HEADER CHAPERONE 23-DEC-18 6NHK
TITLE MORTALIN NUCLEOTIDE BINDING DOMAIN IN THE ADP-BOUND STATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: STRESS-70 PROTEIN, MITOCHONDRIAL;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: 75 KDA GLUCOSE-REGULATED PROTEIN,GRP-75,HEAT SHOCK 70 KDA
COMPND 5 PROTEIN 9,MORTALIN,MOT,PEPTIDE-BINDING PROTEIN 74,PBP74;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: HSPA9, GRP75, HSPA9B, MT-HSP70;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA 2(DE3)
KEYWDS HSP70, MITOCHONDRIAL, CHAPERONE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.C.PAGE,M.A.MOSENG,J.C.NIX
REVDAT 4 11-OCT-23 6NHK 1 LINK
REVDAT 3 27-NOV-19 6NHK 1 REMARK
REVDAT 2 08-MAY-19 6NHK 1 JRNL
REVDAT 1 17-APR-19 6NHK 0
JRNL AUTH M.A.MOSENG,J.C.NIX,R.C.PAGE
JRNL TITL BIOPHYSICAL CONSEQUENCES OF EVEN-PLUS SYNDROME MUTATIONS FOR
JRNL TITL 2 THE FUNCTION OF MORTALIN.
JRNL REF J.PHYS.CHEM.B V. 123 3383 2019
JRNL REFN ISSN 1089-5647
JRNL PMID 30933555
JRNL DOI 10.1021/ACS.JPCB.9B00071
REMARK 2
REMARK 2 RESOLUTION. 2.78 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.13_2998
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.78
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 56.87
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 24273
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.259
REMARK 3 R VALUE (WORKING SET) : 0.256
REMARK 3 FREE R VALUE : 0.296
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.190
REMARK 3 FREE R VALUE TEST SET COUNT : 1989
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 56.8796 - 6.6907 0.99 1661 147 0.1715 0.2032
REMARK 3 2 6.6907 - 5.3119 1.00 1631 146 0.2418 0.2717
REMARK 3 3 5.3119 - 4.6408 1.00 1603 144 0.2325 0.2776
REMARK 3 4 4.6408 - 4.2166 1.00 1602 143 0.2338 0.2762
REMARK 3 5 4.2166 - 3.9144 1.00 1617 145 0.2531 0.2827
REMARK 3 6 3.9144 - 3.6837 1.00 1595 143 0.2822 0.3050
REMARK 3 7 3.6837 - 3.4992 1.00 1592 143 0.2916 0.3698
REMARK 3 8 3.4992 - 3.3469 1.00 1585 141 0.3041 0.3688
REMARK 3 9 3.3469 - 3.2181 1.00 1582 140 0.3103 0.3086
REMARK 3 10 3.2181 - 3.1071 1.00 1604 142 0.3379 0.4333
REMARK 3 11 3.1071 - 3.0099 0.99 1570 142 0.3578 0.3991
REMARK 3 12 3.0099 - 2.9239 1.00 1590 143 0.3684 0.4244
REMARK 3 13 2.9239 - 2.8469 0.99 1573 141 0.3926 0.4379
REMARK 3 14 2.8469 - 2.7775 0.92 1479 129 0.4071 0.4524
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.540
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 37.200
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 73.51
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 : 0.003 5434
REMARK 3 ANGLE : 0.607 7424
REMARK 3 CHIRALITY : 0.045 888
REMARK 3 PLANARITY : 0.005 983
REMARK 3 DIHEDRAL : 12.630 1849
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 6NHK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JAN-19.
REMARK 100 THE DEPOSITION ID IS D_1000238365.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-APR-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 4.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NOIR-1
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24320
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.777
REMARK 200 RESOLUTION RANGE LOW (A) : 56.870
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.6100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.78
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.88
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.100
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: 3ATU
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.17 M AMMONIUM ACETATE, 0.085 M
REMARK 280 SODIUM CITRATE:HCL PH 5.6, 25.5% (W/V) PEG 4000, 15% (V/V)
REMARK 280 GLYCEROL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 88.63150
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.05100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 88.63150
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 30.05100
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 47
REMARK 465 ALA A 48
REMARK 465 MET A 49
REMARK 465 GLY A 50
REMARK 465 SER A 51
REMARK 465 LYS A 52
REMARK 465 GLY A 53
REMARK 465 GLY B 47
REMARK 465 ALA B 48
REMARK 465 MET B 49
REMARK 465 GLY B 50
REMARK 465 SER B 51
REMARK 465 LYS B 52
REMARK 465 GLY B 53
REMARK 465 GLY B 72
REMARK 465 LYS B 73
REMARK 465 SER B 235
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 GLU A 71 CG CD OE1 OE2
REMARK 470 LYS A 73 CG CD CE NZ
REMARK 470 GLN A 74 CG CD OE1 NE2
REMARK 470 LYS A 76 CG CD CE NZ
REMARK 470 GLU A 98 CG CD OE1 OE2
REMARK 470 ARG A 127 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 135 CG CD CE NZ
REMARK 470 ILE A 137 CG1 CG2 CD1
REMARK 470 LYS A 143 CG CD CE NZ
REMARK 470 ILE A 144 CG1 CG2 CD1
REMARK 470 ARG A 146 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 155 CG CD OE1 OE2
REMARK 470 LYS A 159 CG CD CE NZ
REMARK 470 LEU A 160 CG CD1 CD2
REMARK 470 LYS A 175 CG CD CE NZ
REMARK 470 LYS A 187 CG CD CE NZ
REMARK 470 LYS A 234 CG CD CE NZ
REMARK 470 GLU A 236 CG CD OE1 OE2
REMARK 470 ASP A 237 CG OD1 OD2
REMARK 470 LYS A 238 CG CD CE NZ
REMARK 470 ILE A 257 CG1 CG2 CD1
REMARK 470 LYS A 259 CG CD CE NZ
REMARK 470 VAL A 261 CG1 CG2
REMARK 470 GLU A 263 CG CD OE1 OE2
REMARK 470 LYS A 265 CG CD CE NZ
REMARK 470 LYS A 291 CG CD CE NZ
REMARK 470 ARG A 292 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 293 CG CD OE1 OE2
REMARK 470 THR A 294 OG1 CG2
REMARK 470 VAL A 296 CG1 CG2
REMARK 470 LYS A 300 CG CD CE NZ
REMARK 470 GLN A 324 CG CD OE1 NE2
REMARK 470 LYS A 340 CG CD CE NZ
REMARK 470 LYS A 345 CG CD CE NZ
REMARK 470 ARG A 360 CG CD NE CZ NH1 NH2
REMARK 470 PRO A 365 CG CD
REMARK 470 LYS A 368 CG CD CE NZ
REMARK 470 GLU A 374 CG CD OE1 OE2
REMARK 470 VAL A 375 CG1 CG2
REMARK 470 LYS A 377 CG CD CE NZ
REMARK 470 LYS A 409 CG CD CE NZ
REMARK 470 GLN B 74 CG CD OE1 NE2
REMARK 470 LYS B 76 CG CD CE NZ
REMARK 470 GLU B 82 CG CD OE1 OE2
REMARK 470 ASP B 96 CG OD1 OD2
REMARK 470 ARG B 127 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 129 CG OD1 OD2
REMARK 470 GLU B 132 CG CD OE1 OE2
REMARK 470 LYS B 138 CG CD CE NZ
REMARK 470 LYS B 143 CG CD CE NZ
REMARK 470 ARG B 146 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 159 CG CD CE NZ
REMARK 470 LYS B 173 CG CD CE NZ
REMARK 470 LYS B 175 CG CD CE NZ
REMARK 470 LEU B 182 CG CD1 CD2
REMARK 470 LYS B 187 CG CD CE NZ
REMARK 470 LYS B 206 CG CD CE NZ
REMARK 470 ARG B 218 CG CD NE CZ NH1 NH2
REMARK 470 PRO B 223 CG CD
REMARK 470 LEU B 232 CG CD1 CD2
REMARK 470 ASP B 233 CG OD1 OD2
REMARK 470 LYS B 234 CG CD CE NZ
REMARK 470 GLU B 236 CG CD OE1 OE2
REMARK 470 ASP B 237 CG OD1 OD2
REMARK 470 LYS B 238 CG CD CE NZ
REMARK 470 VAL B 239 CG1 CG2
REMARK 470 ILE B 240 CG1 CG2 CD1
REMARK 470 ILE B 252 CG1 CG2 CD1
REMARK 470 LEU B 255 CG CD1 CD2
REMARK 470 GLU B 256 CG CD OE1 OE2
REMARK 470 ILE B 257 CG1 CG2 CD1
REMARK 470 GLN B 258 CG CD OE1 NE2
REMARK 470 LYS B 259 CG CD CE NZ
REMARK 470 VAL B 261 CG1 CG2
REMARK 470 GLU B 263 CG CD OE1 OE2
REMARK 470 LYS B 265 CG CD CE NZ
REMARK 470 ARG B 284 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 288 CG CD CE NZ
REMARK 470 LYS B 291 CG CD CE NZ
REMARK 470 LYS B 300 CG CD CE NZ
REMARK 470 ARG B 309 CG CD NE CZ NH1 NH2
REMARK 470 MET B 334 CG SD CE
REMARK 470 ASP B 335 CG OD1 OD2
REMARK 470 SER B 336 OG
REMARK 470 LYS B 340 CG CD CE NZ
REMARK 470 LYS B 345 CG CD CE NZ
REMARK 470 ASP B 357 CG OD1 OD2
REMARK 470 ARG B 360 CG CD NE CZ NH1 NH2
REMARK 470 ILE B 363 CG1 CG2 CD1
REMARK 470 PRO B 365 CG CD
REMARK 470 GLN B 367 CG CD OE1 NE2
REMARK 470 LYS B 368 CG CD CE NZ
REMARK 470 GLN B 371 CG CD OE1 NE2
REMARK 470 GLU B 374 CG CD OE1 OE2
REMARK 470 VAL B 375 CG1 CG2
REMARK 470 SER B 376 OG
REMARK 470 LYS B 377 CG CD CE NZ
REMARK 470 SER B 378 OG
REMARK 470 ILE B 380 CG1 CG2 CD1
REMARK 470 VAL B 383 CG1 CG2
REMARK 470 VAL B 386 CG1 CG2
REMARK 470 LEU B 402 CG CD1 CD2
REMARK 470 LYS B 409 CG CD CE NZ
REMARK 470 GLN B 424 CG CD OE1 NE2
REMARK 470 VAL B 427 CG1 CG2
REMARK 470 LEU B 428 CG CD1 CD2
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 ASN A 80 -165.57 -77.50
REMARK 500 ARG A 107 4.92 -69.27
REMARK 500 ASN A 115 30.52 -90.52
REMARK 500 TYR A 181 -63.60 -97.81
REMARK 500 HIS A 184 -130.99 57.60
REMARK 500 GLU A 236 -65.60 -94.71
REMARK 500 LYS A 259 14.65 59.43
REMARK 500 LYS A 409 46.85 -106.70
REMARK 500 ASN B 112 74.14 -119.44
REMARK 500 ASN B 115 30.67 -85.56
REMARK 500 TYR B 181 -67.64 -95.15
REMARK 500 HIS B 184 -154.25 -105.90
REMARK 500 ALA B 186 78.75 -103.06
REMARK 500 LYS B 259 18.10 56.06
REMARK 500 TYR B 331 71.58 58.36
REMARK 500 ASP B 335 5.93 82.49
REMARK 500 LYS B 409 35.48 -98.44
REMARK 500
REMARK 500 REMARK: NULL
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 503 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP A 501 O1B
REMARK 620 2 PO4 A 502 O1 77.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 602 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 244 OD2
REMARK 620 2 ADP B 600 O1B 165.3
REMARK 620 3 PO4 B 601 O1 114.0 80.7
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ADP A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ADP B 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 602
DBREF 6NHK A 54 429 UNP P38646 GRP75_HUMAN 54 429
DBREF 6NHK B 54 429 UNP P38646 GRP75_HUMAN 54 429
SEQADV 6NHK GLY A 47 UNP P38646 EXPRESSION TAG
SEQADV 6NHK ALA A 48 UNP P38646 EXPRESSION TAG
SEQADV 6NHK MET A 49 UNP P38646 EXPRESSION TAG
SEQADV 6NHK GLY A 50 UNP P38646 EXPRESSION TAG
SEQADV 6NHK SER A 51 UNP P38646 EXPRESSION TAG
SEQADV 6NHK LYS A 52 UNP P38646 EXPRESSION TAG
SEQADV 6NHK GLY A 53 UNP P38646 EXPRESSION TAG
SEQADV 6NHK GLY B 47 UNP P38646 EXPRESSION TAG
SEQADV 6NHK ALA B 48 UNP P38646 EXPRESSION TAG
SEQADV 6NHK MET B 49 UNP P38646 EXPRESSION TAG
SEQADV 6NHK GLY B 50 UNP P38646 EXPRESSION TAG
SEQADV 6NHK SER B 51 UNP P38646 EXPRESSION TAG
SEQADV 6NHK LYS B 52 UNP P38646 EXPRESSION TAG
SEQADV 6NHK GLY B 53 UNP P38646 EXPRESSION TAG
SEQRES 1 A 383 GLY ALA MET GLY SER LYS GLY ALA VAL VAL GLY ILE ASP
SEQRES 2 A 383 LEU GLY THR THR ASN SER CYS VAL ALA VAL MET GLU GLY
SEQRES 3 A 383 LYS GLN ALA LYS VAL LEU GLU ASN ALA GLU GLY ALA ARG
SEQRES 4 A 383 THR THR PRO SER VAL VAL ALA PHE THR ALA ASP GLY GLU
SEQRES 5 A 383 ARG LEU VAL GLY MET PRO ALA LYS ARG GLN ALA VAL THR
SEQRES 6 A 383 ASN PRO ASN ASN THR PHE TYR ALA THR LYS ARG LEU ILE
SEQRES 7 A 383 GLY ARG ARG TYR ASP ASP PRO GLU VAL GLN LYS ASP ILE
SEQRES 8 A 383 LYS ASN VAL PRO PHE LYS ILE VAL ARG ALA SER ASN GLY
SEQRES 9 A 383 ASP ALA TRP VAL GLU ALA HIS GLY LYS LEU TYR SER PRO
SEQRES 10 A 383 SER GLN ILE GLY ALA PHE VAL LEU MET LYS MET LYS GLU
SEQRES 11 A 383 THR ALA GLU ASN TYR LEU GLY HIS THR ALA LYS ASN ALA
SEQRES 12 A 383 VAL ILE THR VAL PRO ALA TYR PHE ASN ASP SER GLN ARG
SEQRES 13 A 383 GLN ALA THR LYS ASP ALA GLY GLN ILE SER GLY LEU ASN
SEQRES 14 A 383 VAL LEU ARG VAL ILE ASN GLU PRO THR ALA ALA ALA LEU
SEQRES 15 A 383 ALA TYR GLY LEU ASP LYS SER GLU ASP LYS VAL ILE ALA
SEQRES 16 A 383 VAL TYR ASP LEU GLY GLY GLY THR PHE ASP ILE SER ILE
SEQRES 17 A 383 LEU GLU ILE GLN LYS GLY VAL PHE GLU VAL LYS SER THR
SEQRES 18 A 383 ASN GLY ASP THR PHE LEU GLY GLY GLU ASP PHE ASP GLN
SEQRES 19 A 383 ALA LEU LEU ARG HIS ILE VAL LYS GLU PHE LYS ARG GLU
SEQRES 20 A 383 THR GLY VAL ASP LEU THR LYS ASP ASN MET ALA LEU GLN
SEQRES 21 A 383 ARG VAL ARG GLU ALA ALA GLU LYS ALA LYS CYS GLU LEU
SEQRES 22 A 383 SER SER SER VAL GLN THR ASP ILE ASN LEU PRO TYR LEU
SEQRES 23 A 383 THR MET ASP SER SER GLY PRO LYS HIS LEU ASN MET LYS
SEQRES 24 A 383 LEU THR ARG ALA GLN PHE GLU GLY ILE VAL THR ASP LEU
SEQRES 25 A 383 ILE ARG ARG THR ILE ALA PRO CYS GLN LYS ALA MET GLN
SEQRES 26 A 383 ASP ALA GLU VAL SER LYS SER ASP ILE GLY GLU VAL ILE
SEQRES 27 A 383 LEU VAL GLY GLY MET THR ARG MET PRO LYS VAL GLN GLN
SEQRES 28 A 383 THR VAL GLN ASP LEU PHE GLY ARG ALA PRO SER LYS ALA
SEQRES 29 A 383 VAL ASN PRO ASP GLU ALA VAL ALA ILE GLY ALA ALA ILE
SEQRES 30 A 383 GLN GLY GLY VAL LEU ALA
SEQRES 1 B 383 GLY ALA MET GLY SER LYS GLY ALA VAL VAL GLY ILE ASP
SEQRES 2 B 383 LEU GLY THR THR ASN SER CYS VAL ALA VAL MET GLU GLY
SEQRES 3 B 383 LYS GLN ALA LYS VAL LEU GLU ASN ALA GLU GLY ALA ARG
SEQRES 4 B 383 THR THR PRO SER VAL VAL ALA PHE THR ALA ASP GLY GLU
SEQRES 5 B 383 ARG LEU VAL GLY MET PRO ALA LYS ARG GLN ALA VAL THR
SEQRES 6 B 383 ASN PRO ASN ASN THR PHE TYR ALA THR LYS ARG LEU ILE
SEQRES 7 B 383 GLY ARG ARG TYR ASP ASP PRO GLU VAL GLN LYS ASP ILE
SEQRES 8 B 383 LYS ASN VAL PRO PHE LYS ILE VAL ARG ALA SER ASN GLY
SEQRES 9 B 383 ASP ALA TRP VAL GLU ALA HIS GLY LYS LEU TYR SER PRO
SEQRES 10 B 383 SER GLN ILE GLY ALA PHE VAL LEU MET LYS MET LYS GLU
SEQRES 11 B 383 THR ALA GLU ASN TYR LEU GLY HIS THR ALA LYS ASN ALA
SEQRES 12 B 383 VAL ILE THR VAL PRO ALA TYR PHE ASN ASP SER GLN ARG
SEQRES 13 B 383 GLN ALA THR LYS ASP ALA GLY GLN ILE SER GLY LEU ASN
SEQRES 14 B 383 VAL LEU ARG VAL ILE ASN GLU PRO THR ALA ALA ALA LEU
SEQRES 15 B 383 ALA TYR GLY LEU ASP LYS SER GLU ASP LYS VAL ILE ALA
SEQRES 16 B 383 VAL TYR ASP LEU GLY GLY GLY THR PHE ASP ILE SER ILE
SEQRES 17 B 383 LEU GLU ILE GLN LYS GLY VAL PHE GLU VAL LYS SER THR
SEQRES 18 B 383 ASN GLY ASP THR PHE LEU GLY GLY GLU ASP PHE ASP GLN
SEQRES 19 B 383 ALA LEU LEU ARG HIS ILE VAL LYS GLU PHE LYS ARG GLU
SEQRES 20 B 383 THR GLY VAL ASP LEU THR LYS ASP ASN MET ALA LEU GLN
SEQRES 21 B 383 ARG VAL ARG GLU ALA ALA GLU LYS ALA LYS CYS GLU LEU
SEQRES 22 B 383 SER SER SER VAL GLN THR ASP ILE ASN LEU PRO TYR LEU
SEQRES 23 B 383 THR MET ASP SER SER GLY PRO LYS HIS LEU ASN MET LYS
SEQRES 24 B 383 LEU THR ARG ALA GLN PHE GLU GLY ILE VAL THR ASP LEU
SEQRES 25 B 383 ILE ARG ARG THR ILE ALA PRO CYS GLN LYS ALA MET GLN
SEQRES 26 B 383 ASP ALA GLU VAL SER LYS SER ASP ILE GLY GLU VAL ILE
SEQRES 27 B 383 LEU VAL GLY GLY MET THR ARG MET PRO LYS VAL GLN GLN
SEQRES 28 B 383 THR VAL GLN ASP LEU PHE GLY ARG ALA PRO SER LYS ALA
SEQRES 29 B 383 VAL ASN PRO ASP GLU ALA VAL ALA ILE GLY ALA ALA ILE
SEQRES 30 B 383 GLN GLY GLY VAL LEU ALA
HET ADP A 501 27
HET PO4 A 502 5
HET MG A 503 1
HET GOL A 504 6
HET ADP B 600 27
HET PO4 B 601 5
HET MG B 602 1
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM PO4 PHOSPHATE ION
HETNAM MG MAGNESIUM ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 ADP 2(C10 H15 N5 O10 P2)
FORMUL 4 PO4 2(O4 P 3-)
FORMUL 5 MG 2(MG 2+)
FORMUL 6 GOL C3 H8 O3
FORMUL 10 HOH *8(H2 O)
HELIX 1 AA1 GLY A 102 ARG A 107 1 6
HELIX 2 AA2 THR A 120 LEU A 123 5 4
HELIX 3 AA3 ASP A 130 ASN A 139 1 10
HELIX 4 AA4 SER A 162 GLY A 183 1 22
HELIX 5 AA5 ASN A 198 SER A 212 1 15
HELIX 6 AA6 GLU A 222 TYR A 230 1 9
HELIX 7 AA7 GLY A 231 SER A 235 5 5
HELIX 8 AA8 GLY A 274 ARG A 292 1 19
HELIX 9 AA9 ASP A 297 LYS A 300 5 4
HELIX 10 AB1 ASP A 301 LEU A 319 1 19
HELIX 11 AB2 ARG A 348 VAL A 355 1 8
HELIX 12 AB3 VAL A 355 ARG A 361 1 7
HELIX 13 AB4 THR A 362 ALA A 373 1 12
HELIX 14 AB5 GLY A 387 ARG A 391 5 5
HELIX 15 AB6 MET A 392 GLY A 404 1 13
HELIX 16 AB7 GLU A 415 ALA A 429 1 15
HELIX 17 AB8 GLY B 102 ARG B 107 1 6
HELIX 18 AB9 THR B 120 LEU B 123 5 4
HELIX 19 AC1 ASP B 130 ASN B 139 1 10
HELIX 20 AC2 SER B 162 LEU B 182 1 21
HELIX 21 AC3 ASN B 198 GLY B 213 1 16
HELIX 22 AC4 GLU B 222 TYR B 230 1 9
HELIX 23 AC5 GLY B 274 GLY B 295 1 22
HELIX 24 AC6 ASP B 297 LYS B 300 5 4
HELIX 25 AC7 ASP B 301 LEU B 319 1 19
HELIX 26 AC8 ARG B 348 VAL B 355 1 8
HELIX 27 AC9 VAL B 355 ARG B 361 1 7
HELIX 28 AD1 THR B 362 GLU B 374 1 13
HELIX 29 AD2 GLY B 387 ARG B 391 5 5
HELIX 30 AD3 MET B 392 GLY B 404 1 13
HELIX 31 AD4 GLU B 415 ALA B 429 1 15
SHEET 1 AA1 3 GLN A 74 VAL A 77 0
SHEET 2 AA1 3 ASN A 64 GLU A 71 -1 N GLU A 71 O GLN A 74
SHEET 3 AA1 3 THR A 87 PRO A 88 -1 O THR A 87 N SER A 65
SHEET 1 AA2 5 GLN A 74 VAL A 77 0
SHEET 2 AA2 5 ASN A 64 GLU A 71 -1 N GLU A 71 O GLN A 74
SHEET 3 AA2 5 VAL A 55 ASP A 59 -1 N GLY A 57 O ALA A 68
SHEET 4 AA2 5 ASN A 188 VAL A 193 1 O VAL A 190 N ILE A 58
SHEET 5 AA2 5 ASN A 215 ASN A 221 1 O ASN A 215 N ALA A 189
SHEET 1 AA3 3 ARG A 99 VAL A 101 0
SHEET 2 AA3 3 VAL A 90 PHE A 93 -1 N ALA A 92 O LEU A 100
SHEET 3 AA3 3 THR A 116 TYR A 118 -1 O PHE A 117 N VAL A 91
SHEET 1 AA4 3 LYS A 143 ARG A 146 0
SHEET 2 AA4 3 ALA A 152 ALA A 156 -1 O TRP A 153 N VAL A 145
SHEET 3 AA4 3 LYS A 159 TYR A 161 -1 O TYR A 161 N VAL A 154
SHEET 1 AA5 4 VAL A 261 ASP A 270 0
SHEET 2 AA5 4 PHE A 250 GLN A 258 -1 N PHE A 250 O ASP A 270
SHEET 3 AA5 4 ASP A 237 LEU A 245 -1 N ILE A 240 O LEU A 255
SHEET 4 AA5 4 ILE A 380 VAL A 386 1 O VAL A 386 N TYR A 243
SHEET 1 AA6 2 GLN A 324 MET A 334 0
SHEET 2 AA6 2 PRO A 339 THR A 347 -1 O LEU A 342 N LEU A 329
SHEET 1 AA7 3 LYS B 76 VAL B 77 0
SHEET 2 AA7 3 ASN B 64 VAL B 69 -1 N VAL B 69 O LYS B 76
SHEET 3 AA7 3 THR B 87 PRO B 88 -1 O THR B 87 N SER B 65
SHEET 1 AA8 5 LYS B 76 VAL B 77 0
SHEET 2 AA8 5 ASN B 64 VAL B 69 -1 N VAL B 69 O LYS B 76
SHEET 3 AA8 5 VAL B 55 ASP B 59 -1 N GLY B 57 O ALA B 68
SHEET 4 AA8 5 ASN B 188 VAL B 193 1 O VAL B 190 N ILE B 58
SHEET 5 AA8 5 ASN B 215 ASN B 221 1 O ASN B 215 N ALA B 189
SHEET 1 AA9 3 ARG B 99 VAL B 101 0
SHEET 2 AA9 3 VAL B 90 PHE B 93 -1 N ALA B 92 O LEU B 100
SHEET 3 AA9 3 THR B 116 TYR B 118 -1 O PHE B 117 N VAL B 91
SHEET 1 AB1 3 LYS B 143 ARG B 146 0
SHEET 2 AB1 3 ALA B 152 ALA B 156 -1 O TRP B 153 N VAL B 145
SHEET 3 AB1 3 LYS B 159 TYR B 161 -1 O TYR B 161 N VAL B 154
SHEET 1 AB2 4 VAL B 261 ASN B 268 0
SHEET 2 AB2 4 PHE B 250 GLN B 258 -1 N ILE B 254 O LYS B 265
SHEET 3 AB2 4 LYS B 238 LEU B 245 -1 N VAL B 242 O SER B 253
SHEET 4 AB2 4 ILE B 380 VAL B 386 1 O GLY B 381 N VAL B 239
SHEET 1 AB3 2 GLN B 324 THR B 333 0
SHEET 2 AB3 2 LYS B 340 THR B 347 -1 O LEU B 346 N THR B 325
LINK O1B ADP A 501 MG MG A 503 1555 1555 2.35
LINK O1 PO4 A 502 MG MG A 503 1555 1555 1.80
LINK OD2 ASP B 244 MG MG B 602 1555 1555 2.92
LINK O1B ADP B 600 MG MG B 602 1555 1555 2.39
LINK O1 PO4 B 601 MG MG B 602 1555 1555 2.06
CISPEP 1 SER B 337 GLY B 338 0 19.57
SITE 1 AC1 14 THR A 63 ASN A 64 GLY A 247 GLU A 313
SITE 2 AC1 14 LYS A 316 CYS A 317 SER A 320 GLY A 388
SITE 3 AC1 14 MET A 389 ARG A 391 ASP A 414 PO4 A 502
SITE 4 AC1 14 MG A 503 HOH A 605
SITE 1 AC2 8 GLY A 61 THR A 62 LYS A 121 GLU A 222
SITE 2 AC2 8 THR A 249 ASP A 251 ADP A 501 MG A 503
SITE 1 AC3 3 ASP A 244 ADP A 501 PO4 A 502
SITE 1 AC4 6 TYR A 196 ASP A 251 THR A 267 ASN A 268
SITE 2 AC4 6 GLY A 269 HOH A 601
SITE 1 AC5 15 THR B 63 ASN B 64 GLY B 246 GLY B 247
SITE 2 AC5 15 GLU B 313 LYS B 316 CYS B 317 SER B 320
SITE 3 AC5 15 GLY B 387 GLY B 388 MET B 389 ARG B 391
SITE 4 AC5 15 ASP B 414 PO4 B 601 MG B 602
SITE 1 AC6 8 GLY B 61 THR B 62 LYS B 121 GLU B 222
SITE 2 AC6 8 THR B 249 ASP B 251 ADP B 600 MG B 602
SITE 1 AC7 3 ASP B 244 ADP B 600 PO4 B 601
CRYST1 177.263 60.102 91.699 90.00 97.56 90.00 C 1 2 1 8
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 0.005641 0.000000 0.000749 0.00000
SCALE2 0.000000 0.016638 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011001 0.00000
(ATOM LINES ARE NOT SHOWN.)
END