HEADER CHAPERONE 14-JAN-18 6FHK
TITLE STRUCTURE OF A MODIFIED PROTEIN CONTAINING A GENETICALLY ENCODED
TITLE 2 PHOSPHOSERINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEAT SHOCK 70 KDA PROTEIN 1A;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: HEAT SHOCK 70 KDA PROTEIN 1,HSP70.1;
COMPND 5 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: HSPA1A, HSP72, HSPA1, HSX70;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CHAPERONE, PHOSPHOSERINE, ADP
EXPDTA X-RAY DIFFRACTION
AUTHOR M.MUKHERJEE,R.BAYLISS
REVDAT 2 17-JAN-24 6FHK 1 LINK
REVDAT 1 24-OCT-18 6FHK 0
JRNL AUTH M.MUKHERJEE,S.SABIR,L.O'REGAN,J.SAMPSON,M.W.RICHARDS,
JRNL AUTH 2 N.HUGUENIN-DEZOT,J.R.AULT,J.W.CHIN,A.ZHURAVLEVA,A.M.FRY,
JRNL AUTH 3 R.BAYLISS
JRNL TITL MITOTIC PHOSPHORYLATION REGULATES HSP72 SPINDLE LOCALIZATION
JRNL TITL 2 BY UNCOUPLING ATP BINDING FROM SUBSTRATE RELEASE.
JRNL REF SCI SIGNAL V. 11 2018
JRNL REFN ESSN 1937-9145
JRNL PMID 30108182
JRNL DOI 10.1126/SCISIGNAL.AAO2464
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.MUKHERJEE,S.SABIR,L.O'REGAN,J.SAMPSON,M.W.RICHARDS,
REMARK 1 AUTH 2 N.HUGUENIN-DEZOT,J.R.AULT,J.W.CHIN,A.ZHURAVLEVA,A.M.FRY,
REMARK 1 AUTH 3 R.BAYLISS
REMARK 1 TITL MITOTIC PHOSPHORYLATION REGULATES HSP72 SPINDLE LOCALIZATION
REMARK 1 TITL 2 BY UNCOUPLING ATP BINDING FROM SUBSTRATE RELEASE.
REMARK 1 REF SCI SIGNAL V. 11 2018
REMARK 1 REFN ESSN 1937-9145
REMARK 1 PMID 30108182
REMARK 1 DOI 10.1126/SCISIGNAL.AAO2464
REMARK 2
REMARK 2 RESOLUTION. 1.66 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.1_1168
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) : 1.66
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 55.09
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 83150
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.162
REMARK 3 FREE R VALUE : 0.194
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980
REMARK 3 FREE R VALUE TEST SET COUNT : 4139
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 55.1212 - 5.1471 0.99 2716 147 0.1659 0.1802
REMARK 3 2 5.1471 - 4.0858 1.00 2705 134 0.1449 0.1601
REMARK 3 3 4.0858 - 3.5694 1.00 2711 118 0.1420 0.1542
REMARK 3 4 3.5694 - 3.2431 1.00 2664 156 0.1551 0.1744
REMARK 3 5 3.2431 - 3.0107 1.00 2688 148 0.1667 0.1856
REMARK 3 6 3.0107 - 2.8332 1.00 2653 158 0.1718 0.1966
REMARK 3 7 2.8332 - 2.6913 1.00 2710 122 0.1674 0.2140
REMARK 3 8 2.6913 - 2.5741 1.00 2658 150 0.1634 0.2095
REMARK 3 9 2.5741 - 2.4750 1.00 2689 128 0.1685 0.2035
REMARK 3 10 2.4750 - 2.3896 1.00 2675 158 0.1605 0.2196
REMARK 3 11 2.3896 - 2.3149 1.00 2658 142 0.1556 0.2017
REMARK 3 12 2.3149 - 2.2487 1.00 2654 149 0.1584 0.2027
REMARK 3 13 2.2487 - 2.1895 1.00 2678 146 0.1528 0.2092
REMARK 3 14 2.1895 - 2.1361 1.00 2651 154 0.1555 0.1986
REMARK 3 15 2.1361 - 2.0876 1.00 2656 153 0.1579 0.2151
REMARK 3 16 2.0876 - 2.0431 1.00 2673 144 0.1710 0.2113
REMARK 3 17 2.0431 - 2.0023 1.00 2664 113 0.1628 0.2216
REMARK 3 18 2.0023 - 1.9645 1.00 2678 148 0.1687 0.1982
REMARK 3 19 1.9645 - 1.9294 1.00 2723 102 0.1643 0.1951
REMARK 3 20 1.9294 - 1.8967 0.83 2199 128 0.1926 0.2276
REMARK 3 21 1.8967 - 1.8661 1.00 2666 131 0.1662 0.1983
REMARK 3 22 1.8661 - 1.8374 1.00 2675 131 0.1629 0.2260
REMARK 3 23 1.8374 - 1.8103 0.99 2625 155 0.1676 0.2186
REMARK 3 24 1.8103 - 1.7848 0.99 2638 143 0.1742 0.2226
REMARK 3 25 1.7848 - 1.7607 0.99 2635 166 0.1820 0.2535
REMARK 3 26 1.7607 - 1.7379 0.99 2680 123 0.1965 0.2187
REMARK 3 27 1.7379 - 1.7161 0.99 2616 139 0.2089 0.2828
REMARK 3 28 1.7161 - 1.6955 0.97 2654 114 0.2170 0.2660
REMARK 3 29 1.6955 - 1.6757 0.92 2403 125 0.2180 0.2681
REMARK 3 30 1.6757 - 1.6569 0.85 2316 114 0.2128 0.2466
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) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.180
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 : 0.010 6036
REMARK 3 ANGLE : 1.394 8172
REMARK 3 CHIRALITY : 0.094 924
REMARK 3 PLANARITY : 0.006 1060
REMARK 3 DIHEDRAL : 14.056 2240
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 14.6467 6.5478 79.3449
REMARK 3 T TENSOR
REMARK 3 T11: 0.0997 T22: 0.1277
REMARK 3 T33: 0.1355 T12: -0.0051
REMARK 3 T13: -0.0055 T23: 0.0140
REMARK 3 L TENSOR
REMARK 3 L11: 0.0894 L22: 0.3566
REMARK 3 L33: 0.4534 L12: -0.0712
REMARK 3 L13: -0.0710 L23: 0.2556
REMARK 3 S TENSOR
REMARK 3 S11: 0.0072 S12: -0.0010 S13: 0.0033
REMARK 3 S21: 0.0027 S22: 0.0054 S23: -0.0139
REMARK 3 S31: 0.0083 S32: 0.0094 S33: -0.0157
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 6FHK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-JAN-18.
REMARK 100 THE DEPOSITION ID IS D_1200008328.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-JUN-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
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 : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 83152
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.657
REMARK 200 RESOLUTION RANGE LOW (A) : 55.090
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.66
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
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 <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: PHASER
REMARK 200 STARTING MODEL: 3AY9
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SUCCINIC ACID PH 7.0, 15% W/V
REMARK 280 POLYETHYLENE GLYCOL 3,350, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 55.43800
REMARK 290 SMTRY3 2 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 MET A 1
REMARK 465 ALA A 2
REMARK 465 LYS A 3
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 LYS B 3
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 OD2 ASP A 323 O HOH A 501 2.11
REMARK 500 OD1 ASP B 32 O HOH B 501 2.18
REMARK 500 NZ LYS B 325 O HOH B 502 2.19
REMARK 500 O HOH A 695 O HOH A 746 2.19
REMARK 500 O HOH A 599 O HOH A 751 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 775 O HOH B 518 1554 2.10
REMARK 500 O HOH A 775 O HOH B 710 1554 2.11
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 ARG A 187 36.04 -87.45
REMARK 500 PHE A 354 30.37 -96.16
REMARK 500 LYS A 361 13.94 -149.17
REMARK 500 VAL B 59 79.01 -109.89
REMARK 500 ARG B 171 148.26 -170.19
REMARK 500 THR B 188 -18.27 -157.07
REMARK 500 PHE B 288 -97.02 -120.96
REMARK 500 GLU B 289 -109.35 -78.12
REMARK 500 LYS B 361 16.07 -142.48
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY B 189 LYS B 190 -144.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 775 DISTANCE = 6.22 ANGSTROMS
REMARK 525 HOH B 776 DISTANCE = 7.44 ANGSTROMS
REMARK 525 HOH B 777 DISTANCE = 10.40 ANGSTROMS
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 K A 404 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 10 OD2
REMARK 620 2 TYR A 15 O 119.6
REMARK 620 3 ADP A 401 O1B 120.4 102.7
REMARK 620 4 ADP A 401 O3A 157.7 82.4 51.8
REMARK 620 5 HOH A 556 O 70.2 113.0 54.7 106.5
REMARK 620 6 HOH A 585 O 71.0 166.5 63.8 87.9 60.9
REMARK 620 7 HOH A 598 O 92.9 92.3 127.3 81.5 154.1 95.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 403 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP A 401 O1B
REMARK 620 2 PO4 A 402 O3 100.7
REMARK 620 3 HOH A 519 O 169.1 89.8
REMARK 620 4 HOH A 556 O 88.5 89.4 88.6
REMARK 620 5 HOH A 585 O 79.8 173.4 90.1 97.3
REMARK 620 6 HOH A 602 O 92.7 91.7 89.9 178.2 81.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B 404 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 10 OD1
REMARK 620 2 ASP B 10 OD2 38.9
REMARK 620 3 TYR B 15 O 99.9 121.0
REMARK 620 4 ADP B 401 O3B 99.6 120.7 101.9
REMARK 620 5 ADP B 401 O3A 150.6 156.2 82.3 51.8
REMARK 620 6 HOH B 548 O 80.3 68.7 164.2 62.7 90.0
REMARK 620 7 HOH B 579 O 128.5 92.6 92.4 126.5 80.4 99.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 403 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP B 401 O3B
REMARK 620 2 PO4 B 402 O2 98.9
REMARK 620 3 HOH B 520 O 172.6 86.1
REMARK 620 4 HOH B 540 O 89.0 86.4 85.9
REMARK 620 5 HOH B 548 O 82.0 179.1 93.0 93.6
REMARK 620 6 HOH B 566 O 92.2 90.6 93.3 176.9 89.5
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 MG A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ADP B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K B 404
DBREF 6FHK A 1 381 UNP P0DMV8 HS71A_HUMAN 1 381
DBREF 6FHK B 1 381 UNP P0DMV8 HS71A_HUMAN 1 381
SEQRES 1 A 381 MET ALA LYS ALA ALA ALA ILE GLY ILE ASP LEU GLY THR
SEQRES 2 A 381 THR TYR SER CYS VAL GLY VAL PHE GLN HIS GLY LYS VAL
SEQRES 3 A 381 GLU ILE ILE ALA ASN ASP GLN GLY ASN ARG THR THR PRO
SEQRES 4 A 381 SER TYR VAL ALA PHE THR ASP THR GLU ARG LEU ILE GLY
SEQRES 5 A 381 ASP ALA ALA LYS ASN GLN VAL ALA LEU ASN PRO GLN ASN
SEQRES 6 A 381 SEP VAL PHE ASP ALA LYS ARG LEU ILE GLY ARG LYS PHE
SEQRES 7 A 381 GLY ASP PRO VAL VAL GLN SER ASP MET LYS HIS TRP PRO
SEQRES 8 A 381 PHE GLN VAL ILE ASN ASP GLY ASP LYS PRO LYS VAL GLN
SEQRES 9 A 381 VAL SER TYR LYS GLY GLU THR LYS ALA PHE TYR PRO GLU
SEQRES 10 A 381 GLU ILE SER SER MET VAL LEU THR LYS MET LYS GLU ILE
SEQRES 11 A 381 ALA GLU ALA TYR LEU GLY TYR PRO VAL THR ASN ALA VAL
SEQRES 12 A 381 ILE THR VAL PRO ALA TYR PHE ASN ASP SER GLN ARG GLN
SEQRES 13 A 381 ALA THR LYS ASP ALA GLY VAL ILE ALA GLY LEU ASN VAL
SEQRES 14 A 381 LEU ARG ILE ILE ASN GLU PRO THR ALA ALA ALA ILE ALA
SEQRES 15 A 381 TYR GLY LEU ASP ARG THR GLY LYS GLY GLU ARG ASN VAL
SEQRES 16 A 381 LEU ILE PHE ASP LEU GLY GLY GLY THR PHE ASP VAL SER
SEQRES 17 A 381 ILE LEU THR ILE ASP ASP GLY ILE PHE GLU VAL LYS ALA
SEQRES 18 A 381 THR ALA GLY ASP THR HIS LEU GLY GLY GLU ASP PHE ASP
SEQRES 19 A 381 ASN ARG LEU VAL ASN HIS PHE VAL GLU GLU PHE LYS ARG
SEQRES 20 A 381 LYS HIS LYS LYS ASP ILE SER GLN ASN LYS ARG ALA VAL
SEQRES 21 A 381 ARG ARG LEU ARG THR ALA CYS GLU ARG ALA LYS ARG THR
SEQRES 22 A 381 LEU SER SER SER THR GLN ALA SER LEU GLU ILE ASP SER
SEQRES 23 A 381 LEU PHE GLU GLY ILE ASP PHE TYR THR SER ILE THR ARG
SEQRES 24 A 381 ALA ARG PHE GLU GLU LEU CYS SER ASP LEU PHE ARG SER
SEQRES 25 A 381 THR LEU GLU PRO VAL GLU LYS ALA LEU ARG ASP ALA LYS
SEQRES 26 A 381 LEU ASP LYS ALA GLN ILE HIS ASP LEU VAL LEU VAL GLY
SEQRES 27 A 381 GLY SER THR ARG ILE PRO LYS VAL GLN LYS LEU LEU GLN
SEQRES 28 A 381 ASP PHE PHE ASN GLY ARG ASP LEU ASN LYS SER ILE ASN
SEQRES 29 A 381 PRO ASP GLU ALA VAL ALA TYR GLY ALA ALA VAL GLN ALA
SEQRES 30 A 381 ALA ILE LEU MET
SEQRES 1 B 381 MET ALA LYS ALA ALA ALA ILE GLY ILE ASP LEU GLY THR
SEQRES 2 B 381 THR TYR SER CYS VAL GLY VAL PHE GLN HIS GLY LYS VAL
SEQRES 3 B 381 GLU ILE ILE ALA ASN ASP GLN GLY ASN ARG THR THR PRO
SEQRES 4 B 381 SER TYR VAL ALA PHE THR ASP THR GLU ARG LEU ILE GLY
SEQRES 5 B 381 ASP ALA ALA LYS ASN GLN VAL ALA LEU ASN PRO GLN ASN
SEQRES 6 B 381 SEP VAL PHE ASP ALA LYS ARG LEU ILE GLY ARG LYS PHE
SEQRES 7 B 381 GLY ASP PRO VAL VAL GLN SER ASP MET LYS HIS TRP PRO
SEQRES 8 B 381 PHE GLN VAL ILE ASN ASP GLY ASP LYS PRO LYS VAL GLN
SEQRES 9 B 381 VAL SER TYR LYS GLY GLU THR LYS ALA PHE TYR PRO GLU
SEQRES 10 B 381 GLU ILE SER SER MET VAL LEU THR LYS MET LYS GLU ILE
SEQRES 11 B 381 ALA GLU ALA TYR LEU GLY TYR PRO VAL THR ASN ALA VAL
SEQRES 12 B 381 ILE THR VAL PRO ALA TYR PHE ASN ASP SER GLN ARG GLN
SEQRES 13 B 381 ALA THR LYS ASP ALA GLY VAL ILE ALA GLY LEU ASN VAL
SEQRES 14 B 381 LEU ARG ILE ILE ASN GLU PRO THR ALA ALA ALA ILE ALA
SEQRES 15 B 381 TYR GLY LEU ASP ARG THR GLY LYS GLY GLU ARG ASN VAL
SEQRES 16 B 381 LEU ILE PHE ASP LEU GLY GLY GLY THR PHE ASP VAL SER
SEQRES 17 B 381 ILE LEU THR ILE ASP ASP GLY ILE PHE GLU VAL LYS ALA
SEQRES 18 B 381 THR ALA GLY ASP THR HIS LEU GLY GLY GLU ASP PHE ASP
SEQRES 19 B 381 ASN ARG LEU VAL ASN HIS PHE VAL GLU GLU PHE LYS ARG
SEQRES 20 B 381 LYS HIS LYS LYS ASP ILE SER GLN ASN LYS ARG ALA VAL
SEQRES 21 B 381 ARG ARG LEU ARG THR ALA CYS GLU ARG ALA LYS ARG THR
SEQRES 22 B 381 LEU SER SER SER THR GLN ALA SER LEU GLU ILE ASP SER
SEQRES 23 B 381 LEU PHE GLU GLY ILE ASP PHE TYR THR SER ILE THR ARG
SEQRES 24 B 381 ALA ARG PHE GLU GLU LEU CYS SER ASP LEU PHE ARG SER
SEQRES 25 B 381 THR LEU GLU PRO VAL GLU LYS ALA LEU ARG ASP ALA LYS
SEQRES 26 B 381 LEU ASP LYS ALA GLN ILE HIS ASP LEU VAL LEU VAL GLY
SEQRES 27 B 381 GLY SER THR ARG ILE PRO LYS VAL GLN LYS LEU LEU GLN
SEQRES 28 B 381 ASP PHE PHE ASN GLY ARG ASP LEU ASN LYS SER ILE ASN
SEQRES 29 B 381 PRO ASP GLU ALA VAL ALA TYR GLY ALA ALA VAL GLN ALA
SEQRES 30 B 381 ALA ILE LEU MET
MODRES 6FHK SEP A 66 THR MODIFIED RESIDUE
MODRES 6FHK SEP B 66 THR MODIFIED RESIDUE
HET SEP A 66 10
HET SEP B 66 10
HET ADP A 401 27
HET PO4 A 402 5
HET MG A 403 1
HET K A 404 1
HET ADP B 401 27
HET PO4 B 402 5
HET MG B 403 1
HET K B 404 1
HETNAM SEP PHOSPHOSERINE
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM PO4 PHOSPHATE ION
HETNAM MG MAGNESIUM ION
HETNAM K POTASSIUM ION
HETSYN SEP PHOSPHONOSERINE
FORMUL 1 SEP 2(C3 H8 N O6 P)
FORMUL 3 ADP 2(C10 H15 N5 O10 P2)
FORMUL 4 PO4 2(O4 P 3-)
FORMUL 5 MG 2(MG 2+)
FORMUL 6 K 2(K 1+)
FORMUL 11 HOH *579(H2 O)
HELIX 1 AA1 GLY A 52 ASN A 57 1 6
HELIX 2 AA2 ASN A 62 GLN A 64 5 3
HELIX 3 AA3 ALA A 70 LEU A 73 5 4
HELIX 4 AA4 ASP A 80 LYS A 88 1 9
HELIX 5 AA5 TYR A 115 GLY A 136 1 22
HELIX 6 AA6 ASN A 151 ALA A 165 1 15
HELIX 7 AA7 GLU A 175 TYR A 183 1 9
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 LYS A 325 1 13
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 LEU A 380 1 14
HELIX 17 AB8 GLY B 52 ASN B 57 1 6
HELIX 18 AB9 ASN B 62 GLN B 64 5 3
HELIX 19 AC1 ALA B 70 LEU B 73 5 4
HELIX 20 AC2 ASP B 80 LYS B 88 1 9
HELIX 21 AC3 TYR B 115 GLY B 136 1 22
HELIX 22 AC4 ASN B 151 ALA B 165 1 15
HELIX 23 AC5 GLU B 175 TYR B 183 1 9
HELIX 24 AC6 GLY B 229 LYS B 250 1 22
HELIX 25 AC7 ASN B 256 LEU B 274 1 19
HELIX 26 AC8 ARG B 299 CYS B 306 1 8
HELIX 27 AC9 CYS B 306 SER B 312 1 7
HELIX 28 AD1 THR B 313 LYS B 325 1 13
HELIX 29 AD2 ASP B 327 ILE B 331 5 5
HELIX 30 AD3 GLY B 338 ARG B 342 5 5
HELIX 31 AD4 ILE B 343 PHE B 354 1 12
HELIX 32 AD5 ASN B 364 ASP B 366 5 3
HELIX 33 AD6 GLU B 367 LEU B 380 1 14
SHEET 1 AA1 3 LYS A 25 ILE A 28 0
SHEET 2 AA1 3 TYR A 15 GLN A 22 -1 N VAL A 20 O GLU A 27
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 VAL A 20 O GLU A 27
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 TYR A 41 PHE A 44 -1 N ALA A 43 O LEU A 50
SHEET 3 AA3 3 SEP A 66 PHE A 68 -1 O VAL A 67 N VAL A 42
SHEET 1 AA4 3 GLN A 93 ASP A 97 0
SHEET 2 AA4 3 LYS A 100 TYR A 107 -1 O LYS A 102 N ILE A 95
SHEET 3 AA4 3 GLU A 110 PHE A 114 -1 O LYS A 112 N VAL A 105
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 VAL A 195 O LEU A 210
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 THR A 295 N LEU A 282
SHEET 1 AA7 3 LYS B 25 ILE B 28 0
SHEET 2 AA7 3 TYR B 15 GLN B 22 -1 N VAL B 20 O GLU B 27
SHEET 3 AA7 3 THR B 38 PRO B 39 -1 O THR B 38 N SER B 16
SHEET 1 AA8 5 LYS B 25 ILE B 28 0
SHEET 2 AA8 5 TYR B 15 GLN B 22 -1 N VAL B 20 O GLU B 27
SHEET 3 AA8 5 ILE B 7 ASP B 10 -1 N ASP B 10 O CYS B 17
SHEET 4 AA8 5 ASN B 141 VAL B 146 1 O VAL B 143 N ILE B 9
SHEET 5 AA8 5 ASN B 168 ASN B 174 1 O LEU B 170 N ALA B 142
SHEET 1 AA9 3 ARG B 49 ILE B 51 0
SHEET 2 AA9 3 TYR B 41 PHE B 44 -1 N ALA B 43 O LEU B 50
SHEET 3 AA9 3 SEP B 66 PHE B 68 -1 O VAL B 67 N VAL B 42
SHEET 1 AB1 3 GLN B 93 ASP B 97 0
SHEET 2 AB1 3 LYS B 100 TYR B 107 -1 O LYS B 100 N ASP B 97
SHEET 3 AB1 3 GLU B 110 PHE B 114 -1 O GLU B 110 N TYR B 107
SHEET 1 AB2 4 ILE B 216 ASP B 225 0
SHEET 2 AB2 4 PHE B 205 ASP B 213 -1 N VAL B 207 O ALA B 223
SHEET 3 AB2 4 ARG B 193 LEU B 200 -1 N ILE B 197 O SER B 208
SHEET 4 AB2 4 ASP B 333 VAL B 337 1 O ASP B 333 N LEU B 196
SHEET 1 AB3 2 GLN B 279 ILE B 284 0
SHEET 2 AB3 2 PHE B 293 THR B 298 -1 O PHE B 293 N ILE B 284
LINK C ASN A 65 N SEP A 66 1555 1555 1.33
LINK C SEP A 66 N VAL A 67 1555 1555 1.33
LINK C ASN B 65 N SEP B 66 1555 1555 1.32
LINK C SEP B 66 N VAL B 67 1555 1555 1.33
LINK OD2 ASP A 10 K K A 404 1555 1555 2.42
LINK O TYR A 15 K K A 404 1555 1555 2.46
LINK O1B ADP A 401 MG MG A 403 1555 1555 2.01
LINK O1B ADP A 401 K K A 404 1555 1555 2.33
LINK O3A ADP A 401 K K A 404 1555 1555 3.17
LINK O3 PO4 A 402 MG MG A 403 1555 1555 2.00
LINK MG MG A 403 O HOH A 519 1555 1555 2.14
LINK MG MG A 403 O HOH A 556 1555 1555 2.04
LINK MG MG A 403 O HOH A 585 1555 1555 2.20
LINK MG MG A 403 O HOH A 602 1555 1555 2.08
LINK K K A 404 O HOH A 556 1555 1555 3.43
LINK K K A 404 O HOH A 585 1555 1555 2.74
LINK K K A 404 O HOH A 598 1555 1555 2.40
LINK OD1 ASP B 10 K K B 404 1555 1555 3.49
LINK OD2 ASP B 10 K K B 404 1555 1555 2.45
LINK O TYR B 15 K K B 404 1555 1555 2.43
LINK O3B ADP B 401 MG MG B 403 1555 1555 1.99
LINK O3B ADP B 401 K K B 404 1555 1555 2.41
LINK O3A ADP B 401 K K B 404 1555 1555 3.14
LINK O2 PO4 B 402 MG MG B 403 1555 1555 1.96
LINK MG MG B 403 O HOH B 520 1555 1555 2.08
LINK MG MG B 403 O HOH B 540 1555 1555 2.05
LINK MG MG B 403 O HOH B 548 1555 1555 2.08
LINK MG MG B 403 O HOH B 566 1555 1555 2.05
LINK K K B 404 O HOH B 548 1555 1555 2.70
LINK K K B 404 O HOH B 579 1555 1555 2.41
SITE 1 AC1 28 THR A 13 THR A 14 TYR A 15 GLY A 201
SITE 2 AC1 28 GLY A 202 GLY A 230 GLU A 268 LYS A 271
SITE 3 AC1 28 ARG A 272 SER A 275 GLY A 338 GLY A 339
SITE 4 AC1 28 SER A 340 ARG A 342 ASP A 366 PO4 A 402
SITE 5 AC1 28 MG A 403 K A 404 HOH A 514 HOH A 535
SITE 6 AC1 28 HOH A 556 HOH A 585 HOH A 593 HOH A 598
SITE 7 AC1 28 HOH A 602 HOH A 615 HOH A 701 HOH A 739
SITE 1 AC2 14 GLY A 12 THR A 13 LYS A 71 PRO A 147
SITE 2 AC2 14 GLU A 175 THR A 204 ADP A 401 MG A 403
SITE 3 AC2 14 HOH A 510 HOH A 519 HOH A 535 HOH A 556
SITE 4 AC2 14 HOH A 602 HOH A 636
SITE 1 AC3 7 ADP A 401 PO4 A 402 K A 404 HOH A 519
SITE 2 AC3 7 HOH A 556 HOH A 585 HOH A 602
SITE 1 AC4 6 ASP A 10 TYR A 15 ADP A 401 MG A 403
SITE 2 AC4 6 HOH A 585 HOH A 598
SITE 1 AC5 25 THR B 13 THR B 14 TYR B 15 GLY B 201
SITE 2 AC5 25 GLY B 202 GLY B 230 GLU B 268 LYS B 271
SITE 3 AC5 25 ARG B 272 SER B 275 GLY B 338 GLY B 339
SITE 4 AC5 25 SER B 340 ASP B 366 PO4 B 402 MG B 403
SITE 5 AC5 25 K B 404 HOH B 512 HOH B 536 HOH B 540
SITE 6 AC5 25 HOH B 544 HOH B 548 HOH B 562 HOH B 566
SITE 7 AC5 25 HOH B 579
SITE 1 AC6 14 GLY B 12 THR B 13 LYS B 71 PRO B 147
SITE 2 AC6 14 GLU B 175 THR B 204 ADP B 401 MG B 403
SITE 3 AC6 14 HOH B 505 HOH B 520 HOH B 536 HOH B 540
SITE 4 AC6 14 HOH B 566 HOH B 667
SITE 1 AC7 7 ADP B 401 PO4 B 402 K B 404 HOH B 520
SITE 2 AC7 7 HOH B 540 HOH B 548 HOH B 566
SITE 1 AC8 6 ASP B 10 TYR B 15 ADP B 401 MG B 403
SITE 2 AC8 6 HOH B 548 HOH B 579
CRYST1 51.625 110.876 63.483 90.00 90.41 90.00 P 1 21 1 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 0.019370 0.000000 0.000138 0.00000
SCALE2 0.000000 0.009019 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015753 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
