HEADER CHAPERONE 24-NOV-15 5EXW
TITLE CRYSTAL STRUCTURE OF HUMAN GRP78 (70KDA HEAT SHOCK PROTEIN 5 / BIP)
TITLE 2 ATPASE DOMAIN IN COMPLEX WITH 7-DEAZA-ATP
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 5EXW 1 REMARK
REVDAT 1 15-JUN-16 5EXW 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) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 54459
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) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2910
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) : 3989
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.93
REMARK 3 BIN R VALUE (WORKING SET) : 0.1710
REMARK 3 BIN FREE R VALUE SET COUNT : 214
REMARK 3 BIN FREE R VALUE : 0.2230
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5905
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 62
REMARK 3 SOLVENT ATOMS : 653
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.28
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.60000
REMARK 3 B22 (A**2) : -0.19000
REMARK 3 B33 (A**2) : -0.25000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.93000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.156
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.141
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.089
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.321
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6098 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5921 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8241 ; 1.177 ; 1.977
REMARK 3 BOND ANGLES OTHERS (DEGREES): 13642 ; 0.713 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 766 ; 5.178 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 278 ;35.249 ;24.892
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1104 ;11.937 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 39 ;11.320 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 928 ; 0.071 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6905 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1334 ; 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): 3061 ; 1.169 ; 1.219
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3060 ; 1.166 ; 1.218
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3828 ; 1.728 ; 1.820
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 27 A 63
REMARK 3 RESIDUE RANGE : A 142 A 214
REMARK 3 ORIGIN FOR THE GROUP (A): 27.1764 0.5730 -8.1680
REMARK 3 T TENSOR
REMARK 3 T11: 0.0502 T22: 0.0352
REMARK 3 T33: 0.0054 T12: 0.0239
REMARK 3 T13: 0.0004 T23: 0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 1.0371 L22: 2.5082
REMARK 3 L33: 1.2466 L12: 0.0108
REMARK 3 L13: -0.2169 L23: 0.2464
REMARK 3 S TENSOR
REMARK 3 S11: 0.0574 S12: 0.1681 S13: 0.0186
REMARK 3 S21: -0.2936 S22: -0.0999 S23: -0.0329
REMARK 3 S31: -0.0173 S32: 0.0210 S33: 0.0425
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): 13.5188 -11.2679 -39.1152
REMARK 3 T TENSOR
REMARK 3 T11: 0.0077 T22: 0.0349
REMARK 3 T33: 0.0244 T12: 0.0007
REMARK 3 T13: -0.0109 T23: -0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 1.3393 L22: 2.6343
REMARK 3 L33: 1.6654 L12: 0.0572
REMARK 3 L13: 0.1784 L23: -0.0745
REMARK 3 S TENSOR
REMARK 3 S11: -0.0580 S12: -0.1009 S13: 0.0133
REMARK 3 S21: 0.0617 S22: 0.0240 S23: -0.1926
REMARK 3 S31: -0.0496 S32: 0.1951 S33: 0.0340
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): 35.1081 4.4705 11.3004
REMARK 3 T TENSOR
REMARK 3 T11: 0.0632 T22: 0.0645
REMARK 3 T33: 0.0482 T12: -0.0083
REMARK 3 T13: -0.0323 T23: 0.0161
REMARK 3 L TENSOR
REMARK 3 L11: 1.3978 L22: 3.9529
REMARK 3 L33: 1.5339 L12: -0.3772
REMARK 3 L13: 0.1936 L23: 0.3419
REMARK 3 S TENSOR
REMARK 3 S11: 0.0257 S12: -0.1566 S13: -0.1231
REMARK 3 S21: 0.3501 S22: 0.0224 S23: -0.3284
REMARK 3 S31: 0.0662 S32: 0.2319 S33: -0.0481
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): 2.7132 -15.9425 -56.8438
REMARK 3 T TENSOR
REMARK 3 T11: 0.1194 T22: 0.0555
REMARK 3 T33: 0.0543 T12: 0.0147
REMARK 3 T13: -0.0359 T23: 0.0046
REMARK 3 L TENSOR
REMARK 3 L11: 1.2061 L22: 4.5140
REMARK 3 L33: 1.9296 L12: 0.7935
REMARK 3 L13: 0.0316 L23: -0.2710
REMARK 3 S TENSOR
REMARK 3 S11: -0.0398 S12: 0.2324 S13: 0.1115
REMARK 3 S21: -0.5941 S22: 0.0693 S23: 0.1411
REMARK 3 S31: -0.0633 S32: -0.0484 S33: -0.0295
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): 7.6505 3.6158 -2.3128
REMARK 3 T TENSOR
REMARK 3 T11: 0.0729 T22: 0.0922
REMARK 3 T33: 0.0829 T12: 0.0391
REMARK 3 T13: -0.0526 T23: -0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 2.5947 L22: 1.2349
REMARK 3 L33: 2.4886 L12: -0.1489
REMARK 3 L13: -0.6320 L23: -0.1167
REMARK 3 S TENSOR
REMARK 3 S11: 0.0469 S12: 0.1222 S13: 0.0757
REMARK 3 S21: -0.1334 S22: 0.0009 S23: 0.2347
REMARK 3 S31: -0.1736 S32: -0.4699 S33: -0.0477
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): -2.9446 -13.3149 -26.7731
REMARK 3 T TENSOR
REMARK 3 T11: 0.0906 T22: 0.1492
REMARK 3 T33: 0.0582 T12: 0.0719
REMARK 3 T13: 0.0221 T23: 0.0290
REMARK 3 L TENSOR
REMARK 3 L11: 3.1213 L22: 1.0838
REMARK 3 L33: 2.4001 L12: -0.0901
REMARK 3 L13: 0.3446 L23: -0.8328
REMARK 3 S TENSOR
REMARK 3 S11: -0.1193 S12: -0.4750 S13: -0.1647
REMARK 3 S21: 0.2670 S22: 0.2409 S23: 0.1230
REMARK 3 S31: -0.0878 S32: -0.3859 S33: -0.1216
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): 17.8371 -13.7172 19.7700
REMARK 3 T TENSOR
REMARK 3 T11: 0.1856 T22: 0.1414
REMARK 3 T33: 0.2041 T12: -0.0348
REMARK 3 T13: -0.0981 T23: 0.0558
REMARK 3 L TENSOR
REMARK 3 L11: 3.1443 L22: 3.8339
REMARK 3 L33: 4.2089 L12: -0.4543
REMARK 3 L13: 1.8464 L23: -0.3891
REMARK 3 S TENSOR
REMARK 3 S11: 0.1838 S12: -0.4574 S13: -0.3413
REMARK 3 S21: 0.5306 S22: 0.0628 S23: -0.3404
REMARK 3 S31: 0.4259 S32: 0.0285 S33: -0.2466
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): -14.5739 3.4350 -48.5995
REMARK 3 T TENSOR
REMARK 3 T11: 0.1579 T22: 0.1721
REMARK 3 T33: 0.1084 T12: 0.0451
REMARK 3 T13: -0.0143 T23: 0.0262
REMARK 3 L TENSOR
REMARK 3 L11: 1.8635 L22: 4.7957
REMARK 3 L33: 5.5635 L12: -1.4663
REMARK 3 L13: 1.5759 L23: -3.1830
REMARK 3 S TENSOR
REMARK 3 S11: -0.1324 S12: 0.0700 S13: 0.1159
REMARK 3 S21: -0.3208 S22: 0.2374 S23: 0.1378
REMARK 3 S31: -0.3784 S32: -0.3860 S33: -0.1051
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.00
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 U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 5EXW 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_1000215593.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-MAY-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 : 57406
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.851
REMARK 200 RESOLUTION RANGE LOW (A) : 88.593
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 4.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.1000
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.17600
REMARK 200 R SYM FOR SHELL (I) : 0.17600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.600
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 3LDN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
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 37.41300
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 ASP A 26
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 LEU B 84
REMARK 465 THR B 85
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 O2B 7DT A 501 O HOH A 601 2.16
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 THR A 124 -0.26 69.51
REMARK 500 LYS A 213 46.08 -94.11
REMARK 500 ASN A 248 -167.85 -161.57
REMARK 500 ASN B 87 66.74 -167.29
REMARK 500 PHE B 379 31.79 -97.43
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7DT A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7DT B 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5EVZ RELATED DB: PDB
REMARK 900 RELATED ID: 5EX5 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 5EXW A 26 407 UNP P11021 GRP78_HUMAN 26 407
DBREF 5EXW B 26 407 UNP P11021 GRP78_HUMAN 26 407
SEQADV 5EXW MET A 8 UNP P11021 EXPRESSION TAG
SEQADV 5EXW HIS A 9 UNP P11021 EXPRESSION TAG
SEQADV 5EXW HIS A 10 UNP P11021 EXPRESSION TAG
SEQADV 5EXW HIS A 11 UNP P11021 EXPRESSION TAG
SEQADV 5EXW HIS A 12 UNP P11021 EXPRESSION TAG
SEQADV 5EXW HIS A 13 UNP P11021 EXPRESSION TAG
SEQADV 5EXW HIS A 14 UNP P11021 EXPRESSION TAG
SEQADV 5EXW SER A 15 UNP P11021 EXPRESSION TAG
SEQADV 5EXW SER A 16 UNP P11021 EXPRESSION TAG
SEQADV 5EXW GLY A 17 UNP P11021 EXPRESSION TAG
SEQADV 5EXW ARG A 18 UNP P11021 EXPRESSION TAG
SEQADV 5EXW GLU A 19 UNP P11021 EXPRESSION TAG
SEQADV 5EXW ASN A 20 UNP P11021 EXPRESSION TAG
SEQADV 5EXW LEU A 21 UNP P11021 EXPRESSION TAG
SEQADV 5EXW TYR A 22 UNP P11021 EXPRESSION TAG
SEQADV 5EXW PHE A 23 UNP P11021 EXPRESSION TAG
SEQADV 5EXW GLN A 24 UNP P11021 EXPRESSION TAG
SEQADV 5EXW GLY A 25 UNP P11021 EXPRESSION TAG
SEQADV 5EXW MET B 8 UNP P11021 EXPRESSION TAG
SEQADV 5EXW HIS B 9 UNP P11021 EXPRESSION TAG
SEQADV 5EXW HIS B 10 UNP P11021 EXPRESSION TAG
SEQADV 5EXW HIS B 11 UNP P11021 EXPRESSION TAG
SEQADV 5EXW HIS B 12 UNP P11021 EXPRESSION TAG
SEQADV 5EXW HIS B 13 UNP P11021 EXPRESSION TAG
SEQADV 5EXW HIS B 14 UNP P11021 EXPRESSION TAG
SEQADV 5EXW SER B 15 UNP P11021 EXPRESSION TAG
SEQADV 5EXW SER B 16 UNP P11021 EXPRESSION TAG
SEQADV 5EXW GLY B 17 UNP P11021 EXPRESSION TAG
SEQADV 5EXW ARG B 18 UNP P11021 EXPRESSION TAG
SEQADV 5EXW GLU B 19 UNP P11021 EXPRESSION TAG
SEQADV 5EXW ASN B 20 UNP P11021 EXPRESSION TAG
SEQADV 5EXW LEU B 21 UNP P11021 EXPRESSION TAG
SEQADV 5EXW TYR B 22 UNP P11021 EXPRESSION TAG
SEQADV 5EXW PHE B 23 UNP P11021 EXPRESSION TAG
SEQADV 5EXW GLN B 24 UNP P11021 EXPRESSION TAG
SEQADV 5EXW 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 7DT A 501 31
HET 7DT B 501 31
HETNAM 7DT 7-DEAZAADENOSINE-5'-TRIPHOSPHATE
FORMUL 3 7DT 2(C11 H17 N4 O13 P3)
FORMUL 5 HOH *653(H2 O)
HELIX 1 AA1 GLY A 77 ASN A 82 1 6
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 ALA A 141 GLY A 162 1 22
HELIX 6 AA6 ASN A 177 ALA A 191 1 15
HELIX 7 AA7 GLU A 201 TYR A 209 1 9
HELIX 8 AA8 GLY A 254 GLY A 275 1 22
HELIX 9 AA9 ASP A 277 LYS A 280 5 4
HELIX 10 AB1 ASP A 281 SER A 300 1 20
HELIX 11 AB2 ARG A 324 THR A 338 1 15
HELIX 12 AB3 THR A 338 ASP A 350 1 13
HELIX 13 AB4 LYS A 352 ILE A 356 5 5
HELIX 14 AB5 GLY A 363 ARG A 367 5 5
HELIX 15 AB6 ILE A 368 PHE A 379 1 12
HELIX 16 AB7 GLU A 392 GLY A 407 1 16
HELIX 17 AB8 GLY B 77 ASN B 82 1 6
HELIX 18 AB9 ASP B 94 LEU B 98 5 5
HELIX 19 AC1 ASP B 105 ILE B 112 1 8
HELIX 20 AC2 ALA B 141 GLY B 162 1 22
HELIX 21 AC3 ASN B 177 ALA B 191 1 15
HELIX 22 AC4 GLU B 201 TYR B 209 1 9
HELIX 23 AC5 GLY B 210 ARG B 214 5 5
HELIX 24 AC6 GLY B 254 GLY B 275 1 22
HELIX 25 AC7 ASP B 277 LYS B 280 5 4
HELIX 26 AC8 ASP B 281 LEU B 299 1 19
HELIX 27 AC9 ARG B 324 THR B 338 1 15
HELIX 28 AD1 THR B 338 SER B 349 1 12
HELIX 29 AD2 LYS B 352 ILE B 356 5 5
HELIX 30 AD3 GLY B 363 ARG B 367 5 5
HELIX 31 AD4 ILE B 368 PHE B 379 1 12
HELIX 32 AD5 GLU B 392 GLY B 407 1 16
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 ASP A 131 -1 O TYR A 127 N VAL A 120
SHEET 3 AA4 3 THR A 137 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 ILE A 220 O LEU A 235
SHEET 4 AA5 4 GLU A 358 VAL A 362 1 O VAL A 362 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 LYS B 46 O ARG B 49
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 LYS B 46 O ARG B 49
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 ILE B 33
SHEET 5 AA8 5 ASN B 194 ASN B 200 1 O ASN B 194 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 GLY B 133 -1 O TYR B 127 N VAL B 120
SHEET 3 AB1 3 GLN B 136 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
SITE 1 AC1 27 GLY A 36 THR A 37 THR A 38 TYR A 39
SITE 2 AC1 27 GLY A 226 GLY A 227 GLY A 228 THR A 229
SITE 3 AC1 27 GLY A 255 GLU A 293 LYS A 296 ARG A 297
SITE 4 AC1 27 SER A 300 GLY A 363 GLY A 364 SER A 365
SITE 5 AC1 27 ARG A 367 ASP A 391 HOH A 601 HOH A 616
SITE 6 AC1 27 HOH A 620 HOH A 726 HOH A 745 HOH A 758
SITE 7 AC1 27 HOH A 759 HOH A 818 HOH A 860
SITE 1 AC2 28 GLY B 36 THR B 37 THR B 38 TYR B 39
SITE 2 AC2 28 GLY B 226 GLY B 227 GLY B 228 THR B 229
SITE 3 AC2 28 GLY B 255 GLU B 293 LYS B 296 ARG B 297
SITE 4 AC2 28 SER B 300 GLY B 363 GLY B 364 SER B 365
SITE 5 AC2 28 ARG B 367 ILE B 368 ASP B 391 HOH B 601
SITE 6 AC2 28 HOH B 653 HOH B 673 HOH B 705 HOH B 720
SITE 7 AC2 28 HOH B 769 HOH B 771 HOH B 784 HOH B 796
CRYST1 55.682 74.826 89.658 90.00 98.84 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 0.017959 0.000000 0.002793 0.00000
SCALE2 0.000000 0.013364 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011288 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
