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HEADER LIPID BINDING PROTEIN 03-JUL-20 6ZMM
TITLE CRYSTAL STRUCTURE OF HUMAN NDRG1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN NDRG1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: DIFFERENTIATION-RELATED GENE 1 PROTEIN,DRG-1,N-MYC
COMPND 5 DOWNSTREAM-REGULATED GENE 1 PROTEIN,NICKEL-SPECIFIC INDUCTION PROTEIN
COMPND 6 CAP43,REDUCING AGENTS AND TUNICAMYCIN-RESPONSIVE PROTEIN,RTP,RIT42;
COMPND 7 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: NDRG1, CAP43, DRG1, RTP;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TUMOR SUPPRESSOR, LIPID BINDING PROTEIN, METAL BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR V.MUSTONEN,P.KURSULA,S.RUSKAMO
REVDAT 1 23-DEC-20 6ZMM 0
JRNL AUTH V.MUSTONEN,G.MURUGANANDAM,R.LORIS,P.KURSULA,S.RUSKAMO
JRNL TITL CRYSTAL AND SOLUTION STRUCTURE OF NDRG1, A MEMBRANE-BINDING
JRNL TITL 2 PROTEIN LINKED TO MYELINATION AND TUMOUR SUPPRESSION.
JRNL REF FEBS J. 2020
JRNL REFN ISSN 1742-464X
JRNL PMID 33305529
JRNL DOI 10.1111/FEBS.15660
REMARK 2
REMARK 2 RESOLUTION. 2.96 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.17.1_3660
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.96
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.55
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 3 NUMBER OF REFLECTIONS : 14733
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.270
REMARK 3 R VALUE (WORKING SET) : 0.269
REMARK 3 FREE R VALUE : 0.295
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980
REMARK 3 FREE R VALUE TEST SET COUNT : 733
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 48.5500 - 5.0700 0.94 2905 153 0.2588 0.2833
REMARK 3 2 5.0600 - 4.0200 0.95 2768 143 0.2309 0.2648
REMARK 3 3 4.0200 - 3.5100 0.98 2820 149 0.2584 0.2761
REMARK 3 4 3.5100 - 3.1900 0.98 2812 147 0.2953 0.3011
REMARK 3 5 3.1900 - 2.9600 0.94 2695 141 0.3793 0.4457
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) : 0.512
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 35.078
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 63.71
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 65.42
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 : 0.002 3942
REMARK 3 ANGLE : 0.577 5355
REMARK 3 CHIRALITY : 0.045 610
REMARK 3 PLANARITY : 0.004 702
REMARK 3 DIHEDRAL : 18.032 1435
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 : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: (CHAIN 'A' AND (RESID 32 THROUGH 168 OR
REMARK 3 RESID 185 THROUGH 196 OR RESID 207
REMARK 3 THROUGH 241 OR RESID 249 THROUGH 316))
REMARK 3 SELECTION : (CHAIN 'B' AND (RESID 32 THROUGH 51 OR
REMARK 3 RESID 56 THROUGH 168 OR RESID 185 THROUGH
REMARK 3 196 OR RESID 207 THROUGH 316))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6ZMM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-JUL-20.
REMARK 100 THE DEPOSITION ID IS D_1292109808.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-MAY-20
REMARK 200 TEMPERATURE (KELVIN) : 80
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PETRA III, DESY
REMARK 200 BEAMLINE : P11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9762
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 : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14800
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.960
REMARK 200 RESOLUTION RANGE LOW (A) : 48.550
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 200 DATA REDUNDANCY : 4.260
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 4.3300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.96
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.07
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 FOR SHELL : 1.420
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: 2XMQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4 M SODIUM MALONATE (PH 6.25), 10 MM
REMARK 280 TCEP, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 285.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 59.66500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 54.28500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 54.28500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 89.49750
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 54.28500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 54.28500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 29.83250
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 54.28500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 54.28500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 89.49750
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 54.28500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 54.28500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 29.83250
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 59.66500
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: 1820 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 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 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 CL CL A 401 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 ASP A 31
REMARK 465 PRO A 52
REMARK 465 LYS A 53
REMARK 465 GLY A 54
REMARK 465 ASN A 55
REMARK 465 GLU A 170
REMARK 465 GLY A 171
REMARK 465 TRP A 172
REMARK 465 MET A 173
REMARK 465 ASP A 174
REMARK 465 TRP A 175
REMARK 465 ALA A 176
REMARK 465 ALA A 177
REMARK 465 SER A 178
REMARK 465 LYS A 179
REMARK 465 ILE A 180
REMARK 465 SER A 181
REMARK 465 GLY A 182
REMARK 465 TRP A 183
REMARK 465 THR A 184
REMARK 465 LYS A 198
REMARK 465 GLU A 199
REMARK 465 GLU A 200
REMARK 465 MET A 201
REMARK 465 GLN A 202
REMARK 465 SER A 203
REMARK 465 ASN A 204
REMARK 465 VAL A 205
REMARK 465 GLU A 206
REMARK 465 MET A 243
REMARK 465 PRO A 244
REMARK 465 GLY A 245
REMARK 465 THR A 246
REMARK 465 HIS A 247
REMARK 465 THR A 248
REMARK 465 SER A 317
REMARK 465 ALA A 318
REMARK 465 SER A 319
REMARK 465 ASP B 31
REMARK 465 PRO B 52
REMARK 465 LYS B 53
REMARK 465 GLY B 54
REMARK 465 ALA B 169
REMARK 465 GLU B 170
REMARK 465 GLY B 171
REMARK 465 TRP B 172
REMARK 465 MET B 173
REMARK 465 ASP B 174
REMARK 465 TRP B 175
REMARK 465 ALA B 176
REMARK 465 ALA B 177
REMARK 465 SER B 178
REMARK 465 LYS B 179
REMARK 465 ILE B 180
REMARK 465 SER B 181
REMARK 465 GLY B 182
REMARK 465 TRP B 183
REMARK 465 GLY B 197
REMARK 465 LYS B 198
REMARK 465 GLU B 199
REMARK 465 GLU B 200
REMARK 465 MET B 201
REMARK 465 GLN B 202
REMARK 465 SER B 203
REMARK 465 ASN B 204
REMARK 465 PRO B 242
REMARK 465 MET B 243
REMARK 465 PRO B 244
REMARK 465 GLY B 245
REMARK 465 THR B 246
REMARK 465 HIS B 247
REMARK 465 THR B 248
REMARK 465 SER B 317
REMARK 465 ALA B 318
REMARK 465 SER B 319
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 TYR A 73 -31.53 -130.04
REMARK 500 ASP A 81 0.93 -68.33
REMARK 500 PRO A 167 31.02 -89.79
REMARK 500 ASP A 288 67.04 -112.68
REMARK 500 TYR B 73 -31.56 -131.66
REMARK 500 ASP B 81 0.47 -68.01
REMARK 500 PRO B 167 32.36 -88.47
REMARK 500 ASP B 288 68.09 -104.69
REMARK 500 CYS B 289 -63.58 -129.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 401
DBREF 6ZMM A 31 319 UNP Q92597 NDRG1_HUMAN 31 319
DBREF 6ZMM B 31 319 UNP Q92597 NDRG1_HUMAN 31 319
SEQRES 1 A 289 ASP VAL GLN GLU GLN ASP ILE GLU THR LEU HIS GLY SER
SEQRES 2 A 289 VAL HIS VAL THR LEU CYS GLY THR PRO LYS GLY ASN ARG
SEQRES 3 A 289 PRO VAL ILE LEU THR TYR HIS ASP ILE GLY MET ASN HIS
SEQRES 4 A 289 LYS THR CYS TYR ASN PRO LEU PHE ASN TYR GLU ASP MET
SEQRES 5 A 289 GLN GLU ILE THR GLN HIS PHE ALA VAL CYS HIS VAL ASP
SEQRES 6 A 289 ALA PRO GLY GLN GLN ASP GLY ALA ALA SER PHE PRO ALA
SEQRES 7 A 289 GLY TYR MET TYR PRO SER MET ASP GLN LEU ALA GLU MET
SEQRES 8 A 289 LEU PRO GLY VAL LEU GLN GLN PHE GLY LEU LYS SER ILE
SEQRES 9 A 289 ILE GLY MET GLY THR GLY ALA GLY ALA TYR ILE LEU THR
SEQRES 10 A 289 ARG PHE ALA LEU ASN ASN PRO GLU MET VAL GLU GLY LEU
SEQRES 11 A 289 VAL LEU ILE ASN VAL ASN PRO CYS ALA GLU GLY TRP MET
SEQRES 12 A 289 ASP TRP ALA ALA SER LYS ILE SER GLY TRP THR GLN ALA
SEQRES 13 A 289 LEU PRO ASP MET VAL VAL SER HIS LEU PHE GLY LYS GLU
SEQRES 14 A 289 GLU MET GLN SER ASN VAL GLU VAL VAL HIS THR TYR ARG
SEQRES 15 A 289 GLN HIS ILE VAL ASN ASP MET ASN PRO GLY ASN LEU HIS
SEQRES 16 A 289 LEU PHE ILE ASN ALA TYR ASN SER ARG ARG ASP LEU GLU
SEQRES 17 A 289 ILE GLU ARG PRO MET PRO GLY THR HIS THR VAL THR LEU
SEQRES 18 A 289 GLN CYS PRO ALA LEU LEU VAL VAL GLY ASP SER SER PRO
SEQRES 19 A 289 ALA VAL ASP ALA VAL VAL GLU CYS ASN SER LYS LEU ASP
SEQRES 20 A 289 PRO THR LYS THR THR LEU LEU LYS MET ALA ASP CYS GLY
SEQRES 21 A 289 GLY LEU PRO GLN ILE SER GLN PRO ALA LYS LEU ALA GLU
SEQRES 22 A 289 ALA PHE LYS TYR PHE VAL GLN GLY MET GLY TYR MET PRO
SEQRES 23 A 289 SER ALA SER
SEQRES 1 B 289 ASP VAL GLN GLU GLN ASP ILE GLU THR LEU HIS GLY SER
SEQRES 2 B 289 VAL HIS VAL THR LEU CYS GLY THR PRO LYS GLY ASN ARG
SEQRES 3 B 289 PRO VAL ILE LEU THR TYR HIS ASP ILE GLY MET ASN HIS
SEQRES 4 B 289 LYS THR CYS TYR ASN PRO LEU PHE ASN TYR GLU ASP MET
SEQRES 5 B 289 GLN GLU ILE THR GLN HIS PHE ALA VAL CYS HIS VAL ASP
SEQRES 6 B 289 ALA PRO GLY GLN GLN ASP GLY ALA ALA SER PHE PRO ALA
SEQRES 7 B 289 GLY TYR MET TYR PRO SER MET ASP GLN LEU ALA GLU MET
SEQRES 8 B 289 LEU PRO GLY VAL LEU GLN GLN PHE GLY LEU LYS SER ILE
SEQRES 9 B 289 ILE GLY MET GLY THR GLY ALA GLY ALA TYR ILE LEU THR
SEQRES 10 B 289 ARG PHE ALA LEU ASN ASN PRO GLU MET VAL GLU GLY LEU
SEQRES 11 B 289 VAL LEU ILE ASN VAL ASN PRO CYS ALA GLU GLY TRP MET
SEQRES 12 B 289 ASP TRP ALA ALA SER LYS ILE SER GLY TRP THR GLN ALA
SEQRES 13 B 289 LEU PRO ASP MET VAL VAL SER HIS LEU PHE GLY LYS GLU
SEQRES 14 B 289 GLU MET GLN SER ASN VAL GLU VAL VAL HIS THR TYR ARG
SEQRES 15 B 289 GLN HIS ILE VAL ASN ASP MET ASN PRO GLY ASN LEU HIS
SEQRES 16 B 289 LEU PHE ILE ASN ALA TYR ASN SER ARG ARG ASP LEU GLU
SEQRES 17 B 289 ILE GLU ARG PRO MET PRO GLY THR HIS THR VAL THR LEU
SEQRES 18 B 289 GLN CYS PRO ALA LEU LEU VAL VAL GLY ASP SER SER PRO
SEQRES 19 B 289 ALA VAL ASP ALA VAL VAL GLU CYS ASN SER LYS LEU ASP
SEQRES 20 B 289 PRO THR LYS THR THR LEU LEU LYS MET ALA ASP CYS GLY
SEQRES 21 B 289 GLY LEU PRO GLN ILE SER GLN PRO ALA LYS LEU ALA GLU
SEQRES 22 B 289 ALA PHE LYS TYR PHE VAL GLN GLY MET GLY TYR MET PRO
SEQRES 23 B 289 SER ALA SER
HET CL A 401 1
HETNAM CL CHLORIDE ION
FORMUL 3 CL CL 1-
FORMUL 4 HOH *12(H2 O)
HELIX 1 AA1 ASN A 68 TYR A 73 1 6
HELIX 2 AA2 TYR A 73 ASN A 78 1 6
HELIX 3 AA3 TYR A 79 ASP A 81 5 3
HELIX 4 AA4 MET A 82 PHE A 89 1 8
HELIX 5 AA5 SER A 114 MET A 121 1 8
HELIX 6 AA6 MET A 121 PHE A 129 1 9
HELIX 7 AA7 GLY A 140 ASN A 153 1 14
HELIX 8 AA8 ALA A 186 PHE A 196 1 11
HELIX 9 AA9 VAL A 208 ASP A 218 1 11
HELIX 10 AB1 ASN A 220 SER A 233 1 14
HELIX 11 AB2 ALA A 265 LYS A 275 1 11
HELIX 12 AB3 LEU A 292 GLN A 297 1 6
HELIX 13 AB4 GLN A 297 MET A 312 1 16
HELIX 14 AB5 ASN B 68 TYR B 73 1 6
HELIX 15 AB6 TYR B 73 ASN B 78 1 6
HELIX 16 AB7 TYR B 79 PHE B 89 1 11
HELIX 17 AB8 SER B 114 GLU B 120 1 7
HELIX 18 AB9 GLU B 120 PHE B 129 1 10
HELIX 19 AC1 GLY B 140 ASN B 153 1 14
HELIX 20 AC2 ALA B 186 PHE B 196 1 11
HELIX 21 AC3 GLU B 206 MET B 219 1 14
HELIX 22 AC4 ASN B 220 SER B 233 1 14
HELIX 23 AC5 ALA B 265 LYS B 275 1 11
HELIX 24 AC6 LEU B 292 GLN B 297 1 6
HELIX 25 AC7 GLN B 297 MET B 312 1 16
SHEET 1 AA1 8 GLN A 33 THR A 39 0
SHEET 2 AA1 8 GLY A 42 LEU A 48 -1 O VAL A 46 N GLN A 35
SHEET 3 AA1 8 ALA A 90 ASP A 95 -1 O ASP A 95 N HIS A 45
SHEET 4 AA1 8 VAL A 58 TYR A 62 1 N ILE A 59 O CYS A 92
SHEET 5 AA1 8 ILE A 134 THR A 139 1 O ILE A 135 N VAL A 58
SHEET 6 AA1 8 VAL A 157 ILE A 163 1 O VAL A 161 N GLY A 136
SHEET 7 AA1 8 ALA A 255 GLY A 260 1 O LEU A 256 N LEU A 160
SHEET 8 AA1 8 THR A 281 MET A 286 1 O MET A 286 N VAL A 259
SHEET 1 AA2 8 GLN B 33 THR B 39 0
SHEET 2 AA2 8 GLY B 42 LEU B 48 -1 O VAL B 46 N GLN B 35
SHEET 3 AA2 8 ALA B 90 ASP B 95 -1 O ASP B 95 N HIS B 45
SHEET 4 AA2 8 VAL B 58 TYR B 62 1 N ILE B 59 O CYS B 92
SHEET 5 AA2 8 ILE B 134 THR B 139 1 O ILE B 135 N VAL B 58
SHEET 6 AA2 8 VAL B 157 ILE B 163 1 O VAL B 161 N GLY B 136
SHEET 7 AA2 8 ALA B 255 GLY B 260 1 O LEU B 256 N LEU B 160
SHEET 8 AA2 8 THR B 281 MET B 286 1 O THR B 282 N LEU B 257
SITE 1 AC1 1 THR A 281
CRYST1 108.570 108.570 119.330 90.00 90.00 90.00 P 43 21 2 16
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 0.009211 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009211 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008380 0.00000
TER 3809 PRO A 316
TER 7646 PRO B 316
MASTER 343 0 1 25 16 0 1 6 3874 2 0 46
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