HEADER CHAPERONE 18-SEP-17 6B1N
TITLE DISRUPTED HYDROGEN BOND NETWORK IMPAIRS ATPASE ACTIVITY IN AN HSC70
TITLE 2 CYSTEINE MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEAT SHOCK PROTEIN FAMILY A (HSP70) MEMBER 8;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_TAXID: 9606;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HSP70 FAMILY MEMBER, CHAPERONE, ATPASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.P.O'DONNELL
REVDAT 4 04-OCT-23 6B1N 1 LINK
REVDAT 3 01-JAN-20 6B1N 1 REMARK
REVDAT 2 28-FEB-18 6B1N 1 JRNL
REVDAT 1 17-JAN-18 6B1N 0
JRNL AUTH J.P.O'DONNELL,H.M.MARSH,H.SONDERMANN,C.S.SEVIER
JRNL TITL DISRUPTED HYDROGEN-BOND NETWORK AND IMPAIRED ATPASE ACTIVITY
JRNL TITL 2 IN AN HSC70 CYSTEINE MUTANT.
JRNL REF BIOCHEMISTRY V. 57 1073 2018
JRNL REFN ISSN 1520-4995
JRNL PMID 29300467
JRNL DOI 10.1021/ACS.BIOCHEM.7B01005
REMARK 2
REMARK 2 RESOLUTION. 1.80 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.05
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 76460
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.290
REMARK 3 FREE R VALUE TEST SET COUNT : 1748
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 37.0555 - 4.1192 0.99 6324 152 0.1650 0.1934
REMARK 3 2 4.1192 - 3.2702 1.00 6307 146 0.1543 0.1711
REMARK 3 3 3.2702 - 2.8570 1.00 6286 145 0.1768 0.2238
REMARK 3 4 2.8570 - 2.5958 1.00 6260 146 0.1773 0.2211
REMARK 3 5 2.5958 - 2.4098 1.00 6259 142 0.1848 0.2349
REMARK 3 6 2.4098 - 2.2678 0.99 6210 146 0.1805 0.2251
REMARK 3 7 2.2678 - 2.1542 0.99 6214 147 0.1752 0.2260
REMARK 3 8 2.1542 - 2.0604 0.99 6229 143 0.1911 0.2418
REMARK 3 9 2.0604 - 1.9811 0.99 6136 136 0.2177 0.2741
REMARK 3 10 1.9811 - 1.9128 0.99 6206 152 0.2287 0.2840
REMARK 3 11 1.9128 - 1.8530 0.99 6159 142 0.2438 0.3029
REMARK 3 12 1.8530 - 1.8000 0.98 6122 151 0.2804 0.3288
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) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.180
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 : 0.012 6052
REMARK 3 ANGLE : 1.193 8201
REMARK 3 CHIRALITY : 0.064 934
REMARK 3 PLANARITY : 0.007 1064
REMARK 3 DIHEDRAL : 14.487 2226
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ( CHAIN A AND RESID 0:119 )
REMARK 3 ORIGIN FOR THE GROUP (A): 62.3591 15.2405 62.4402
REMARK 3 T TENSOR
REMARK 3 T11: 0.1431 T22: 0.0959
REMARK 3 T33: 0.0548 T12: 0.0285
REMARK 3 T13: -0.0135 T23: 0.0134
REMARK 3 L TENSOR
REMARK 3 L11: 2.4923 L22: 1.5675
REMARK 3 L33: 1.7969 L12: 0.7203
REMARK 3 L13: -0.6323 L23: -0.2741
REMARK 3 S TENSOR
REMARK 3 S11: 0.0509 S12: 0.1316 S13: 0.0226
REMARK 3 S21: -0.1776 S22: -0.0674 S23: -0.0996
REMARK 3 S31: 0.0095 S32: 0.1021 S33: 0.0223
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: ( CHAIN A AND RESID 120:231 )
REMARK 3 ORIGIN FOR THE GROUP (A): 50.7656 19.9869 73.9226
REMARK 3 T TENSOR
REMARK 3 T11: 0.1206 T22: 0.1032
REMARK 3 T33: 0.0919 T12: 0.0168
REMARK 3 T13: -0.0335 T23: -0.0034
REMARK 3 L TENSOR
REMARK 3 L11: 0.7562 L22: 1.2814
REMARK 3 L33: 1.4214 L12: -0.0255
REMARK 3 L13: 0.8401 L23: 0.1483
REMARK 3 S TENSOR
REMARK 3 S11: -0.0715 S12: -0.0566 S13: 0.0900
REMARK 3 S21: -0.0075 S22: -0.0232 S23: 0.0920
REMARK 3 S31: -0.0971 S32: -0.1439 S33: 0.0912
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: ( CHAIN A AND RESID 232:381 )
REMARK 3 ORIGIN FOR THE GROUP (A): 67.4271 9.1161 83.3995
REMARK 3 T TENSOR
REMARK 3 T11: 0.1383 T22: 0.0769
REMARK 3 T33: 0.0722 T12: -0.0080
REMARK 3 T13: -0.0449 T23: 0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 0.9867 L22: 1.2313
REMARK 3 L33: 0.5854 L12: -0.6596
REMARK 3 L13: -0.1613 L23: 0.0996
REMARK 3 S TENSOR
REMARK 3 S11: -0.0638 S12: -0.0428 S13: 0.0537
REMARK 3 S21: 0.0761 S22: 0.0388 S23: -0.1102
REMARK 3 S31: 0.0305 S32: 0.0281 S33: 0.0106
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: ( CHAIN B AND RESID 0:126 )
REMARK 3 ORIGIN FOR THE GROUP (A): 100.4274 24.5739 110.6647
REMARK 3 T TENSOR
REMARK 3 T11: 0.1127 T22: 0.1052
REMARK 3 T33: 0.1586 T12: -0.0081
REMARK 3 T13: -0.0455 T23: 0.0488
REMARK 3 L TENSOR
REMARK 3 L11: 2.2257 L22: 1.7802
REMARK 3 L33: 2.4839 L12: -0.6203
REMARK 3 L13: -0.4890 L23: 0.4761
REMARK 3 S TENSOR
REMARK 3 S11: 0.0253 S12: 0.0949 S13: 0.0258
REMARK 3 S21: -0.0191 S22: -0.1348 S23: -0.3018
REMARK 3 S31: -0.0033 S32: 0.2160 S33: 0.0648
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: ( CHAIN B AND RESID 127:231 )
REMARK 3 ORIGIN FOR THE GROUP (A): 85.1858 19.1402 119.1252
REMARK 3 T TENSOR
REMARK 3 T11: 0.1522 T22: 0.0979
REMARK 3 T33: 0.0993 T12: -0.0173
REMARK 3 T13: -0.0494 T23: 0.0191
REMARK 3 L TENSOR
REMARK 3 L11: 0.9152 L22: 1.1569
REMARK 3 L33: 0.6946 L12: -0.1372
REMARK 3 L13: 0.4645 L23: -0.1745
REMARK 3 S TENSOR
REMARK 3 S11: 0.0117 S12: -0.0961 S13: -0.0440
REMARK 3 S21: 0.1182 S22: -0.0163 S23: -0.0088
REMARK 3 S31: 0.0607 S32: -0.0525 S33: -0.0340
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: ( CHAIN B AND RESID 232:381 )
REMARK 3 ORIGIN FOR THE GROUP (A): 81.0708 30.3804 100.7442
REMARK 3 T TENSOR
REMARK 3 T11: 0.1299 T22: 0.0785
REMARK 3 T33: 0.0902 T12: 0.0110
REMARK 3 T13: -0.0545 T23: -0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 0.6288 L22: 1.1530
REMARK 3 L33: 1.1350 L12: 0.2555
REMARK 3 L13: -0.1174 L23: -0.6360
REMARK 3 S TENSOR
REMARK 3 S11: 0.0169 S12: 0.0597 S13: -0.0054
REMARK 3 S21: -0.0782 S22: 0.0392 S23: 0.0278
REMARK 3 S31: 0.0705 S32: -0.0327 S33: -0.0470
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 6B1N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-SEP-17.
REMARK 100 THE DEPOSITION ID IS D_1000230145.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-MAY-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : .977
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 87978
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 47.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
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: 6B1I
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NACL, TRIS, PEG 3350, MGCL2, ADP,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293.15K
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 38.79900
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 -22
REMARK 465 GLY A -21
REMARK 465 SER A -20
REMARK 465 SER A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 SER A -12
REMARK 465 SER A -11
REMARK 465 GLY A -10
REMARK 465 LEU A -9
REMARK 465 VAL A -8
REMARK 465 PRO A -7
REMARK 465 ARG A -6
REMARK 465 GLY A -5
REMARK 465 SER A -4
REMARK 465 HIS A -3
REMARK 465 MET A -2
REMARK 465 ALA A -1
REMARK 465 VAL A 189
REMARK 465 MET B -22
REMARK 465 GLY B -21
REMARK 465 SER B -20
REMARK 465 SER B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 SER B -12
REMARK 465 SER B -11
REMARK 465 GLY B -10
REMARK 465 LEU B -9
REMARK 465 VAL B -8
REMARK 465 PRO B -7
REMARK 465 ARG B -6
REMARK 465 GLY B -5
REMARK 465 SER B -4
REMARK 465 HIS B -3
REMARK 465 MET B -2
REMARK 465 ALA B -1
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 LYS A 25 CG CD CE NZ
REMARK 470 MET A 61 CG SD CE
REMARK 470 ASP A 79 CG OD1 OD2
REMARK 470 HIS A 89 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 187 CE NZ
REMARK 470 GLU A 192 CG CD OE1 OE2
REMARK 470 ILE A 216 CG1 CG2 CD1
REMARK 470 LYS A 250 CG CD CE NZ
REMARK 470 LYS A 257 CG CD CE NZ
REMARK 470 LYS B 25 CG CD CE NZ
REMARK 470 MET B 61 CG SD CE
REMARK 470 ASP B 79 CG OD1 OD2
REMARK 470 LYS B 88 CG CD CE NZ
REMARK 470 LYS B 187 CE NZ
REMARK 470 LYS B 248 CG CD CE NZ
REMARK 470 LYS B 250 CG CD CE NZ
REMARK 470 GLU B 358 CG CD OE1 OE2
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 B 834 O HOH B 879 1.96
REMARK 500 O1 GOL B 403 O HOH B 501 2.04
REMARK 500 OD1 ASP B 46 O HOH B 502 2.04
REMARK 500 OD1 ASP B 315 O HOH B 503 2.05
REMARK 500 O HOH A 862 O HOH A 887 2.06
REMARK 500 O HOH A 563 O HOH A 628 2.08
REMARK 500 O HOH A 603 O HOH B 866 2.08
REMARK 500 NH2 ARG B 311 O HOH B 504 2.09
REMARK 500 O ARG B 171 O HOH B 505 2.09
REMARK 500 OD1 ASP B 352 O HOH B 506 2.10
REMARK 500 O HOH B 516 O HOH B 645 2.10
REMARK 500 O HOH A 714 O HOH A 802 2.11
REMARK 500 NH2 ARG A 49 O HOH A 501 2.12
REMARK 500 O PRO B 5 O HOH B 507 2.13
REMARK 500 O HOH A 563 O HOH A 670 2.13
REMARK 500 O HOH B 807 O HOH B 898 2.13
REMARK 500 O HOH B 598 O HOH B 712 2.15
REMARK 500 O GLY B 190 O3 GOL B 406 2.16
REMARK 500 O HOH A 652 O HOH B 503 2.16
REMARK 500 O HOH A 784 O HOH A 806 2.17
REMARK 500 O HOH A 567 O HOH A 824 2.17
REMARK 500 O HOH B 876 O HOH B 884 2.18
REMARK 500 O HOH A 650 O HOH A 696 2.18
REMARK 500 OE1 GLN A 156 O HOH A 502 2.18
REMARK 500 NE2 GLN B 33 O HOH B 508 2.19
REMARK 500 O HOH B 556 O HOH B 815 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 366 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP B 10 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
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 ASN A 62 50.82 -143.09
REMARK 500 THR A 140 -53.30 -122.83
REMARK 500 ALA A 191 -164.02 -73.07
REMARK 500 ASN B 62 53.28 -144.28
REMARK 500 ALA B 191 -131.96 -99.41
REMARK 500 TYR B 288 118.65 -164.06
REMARK 500 LYS B 361 13.11 -146.08
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 915 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH B 916 DISTANCE = 6.24 ANGSTROMS
REMARK 525 HOH B 917 DISTANCE = 7.96 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 MG A 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP A 401 O2B
REMARK 620 2 ADP A 401 O2A 86.4
REMARK 620 3 HOH A 556 O 85.7 95.0
REMARK 620 4 HOH A 645 O 89.2 88.2 173.8
REMARK 620 5 HOH A 702 O 168.8 86.4 103.5 82.0
REMARK 620 6 HOH A 721 O 100.4 168.5 94.8 82.7 85.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP B 401 O2B
REMARK 620 2 ADP B 401 O2A 96.5
REMARK 620 3 HOH B 528 O 89.6 94.7
REMARK 620 4 HOH B 641 O 173.0 83.0 97.5
REMARK 620 5 HOH B 680 O 98.3 91.2 169.6 74.7
REMARK 620 6 HOH B 708 O 99.4 163.4 90.2 80.6 81.8
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 MG A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL 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 MG B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 407
DBREF 6B1N A 5 381 UNP P11142 HSP7C_HUMAN 5 381
DBREF 6B1N B 5 381 UNP P11142 HSP7C_HUMAN 5 381
SEQADV 6B1N MET A -22 UNP P11142 INITIATING METHIONINE
SEQADV 6B1N GLY A -21 UNP P11142 EXPRESSION TAG
SEQADV 6B1N SER A -20 UNP P11142 EXPRESSION TAG
SEQADV 6B1N SER A -19 UNP P11142 EXPRESSION TAG
SEQADV 6B1N HIS A -18 UNP P11142 EXPRESSION TAG
SEQADV 6B1N HIS A -17 UNP P11142 EXPRESSION TAG
SEQADV 6B1N HIS A -16 UNP P11142 EXPRESSION TAG
SEQADV 6B1N HIS A -15 UNP P11142 EXPRESSION TAG
SEQADV 6B1N HIS A -14 UNP P11142 EXPRESSION TAG
SEQADV 6B1N HIS A -13 UNP P11142 EXPRESSION TAG
SEQADV 6B1N SER A -12 UNP P11142 EXPRESSION TAG
SEQADV 6B1N SER A -11 UNP P11142 EXPRESSION TAG
SEQADV 6B1N GLY A -10 UNP P11142 EXPRESSION TAG
SEQADV 6B1N LEU A -9 UNP P11142 EXPRESSION TAG
SEQADV 6B1N VAL A -8 UNP P11142 EXPRESSION TAG
SEQADV 6B1N PRO A -7 UNP P11142 EXPRESSION TAG
SEQADV 6B1N ARG A -6 UNP P11142 EXPRESSION TAG
SEQADV 6B1N GLY A -5 UNP P11142 EXPRESSION TAG
SEQADV 6B1N SER A -4 UNP P11142 EXPRESSION TAG
SEQADV 6B1N HIS A -3 UNP P11142 EXPRESSION TAG
SEQADV 6B1N MET A -2 UNP P11142 EXPRESSION TAG
SEQADV 6B1N ALA A -1 UNP P11142 EXPRESSION TAG
SEQADV 6B1N SER A 0 UNP P11142 EXPRESSION TAG
SEQADV 6B1N TRP A 17 UNP P11142 CYS 17 ENGINEERED MUTATION
SEQADV 6B1N MET B -22 UNP P11142 INITIATING METHIONINE
SEQADV 6B1N GLY B -21 UNP P11142 EXPRESSION TAG
SEQADV 6B1N SER B -20 UNP P11142 EXPRESSION TAG
SEQADV 6B1N SER B -19 UNP P11142 EXPRESSION TAG
SEQADV 6B1N HIS B -18 UNP P11142 EXPRESSION TAG
SEQADV 6B1N HIS B -17 UNP P11142 EXPRESSION TAG
SEQADV 6B1N HIS B -16 UNP P11142 EXPRESSION TAG
SEQADV 6B1N HIS B -15 UNP P11142 EXPRESSION TAG
SEQADV 6B1N HIS B -14 UNP P11142 EXPRESSION TAG
SEQADV 6B1N HIS B -13 UNP P11142 EXPRESSION TAG
SEQADV 6B1N SER B -12 UNP P11142 EXPRESSION TAG
SEQADV 6B1N SER B -11 UNP P11142 EXPRESSION TAG
SEQADV 6B1N GLY B -10 UNP P11142 EXPRESSION TAG
SEQADV 6B1N LEU B -9 UNP P11142 EXPRESSION TAG
SEQADV 6B1N VAL B -8 UNP P11142 EXPRESSION TAG
SEQADV 6B1N PRO B -7 UNP P11142 EXPRESSION TAG
SEQADV 6B1N ARG B -6 UNP P11142 EXPRESSION TAG
SEQADV 6B1N GLY B -5 UNP P11142 EXPRESSION TAG
SEQADV 6B1N SER B -4 UNP P11142 EXPRESSION TAG
SEQADV 6B1N HIS B -3 UNP P11142 EXPRESSION TAG
SEQADV 6B1N MET B -2 UNP P11142 EXPRESSION TAG
SEQADV 6B1N ALA B -1 UNP P11142 EXPRESSION TAG
SEQADV 6B1N SER B 0 UNP P11142 EXPRESSION TAG
SEQADV 6B1N TRP B 17 UNP P11142 CYS 17 ENGINEERED MUTATION
SEQRES 1 A 400 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 400 LEU VAL PRO ARG GLY SER HIS MET ALA SER PRO ALA VAL
SEQRES 3 A 400 GLY ILE ASP LEU GLY THR THR TYR SER TRP VAL GLY VAL
SEQRES 4 A 400 PHE GLN HIS GLY LYS VAL GLU ILE ILE ALA ASN ASP GLN
SEQRES 5 A 400 GLY ASN ARG THR THR PRO SER TYR VAL ALA PHE THR ASP
SEQRES 6 A 400 THR GLU ARG LEU ILE GLY ASP ALA ALA LYS ASN GLN VAL
SEQRES 7 A 400 ALA MET ASN PRO THR ASN THR VAL PHE ASP ALA LYS ARG
SEQRES 8 A 400 LEU ILE GLY ARG ARG PHE ASP ASP ALA VAL VAL GLN SER
SEQRES 9 A 400 ASP MET LYS HIS TRP PRO PHE MET VAL VAL ASN ASP ALA
SEQRES 10 A 400 GLY ARG PRO LYS VAL GLN VAL GLU TYR LYS GLY GLU THR
SEQRES 11 A 400 LYS SER PHE TYR PRO GLU GLU VAL SER SER MET VAL LEU
SEQRES 12 A 400 THR LYS MET LYS GLU ILE ALA GLU ALA TYR LEU GLY LYS
SEQRES 13 A 400 THR VAL THR ASN ALA VAL VAL THR VAL PRO ALA TYR PHE
SEQRES 14 A 400 ASN ASP SER GLN ARG GLN ALA THR LYS ASP ALA GLY THR
SEQRES 15 A 400 ILE ALA GLY LEU ASN VAL LEU ARG ILE ILE ASN GLU PRO
SEQRES 16 A 400 THR ALA ALA ALA ILE ALA TYR GLY LEU ASP LYS LYS VAL
SEQRES 17 A 400 GLY ALA GLU ARG ASN VAL LEU ILE PHE ASP LEU GLY GLY
SEQRES 18 A 400 GLY THR PHE ASP VAL SER ILE LEU THR ILE GLU ASP GLY
SEQRES 19 A 400 ILE PHE GLU VAL LYS SER THR ALA GLY ASP THR HIS LEU
SEQRES 20 A 400 GLY GLY GLU ASP PHE ASP ASN ARG MET VAL ASN HIS PHE
SEQRES 21 A 400 ILE ALA GLU PHE LYS ARG LYS HIS LYS LYS ASP ILE SER
SEQRES 22 A 400 GLU ASN LYS ARG ALA VAL ARG ARG LEU ARG THR ALA CYS
SEQRES 23 A 400 GLU ARG ALA LYS ARG THR LEU SER SER SER THR GLN ALA
SEQRES 24 A 400 SER ILE GLU ILE ASP SER LEU TYR GLU GLY ILE ASP PHE
SEQRES 25 A 400 TYR THR SER ILE THR ARG ALA ARG PHE GLU GLU LEU ASN
SEQRES 26 A 400 ALA ASP LEU PHE ARG GLY THR LEU ASP PRO VAL GLU LYS
SEQRES 27 A 400 ALA LEU ARG ASP ALA LYS LEU ASP LYS SER GLN ILE HIS
SEQRES 28 A 400 ASP ILE VAL LEU VAL GLY GLY SER THR ARG ILE PRO LYS
SEQRES 29 A 400 ILE GLN LYS LEU LEU GLN ASP PHE PHE ASN GLY LYS GLU
SEQRES 30 A 400 LEU ASN LYS SER ILE ASN PRO ASP GLU ALA VAL ALA TYR
SEQRES 31 A 400 GLY ALA ALA VAL GLN ALA ALA ILE LEU SER
SEQRES 1 B 400 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 400 LEU VAL PRO ARG GLY SER HIS MET ALA SER PRO ALA VAL
SEQRES 3 B 400 GLY ILE ASP LEU GLY THR THR TYR SER TRP VAL GLY VAL
SEQRES 4 B 400 PHE GLN HIS GLY LYS VAL GLU ILE ILE ALA ASN ASP GLN
SEQRES 5 B 400 GLY ASN ARG THR THR PRO SER TYR VAL ALA PHE THR ASP
SEQRES 6 B 400 THR GLU ARG LEU ILE GLY ASP ALA ALA LYS ASN GLN VAL
SEQRES 7 B 400 ALA MET ASN PRO THR ASN THR VAL PHE ASP ALA LYS ARG
SEQRES 8 B 400 LEU ILE GLY ARG ARG PHE ASP ASP ALA VAL VAL GLN SER
SEQRES 9 B 400 ASP MET LYS HIS TRP PRO PHE MET VAL VAL ASN ASP ALA
SEQRES 10 B 400 GLY ARG PRO LYS VAL GLN VAL GLU TYR LYS GLY GLU THR
SEQRES 11 B 400 LYS SER PHE TYR PRO GLU GLU VAL SER SER MET VAL LEU
SEQRES 12 B 400 THR LYS MET LYS GLU ILE ALA GLU ALA TYR LEU GLY LYS
SEQRES 13 B 400 THR VAL THR ASN ALA VAL VAL THR VAL PRO ALA TYR PHE
SEQRES 14 B 400 ASN ASP SER GLN ARG GLN ALA THR LYS ASP ALA GLY THR
SEQRES 15 B 400 ILE ALA GLY LEU ASN VAL LEU ARG ILE ILE ASN GLU PRO
SEQRES 16 B 400 THR ALA ALA ALA ILE ALA TYR GLY LEU ASP LYS LYS VAL
SEQRES 17 B 400 GLY ALA GLU ARG ASN VAL LEU ILE PHE ASP LEU GLY GLY
SEQRES 18 B 400 GLY THR PHE ASP VAL SER ILE LEU THR ILE GLU ASP GLY
SEQRES 19 B 400 ILE PHE GLU VAL LYS SER THR ALA GLY ASP THR HIS LEU
SEQRES 20 B 400 GLY GLY GLU ASP PHE ASP ASN ARG MET VAL ASN HIS PHE
SEQRES 21 B 400 ILE ALA GLU PHE LYS ARG LYS HIS LYS LYS ASP ILE SER
SEQRES 22 B 400 GLU ASN LYS ARG ALA VAL ARG ARG LEU ARG THR ALA CYS
SEQRES 23 B 400 GLU ARG ALA LYS ARG THR LEU SER SER SER THR GLN ALA
SEQRES 24 B 400 SER ILE GLU ILE ASP SER LEU TYR GLU GLY ILE ASP PHE
SEQRES 25 B 400 TYR THR SER ILE THR ARG ALA ARG PHE GLU GLU LEU ASN
SEQRES 26 B 400 ALA ASP LEU PHE ARG GLY THR LEU ASP PRO VAL GLU LYS
SEQRES 27 B 400 ALA LEU ARG ASP ALA LYS LEU ASP LYS SER GLN ILE HIS
SEQRES 28 B 400 ASP ILE VAL LEU VAL GLY GLY SER THR ARG ILE PRO LYS
SEQRES 29 B 400 ILE GLN LYS LEU LEU GLN ASP PHE PHE ASN GLY LYS GLU
SEQRES 30 B 400 LEU ASN LYS SER ILE ASN PRO ASP GLU ALA VAL ALA TYR
SEQRES 31 B 400 GLY ALA ALA VAL GLN ALA ALA ILE LEU SER
HET ADP A 401 27
HET MG A 402 1
HET GOL A 403 6
HET GOL A 404 6
HET ADP B 401 27
HET MG B 402 1
HET GOL B 403 6
HET GOL B 404 6
HET GOL B 405 6
HET GOL B 406 6
HET GOL B 407 6
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
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 MG 2(MG 2+)
FORMUL 5 GOL 7(C3 H8 O3)
FORMUL 14 HOH *806(H2 O)
HELIX 1 AA1 GLY A 52 ASN A 57 1 6
HELIX 2 AA2 ASN A 62 THR A 64 5 3
HELIX 3 AA3 ASP A 69 ILE A 74 1 6
HELIX 4 AA4 ASP A 80 MET A 87 1 8
HELIX 5 AA5 LYS A 88 TRP A 90 5 3
HELIX 6 AA6 TYR A 115 GLY A 136 1 22
HELIX 7 AA7 ASN A 151 ALA A 165 1 15
HELIX 8 AA8 GLU A 175 TYR A 183 1 9
HELIX 9 AA9 GLY A 184 LYS A 188 5 5
HELIX 10 AB1 GLY A 229 LYS A 250 1 22
HELIX 11 AB2 ASN A 256 LEU A 274 1 19
HELIX 12 AB3 ARG A 299 ASN A 306 1 8
HELIX 13 AB4 ASN A 306 THR A 313 1 8
HELIX 14 AB5 THR A 313 ALA A 324 1 12
HELIX 15 AB6 ASP A 327 ILE A 331 5 5
HELIX 16 AB7 GLY A 338 ARG A 342 5 5
HELIX 17 AB8 ILE A 343 PHE A 354 1 12
HELIX 18 AB9 ASN A 364 ASP A 366 5 3
HELIX 19 AC1 GLU A 367 SER A 381 1 15
HELIX 20 AC2 GLY B 52 GLN B 58 1 7
HELIX 21 AC3 VAL B 59 THR B 64 5 6
HELIX 22 AC4 ASP B 69 ILE B 74 1 6
HELIX 23 AC5 ASP B 80 LYS B 88 1 9
HELIX 24 AC6 TYR B 115 GLY B 136 1 22
HELIX 25 AC7 ASN B 151 ALA B 165 1 15
HELIX 26 AC8 GLU B 175 TYR B 183 1 9
HELIX 27 AC9 GLY B 229 LYS B 250 1 22
HELIX 28 AD1 ASN B 256 LEU B 274 1 19
HELIX 29 AD2 ARG B 299 ASN B 306 1 8
HELIX 30 AD3 ASN B 306 THR B 313 1 8
HELIX 31 AD4 THR B 313 ALA B 324 1 12
HELIX 32 AD5 ASP B 327 ILE B 331 5 5
HELIX 33 AD6 GLY B 338 ARG B 342 5 5
HELIX 34 AD7 ILE B 343 PHE B 354 1 12
HELIX 35 AD8 ASN B 364 ASP B 366 5 3
HELIX 36 AD9 GLU B 367 SER B 381 1 15
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 ALA A 6 ASP A 10 -1 N GLY A 8 O GLY A 19
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 MET A 93 ASP A 97 0
SHEET 2 AA4 3 ARG A 100 TYR A 107 -1 O LYS A 102 N VAL 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 GLU A 213 -1 N VAL A 207 O ALA A 223
SHEET 3 AA5 4 ARG A 193 LEU A 200 -1 N ASP A 199 O ASP A 206
SHEET 4 AA5 4 ASP A 333 VAL A 337 1 O VAL A 335 N LEU A 196
SHEET 1 AA6 2 GLN A 279 TYR A 288 0
SHEET 2 AA6 2 ILE A 291 THR A 298 -1 O PHE A 293 N ILE A 284
SHEET 1 AA7 3 LYS B 25 ILE B 28 0
SHEET 2 AA7 3 TYR B 15 GLN B 22 -1 N GLN B 22 O LYS B 25
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 GLN B 22 O LYS B 25
SHEET 3 AA8 5 ALA B 6 ASP B 10 -1 N GLY B 8 O GLY B 19
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 THR B 66 PHE B 68 -1 O VAL B 67 N VAL B 42
SHEET 1 AB1 3 MET B 93 ASP B 97 0
SHEET 2 AB1 3 ARG B 100 TYR B 107 -1 O ARG B 100 N ASP B 97
SHEET 3 AB1 3 GLU B 110 PHE B 114 -1 O LYS B 112 N VAL B 105
SHEET 1 AB2 4 ILE B 216 ASP B 225 0
SHEET 2 AB2 4 PHE B 205 GLU 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 VAL B 335 N LEU B 196
SHEET 1 AB3 2 GLN B 279 TYR B 288 0
SHEET 2 AB3 2 ILE B 291 THR B 298 -1 O PHE B 293 N ILE B 284
LINK O2B ADP A 401 MG MG A 402 1555 1555 1.93
LINK O2A ADP A 401 MG MG A 402 1555 1555 2.05
LINK MG MG A 402 O HOH A 556 1555 1555 2.13
LINK MG MG A 402 O HOH A 645 1555 1555 2.06
LINK MG MG A 402 O HOH A 702 1555 1555 2.10
LINK MG MG A 402 O HOH A 721 1555 1555 2.06
LINK O2B ADP B 401 MG MG B 402 1555 1555 1.84
LINK O2A ADP B 401 MG MG B 402 1555 1555 1.99
LINK MG MG B 402 O HOH B 528 1555 1555 2.19
LINK MG MG B 402 O HOH B 641 1555 1555 2.11
LINK MG MG B 402 O HOH B 680 1555 1555 2.12
LINK MG MG B 402 O HOH B 708 1555 1555 2.22
SITE 1 AC1 31 GLY A 12 THR A 13 THR A 14 TYR A 15
SITE 2 AC1 31 TRP A 17 GLY A 201 GLY A 202 GLY A 230
SITE 3 AC1 31 GLU A 268 LYS A 271 ARG A 272 SER A 275
SITE 4 AC1 31 GLY A 338 GLY A 339 SER A 340 ARG A 342
SITE 5 AC1 31 ILE A 343 ASP A 366 MG A 402 HOH A 520
SITE 6 AC1 31 HOH A 537 HOH A 546 HOH A 554 HOH A 556
SITE 7 AC1 31 HOH A 645 HOH A 682 HOH A 702 HOH A 721
SITE 8 AC1 31 HOH A 729 HOH A 745 HOH A 780
SITE 1 AC2 5 ADP A 401 HOH A 556 HOH A 645 HOH A 702
SITE 2 AC2 5 HOH A 721
SITE 1 AC3 5 TYR A 15 ASN A 35 ASP A 53 ARG A 272
SITE 2 AC3 5 HOH A 681
SITE 1 AC4 7 PHE A 68 ASP A 69 ARG A 72 GLU A 231
SITE 2 AC4 7 HOH A 565 HOH A 646 HOH A 803
SITE 1 AC5 29 GLY B 12 THR B 13 THR B 14 TYR B 15
SITE 2 AC5 29 TRP B 17 GLY B 201 GLY B 202 GLY B 230
SITE 3 AC5 29 GLU B 268 LYS B 271 ARG B 272 SER B 275
SITE 4 AC5 29 GLY B 338 GLY B 339 SER B 340 ARG B 342
SITE 5 AC5 29 ILE B 343 ASP B 366 MG B 402 HOH B 528
SITE 6 AC5 29 HOH B 531 HOH B 567 HOH B 631 HOH B 641
SITE 7 AC5 29 HOH B 656 HOH B 672 HOH B 680 HOH B 714
SITE 8 AC5 29 HOH B 741
SITE 1 AC6 5 ADP B 401 HOH B 528 HOH B 641 HOH B 680
SITE 2 AC6 5 HOH B 708
SITE 1 AC7 5 ILE B 51 ASP B 53 ALA B 54 LYS B 126
SITE 2 AC7 5 HOH B 501
SITE 1 AC8 7 TYR B 15 ASN B 35 ASP B 53 LYS B 56
SITE 2 AC8 7 ARG B 272 HOH B 511 HOH B 623
SITE 1 AC9 7 HOH A 654 ASP B 186 LYS B 187 LYS B 188
SITE 2 AC9 7 VAL B 189 GLY B 190 GOL B 406
SITE 1 AD1 8 GLY B 190 ALA B 191 GLU B 213 ASP B 214
SITE 2 AD1 8 GOL B 405 HOH B 544 HOH B 606 HOH B 625
SITE 1 AD2 7 PHE B 68 ASP B 69 ASP B 86 HIS B 227
SITE 2 AD2 7 GLU B 231 HOH B 589 HOH B 696
CRYST1 73.388 77.598 75.523 90.00 101.16 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 0.013626 0.000000 0.002688 0.00000
SCALE2 0.000000 0.012887 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013496 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
