HEADER CHAPERONE 23-NOV-15 5EX5
TITLE CRYSTAL STRUCTURE OF HUMAN GRP78 (70KDA HEAT SHOCK PROTEIN 5 / BIP)
TITLE 2 ATPASE DOMAIN IN COMPLEX WITH 7-DEAZA-ADP AND INORGANIC PHOSPHATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 78 KDA GLUCOSE-REGULATED PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: ATPASE DOMAIN (UNP RESIDUES 26-407);
COMPND 5 SYNONYM: GRP-78, ENDOPLASMIC RETICULUM LUMENAL CA(2+)-BINDING PROTEIN
COMPND 6 GRP78, HEAT SHOCK 70 KDA PROTEIN 5, IMMUNOGLOBULIN HEAVY CHAIN-
COMPND 7 BINDING PROTEIN, BIP;
COMPND 8 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: HSPA5, GRP78;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS CHAPERONE, ATPASE DOMAIN, NUCLEOTIDE-BINDING, ENDOPLASMIC RETICULUM
EXPDTA X-RAY DIFFRACTION
AUTHOR S.J.HUGHES,T.ANTOSHCHENKO,J.H.SONG,J.PIZARRO,H.W.PARK
REVDAT 2 27-SEP-23 5EX5 1 REMARK LINK
REVDAT 1 15-JUN-16 5EX5 0
JRNL AUTH S.J.HUGHES,T.ANTOSHCHENKO,Y.CHEN,H.LU,J.C.PIZARRO,H.W.PARK
JRNL TITL PROBING THE ATP SITE OF GRP78 WITH NUCLEOTIDE TRIPHOSPHATE
JRNL TITL 2 ANALOGS.
JRNL REF PLOS ONE V. 11 54862 2016
JRNL REFN ESSN 1932-6203
JRNL PMID 27144892
JRNL DOI 10.1371/JOURNAL.PONE.0154862
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.87
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 52967
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2824
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3851
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.05
REMARK 3 BIN R VALUE (WORKING SET) : 0.2040
REMARK 3 BIN FREE R VALUE SET COUNT : 207
REMARK 3 BIN FREE R VALUE : 0.2430
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5908
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 66
REMARK 3 SOLVENT ATOMS : 500
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.44
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.00000
REMARK 3 B22 (A**2) : -0.15000
REMARK 3 B33 (A**2) : -0.65000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.10000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.163
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.144
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.099
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.001
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6093 ; 0.009 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5915 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8231 ; 1.286 ; 1.977
REMARK 3 BOND ANGLES OTHERS (DEGREES): 13628 ; 0.712 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 764 ; 5.172 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 278 ;34.734 ;24.892
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1104 ;12.354 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 39 ;15.682 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 928 ; 0.069 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6891 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1332 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3056 ; 1.091 ; 0.942
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3055 ; 1.090 ; 0.942
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3820 ; 1.635 ; 1.406
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 26 A 63
REMARK 3 RESIDUE RANGE : A 142 A 214
REMARK 3 ORIGIN FOR THE GROUP (A): 27.1528 0.9498 -8.2701
REMARK 3 T TENSOR
REMARK 3 T11: 0.0477 T22: 0.0230
REMARK 3 T33: 0.0045 T12: 0.0051
REMARK 3 T13: 0.0089 T23: 0.0058
REMARK 3 L TENSOR
REMARK 3 L11: 1.5105 L22: 2.8180
REMARK 3 L33: 1.3673 L12: -0.1461
REMARK 3 L13: -0.0135 L23: 0.4679
REMARK 3 S TENSOR
REMARK 3 S11: 0.0193 S12: 0.1757 S13: 0.0281
REMARK 3 S21: -0.3654 S22: -0.0333 S23: -0.0622
REMARK 3 S31: -0.0512 S32: 0.0433 S33: 0.0140
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 26 B 63
REMARK 3 RESIDUE RANGE : B 142 B 214
REMARK 3 ORIGIN FOR THE GROUP (A): 13.0055 -11.4105 -38.7385
REMARK 3 T TENSOR
REMARK 3 T11: 0.0572 T22: 0.0597
REMARK 3 T33: 0.0357 T12: 0.0367
REMARK 3 T13: -0.0121 T23: 0.0032
REMARK 3 L TENSOR
REMARK 3 L11: 1.4081 L22: 2.9315
REMARK 3 L33: 1.6126 L12: 0.1977
REMARK 3 L13: 0.3273 L23: -0.1343
REMARK 3 S TENSOR
REMARK 3 S11: -0.0851 S12: -0.0889 S13: -0.0008
REMARK 3 S21: 0.1007 S22: 0.0063 S23: -0.2605
REMARK 3 S31: -0.0776 S32: 0.1671 S33: 0.0787
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 64 A 141
REMARK 3 ORIGIN FOR THE GROUP (A): 34.8734 4.8363 11.3048
REMARK 3 T TENSOR
REMARK 3 T11: 0.0284 T22: 0.0739
REMARK 3 T33: 0.0601 T12: 0.0008
REMARK 3 T13: -0.0160 T23: 0.0083
REMARK 3 L TENSOR
REMARK 3 L11: 0.8188 L22: 4.8350
REMARK 3 L33: 1.1663 L12: -0.8332
REMARK 3 L13: 0.1922 L23: 0.1410
REMARK 3 S TENSOR
REMARK 3 S11: -0.0558 S12: -0.1160 S13: -0.0233
REMARK 3 S21: 0.3611 S22: 0.0524 S23: -0.2929
REMARK 3 S31: 0.0150 S32: 0.1269 S33: 0.0034
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 64 B 141
REMARK 3 ORIGIN FOR THE GROUP (A): 2.5509 -15.7965 -56.5979
REMARK 3 T TENSOR
REMARK 3 T11: 0.1361 T22: 0.0966
REMARK 3 T33: 0.0624 T12: 0.0285
REMARK 3 T13: -0.0470 T23: -0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 1.0246 L22: 5.1513
REMARK 3 L33: 2.3879 L12: 1.2965
REMARK 3 L13: -0.1792 L23: -1.4110
REMARK 3 S TENSOR
REMARK 3 S11: -0.0321 S12: 0.1533 S13: 0.1080
REMARK 3 S21: -0.4872 S22: 0.0704 S23: 0.2593
REMARK 3 S31: -0.0297 S32: -0.1359 S33: -0.0383
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 215 A 253
REMARK 3 RESIDUE RANGE : A 332 A 407
REMARK 3 ORIGIN FOR THE GROUP (A): 7.5007 3.6043 -2.1622
REMARK 3 T TENSOR
REMARK 3 T11: 0.0338 T22: 0.0730
REMARK 3 T33: 0.0775 T12: 0.0197
REMARK 3 T13: -0.0250 T23: -0.0130
REMARK 3 L TENSOR
REMARK 3 L11: 2.3382 L22: 1.4025
REMARK 3 L33: 2.1806 L12: -0.3589
REMARK 3 L13: -0.6713 L23: -0.1052
REMARK 3 S TENSOR
REMARK 3 S11: 0.0330 S12: 0.0712 S13: 0.0688
REMARK 3 S21: -0.1532 S22: -0.0264 S23: 0.2017
REMARK 3 S31: -0.1402 S32: -0.3460 S33: -0.0067
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 215 B 253
REMARK 3 RESIDUE RANGE : B 332 B 407
REMARK 3 ORIGIN FOR THE GROUP (A): -3.5799 -14.0047 -26.7001
REMARK 3 T TENSOR
REMARK 3 T11: 0.1623 T22: 0.2129
REMARK 3 T33: 0.0701 T12: 0.0867
REMARK 3 T13: 0.0356 T23: 0.0365
REMARK 3 L TENSOR
REMARK 3 L11: 4.0768 L22: 1.2650
REMARK 3 L33: 2.0746 L12: -0.2207
REMARK 3 L13: -0.1969 L23: -0.4465
REMARK 3 S TENSOR
REMARK 3 S11: -0.1489 S12: -0.6097 S13: -0.2970
REMARK 3 S21: 0.3277 S22: 0.2256 S23: 0.1410
REMARK 3 S31: -0.0182 S32: -0.3463 S33: -0.0768
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 254 A 331
REMARK 3 ORIGIN FOR THE GROUP (A): 17.7895 -13.5867 19.6578
REMARK 3 T TENSOR
REMARK 3 T11: 0.1340 T22: 0.1595
REMARK 3 T33: 0.1445 T12: 0.0033
REMARK 3 T13: -0.0592 T23: 0.0279
REMARK 3 L TENSOR
REMARK 3 L11: 4.2489 L22: 4.1722
REMARK 3 L33: 4.4261 L12: -0.7414
REMARK 3 L13: 2.4016 L23: -0.5462
REMARK 3 S TENSOR
REMARK 3 S11: 0.0826 S12: -0.5524 S13: -0.2679
REMARK 3 S21: 0.5645 S22: 0.1316 S23: -0.4642
REMARK 3 S31: 0.3446 S32: -0.0702 S33: -0.2142
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 254 B 331
REMARK 3 ORIGIN FOR THE GROUP (A): -15.3577 3.2327 -48.0971
REMARK 3 T TENSOR
REMARK 3 T11: 0.1786 T22: 0.2356
REMARK 3 T33: 0.1192 T12: 0.0427
REMARK 3 T13: 0.0098 T23: 0.0241
REMARK 3 L TENSOR
REMARK 3 L11: 1.6090 L22: 5.9686
REMARK 3 L33: 8.1728 L12: -1.6697
REMARK 3 L13: 2.0874 L23: -5.0575
REMARK 3 S TENSOR
REMARK 3 S11: -0.1944 S12: -0.0168 S13: 0.0404
REMARK 3 S21: -0.2419 S22: 0.4580 S23: 0.1787
REMARK 3 S31: -0.3087 S32: -0.5582 S33: -0.2636
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.70
REMARK 3 SHRINKAGE RADIUS : 0.70
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5EX5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-DEC-15.
REMARK 100 THE DEPOSITION ID IS D_1000215588.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-OCT-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CLSI
REMARK 200 BEAMLINE : 08ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97949
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.21
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55831
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.11700
REMARK 200 R SYM (I) : 0.11700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.50200
REMARK 200 R SYM FOR SHELL (I) : 0.05600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 5EXW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 24-26% PEG3350, 0.1 M TRIS-HCL, 0.2 M
REMARK 280 SODIUM CHLORIDE, PH 8.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 289K
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 37.35450
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 8
REMARK 465 HIS A 9
REMARK 465 HIS A 10
REMARK 465 HIS A 11
REMARK 465 HIS A 12
REMARK 465 HIS A 13
REMARK 465 HIS A 14
REMARK 465 SER A 15
REMARK 465 SER A 16
REMARK 465 GLY A 17
REMARK 465 ARG A 18
REMARK 465 GLU A 19
REMARK 465 ASN A 20
REMARK 465 LEU A 21
REMARK 465 TYR A 22
REMARK 465 PHE A 23
REMARK 465 GLN A 24
REMARK 465 GLY A 25
REMARK 465 MET B 8
REMARK 465 HIS B 9
REMARK 465 HIS B 10
REMARK 465 HIS B 11
REMARK 465 HIS B 12
REMARK 465 HIS B 13
REMARK 465 HIS B 14
REMARK 465 SER B 15
REMARK 465 SER B 16
REMARK 465 GLY B 17
REMARK 465 ARG B 18
REMARK 465 GLU B 19
REMARK 465 ASN B 20
REMARK 465 LEU B 21
REMARK 465 TYR B 22
REMARK 465 PHE B 23
REMARK 465 GLN B 24
REMARK 465 GLY B 25
REMARK 465 ASP B 26
REMARK 465 LEU B 84
REMARK 465 GLY B 407
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 THR A 124 -5.78 75.49
REMARK 500 LYS A 213 32.34 -94.81
REMARK 500 ASN B 87 50.66 -157.74
REMARK 500 LYS B 213 30.77 -96.30
REMARK 500 PHE B 379 36.08 -93.50
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 501 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PO4 A 502 O3
REMARK 620 2 7DD A 503 O3B 94.8
REMARK 620 3 HOH A 612 O 90.3 174.6
REMARK 620 4 HOH A 620 O 91.8 92.9 88.7
REMARK 620 5 HOH A 643 O 90.5 89.5 88.7 176.5
REMARK 620 6 HOH A 693 O 174.1 81.8 93.2 83.6 94.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 501 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PO4 B 502 O4
REMARK 620 2 7DD B 503 O2B 96.8
REMARK 620 3 HOH B 608 O 94.6 168.6
REMARK 620 4 HOH B 622 O 94.3 92.5 86.5
REMARK 620 5 HOH B 624 O 93.3 91.2 88.2 171.1
REMARK 620 6 HOH B 691 O 175.3 81.9 86.7 90.3 82.3
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 MG 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 7DD A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7DD B 503
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5EVZ RELATED DB: PDB
REMARK 900 RELATED ID: 5EXW RELATED DB: PDB
REMARK 900 RELATED ID: 5EY4 RELATED DB: PDB
REMARK 900 RELATED ID: 5F0X RELATED DB: PDB
REMARK 900 RELATED ID: 5F1X RELATED DB: PDB
REMARK 900 RELATED ID: 5F2R RELATED DB: PDB
DBREF 5EX5 A 26 407 UNP P11021 GRP78_HUMAN 26 407
DBREF 5EX5 B 26 407 UNP P11021 GRP78_HUMAN 26 407
SEQADV 5EX5 MET A 8 UNP P11021 EXPRESSION TAG
SEQADV 5EX5 HIS A 9 UNP P11021 EXPRESSION TAG
SEQADV 5EX5 HIS A 10 UNP P11021 EXPRESSION TAG
SEQADV 5EX5 HIS A 11 UNP P11021 EXPRESSION TAG
SEQADV 5EX5 HIS A 12 UNP P11021 EXPRESSION TAG
SEQADV 5EX5 HIS A 13 UNP P11021 EXPRESSION TAG
SEQADV 5EX5 HIS A 14 UNP P11021 EXPRESSION TAG
SEQADV 5EX5 SER A 15 UNP P11021 EXPRESSION TAG
SEQADV 5EX5 SER A 16 UNP P11021 EXPRESSION TAG
SEQADV 5EX5 GLY A 17 UNP P11021 EXPRESSION TAG
SEQADV 5EX5 ARG A 18 UNP P11021 EXPRESSION TAG
SEQADV 5EX5 GLU A 19 UNP P11021 EXPRESSION TAG
SEQADV 5EX5 ASN A 20 UNP P11021 EXPRESSION TAG
SEQADV 5EX5 LEU A 21 UNP P11021 EXPRESSION TAG
SEQADV 5EX5 TYR A 22 UNP P11021 EXPRESSION TAG
SEQADV 5EX5 PHE A 23 UNP P11021 EXPRESSION TAG
SEQADV 5EX5 GLN A 24 UNP P11021 EXPRESSION TAG
SEQADV 5EX5 GLY A 25 UNP P11021 EXPRESSION TAG
SEQADV 5EX5 MET B 8 UNP P11021 EXPRESSION TAG
SEQADV 5EX5 HIS B 9 UNP P11021 EXPRESSION TAG
SEQADV 5EX5 HIS B 10 UNP P11021 EXPRESSION TAG
SEQADV 5EX5 HIS B 11 UNP P11021 EXPRESSION TAG
SEQADV 5EX5 HIS B 12 UNP P11021 EXPRESSION TAG
SEQADV 5EX5 HIS B 13 UNP P11021 EXPRESSION TAG
SEQADV 5EX5 HIS B 14 UNP P11021 EXPRESSION TAG
SEQADV 5EX5 SER B 15 UNP P11021 EXPRESSION TAG
SEQADV 5EX5 SER B 16 UNP P11021 EXPRESSION TAG
SEQADV 5EX5 GLY B 17 UNP P11021 EXPRESSION TAG
SEQADV 5EX5 ARG B 18 UNP P11021 EXPRESSION TAG
SEQADV 5EX5 GLU B 19 UNP P11021 EXPRESSION TAG
SEQADV 5EX5 ASN B 20 UNP P11021 EXPRESSION TAG
SEQADV 5EX5 LEU B 21 UNP P11021 EXPRESSION TAG
SEQADV 5EX5 TYR B 22 UNP P11021 EXPRESSION TAG
SEQADV 5EX5 PHE B 23 UNP P11021 EXPRESSION TAG
SEQADV 5EX5 GLN B 24 UNP P11021 EXPRESSION TAG
SEQADV 5EX5 GLY B 25 UNP P11021 EXPRESSION TAG
SEQRES 1 A 400 MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN
SEQRES 2 A 400 LEU TYR PHE GLN GLY ASP VAL GLY THR VAL VAL GLY ILE
SEQRES 3 A 400 ASP LEU GLY THR THR TYR SER CYS VAL GLY VAL PHE LYS
SEQRES 4 A 400 ASN GLY ARG VAL GLU ILE ILE ALA ASN ASP GLN GLY ASN
SEQRES 5 A 400 ARG ILE THR PRO SER TYR VAL ALA PHE THR PRO GLU GLY
SEQRES 6 A 400 GLU ARG LEU ILE GLY ASP ALA ALA LYS ASN GLN LEU THR
SEQRES 7 A 400 SER ASN PRO GLU ASN THR VAL PHE ASP ALA LYS ARG LEU
SEQRES 8 A 400 ILE GLY ARG THR TRP ASN ASP PRO SER VAL GLN GLN ASP
SEQRES 9 A 400 ILE LYS PHE LEU PRO PHE LYS VAL VAL GLU LYS LYS THR
SEQRES 10 A 400 LYS PRO TYR ILE GLN VAL ASP ILE GLY GLY GLY GLN THR
SEQRES 11 A 400 LYS THR PHE ALA PRO GLU GLU ILE SER ALA MET VAL LEU
SEQRES 12 A 400 THR LYS MET LYS GLU THR ALA GLU ALA TYR LEU GLY LYS
SEQRES 13 A 400 LYS VAL THR HIS ALA VAL VAL THR VAL PRO ALA TYR PHE
SEQRES 14 A 400 ASN ASP ALA GLN ARG GLN ALA THR LYS ASP ALA GLY THR
SEQRES 15 A 400 ILE ALA GLY LEU ASN VAL MET ARG ILE ILE ASN GLU PRO
SEQRES 16 A 400 THR ALA ALA ALA ILE ALA TYR GLY LEU ASP LYS ARG GLU
SEQRES 17 A 400 GLY GLU LYS ASN ILE LEU VAL PHE ASP LEU GLY GLY GLY
SEQRES 18 A 400 THR PHE ASP VAL SER LEU LEU THR ILE ASP ASN GLY VAL
SEQRES 19 A 400 PHE GLU VAL VAL ALA THR ASN GLY ASP THR HIS LEU GLY
SEQRES 20 A 400 GLY GLU ASP PHE ASP GLN ARG VAL MET GLU HIS PHE ILE
SEQRES 21 A 400 LYS LEU TYR LYS LYS LYS THR GLY LYS ASP VAL ARG LYS
SEQRES 22 A 400 ASP ASN ARG ALA VAL GLN LYS LEU ARG ARG GLU VAL GLU
SEQRES 23 A 400 LYS ALA LYS ARG ALA LEU SER SER GLN HIS GLN ALA ARG
SEQRES 24 A 400 ILE GLU ILE GLU SER PHE TYR GLU GLY GLU ASP PHE SER
SEQRES 25 A 400 GLU THR LEU THR ARG ALA LYS PHE GLU GLU LEU ASN MET
SEQRES 26 A 400 ASP LEU PHE ARG SER THR MET LYS PRO VAL GLN LYS VAL
SEQRES 27 A 400 LEU GLU ASP SER ASP LEU LYS LYS SER ASP ILE ASP GLU
SEQRES 28 A 400 ILE VAL LEU VAL GLY GLY SER THR ARG ILE PRO LYS ILE
SEQRES 29 A 400 GLN GLN LEU VAL LYS GLU PHE PHE ASN GLY LYS GLU PRO
SEQRES 30 A 400 SER ARG GLY ILE ASN PRO ASP GLU ALA VAL ALA TYR GLY
SEQRES 31 A 400 ALA ALA VAL GLN ALA GLY VAL LEU SER GLY
SEQRES 1 B 400 MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN
SEQRES 2 B 400 LEU TYR PHE GLN GLY ASP VAL GLY THR VAL VAL GLY ILE
SEQRES 3 B 400 ASP LEU GLY THR THR TYR SER CYS VAL GLY VAL PHE LYS
SEQRES 4 B 400 ASN GLY ARG VAL GLU ILE ILE ALA ASN ASP GLN GLY ASN
SEQRES 5 B 400 ARG ILE THR PRO SER TYR VAL ALA PHE THR PRO GLU GLY
SEQRES 6 B 400 GLU ARG LEU ILE GLY ASP ALA ALA LYS ASN GLN LEU THR
SEQRES 7 B 400 SER ASN PRO GLU ASN THR VAL PHE ASP ALA LYS ARG LEU
SEQRES 8 B 400 ILE GLY ARG THR TRP ASN ASP PRO SER VAL GLN GLN ASP
SEQRES 9 B 400 ILE LYS PHE LEU PRO PHE LYS VAL VAL GLU LYS LYS THR
SEQRES 10 B 400 LYS PRO TYR ILE GLN VAL ASP ILE GLY GLY GLY GLN THR
SEQRES 11 B 400 LYS THR PHE ALA PRO GLU GLU ILE SER ALA MET VAL LEU
SEQRES 12 B 400 THR LYS MET LYS GLU THR ALA GLU ALA TYR LEU GLY LYS
SEQRES 13 B 400 LYS VAL THR HIS ALA VAL VAL THR VAL PRO ALA TYR PHE
SEQRES 14 B 400 ASN ASP ALA GLN ARG GLN ALA THR LYS ASP ALA GLY THR
SEQRES 15 B 400 ILE ALA GLY LEU ASN VAL MET ARG ILE ILE ASN GLU PRO
SEQRES 16 B 400 THR ALA ALA ALA ILE ALA TYR GLY LEU ASP LYS ARG GLU
SEQRES 17 B 400 GLY GLU LYS ASN ILE LEU VAL PHE ASP LEU GLY GLY GLY
SEQRES 18 B 400 THR PHE ASP VAL SER LEU LEU THR ILE ASP ASN GLY VAL
SEQRES 19 B 400 PHE GLU VAL VAL ALA THR ASN GLY ASP THR HIS LEU GLY
SEQRES 20 B 400 GLY GLU ASP PHE ASP GLN ARG VAL MET GLU HIS PHE ILE
SEQRES 21 B 400 LYS LEU TYR LYS LYS LYS THR GLY LYS ASP VAL ARG LYS
SEQRES 22 B 400 ASP ASN ARG ALA VAL GLN LYS LEU ARG ARG GLU VAL GLU
SEQRES 23 B 400 LYS ALA LYS ARG ALA LEU SER SER GLN HIS GLN ALA ARG
SEQRES 24 B 400 ILE GLU ILE GLU SER PHE TYR GLU GLY GLU ASP PHE SER
SEQRES 25 B 400 GLU THR LEU THR ARG ALA LYS PHE GLU GLU LEU ASN MET
SEQRES 26 B 400 ASP LEU PHE ARG SER THR MET LYS PRO VAL GLN LYS VAL
SEQRES 27 B 400 LEU GLU ASP SER ASP LEU LYS LYS SER ASP ILE ASP GLU
SEQRES 28 B 400 ILE VAL LEU VAL GLY GLY SER THR ARG ILE PRO LYS ILE
SEQRES 29 B 400 GLN GLN LEU VAL LYS GLU PHE PHE ASN GLY LYS GLU PRO
SEQRES 30 B 400 SER ARG GLY ILE ASN PRO ASP GLU ALA VAL ALA TYR GLY
SEQRES 31 B 400 ALA ALA VAL GLN ALA GLY VAL LEU SER GLY
HET MG A 501 1
HET PO4 A 502 5
HET 7DD A 503 27
HET MG B 501 1
HET PO4 B 502 5
HET 7DD B 503 27
HETNAM MG MAGNESIUM ION
HETNAM PO4 PHOSPHATE ION
HETNAM 7DD 7-DEAZAADENOSINE-5'-DIPHOSPHATE
FORMUL 3 MG 2(MG 2+)
FORMUL 4 PO4 2(O4 P 3-)
FORMUL 5 7DD 2(C11 H16 N4 O10 P2)
FORMUL 9 HOH *500(H2 O)
HELIX 1 AA1 GLY A 77 GLN A 83 1 7
HELIX 2 AA2 ASN A 87 THR A 91 5 5
HELIX 3 AA3 ASP A 94 LEU A 98 5 5
HELIX 4 AA4 ASP A 105 ILE A 112 1 8
HELIX 5 AA5 LYS A 113 LEU A 115 5 3
HELIX 6 AA6 ALA A 141 GLY A 162 1 22
HELIX 7 AA7 ASN A 177 ALA A 191 1 15
HELIX 8 AA8 GLU A 201 TYR A 209 1 9
HELIX 9 AA9 GLY A 210 ARG A 214 5 5
HELIX 10 AB1 GLY A 254 GLY A 275 1 22
HELIX 11 AB2 ASP A 277 LYS A 280 5 4
HELIX 12 AB3 ASP A 281 LEU A 299 1 19
HELIX 13 AB4 ARG A 324 THR A 338 1 15
HELIX 14 AB5 THR A 338 SER A 349 1 12
HELIX 15 AB6 LYS A 352 ILE A 356 5 5
HELIX 16 AB7 GLY A 363 ARG A 367 5 5
HELIX 17 AB8 ILE A 368 PHE A 379 1 12
HELIX 18 AB9 GLU A 392 GLY A 407 1 16
HELIX 19 AC1 GLY B 77 ASN B 82 1 6
HELIX 20 AC2 ASN B 87 GLU B 89 5 3
HELIX 21 AC3 ASP B 94 LEU B 98 5 5
HELIX 22 AC4 ASP B 105 ILE B 112 1 8
HELIX 23 AC5 ALA B 141 GLY B 162 1 22
HELIX 24 AC6 ASN B 177 ALA B 191 1 15
HELIX 25 AC7 GLU B 201 TYR B 209 1 9
HELIX 26 AC8 GLY B 210 ARG B 214 5 5
HELIX 27 AC9 GLY B 254 GLY B 275 1 22
HELIX 28 AD1 ASP B 277 LYS B 280 5 4
HELIX 29 AD2 ASP B 281 LEU B 299 1 19
HELIX 30 AD3 ARG B 324 THR B 338 1 15
HELIX 31 AD4 THR B 338 SER B 349 1 12
HELIX 32 AD5 LYS B 352 ILE B 356 5 5
HELIX 33 AD6 GLY B 363 ARG B 367 5 5
HELIX 34 AD7 ILE B 368 PHE B 379 1 12
HELIX 35 AD8 GLU B 392 SER B 406 1 15
SHEET 1 AA1 3 ARG A 49 ILE A 52 0
SHEET 2 AA1 3 TYR A 39 LYS A 46 -1 N VAL A 44 O GLU A 51
SHEET 3 AA1 3 THR A 62 PRO A 63 -1 O THR A 62 N SER A 40
SHEET 1 AA2 5 ARG A 49 ILE A 52 0
SHEET 2 AA2 5 TYR A 39 LYS A 46 -1 N VAL A 44 O GLU A 51
SHEET 3 AA2 5 VAL A 31 ASP A 34 -1 N GLY A 32 O GLY A 43
SHEET 4 AA2 5 HIS A 167 VAL A 172 1 O VAL A 169 N ILE A 33
SHEET 5 AA2 5 ASN A 194 ASN A 200 1 O ASN A 194 N ALA A 168
SHEET 1 AA3 2 VAL A 66 PHE A 68 0
SHEET 2 AA3 2 ARG A 74 ILE A 76 -1 O LEU A 75 N ALA A 67
SHEET 1 AA4 3 LYS A 118 LYS A 122 0
SHEET 2 AA4 3 LYS A 125 GLY A 133 -1 O LYS A 125 N LYS A 122
SHEET 3 AA4 3 GLN A 136 PHE A 140 -1 O PHE A 140 N ILE A 128
SHEET 1 AA5 4 VAL A 241 ASP A 250 0
SHEET 2 AA5 4 PHE A 230 ASP A 238 -1 N LEU A 234 O ALA A 246
SHEET 3 AA5 4 LYS A 218 LEU A 225 -1 N VAL A 222 O SER A 233
SHEET 4 AA5 4 GLU A 358 VAL A 362 1 O VAL A 360 N PHE A 223
SHEET 1 AA6 2 GLN A 304 TYR A 313 0
SHEET 2 AA6 2 GLU A 316 THR A 323 -1 O GLU A 320 N ILE A 307
SHEET 1 AA7 3 ARG B 49 ILE B 52 0
SHEET 2 AA7 3 TYR B 39 LYS B 46 -1 N VAL B 44 O GLU B 51
SHEET 3 AA7 3 THR B 62 PRO B 63 -1 O THR B 62 N SER B 40
SHEET 1 AA8 5 ARG B 49 ILE B 52 0
SHEET 2 AA8 5 TYR B 39 LYS B 46 -1 N VAL B 44 O GLU B 51
SHEET 3 AA8 5 VAL B 31 ASP B 34 -1 N GLY B 32 O GLY B 43
SHEET 4 AA8 5 HIS B 167 VAL B 172 1 O VAL B 169 N VAL B 31
SHEET 5 AA8 5 ASN B 194 ASN B 200 1 O MET B 196 N ALA B 168
SHEET 1 AA9 3 ARG B 74 ILE B 76 0
SHEET 2 AA9 3 VAL B 66 PHE B 68 -1 N ALA B 67 O LEU B 75
SHEET 3 AA9 3 THR B 91 VAL B 92 -1 O VAL B 92 N VAL B 66
SHEET 1 AB1 3 LYS B 118 LYS B 122 0
SHEET 2 AB1 3 LYS B 125 ASP B 131 -1 O TYR B 127 N VAL B 120
SHEET 3 AB1 3 THR B 137 PHE B 140 -1 O PHE B 140 N ILE B 128
SHEET 1 AB2 4 VAL B 241 ASP B 250 0
SHEET 2 AB2 4 PHE B 230 ASP B 238 -1 N VAL B 232 O ASN B 248
SHEET 3 AB2 4 LYS B 218 LEU B 225 -1 N ILE B 220 O LEU B 235
SHEET 4 AB2 4 GLU B 358 VAL B 362 1 O GLU B 358 N LEU B 221
SHEET 1 AB3 2 GLN B 304 TYR B 313 0
SHEET 2 AB3 2 GLU B 316 THR B 323 -1 O GLU B 320 N ILE B 307
LINK MG MG A 501 O3 PO4 A 502 1555 1555 2.04
LINK MG MG A 501 O3B 7DD A 503 1555 1555 1.98
LINK MG MG A 501 O HOH A 612 1555 1555 2.16
LINK MG MG A 501 O HOH A 620 1555 1555 2.06
LINK MG MG A 501 O HOH A 643 1555 1555 2.13
LINK MG MG A 501 O HOH A 693 1555 1555 2.13
LINK MG MG B 501 O4 PO4 B 502 1555 1555 2.02
LINK MG MG B 501 O2B 7DD B 503 1555 1555 1.98
LINK MG MG B 501 O HOH B 608 1555 1555 2.16
LINK MG MG B 501 O HOH B 622 1555 1555 2.15
LINK MG MG B 501 O HOH B 624 1555 1555 2.03
LINK MG MG B 501 O HOH B 691 1555 1555 2.23
SITE 1 AC1 6 PO4 A 502 7DD A 503 HOH A 612 HOH A 620
SITE 2 AC1 6 HOH A 643 HOH A 693
SITE 1 AC2 13 GLY A 36 THR A 37 LYS A 96 PRO A 173
SITE 2 AC2 13 GLU A 201 THR A 229 MG A 501 7DD A 503
SITE 3 AC2 13 HOH A 601 HOH A 612 HOH A 620 HOH A 626
SITE 4 AC2 13 HOH A 643
SITE 1 AC3 28 THR A 37 THR A 38 TYR A 39 GLY A 226
SITE 2 AC3 28 GLY A 227 GLY A 255 GLU A 293 LYS A 296
SITE 3 AC3 28 ARG A 297 SER A 300 GLY A 363 GLY A 364
SITE 4 AC3 28 SER A 365 ARG A 367 ASP A 391 MG A 501
SITE 5 AC3 28 PO4 A 502 HOH A 601 HOH A 603 HOH A 613
SITE 6 AC3 28 HOH A 620 HOH A 643 HOH A 679 HOH A 693
SITE 7 AC3 28 HOH A 704 HOH A 721 HOH A 738 HOH A 782
SITE 1 AC4 6 PO4 B 502 7DD B 503 HOH B 608 HOH B 622
SITE 2 AC4 6 HOH B 624 HOH B 691
SITE 1 AC5 13 GLY B 36 THR B 37 LYS B 96 PRO B 173
SITE 2 AC5 13 GLU B 201 THR B 229 MG B 501 7DD B 503
SITE 3 AC5 13 HOH B 601 HOH B 608 HOH B 622 HOH B 624
SITE 4 AC5 13 HOH B 630
SITE 1 AC6 28 THR B 37 THR B 38 TYR B 39 GLY B 226
SITE 2 AC6 28 GLY B 227 GLY B 255 GLU B 293 LYS B 296
SITE 3 AC6 28 ARG B 297 SER B 300 GLY B 363 GLY B 364
SITE 4 AC6 28 SER B 365 ARG B 367 ILE B 368 ASP B 391
SITE 5 AC6 28 MG B 501 PO4 B 502 HOH B 601 HOH B 602
SITE 6 AC6 28 HOH B 617 HOH B 622 HOH B 624 HOH B 654
SITE 7 AC6 28 HOH B 662 HOH B 681 HOH B 691 HOH B 712
CRYST1 55.270 74.709 88.722 90.00 98.38 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 0.018093 0.000000 0.002666 0.00000
SCALE2 0.000000 0.013385 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011393 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
