HEADER HYDROLASE 28-MAY-15 5BPL
TITLE CRYSTAL STRUCTURE OF ADP AND PI BOUND HUMAN HSP70 NBD MUTANT R272K.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEAT SHOCK 70 KDA PROTEIN 1A;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HEAT SHOCK 70 KDA PROTEIN 1,HSP70.1;
COMPND 5 ENGINEERED: YES;
COMPND 6 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: HSPA1A, HSPA1, HSX70;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28B+
KEYWDS HYDROLASE, ATP HYDROLYSIS ACTIVITY
EXPDTA X-RAY DIFFRACTION
AUTHOR D.NARAYANAN,R.A.ENGH
REVDAT 2 10-JAN-24 5BPL 1 LINK
REVDAT 1 14-SEP-16 5BPL 0
JRNL AUTH D.NARAYANAN,A.PFLUG,T.CHRISTOPEIT,P.KYOMUHENDO,R.A.ENGH
JRNL TITL NUCLEOTIDE BINDING TO VARIANTS OF THE HSP70-NBD.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.93 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) : 1.93
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.53
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 31818
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.290
REMARK 3 FREE R VALUE TEST SET COUNT : 2000
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 47.5366 - 4.6401 0.95 2237 150 0.1609 0.1892
REMARK 3 2 4.6401 - 3.6834 0.97 2182 147 0.1429 0.2063
REMARK 3 3 3.6834 - 3.2179 0.98 2173 145 0.1662 0.2248
REMARK 3 4 3.2179 - 2.9238 0.99 2154 145 0.1904 0.2320
REMARK 3 5 2.9238 - 2.7142 0.98 2139 143 0.1833 0.2440
REMARK 3 6 2.7142 - 2.5542 0.98 2139 144 0.1864 0.2615
REMARK 3 7 2.5542 - 2.4263 0.98 2129 142 0.1886 0.2873
REMARK 3 8 2.4263 - 2.3207 0.98 2128 143 0.1957 0.2400
REMARK 3 9 2.3207 - 2.2313 0.98 2127 143 0.2188 0.2914
REMARK 3 10 2.2313 - 2.1543 0.98 2115 142 0.2041 0.2413
REMARK 3 11 2.1543 - 2.0870 0.98 2096 140 0.2114 0.2887
REMARK 3 12 2.0870 - 2.0273 0.97 2100 141 0.2325 0.3048
REMARK 3 13 2.0273 - 1.9740 0.98 2092 141 0.2384 0.2695
REMARK 3 14 1.9740 - 1.9258 0.94 2007 134 0.2589 0.3010
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) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.270
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 : 0.008 3033
REMARK 3 ANGLE : 1.044 4106
REMARK 3 CHIRALITY : 0.041 462
REMARK 3 PLANARITY : 0.005 529
REMARK 3 DIHEDRAL : 14.812 1121
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 3 THROUGH 28 )
REMARK 3 ORIGIN FOR THE GROUP (A): 36.3213 71.9879 16.3902
REMARK 3 T TENSOR
REMARK 3 T11: 0.1184 T22: 0.2199
REMARK 3 T33: 0.1737 T12: -0.0036
REMARK 3 T13: 0.0012 T23: 0.0819
REMARK 3 L TENSOR
REMARK 3 L11: 1.3048 L22: 2.1603
REMARK 3 L33: 2.0097 L12: 0.5223
REMARK 3 L13: 0.2573 L23: 0.8946
REMARK 3 S TENSOR
REMARK 3 S11: 0.0149 S12: 0.0357 S13: -0.0354
REMARK 3 S21: -0.0674 S22: 0.1122 S23: 0.3793
REMARK 3 S31: -0.0779 S32: -0.4700 S33: -0.1223
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 29 THROUGH 109 )
REMARK 3 ORIGIN FOR THE GROUP (A): 52.2995 75.3615 32.9097
REMARK 3 T TENSOR
REMARK 3 T11: 0.2168 T22: 0.1574
REMARK 3 T33: 0.1293 T12: -0.0187
REMARK 3 T13: 0.0273 T23: -0.0128
REMARK 3 L TENSOR
REMARK 3 L11: 1.2147 L22: 1.1847
REMARK 3 L33: 1.6603 L12: -0.1968
REMARK 3 L13: 0.0708 L23: -0.1802
REMARK 3 S TENSOR
REMARK 3 S11: 0.0595 S12: -0.1536 S13: 0.1308
REMARK 3 S21: 0.2857 S22: -0.0023 S23: -0.0522
REMARK 3 S31: -0.3044 S32: 0.0858 S33: -0.0501
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 110 THROUGH 229 )
REMARK 3 ORIGIN FOR THE GROUP (A): 46.3350 65.8877 17.3892
REMARK 3 T TENSOR
REMARK 3 T11: 0.1367 T22: 0.0977
REMARK 3 T33: 0.1352 T12: -0.0080
REMARK 3 T13: 0.0020 T23: 0.0208
REMARK 3 L TENSOR
REMARK 3 L11: 1.3403 L22: 0.7543
REMARK 3 L33: 1.5906 L12: 0.0112
REMARK 3 L13: -0.0752 L23: -0.4466
REMARK 3 S TENSOR
REMARK 3 S11: -0.0660 S12: -0.0583 S13: -0.1456
REMARK 3 S21: 0.0010 S22: 0.0926 S23: 0.0762
REMARK 3 S31: 0.1602 S32: -0.0977 S33: -0.0165
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 230 THROUGH 292 )
REMARK 3 ORIGIN FOR THE GROUP (A): 58.9007 95.2789 23.1799
REMARK 3 T TENSOR
REMARK 3 T11: 0.3295 T22: 0.2819
REMARK 3 T33: 0.2746 T12: -0.0442
REMARK 3 T13: 0.0990 T23: -0.0873
REMARK 3 L TENSOR
REMARK 3 L11: 0.6704 L22: 1.6546
REMARK 3 L33: 2.1722 L12: 0.2883
REMARK 3 L13: 0.2160 L23: 1.2103
REMARK 3 S TENSOR
REMARK 3 S11: 0.1714 S12: -0.3829 S13: 0.3776
REMARK 3 S21: 0.3134 S22: -0.1873 S23: 0.2300
REMARK 3 S31: -0.3874 S32: -0.2086 S33: 0.0319
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 293 THROUGH 382 )
REMARK 3 ORIGIN FOR THE GROUP (A): 54.6404 77.3035 5.5157
REMARK 3 T TENSOR
REMARK 3 T11: 0.1312 T22: 0.1330
REMARK 3 T33: 0.1266 T12: 0.0162
REMARK 3 T13: 0.0016 T23: 0.0136
REMARK 3 L TENSOR
REMARK 3 L11: 1.8355 L22: 0.7439
REMARK 3 L33: 1.2787 L12: 0.8739
REMARK 3 L13: -0.1588 L23: -0.0461
REMARK 3 S TENSOR
REMARK 3 S11: -0.0312 S12: 0.0682 S13: -0.0387
REMARK 3 S21: -0.0278 S22: 0.0895 S23: 0.0176
REMARK 3 S31: -0.0728 S32: 0.0450 S33: -0.0499
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 5BPL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-MAY-15.
REMARK 100 THE DEPOSITION ID IS D_1000210145.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-OCT-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0 - 7.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9184
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31889
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.930
REMARK 200 RESOLUTION RANGE LOW (A) : 47.530
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.14100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.93
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.2
REMARK 200 DATA REDUNDANCY IN SHELL : 5.50
REMARK 200 R MERGE FOR SHELL (I) : 0.84300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP 11.0
REMARK 200 STARTING MODEL: 3ATV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25 % PEG-3350 W/V, 0.1 M HEPES, PH
REMARK 280 7.5, VAPOR DIFFUSION, HANGING 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 23.01850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 71.89900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.66350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 71.89900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.01850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.66350
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -73.0 KCAL/MOL
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; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 ASP A 383
REMARK 465 LYS A 384
REMARK 465 SER A 385
REMARK 465 GLU A 386
REMARK 465 ASN A 387
REMARK 465 VAL A 388
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 LEU A 61 CD1
REMARK 470 ARG A 247 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 250 CG CD CE NZ
REMARK 470 GLN A 279 CG CD OE1 NE2
REMARK 470 LEU A 282 CD1
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 O HOH A 743 O HOH A 846 2.09
REMARK 500 O HOH A 632 O HOH A 790 2.10
REMARK 500 O HOH A 768 O HOH A 794 2.13
REMARK 500 O HOH A 626 O HOH A 762 2.17
REMARK 500 NH1 ARG A 262 O HOH A 501 2.17
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 GLN A 22 147.00 -170.78
REMARK 500 ASN A 62 52.84 -141.40
REMARK 500 LYS A 361 13.85 -140.01
REMARK 500 ASN A 364 118.86 -37.88
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 NA A 406 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 10 OD2
REMARK 620 2 TYR A 15 O 116.9
REMARK 620 3 ADP A 401 O2B 134.0 96.1
REMARK 620 4 HOH A 545 O 76.8 110.4 61.4
REMARK 620 5 HOH A 567 O 84.3 158.1 63.1 67.0
REMARK 620 6 HOH A 644 O 93.4 86.2 121.4 163.1 98.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 407 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 204 OG1
REMARK 620 2 ADP A 401 O1B 133.2
REMARK 620 3 PO4 A 402 O4 48.8 111.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 405 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP A 401 O2B
REMARK 620 2 PO4 A 402 O1 99.0
REMARK 620 3 HOH A 533 O 170.7 89.6
REMARK 620 4 HOH A 545 O 85.2 94.8 90.4
REMARK 620 5 HOH A 559 O 96.3 85.0 88.0 178.4
REMARK 620 6 HOH A 567 O 75.1 166.6 97.2 96.6 83.8
REMARK 620 N 1 2 3 4 5
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 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EPE A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 409
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5BN8 RELATED DB: PDB
REMARK 900 5BN8 CONTAINS THE SAME PROTEIN IN APO STATE.
REMARK 900 RELATED ID: 5BN9 RELATED DB: PDB
REMARK 900 5BN9 CONTAINS THE SAME PROTEIN SINGLE MUTANT (R272K) COMPLEXED WITH
REMARK 900 ADP.
REMARK 900 RELATED ID: 5BPM RELATED DB: PDB
REMARK 900 5BPM CONTAINS THE SAME PROTEIN DOUBLE MUTANT (E268Q+R272K)
REMARK 900 COMPLEXED WITH UNHYDROLYSED ATP.
REMARK 900 RELATED ID: 5BPN RELATED DB: PDB
REMARK 900 5BPN CONTAINS THE SAME PROTEIN DOUBLE MUTANT (E268Q+R272K) IN APO
REMARK 900 STATE.
DBREF 5BPL A 1 388 UNP P0DMV8 HS71A_HUMAN 1 388
SEQADV 5BPL LYS A 272 UNP P0DMV8 ARG 272 ENGINEERED MUTATION
SEQRES 1 A 388 MET ALA LYS ALA ALA ALA ILE GLY ILE ASP LEU GLY THR
SEQRES 2 A 388 THR TYR SER CYS VAL GLY VAL PHE GLN HIS GLY LYS VAL
SEQRES 3 A 388 GLU ILE ILE ALA ASN ASP GLN GLY ASN ARG THR THR PRO
SEQRES 4 A 388 SER TYR VAL ALA PHE THR ASP THR GLU ARG LEU ILE GLY
SEQRES 5 A 388 ASP ALA ALA LYS ASN GLN VAL ALA LEU ASN PRO GLN ASN
SEQRES 6 A 388 THR VAL PHE ASP ALA LYS ARG LEU ILE GLY ARG LYS PHE
SEQRES 7 A 388 GLY ASP PRO VAL VAL GLN SER ASP MET LYS HIS TRP PRO
SEQRES 8 A 388 PHE GLN VAL ILE ASN ASP GLY ASP LYS PRO LYS VAL GLN
SEQRES 9 A 388 VAL SER TYR LYS GLY GLU THR LYS ALA PHE TYR PRO GLU
SEQRES 10 A 388 GLU ILE SER SER MET VAL LEU THR LYS MET LYS GLU ILE
SEQRES 11 A 388 ALA GLU ALA TYR LEU GLY TYR PRO VAL THR ASN ALA VAL
SEQRES 12 A 388 ILE THR VAL PRO ALA TYR PHE ASN ASP SER GLN ARG GLN
SEQRES 13 A 388 ALA THR LYS ASP ALA GLY VAL ILE ALA GLY LEU ASN VAL
SEQRES 14 A 388 LEU ARG ILE ILE ASN GLU PRO THR ALA ALA ALA ILE ALA
SEQRES 15 A 388 TYR GLY LEU ASP ARG THR GLY LYS GLY GLU ARG ASN VAL
SEQRES 16 A 388 LEU ILE PHE ASP LEU GLY GLY GLY THR PHE ASP VAL SER
SEQRES 17 A 388 ILE LEU THR ILE ASP ASP GLY ILE PHE GLU VAL LYS ALA
SEQRES 18 A 388 THR ALA GLY ASP THR HIS LEU GLY GLY GLU ASP PHE ASP
SEQRES 19 A 388 ASN ARG LEU VAL ASN HIS PHE VAL GLU GLU PHE LYS ARG
SEQRES 20 A 388 LYS HIS LYS LYS ASP ILE SER GLN ASN LYS ARG ALA VAL
SEQRES 21 A 388 ARG ARG LEU ARG THR ALA CYS GLU ARG ALA LYS LYS THR
SEQRES 22 A 388 LEU SER SER SER THR GLN ALA SER LEU GLU ILE ASP SER
SEQRES 23 A 388 LEU PHE GLU GLY ILE ASP PHE TYR THR SER ILE THR ARG
SEQRES 24 A 388 ALA ARG PHE GLU GLU LEU CYS SER ASP LEU PHE ARG SER
SEQRES 25 A 388 THR LEU GLU PRO VAL GLU LYS ALA LEU ARG ASP ALA LYS
SEQRES 26 A 388 LEU ASP LYS ALA GLN ILE HIS ASP LEU VAL LEU VAL GLY
SEQRES 27 A 388 GLY SER THR ARG ILE PRO LYS VAL GLN LYS LEU LEU GLN
SEQRES 28 A 388 ASP PHE PHE ASN GLY ARG ASP LEU ASN LYS SER ILE ASN
SEQRES 29 A 388 PRO ASP GLU ALA VAL ALA TYR GLY ALA ALA VAL GLN ALA
SEQRES 30 A 388 ALA ILE LEU MET GLY ASP LYS SER GLU ASN VAL
HET ADP A 401 39
HET PO4 A 402 5
HET PO4 A 403 5
HET PO4 A 404 5
HET MG A 405 1
HET NA A 406 1
HET NA A 407 1
HET EPE A 408 32
HET CL A 409 1
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM PO4 PHOSPHATE ION
HETNAM MG MAGNESIUM ION
HETNAM NA SODIUM ION
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETNAM CL CHLORIDE ION
HETSYN EPE HEPES
FORMUL 2 ADP C10 H15 N5 O10 P2
FORMUL 3 PO4 3(O4 P 3-)
FORMUL 6 MG MG 2+
FORMUL 7 NA 2(NA 1+)
FORMUL 9 EPE C8 H18 N2 O4 S
FORMUL 10 CL CL 1-
FORMUL 11 HOH *352(H2 O)
HELIX 1 AA1 GLY A 52 GLN A 58 1 7
HELIX 2 AA2 ASP A 69 LEU A 73 5 5
HELIX 3 AA3 ASP A 80 LYS A 88 1 9
HELIX 4 AA4 TYR A 115 GLY A 136 1 22
HELIX 5 AA5 ASN A 151 ALA A 165 1 15
HELIX 6 AA6 GLU A 175 TYR A 183 1 9
HELIX 7 AA7 GLY A 184 THR A 188 5 5
HELIX 8 AA8 GLY A 229 LYS A 250 1 22
HELIX 9 AA9 ASN A 256 LEU A 274 1 19
HELIX 10 AB1 ARG A 299 CYS A 306 1 8
HELIX 11 AB2 CYS A 306 SER A 312 1 7
HELIX 12 AB3 THR A 313 ALA A 324 1 12
HELIX 13 AB4 ASP A 327 ILE A 331 5 5
HELIX 14 AB5 GLY A 338 ARG A 342 5 5
HELIX 15 AB6 ILE A 343 PHE A 354 1 12
HELIX 16 AB7 GLU A 367 GLY A 382 1 16
SHEET 1 AA1 3 LYS A 25 ILE A 28 0
SHEET 2 AA1 3 TYR A 15 GLN A 22 -1 N GLN A 22 O LYS A 25
SHEET 3 AA1 3 THR A 38 PRO A 39 -1 O THR A 38 N SER A 16
SHEET 1 AA2 5 LYS A 25 ILE A 28 0
SHEET 2 AA2 5 TYR A 15 GLN A 22 -1 N GLN A 22 O LYS A 25
SHEET 3 AA2 5 ILE A 7 ASP A 10 -1 N ASP A 10 O CYS A 17
SHEET 4 AA2 5 ASN A 141 VAL A 146 1 O VAL A 143 N ILE A 9
SHEET 5 AA2 5 ASN A 168 ASN A 174 1 O LEU A 170 N ALA A 142
SHEET 1 AA3 3 ARG A 49 ILE A 51 0
SHEET 2 AA3 3 VAL A 42 PHE A 44 -1 N ALA A 43 O LEU A 50
SHEET 3 AA3 3 THR A 66 VAL A 67 -1 O VAL A 67 N VAL A 42
SHEET 1 AA4 3 GLN A 93 ASN A 96 0
SHEET 2 AA4 3 PRO A 101 TYR A 107 -1 O LYS A 102 N ILE A 95
SHEET 3 AA4 3 GLU A 110 PHE A 114 -1 O GLU A 110 N TYR A 107
SHEET 1 AA5 4 ILE A 216 ASP A 225 0
SHEET 2 AA5 4 PHE A 205 ASP A 213 -1 N VAL A 207 O ALA A 223
SHEET 3 AA5 4 ARG A 193 LEU A 200 -1 N ILE A 197 O SER A 208
SHEET 4 AA5 4 ASP A 333 VAL A 337 1 O ASP A 333 N LEU A 196
SHEET 1 AA6 2 GLN A 279 PHE A 288 0
SHEET 2 AA6 2 ILE A 291 THR A 298 -1 O PHE A 293 N ILE A 284
LINK OD2 ASP A 10 NA NA A 406 1555 1555 2.24
LINK O TYR A 15 NA NA A 406 1555 1555 2.58
LINK OG1 THR A 204 NA NA A 407 1555 1555 3.08
LINK O2B ADP A 401 MG MG A 405 1555 1555 2.11
LINK O2B ADP A 401 NA NA A 406 1555 1555 2.32
LINK O1B ADP A 401 NA NA A 407 1555 1555 2.45
LINK O1 PO4 A 402 MG MG A 405 1555 1555 2.15
LINK O4 PO4 A 402 NA NA A 407 1555 1555 2.75
LINK MG MG A 405 O HOH A 533 1555 1555 2.15
LINK MG MG A 405 O HOH A 545 1555 1555 2.17
LINK MG MG A 405 O HOH A 559 1555 1555 2.13
LINK MG MG A 405 O HOH A 567 1555 1555 2.16
LINK NA NA A 406 O HOH A 545 1555 1555 3.17
LINK NA NA A 406 O HOH A 567 1555 1555 2.63
LINK NA NA A 406 O HOH A 644 1555 1555 2.43
SITE 1 AC1 26 THR A 13 THR A 14 TYR A 15 GLY A 201
SITE 2 AC1 26 GLY A 202 GLY A 230 GLU A 268 LYS A 271
SITE 3 AC1 26 LYS A 272 SER A 275 GLY A 338 GLY A 339
SITE 4 AC1 26 SER A 340 ARG A 342 ASP A 366 PO4 A 402
SITE 5 AC1 26 MG A 405 NA A 406 NA A 407 HOH A 542
SITE 6 AC1 26 HOH A 544 HOH A 545 HOH A 567 HOH A 627
SITE 7 AC1 26 HOH A 644 HOH A 687
SITE 1 AC2 13 GLY A 12 THR A 13 LYS A 71 GLU A 175
SITE 2 AC2 13 THR A 204 ADP A 401 MG A 405 NA A 407
SITE 3 AC2 13 CL A 409 HOH A 533 HOH A 534 HOH A 545
SITE 4 AC2 13 HOH A 559
SITE 1 AC3 5 LEU A 50 ILE A 51 ALA A 54 LYS A 126
SITE 2 AC3 5 HOH A 710
SITE 1 AC4 4 GLU A 304 SER A 307 ASP A 308 HOH A 516
SITE 1 AC5 7 ADP A 401 PO4 A 402 NA A 406 HOH A 533
SITE 2 AC5 7 HOH A 545 HOH A 559 HOH A 567
SITE 1 AC6 6 ASP A 10 TYR A 15 ADP A 401 MG A 405
SITE 2 AC6 6 HOH A 567 HOH A 644
SITE 1 AC7 5 GLY A 202 GLY A 203 THR A 204 ADP A 401
SITE 2 AC7 5 PO4 A 402
SITE 1 AC8 8 ASN A 57 GLN A 58 LEU A 61 TYR A 115
SITE 2 AC8 8 GLU A 117 ARG A 258 HOH A 646 HOH A 733
SITE 1 AC9 4 ASP A 199 THR A 204 ASP A 206 PO4 A 402
CRYST1 46.037 63.327 143.798 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 0.021722 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015791 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006954 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
