS ARG PRO ALA ILE PHE
SEQRES 4 A 286 THR TYR HIS ASP VAL GLY LEU ASN TYR LYS SER CYS PHE
SEQRES 5 A 286 GLN PRO LEU PHE ARG PHE GLY ASP MET GLN GLU ILE ILE
SEQRES 6 A 286 GLN ASN PHE VAL ARG VAL HIS VAL ASP ALA PRO GLY MET
SEQRES 7 A 286 GLU GLU GLY ALA PRO VAL PHE PRO LEU GLY TYR GLN TYR
SEQRES 8 A 286 PRO SER LEU ASP GLN LEU ALA ASP MET ILE PRO CYS ILE
SEQRES 9 A 286 LEU GLN TYR LEU ASN PHE SER THR ILE ILE GLY VAL GLY
SEQRES 10 A 286 VAL GLY ALA GLY ALA TYR ILE LEU SER ARG TYR ALA LEU
SEQRES 11 A 286 ASN HIS PRO ASP THR VAL GLU GLY LEU VAL LEU ILE ASN
SEQRES 12 A 286 ILE ASP PRO ASN ALA LYS GLY TRP MET ASP TRP ALA ALA
SEQRES 13 A 286 HIS LYS LEU THR GLY LEU THR SER SER ILE PRO ASP MET
SEQRES 14 A 286 ILE LEU GLY HIS LEU PHE SER GLN GLU GLU LEU SER GLY
SEQRES 15 A 286 ASN SER GLU LEU ILE GLN LYS TYR ARG GLY ILE ILE GLN
SEQRES 16 A 286 HIS ALA PRO ASN LEU GLU ASN ILE GLU LEU TYR TRP ASN
SEQRES 17 A 286 SER TYR ASN ASN ARG ARG ASP LEU ASN PHE GLU ARG GLY
SEQRES 18 A 286 GLY GLU THR THR LEU LYS CYS PRO VAL MET LEU VAL VAL
SEQRES 19 A 286 GLY ASP GLN ALA PRO HIS GLU ASP ALA VAL VAL GLU CYS
SEQRES 20 A 286 ASN SER LYS LEU ASP PRO THR GLN THR SER PHE LEU LYS
SEQRES 21 A 286 MET ALA ASP SER GLY GLY GLN PRO GLN LEU THR GLN PRO
SEQRES 22 A 286 GLY LYS LEU THR GLU ALA PHE LYS TYR PHE LEU GLN GLY
HET MG A 1 1
HET MG A 2 1
HET BEZ A 3 9
HET 2PE A 4 16
HETNAM MG MAGNESIUM ION
HETNAM BEZ BENZOIC ACID
HETNAM 2PE NONAETHYLENE GLYCOL
FORMUL 2 MG 2(MG 2+)
FORMUL 4 BEZ C7 H6 O2
FORMUL 5 2PE C18 H38 O10
FORMUL 6 HOH *314(H2 O)
HELIX 1 1 ASN A 74 ARG A 84 1 11
HELIX 2 2 PHE A 85 GLN A 93 1 9
HELIX 3 3 SER A 120 MET A 127 1 8
HELIX 4 4 MET A 127 ASN A 136 1 10
HELIX 5 5 GLY A 146 HIS A 159 1 14
HELIX 6 6 GLY A 177 LEU A 189 1 13
HELIX 7 7 SER A 192 PHE A 202 1 11
HELIX 8 8 SER A 203 GLY A 209 1 7
HELIX 9 9 SER A 211 HIS A 223 1 13
HELIX 10 10 ASN A 226 ASN A 239 1 14
HELIX 11 11 HIS A 267 LEU A 278 1 12
HELIX 12 12 ASP A 279 THR A 281 5 3
HELIX 13 13 GLN A 294 GLN A 299 1 6
HELIX 14 14 GLN A 299 GLN A 312 1 14
SHEET 1 A 8 HIS A -2 THR A 45 0
SHEET 2 A 8 GLY A 48 TYR A 55 -1 O VAL A 54 N HIS A -1
SHEET 3 A 8 ARG A 97 ASP A 101 -1 O ASP A 101 N THR A 51
SHEET 4 A 8 ALA A 64 TYR A 68 1 N ILE A 65 O VAL A 98
SHEET 5 A 8 ILE A 140 VAL A 145 1 O ILE A 141 N PHE A 66
SHEET 6 A 8 VAL A 163 ILE A 169 1 O VAL A 167 N GLY A 142
SHEET 7 A 8 VAL A 257 GLY A 262 1 O MET A 258 N LEU A 166
SHEET 8 A 8 THR A 283 MET A 288 1 O SER A 284 N LEU A 259
SHEET 1 B 2 GLU A 246 ARG A 247 0
SHEET 2 B 2 GLU A 250 THR A 251 -1 O GLU A 250 N ARG A 247
LINK OD1 ASN A 244 MG MG A 2 1555 1555 2.10
LINK MG MG A 1 O HOH A 377 1555 1555 2.00
LINK MG MG A 1 O HOH A 397 1555 1555 1.94
LINK MG MG A 1 O HOH A 392 1555 1555 2.16
LINK MG MG A 1 O HOH A 344 1555 1555 2.07
LINK MG MG A 1 O HOH A 385 1555 1555 2.04
LINK MG MG A 1 O HOH A 358 1555 1555 2.08
LINK MG MG A 2 O HOH A 441 1555 1555 2.08
LINK MG MG A 2 O HOH A 486 1555 1555 2.13
LINK MG MG A 2 O HOH A 421 1555 1555 2.27
LINK MG MG A 2 O HOH A 429 1555 1555 2.17
LINK MG MG A 2 O HOH A 418 1555 1555 2.08
CRYST1 46.371 46.371 214.749 90.00 90.00 120.00 P 31 2 1 6
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 0.021565 0.012451 0.000000 0.00000
SCALE2 0.000000 0.024901 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004657 0.00000
TER 2211 GLY A 313
MASTER 335 0 4 14 10 0 0 6 2551 1 41 22
END |