HEADER ISOMERASE 07-JUN-06 2H8L
TITLE CRYSTAL STRUCTURE OF THE BB' FRAGMENT OF ERP57
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN DISULFIDE-ISOMERASE A3;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: BB' FRAGMENT;
COMPND 5 SYNONYM: DISULFIDE ISOMERASE ER-60, ERP60, 58 KDA MICROSOMAL PROTEIN,
COMPND 6 P58, ERP57, 58 KDA GLUCOSE-REGULATED PROTEIN;
COMPND 7 EC: 5.3.4.1;
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: PDIA3, ERP60, GRP58;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-1
KEYWDS THIOREDOXIN-LIKE FOLD, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.KOZLOV,J.D.SCHRAG,M.CYGLER,K.GEHRING
REVDAT 3 13-JUL-11 2H8L 1 VERSN
REVDAT 2 24-FEB-09 2H8L 1 VERSN
REVDAT 1 29-AUG-06 2H8L 0
JRNL AUTH G.KOZLOV,P.MAATTANEN,J.D.SCHRAG,S.POLLOCK,M.CYGLER,B.NAGAR,
JRNL AUTH 2 D.Y.THOMAS,K.GEHRING
JRNL TITL CRYSTAL STRUCTURE OF THE BB' DOMAINS OF THE PROTEIN
JRNL TITL 2 DISULFIDE ISOMERASE ERP57.
JRNL REF STRUCTURE V. 14 1331 2006
JRNL REFN ISSN 0969-2126
JRNL PMID 16905107
JRNL DOI 10.1016/J.STR.2006.06.019
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.70
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 59353
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) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3162
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4194
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.17
REMARK 3 BIN R VALUE (WORKING SET) : 0.2710
REMARK 3 BIN FREE R VALUE SET COUNT : 250
REMARK 3 BIN FREE R VALUE : 0.3270
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5634
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 453
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.09
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.83000
REMARK 3 B22 (A**2) : -0.44000
REMARK 3 B33 (A**2) : 1.23000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.14000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.165
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.163
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.147
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.012
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
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): 5753 ; 0.025 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7721 ; 1.932 ; 1.943
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 691 ; 6.741 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 306 ;35.851 ;24.412
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1045 ;17.156 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 33 ;19.248 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 807 ; 0.143 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4402 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2591 ; 0.215 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3864 ; 0.308 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 448 ; 0.157 ; 0.200
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): 58 ; 0.307 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 27 ; 0.268 ; 0.200
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): 3561 ; 1.351 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5517 ; 1.697 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2505 ; 3.013 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2204 ; 4.217 ; 4.500
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 134 A 365 6
REMARK 3 1 B 135 B 364 6
REMARK 3 1 C 134 C 365 6
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 LOOSE POSITIONAL 1 A (A): 1868 ; 0.70 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 B (A): 1868 ; 0.78 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 C (A): 1868 ; 0.84 ; 5.00
REMARK 3 LOOSE THERMAL 1 A (A**2): 1868 ; 2.51 ; 10.00
REMARK 3 LOOSE THERMAL 1 B (A**2): 1868 ; 2.50 ; 10.00
REMARK 3 LOOSE THERMAL 1 C (A**2): 1868 ; 2.28 ; 10.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 134 A 245
REMARK 3 ORIGIN FOR THE GROUP (A): 46.4630 36.9480 71.1650
REMARK 3 T TENSOR
REMARK 3 T11: -0.1354 T22: -0.2031
REMARK 3 T33: 0.0108 T12: -0.0159
REMARK 3 T13: -0.0183 T23: 0.0375
REMARK 3 L TENSOR
REMARK 3 L11: 4.4800 L22: 5.7128
REMARK 3 L33: 2.2510 L12: 0.9685
REMARK 3 L13: 1.0294 L23: 0.6689
REMARK 3 S TENSOR
REMARK 3 S11: -0.1353 S12: 0.3610 S13: 0.7974
REMARK 3 S21: -0.1760 S22: 0.1003 S23: 0.1135
REMARK 3 S31: -0.4114 S32: 0.0472 S33: 0.0350
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 246 A 365
REMARK 3 ORIGIN FOR THE GROUP (A): 38.1100 10.1030 66.6880
REMARK 3 T TENSOR
REMARK 3 T11: -0.1121 T22: -0.1830
REMARK 3 T33: -0.1957 T12: -0.0755
REMARK 3 T13: -0.0097 T23: -0.0137
REMARK 3 L TENSOR
REMARK 3 L11: 1.9281 L22: 4.9044
REMARK 3 L33: 5.2923 L12: 0.7922
REMARK 3 L13: -0.1752 L23: -0.0242
REMARK 3 S TENSOR
REMARK 3 S11: -0.0949 S12: 0.2326 S13: 0.0821
REMARK 3 S21: -0.2739 S22: 0.1225 S23: -0.0715
REMARK 3 S31: 0.2359 S32: -0.1883 S33: -0.0276
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 : B 135 B 245
REMARK 3 ORIGIN FOR THE GROUP (A): 36.8600 -0.6870 91.2400
REMARK 3 T TENSOR
REMARK 3 T11: -0.0243 T22: -0.1058
REMARK 3 T33: -0.2495 T12: 0.0253
REMARK 3 T13: 0.0310 T23: -0.0504
REMARK 3 L TENSOR
REMARK 3 L11: 3.9265 L22: 1.4059
REMARK 3 L33: 4.9130 L12: -0.0296
REMARK 3 L13: 2.0266 L23: -0.1209
REMARK 3 S TENSOR
REMARK 3 S11: -0.1552 S12: -0.4377 S13: 0.0842
REMARK 3 S21: 0.2309 S22: 0.2219 S23: -0.1783
REMARK 3 S31: 0.0839 S32: -0.4500 S33: -0.0667
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 246 B 364
REMARK 3 ORIGIN FOR THE GROUP (A): 10.4820 -6.7840 82.0940
REMARK 3 T TENSOR
REMARK 3 T11: -0.0380 T22: 0.3876
REMARK 3 T33: 0.0586 T12: -0.0687
REMARK 3 T13: 0.1343 T23: 0.1889
REMARK 3 L TENSOR
REMARK 3 L11: 6.6958 L22: 4.2253
REMARK 3 L33: 3.3252 L12: -2.5209
REMARK 3 L13: 0.3095 L23: 1.3419
REMARK 3 S TENSOR
REMARK 3 S11: -0.0537 S12: -0.9258 S13: -0.4086
REMARK 3 S21: 0.3684 S22: 0.3136 S23: 0.9380
REMARK 3 S31: -0.2497 S32: -0.8453 S33: -0.2599
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 134 C 245
REMARK 3 ORIGIN FOR THE GROUP (A): 13.6750 36.8060 62.4520
REMARK 3 T TENSOR
REMARK 3 T11: -0.1678 T22: -0.0453
REMARK 3 T33: -0.0299 T12: -0.0232
REMARK 3 T13: -0.0341 T23: 0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 5.7768 L22: 1.8200
REMARK 3 L33: 5.4653 L12: 1.9802
REMARK 3 L13: -3.8130 L23: -0.7384
REMARK 3 S TENSOR
REMARK 3 S11: 0.0794 S12: 0.1571 S13: -0.4137
REMARK 3 S21: -0.0957 S22: -0.0957 S23: -0.1756
REMARK 3 S31: 0.1012 S32: 0.0432 S33: 0.0163
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 246 C 365
REMARK 3 ORIGIN FOR THE GROUP (A): -7.0520 24.3340 78.6530
REMARK 3 T TENSOR
REMARK 3 T11: -0.1581 T22: -0.1312
REMARK 3 T33: -0.0116 T12: -0.0113
REMARK 3 T13: 0.0259 T23: -0.0376
REMARK 3 L TENSOR
REMARK 3 L11: 6.1676 L22: 2.6848
REMARK 3 L33: 4.7182 L12: 1.1769
REMARK 3 L13: 2.4424 L23: -1.4116
REMARK 3 S TENSOR
REMARK 3 S11: 0.1756 S12: 0.2796 S13: -0.7437
REMARK 3 S21: -0.0180 S22: -0.0359 S23: 0.0252
REMARK 3 S31: 0.2833 S32: 0.4112 S33: -0.1397
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 : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2H8L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUN-06.
REMARK 100 THE RCSB ID CODE IS RCSB038065.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JUN-05
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X8C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795, 0.9950
REMARK 200 MONOCHROMATOR : SI (111) DOUBLE-CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : ADSC
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 62742
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.600
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.1
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: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHELXS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 3350, 0.1M AMMONIUM SULPHATE,
REMARK 280 0.1M HEPES, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293K
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 31.20750
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, 3
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 GLY A 129
REMARK 465 PRO A 130
REMARK 465 LEU A 131
REMARK 465 GLY A 132
REMARK 465 SER A 133
REMARK 465 LYS A 366
REMARK 465 SER A 367
REMARK 465 GLU A 368
REMARK 465 PRO A 369
REMARK 465 ILE A 370
REMARK 465 PRO A 371
REMARK 465 GLU A 372
REMARK 465 SER A 373
REMARK 465 ASN A 374
REMARK 465 ASP A 375
REMARK 465 GLY A 376
REMARK 465 ALA A 377
REMARK 465 ALA A 378
REMARK 465 ALA A 379
REMARK 465 SER A 380
REMARK 465 GLY B 129
REMARK 465 PRO B 130
REMARK 465 LEU B 131
REMARK 465 GLY B 132
REMARK 465 SER B 133
REMARK 465 PRO B 134
REMARK 465 LEU B 365
REMARK 465 LYS B 366
REMARK 465 SER B 367
REMARK 465 GLU B 368
REMARK 465 PRO B 369
REMARK 465 ILE B 370
REMARK 465 PRO B 371
REMARK 465 GLU B 372
REMARK 465 SER B 373
REMARK 465 ASN B 374
REMARK 465 ASP B 375
REMARK 465 GLY B 376
REMARK 465 ALA B 377
REMARK 465 ALA B 378
REMARK 465 ALA B 379
REMARK 465 SER B 380
REMARK 465 GLY C 129
REMARK 465 PRO C 130
REMARK 465 LEU C 131
REMARK 465 GLY C 132
REMARK 465 SER C 133
REMARK 465 LYS C 366
REMARK 465 SER C 367
REMARK 465 GLU C 368
REMARK 465 PRO C 369
REMARK 465 ILE C 370
REMARK 465 PRO C 371
REMARK 465 GLU C 372
REMARK 465 SER C 373
REMARK 465 ASN C 374
REMARK 465 ASP C 375
REMARK 465 GLY C 376
REMARK 465 ALA C 377
REMARK 465 ALA C 378
REMARK 465 ALA C 379
REMARK 465 SER C 380
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 CE LYS A 218 O HOH A 418 2.11
REMARK 500 O HOH A 470 O HOH A 531 2.16
REMARK 500 O HOH B 382 O HOH B 507 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NH1 ARG C 282 O HOH A 487 1455 2.09
REMARK 500 CB ALA B 320 O HOH C 516 1545 2.15
REMARK 500 OD1 ASP A 198 NH2 ARG C 282 1655 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 LYS A 218 CE LYS A 218 NZ 0.165
REMARK 500 TRP A 279 CB TRP A 279 CG 0.123
REMARK 500 GLU B 249 CD GLU B 249 OE1 0.097
REMARK 500 TYR B 269 CD1 TYR B 269 CE1 0.092
REMARK 500 GLU B 310 C GLU B 310 O 0.175
REMARK 500 SER B 312 CB SER B 312 OG 0.145
REMARK 500 SER B 312 C ASP B 313 N 0.255
REMARK 500 PHE B 314 C PHE B 314 O 0.115
REMARK 500 PHE B 314 C GLY B 315 N 0.160
REMARK 500 GLU B 317 CG GLU B 317 CD 0.410
REMARK 500 GLU B 317 CD GLU B 317 OE1 0.204
REMARK 500 GLU B 317 C GLU B 317 O 0.152
REMARK 500 ARG C 344 CZ ARG C 344 NH1 0.103
REMARK 500 LEU C 365 C LEU C 365 O 0.131
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 ARG A 207 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ASP A 259 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG A 344 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG B 280 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 GLU B 317 OE1 - CD - OE2 ANGL. DEV. = 8.0 DEGREES
REMARK 500 ARG B 344 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG C 207 NE - CZ - NH1 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ARG C 207 NE - CZ - NH2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ASP C 266 CB - CG - OD1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ARG C 344 NE - CZ - NH1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG C 344 NE - CZ - NH2 ANGL. DEV. = -7.8 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 GLU A 201 91.54 -162.58
REMARK 500 CYS A 244 75.58 -153.55
REMARK 500 TYR A 265 -160.58 -164.78
REMARK 500 ASP A 268 104.19 -171.33
REMARK 500 ASN A 272 51.34 -140.77
REMARK 500 ALA A 293 -175.49 -65.14
REMARK 500 ASP B 151 154.77 -49.91
REMARK 500 CYS B 244 77.29 -157.38
REMARK 500 TYR B 265 -162.73 -161.10
REMARK 500 ASP B 268 104.76 -162.94
REMARK 500 ASN B 272 41.78 -145.25
REMARK 500 PHE B 307 41.23 -102.19
REMARK 500 ALA B 320 -114.46 -109.24
REMARK 500 LYS B 332 -8.29 -51.17
REMARK 500 ARG C 179 -36.59 -35.48
REMARK 500 GLU C 201 88.65 -156.27
REMARK 500 TYR C 265 -163.08 -164.58
REMARK 500 ASP C 268 97.24 -171.34
REMARK 500 ASN C 272 44.78 -143.87
REMARK 500 LEU C 297 143.46 -170.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 TYR A 364 LEU A 365 145.79
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ASP C 161 24.1 L L OUTSIDE RANGE
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 468 DISTANCE = 5.16 ANGSTROMS
DBREF 2H8L A 134 376 UNP P30101 PDIA3_HUMAN 134 376
DBREF 2H8L B 134 376 UNP P30101 PDIA3_HUMAN 134 376
DBREF 2H8L C 134 376 UNP P30101 PDIA3_HUMAN 134 376
SEQADV 2H8L GLY A 129 UNP P30101 CLONING ARTIFACT
SEQADV 2H8L PRO A 130 UNP P30101 CLONING ARTIFACT
SEQADV 2H8L LEU A 131 UNP P30101 CLONING ARTIFACT
SEQADV 2H8L GLY A 132 UNP P30101 CLONING ARTIFACT
SEQADV 2H8L SER A 133 UNP P30101 CLONING ARTIFACT
SEQADV 2H8L MSE A 227 UNP P30101 MET 227 MODIFIED RESIDUE
SEQADV 2H8L MSE A 247 UNP P30101 MET 247 MODIFIED RESIDUE
SEQADV 2H8L MSE A 284 UNP P30101 MET 284 MODIFIED RESIDUE
SEQADV 2H8L MSE A 285 UNP P30101 MET 285 MODIFIED RESIDUE
SEQADV 2H8L MSE A 338 UNP P30101 MET 338 MODIFIED RESIDUE
SEQADV 2H8L ALA A 377 UNP P30101 CLONING ARTIFACT
SEQADV 2H8L ALA A 378 UNP P30101 CLONING ARTIFACT
SEQADV 2H8L ALA A 379 UNP P30101 CLONING ARTIFACT
SEQADV 2H8L SER A 380 UNP P30101 CLONING ARTIFACT
SEQADV 2H8L GLY B 129 UNP P30101 CLONING ARTIFACT
SEQADV 2H8L PRO B 130 UNP P30101 CLONING ARTIFACT
SEQADV 2H8L LEU B 131 UNP P30101 CLONING ARTIFACT
SEQADV 2H8L GLY B 132 UNP P30101 CLONING ARTIFACT
SEQADV 2H8L SER B 133 UNP P30101 CLONING ARTIFACT
SEQADV 2H8L MSE B 227 UNP P30101 MET 227 MODIFIED RESIDUE
SEQADV 2H8L MSE B 247 UNP P30101 MET 247 MODIFIED RESIDUE
SEQADV 2H8L MSE B 284 UNP P30101 MET 284 MODIFIED RESIDUE
SEQADV 2H8L MSE B 285 UNP P30101 MET 285 MODIFIED RESIDUE
SEQADV 2H8L MSE B 338 UNP P30101 MET 338 MODIFIED RESIDUE
SEQADV 2H8L ALA B 377 UNP P30101 CLONING ARTIFACT
SEQADV 2H8L ALA B 378 UNP P30101 CLONING ARTIFACT
SEQADV 2H8L ALA B 379 UNP P30101 CLONING ARTIFACT
SEQADV 2H8L SER B 380 UNP P30101 CLONING ARTIFACT
SEQADV 2H8L GLY C 129 UNP P30101 CLONING ARTIFACT
SEQADV 2H8L PRO C 130 UNP P30101 CLONING ARTIFACT
SEQADV 2H8L LEU C 131 UNP P30101 CLONING ARTIFACT
SEQADV 2H8L GLY C 132 UNP P30101 CLONING ARTIFACT
SEQADV 2H8L SER C 133 UNP P30101 CLONING ARTIFACT
SEQADV 2H8L MSE C 227 UNP P30101 MET 227 MODIFIED RESIDUE
SEQADV 2H8L MSE C 247 UNP P30101 MET 247 MODIFIED RESIDUE
SEQADV 2H8L MSE C 284 UNP P30101 MET 284 MODIFIED RESIDUE
SEQADV 2H8L MSE C 285 UNP P30101 MET 285 MODIFIED RESIDUE
SEQADV 2H8L MSE C 338 UNP P30101 MET 338 MODIFIED RESIDUE
SEQADV 2H8L ALA C 377 UNP P30101 CLONING ARTIFACT
SEQADV 2H8L ALA C 378 UNP P30101 CLONING ARTIFACT
SEQADV 2H8L ALA C 379 UNP P30101 CLONING ARTIFACT
SEQADV 2H8L SER C 380 UNP P30101 CLONING ARTIFACT
SEQRES 1 A 252 GLY PRO LEU GLY SER PRO ALA SER VAL PRO LEU ARG THR
SEQRES 2 A 252 GLU GLU GLU PHE LYS LYS PHE ILE SER ASP LYS ASP ALA
SEQRES 3 A 252 SER ILE VAL GLY PHE PHE ASP ASP SER PHE SER GLU ALA
SEQRES 4 A 252 HIS SER GLU PHE LEU LYS ALA ALA SER ASN LEU ARG ASP
SEQRES 5 A 252 ASN TYR ARG PHE ALA HIS THR ASN VAL GLU SER LEU VAL
SEQRES 6 A 252 ASN GLU TYR ASP ASP ASN GLY GLU GLY ILE ILE LEU PHE
SEQRES 7 A 252 ARG PRO SER HIS LEU THR ASN LYS PHE GLU ASP LYS THR
SEQRES 8 A 252 VAL ALA TYR THR GLU GLN LYS MSE THR SER GLY LYS ILE
SEQRES 9 A 252 LYS LYS PHE ILE GLN GLU ASN ILE PHE GLY ILE CYS PRO
SEQRES 10 A 252 HIS MSE THR GLU ASP ASN LYS ASP LEU ILE GLN GLY LYS
SEQRES 11 A 252 ASP LEU LEU ILE ALA TYR TYR ASP VAL ASP TYR GLU LYS
SEQRES 12 A 252 ASN ALA LYS GLY SER ASN TYR TRP ARG ASN ARG VAL MSE
SEQRES 13 A 252 MSE VAL ALA LYS LYS PHE LEU ASP ALA GLY HIS LYS LEU
SEQRES 14 A 252 ASN PHE ALA VAL ALA SER ARG LYS THR PHE SER HIS GLU
SEQRES 15 A 252 LEU SER ASP PHE GLY LEU GLU SER THR ALA GLY GLU ILE
SEQRES 16 A 252 PRO VAL VAL ALA ILE ARG THR ALA LYS GLY GLU LYS PHE
SEQRES 17 A 252 VAL MSE GLN GLU GLU PHE SER ARG ASP GLY LYS ALA LEU
SEQRES 18 A 252 GLU ARG PHE LEU GLN ASP TYR PHE ASP GLY ASN LEU LYS
SEQRES 19 A 252 ARG TYR LEU LYS SER GLU PRO ILE PRO GLU SER ASN ASP
SEQRES 20 A 252 GLY ALA ALA ALA SER
SEQRES 1 B 252 GLY PRO LEU GLY SER PRO ALA SER VAL PRO LEU ARG THR
SEQRES 2 B 252 GLU GLU GLU PHE LYS LYS PHE ILE SER ASP LYS ASP ALA
SEQRES 3 B 252 SER ILE VAL GLY PHE PHE ASP ASP SER PHE SER GLU ALA
SEQRES 4 B 252 HIS SER GLU PHE LEU LYS ALA ALA SER ASN LEU ARG ASP
SEQRES 5 B 252 ASN TYR ARG PHE ALA HIS THR ASN VAL GLU SER LEU VAL
SEQRES 6 B 252 ASN GLU TYR ASP ASP ASN GLY GLU GLY ILE ILE LEU PHE
SEQRES 7 B 252 ARG PRO SER HIS LEU THR ASN LYS PHE GLU ASP LYS THR
SEQRES 8 B 252 VAL ALA TYR THR GLU GLN LYS MSE THR SER GLY LYS ILE
SEQRES 9 B 252 LYS LYS PHE ILE GLN GLU ASN ILE PHE GLY ILE CYS PRO
SEQRES 10 B 252 HIS MSE THR GLU ASP ASN LYS ASP LEU ILE GLN GLY LYS
SEQRES 11 B 252 ASP LEU LEU ILE ALA TYR TYR ASP VAL ASP TYR GLU LYS
SEQRES 12 B 252 ASN ALA LYS GLY SER ASN TYR TRP ARG ASN ARG VAL MSE
SEQRES 13 B 252 MSE VAL ALA LYS LYS PHE LEU ASP ALA GLY HIS LYS LEU
SEQRES 14 B 252 ASN PHE ALA VAL ALA SER ARG LYS THR PHE SER HIS GLU
SEQRES 15 B 252 LEU SER ASP PHE GLY LEU GLU SER THR ALA GLY GLU ILE
SEQRES 16 B 252 PRO VAL VAL ALA ILE ARG THR ALA LYS GLY GLU LYS PHE
SEQRES 17 B 252 VAL MSE GLN GLU GLU PHE SER ARG ASP GLY LYS ALA LEU
SEQRES 18 B 252 GLU ARG PHE LEU GLN ASP TYR PHE ASP GLY ASN LEU LYS
SEQRES 19 B 252 ARG TYR LEU LYS SER GLU PRO ILE PRO GLU SER ASN ASP
SEQRES 20 B 252 GLY ALA ALA ALA SER
SEQRES 1 C 252 GLY PRO LEU GLY SER PRO ALA SER VAL PRO LEU ARG THR
SEQRES 2 C 252 GLU GLU GLU PHE LYS LYS PHE ILE SER ASP LYS ASP ALA
SEQRES 3 C 252 SER ILE VAL GLY PHE PHE ASP ASP SER PHE SER GLU ALA
SEQRES 4 C 252 HIS SER GLU PHE LEU LYS ALA ALA SER ASN LEU ARG ASP
SEQRES 5 C 252 ASN TYR ARG PHE ALA HIS THR ASN VAL GLU SER LEU VAL
SEQRES 6 C 252 ASN GLU TYR ASP ASP ASN GLY GLU GLY ILE ILE LEU PHE
SEQRES 7 C 252 ARG PRO SER HIS LEU THR ASN LYS PHE GLU ASP LYS THR
SEQRES 8 C 252 VAL ALA TYR THR GLU GLN LYS MSE THR SER GLY LYS ILE
SEQRES 9 C 252 LYS LYS PHE ILE GLN GLU ASN ILE PHE GLY ILE CYS PRO
SEQRES 10 C 252 HIS MSE THR GLU ASP ASN LYS ASP LEU ILE GLN GLY LYS
SEQRES 11 C 252 ASP LEU LEU ILE ALA TYR TYR ASP VAL ASP TYR GLU LYS
SEQRES 12 C 252 ASN ALA LYS GLY SER ASN TYR TRP ARG ASN ARG VAL MSE
SEQRES 13 C 252 MSE VAL ALA LYS LYS PHE LEU ASP ALA GLY HIS LYS LEU
SEQRES 14 C 252 ASN PHE ALA VAL ALA SER ARG LYS THR PHE SER HIS GLU
SEQRES 15 C 252 LEU SER ASP PHE GLY LEU GLU SER THR ALA GLY GLU ILE
SEQRES 16 C 252 PRO VAL VAL ALA ILE ARG THR ALA LYS GLY GLU LYS PHE
SEQRES 17 C 252 VAL MSE GLN GLU GLU PHE SER ARG ASP GLY LYS ALA LEU
SEQRES 18 C 252 GLU ARG PHE LEU GLN ASP TYR PHE ASP GLY ASN LEU LYS
SEQRES 19 C 252 ARG TYR LEU LYS SER GLU PRO ILE PRO GLU SER ASN ASP
SEQRES 20 C 252 GLY ALA ALA ALA SER
MODRES 2H8L MSE A 227 MET SELENOMETHIONINE
MODRES 2H8L MSE A 247 MET SELENOMETHIONINE
MODRES 2H8L MSE A 284 MET SELENOMETHIONINE
MODRES 2H8L MSE A 285 MET SELENOMETHIONINE
MODRES 2H8L MSE A 338 MET SELENOMETHIONINE
MODRES 2H8L MSE B 227 MET SELENOMETHIONINE
MODRES 2H8L MSE B 247 MET SELENOMETHIONINE
MODRES 2H8L MSE B 284 MET SELENOMETHIONINE
MODRES 2H8L MSE B 285 MET SELENOMETHIONINE
MODRES 2H8L MSE B 338 MET SELENOMETHIONINE
MODRES 2H8L MSE C 227 MET SELENOMETHIONINE
MODRES 2H8L MSE C 247 MET SELENOMETHIONINE
MODRES 2H8L MSE C 284 MET SELENOMETHIONINE
MODRES 2H8L MSE C 285 MET SELENOMETHIONINE
MODRES 2H8L MSE C 338 MET SELENOMETHIONINE
HET MSE A 227 8
HET MSE A 247 8
HET MSE A 284 8
HET MSE A 285 8
HET MSE A 338 8
HET MSE B 227 8
HET MSE B 247 8
HET MSE B 284 8
HET MSE B 285 8
HET MSE B 338 8
HET MSE C 227 8
HET MSE C 247 8
HET MSE C 284 8
HET MSE C 285 8
HET MSE C 338 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 15(C5 H11 N O2 SE)
FORMUL 4 HOH *453(H2 O)
HELIX 1 1 THR A 141 SER A 150 1 10
HELIX 2 2 SER A 165 LEU A 178 1 14
HELIX 3 3 VAL A 189 ASP A 197 1 9
HELIX 4 4 PRO A 208 THR A 212 5 5
HELIX 5 5 THR A 228 ILE A 240 1 13
HELIX 6 6 ASN A 251 GLN A 256 1 6
HELIX 7 7 ASN A 272 ALA A 293 1 22
HELIX 8 8 PHE A 307 SER A 312 1 6
HELIX 9 9 ASP A 313 GLY A 315 5 3
HELIX 10 10 GLY A 346 GLY A 359 1 14
HELIX 11 11 THR B 141 SER B 150 1 10
HELIX 12 12 SER B 165 LEU B 178 1 14
HELIX 13 13 VAL B 189 ASP B 197 1 9
HELIX 14 14 PRO B 208 THR B 212 5 5
HELIX 15 15 THR B 228 ILE B 240 1 13
HELIX 16 16 ASN B 251 GLN B 256 1 6
HELIX 17 17 ASN B 272 ALA B 293 1 22
HELIX 18 18 HIS B 309 ASP B 313 5 5
HELIX 19 19 GLY B 346 GLY B 359 1 14
HELIX 20 20 THR C 141 SER C 150 1 10
HELIX 21 21 SER C 165 ARG C 179 1 15
HELIX 22 22 VAL C 189 ASP C 197 1 9
HELIX 23 23 PRO C 208 THR C 212 5 5
HELIX 24 24 THR C 228 ILE C 240 1 13
HELIX 25 25 ASN C 251 GLN C 256 1 6
HELIX 26 26 ASN C 272 ALA C 293 1 22
HELIX 27 27 PHE C 307 ASP C 313 1 7
HELIX 28 28 GLY C 346 GLY C 359 1 14
SHEET 1 A 5 SER A 136 PRO A 138 0
SHEET 2 A 5 ARG A 183 THR A 187 1 O HIS A 186 N VAL A 137
SHEET 3 A 5 SER A 155 PHE A 160 1 N GLY A 158 O ALA A 185
SHEET 4 A 5 GLU A 201 PHE A 206 -1 O GLY A 202 N PHE A 159
SHEET 5 A 5 THR A 219 ALA A 221 -1 O VAL A 220 N LEU A 205
SHEET 1 B 4 ASN A 298 SER A 303 0
SHEET 2 B 4 LEU A 260 TYR A 265 1 N LEU A 261 O ASN A 298
SHEET 3 B 4 VAL A 325 ARG A 329 -1 O ALA A 327 N ILE A 262
SHEET 4 B 4 LYS A 335 VAL A 337 -1 O PHE A 336 N ILE A 328
SHEET 1 C 5 SER B 136 LEU B 139 0
SHEET 2 C 5 PHE B 184 THR B 187 1 O HIS B 186 N VAL B 137
SHEET 3 C 5 SER B 155 PHE B 160 1 N PHE B 160 O THR B 187
SHEET 4 C 5 GLU B 201 PHE B 206 -1 O GLY B 202 N PHE B 159
SHEET 5 C 5 THR B 219 ALA B 221 -1 O VAL B 220 N LEU B 205
SHEET 1 D 5 HIS B 246 MSE B 247 0
SHEET 2 D 5 ASN B 298 SER B 303 1 O VAL B 301 N MSE B 247
SHEET 3 D 5 LEU B 260 TYR B 265 1 N LEU B 261 O ASN B 298
SHEET 4 D 5 VAL B 325 ARG B 329 -1 O ARG B 329 N LEU B 260
SHEET 5 D 5 LYS B 335 VAL B 337 -1 O PHE B 336 N ILE B 328
SHEET 1 E 5 SER C 136 PRO C 138 0
SHEET 2 E 5 PHE C 184 THR C 187 1 O HIS C 186 N VAL C 137
SHEET 3 E 5 SER C 155 PHE C 160 1 N PHE C 160 O THR C 187
SHEET 4 E 5 GLU C 201 PHE C 206 -1 O GLY C 202 N PHE C 159
SHEET 5 E 5 THR C 219 ALA C 221 -1 O VAL C 220 N LEU C 205
SHEET 1 F 5 HIS C 246 MSE C 247 0
SHEET 2 F 5 ASN C 298 SER C 303 1 O VAL C 301 N MSE C 247
SHEET 3 F 5 LEU C 260 TYR C 265 1 N LEU C 261 O ASN C 298
SHEET 4 F 5 VAL C 325 ARG C 329 -1 O VAL C 325 N TYR C 264
SHEET 5 F 5 LYS C 335 VAL C 337 -1 O PHE C 336 N ILE C 328
LINK C LYS A 226 N MSE A 227 1555 1555 1.33
LINK C MSE A 227 N THR A 228 1555 1555 1.34
LINK C HIS A 246 N MSE A 247 1555 1555 1.34
LINK C MSE A 247 N THR A 248 1555 1555 1.34
LINK C VAL A 283 N MSE A 284 1555 1555 1.34
LINK C MSE A 284 N MSE A 285 1555 1555 1.32
LINK C MSE A 285 N VAL A 286 1555 1555 1.34
LINK C VAL A 337 N MSE A 338 1555 1555 1.33
LINK C MSE A 338 N GLN A 339 1555 1555 1.35
LINK C LYS B 226 N MSE B 227 1555 1555 1.33
LINK C MSE B 227 N THR B 228 1555 1555 1.33
LINK C HIS B 246 N MSE B 247 1555 1555 1.33
LINK C MSE B 247 N THR B 248 1555 1555 1.35
LINK C VAL B 283 N MSE B 284 1555 1555 1.34
LINK C MSE B 284 N MSE B 285 1555 1555 1.33
LINK C MSE B 285 N VAL B 286 1555 1555 1.33
LINK C VAL B 337 N MSE B 338 1555 1555 1.34
LINK C MSE B 338 N GLN B 339 1555 1555 1.34
LINK C LYS C 226 N MSE C 227 1555 1555 1.33
LINK C MSE C 227 N THR C 228 1555 1555 1.33
LINK C HIS C 246 N MSE C 247 1555 1555 1.33
LINK C MSE C 247 N THR C 248 1555 1555 1.33
LINK C VAL C 283 N MSE C 284 1555 1555 1.36
LINK C MSE C 284 N MSE C 285 1555 1555 1.31
LINK C MSE C 285 N VAL C 286 1555 1555 1.33
LINK C VAL C 337 N MSE C 338 1555 1555 1.34
LINK C MSE C 338 N GLN C 339 1555 1555 1.32
CRYST1 76.340 62.415 99.293 90.00 98.40 90.00 P 1 21 1 6
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 0.013099 0.000000 0.001934 0.00000
SCALE2 0.000000 0.016022 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010180 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
