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HEADER OXIDOREDUCTASE 23-JAN-13 4IVJ
TITLE STRUCTURE OF A 16 NM PROTEIN CAGE DESIGNED BY FUSING SYMMETRIC
TITLE 2 OLIGOMERIC DOMAINS, TRIPLE MUTANT, I222 FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NON-HAEM BROMOPEROXIDASE BPO-A2, MATRIX PROTEIN 1;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: BPO2, BROMIDE PEROXIDASE, M1;
COMPND 5 EC: 1.11.1.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES AUREOFACIENS, INFLUENZA A VIRUS;
SOURCE 3 ORGANISM_TAXID: 1894, 211044;
SOURCE 4 STRAIN: A/PUERTO RICO/8/1934 H1N1;
SOURCE 5 GENE: BPOA2, BROMOPEROXIDASE A2 AND M1 MATRIX, M;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS PROTEIN DESIGN, BIONANOTECHNOLOGY, PROTEIN ASSEMBLY, SYMMETRIC
KEYWDS 2 OLIGOMERIC DOMAINS, BIOMATERIALS, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.-T.LAI,M.R.SAWAYA,T.O.YEATES
REVDAT 1 24-JUL-13 4IVJ 0
JRNL AUTH Y.T.LAI,K.L.TSAI,M.R.SAWAYA,F.J.ASTURIAS,T.O.YEATES
JRNL TITL STRUCTURE AND FLEXIBILITY OF NANOSCALE PROTEIN CAGES
JRNL TITL 2 DESIGNED BY SYMMETRIC SELF-ASSEMBLY.
JRNL REF J.AM.CHEM.SOC. V. 135 7738 2013
JRNL REFN ISSN 0002-7863
JRNL PMID 23621606
JRNL DOI 10.1021/JA402277F
REMARK 2
REMARK 2 RESOLUTION. 7.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.1_1168)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 7.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.42
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 2431
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.277
REMARK 3 R VALUE (WORKING SET) : 0.276
REMARK 3 FREE R VALUE : 0.288
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980
REMARK 3 FREE R VALUE TEST SET COUNT : 121
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 0.0000 - 0.0000 0.00 0 0 0.0000 0.0000
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.390
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.130
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 383.65
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 318.45
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.015 10425
REMARK 3 ANGLE : 2.390 14187
REMARK 3 CHIRALITY : 0.114 1602
REMARK 3 PLANARITY : 0.008 1848
REMARK 3 DIHEDRAL : 15.896 3702
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: chain A and resid 1:287
REMARK 3 ORIGIN FOR THE GROUP (A): -21.4924 -9.9458 -46.5575
REMARK 3 T TENSOR
REMARK 3 T11: 3.0482 T22: 3.2616
REMARK 3 T33: 1.5458 T12: 0.9584
REMARK 3 T13: -0.1520 T23: 0.1838
REMARK 3 L TENSOR
REMARK 3 L11: -0.1127 L22: 2.6937
REMARK 3 L33: 1.7775 L12: -1.0663
REMARK 3 L13: -0.8059 L23: -0.1502
REMARK 3 S TENSOR
REMARK 3 S11: 1.2449 S12: 1.2203 S13: 0.4773
REMARK 3 S21: -3.2035 S22: -0.7876 S23: -0.2934
REMARK 3 S31: 0.2291 S32: -0.2024 S33: 0.9941
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: chain A and resid 288:440
REMARK 3 ORIGIN FOR THE GROUP (A): -18.4564 10.4953 -9.5139
REMARK 3 T TENSOR
REMARK 3 T11: 2.0737 T22: 2.7266
REMARK 3 T33: 1.6132 T12: -0.1233
REMARK 3 T13: -0.2610 T23: 0.4405
REMARK 3 L TENSOR
REMARK 3 L11: 0.1544 L22: 1.4581
REMARK 3 L33: 4.5457 L12: -0.3267
REMARK 3 L13: -1.2570 L23: 0.0635
REMARK 3 S TENSOR
REMARK 3 S11: -0.7126 S12: 0.8972 S13: 0.9198
REMARK 3 S21: 0.0237 S22: 1.1725 S23: 0.7249
REMARK 3 S31: 1.7696 S32: -3.0428 S33: -1.4010
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: chain B and resid 1:287
REMARK 3 ORIGIN FOR THE GROUP (A): -43.2757 -41.3402 -45.6845
REMARK 3 T TENSOR
REMARK 3 T11: 4.9966 T22: 3.4023
REMARK 3 T33: 5.7894 T12: -1.4471
REMARK 3 T13: -3.3650 T23: 0.3835
REMARK 3 L TENSOR
REMARK 3 L11: 0.3655 L22: 0.3294
REMARK 3 L33: 1.4732 L12: 0.4809
REMARK 3 L13: 0.9107 L23: 0.9790
REMARK 3 S TENSOR
REMARK 3 S11: 0.4068 S12: 0.6485 S13: -0.9438
REMARK 3 S21: -4.3219 S22: 3.0816 S23: 2.7255
REMARK 3 S31: 3.3496 S32: -4.4964 S33: 4.9831
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: chain B and resid 288:440
REMARK 3 ORIGIN FOR THE GROUP (A): -70.7310 -12.6252 -59.4230
REMARK 3 T TENSOR
REMARK 3 T11: 4.3621 T22: 3.1773
REMARK 3 T33: 5.1499 T12: -1.0683
REMARK 3 T13: -0.9445 T23: 0.2081
REMARK 3 L TENSOR
REMARK 3 L11: 2.5681 L22: 3.3008
REMARK 3 L33: 2.6542 L12: -0.9439
REMARK 3 L13: 2.1541 L23: -1.2848
REMARK 3 S TENSOR
REMARK 3 S11: 1.1276 S12: -0.7317 S13: -2.1472
REMARK 3 S21: 0.2036 S22: 2.3021 S23: 3.0470
REMARK 3 S31: -0.5486 S32: -1.6189 S33: 1.3616
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: chain C and resid 1:287
REMARK 3 ORIGIN FOR THE GROUP (A): -20.4393 -33.5752 -16.6105
REMARK 3 T TENSOR
REMARK 3 T11: 1.6115 T22: 2.1174
REMARK 3 T33: 1.1633 T12: 0.4662
REMARK 3 T13: 0.3324 T23: -1.2729
REMARK 3 L TENSOR
REMARK 3 L11: 3.1097 L22: 2.4024
REMARK 3 L33: 5.5959 L12: -1.0853
REMARK 3 L13: 2.7488 L23: -1.2347
REMARK 3 S TENSOR
REMARK 3 S11: 0.7753 S12: 1.1553 S13: -1.7417
REMARK 3 S21: -0.1346 S22: 1.7366 S23: 2.0356
REMARK 3 S31: 1.1200 S32: 1.4808 S33: 8.1279
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: chain C and resid 288:440
REMARK 3 ORIGIN FOR THE GROUP (A): -53.1720 -43.7673 8.3307
REMARK 3 T TENSOR
REMARK 3 T11: 2.3891 T22: 3.0602
REMARK 3 T33: 2.8469 T12: 0.1185
REMARK 3 T13: 1.5078 T23: 0.5015
REMARK 3 L TENSOR
REMARK 3 L11: 2.6100 L22: 2.3415
REMARK 3 L33: 4.0401 L12: 0.3953
REMARK 3 L13: 1.5009 L23: 2.9856
REMARK 3 S TENSOR
REMARK 3 S11: 1.9225 S12: -1.3373 S13: -1.1489
REMARK 3 S21: 1.3102 S22: 0.7601 S23: -0.8581
REMARK 3 S31: 0.0706 S32: 1.1985 S33: 3.4062
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4IVJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JAN-13.
REMARK 100 THE RCSB ID CODE IS RCSB077262.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-AUG-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.542
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS HTC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 2438
REMARK 200 RESOLUTION RANGE HIGH (A) : 7.350
REMARK 200 RESOLUTION RANGE LOW (A) : 29.283
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.08200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.2400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 7.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 7.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.77800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.440
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1BRO AND 1AA7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M NA CITRATE PH 4.4, 10% PEG 3000,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 64.83500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 80.49000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 83.81500
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 64.83500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 80.49000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 83.81500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 64.83500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 80.49000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 83.81500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 64.83500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 80.49000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 83.81500
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: DODECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 34510 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 188550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -112.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 -129.67000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 -129.67000
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 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 0
REMARK 465 GLN A 441
REMARK 465 HIS A 442
REMARK 465 ARG A 443
REMARK 465 SER A 444
REMARK 465 HIS A 445
REMARK 465 ARG A 446
REMARK 465 GLN A 447
REMARK 465 LEU A 448
REMARK 465 GLU A 449
REMARK 465 HIS A 450
REMARK 465 HIS A 451
REMARK 465 HIS A 452
REMARK 465 HIS A 453
REMARK 465 HIS A 454
REMARK 465 HIS A 455
REMARK 465 MET B 0
REMARK 465 GLN B 441
REMARK 465 HIS B 442
REMARK 465 ARG B 443
REMARK 465 SER B 444
REMARK 465 HIS B 445
REMARK 465 ARG B 446
REMARK 465 GLN B 447
REMARK 465 LEU B 448
REMARK 465 GLU B 449
REMARK 465 HIS B 450
REMARK 465 HIS B 451
REMARK 465 HIS B 452
REMARK 465 HIS B 453
REMARK 465 HIS B 454
REMARK 465 HIS B 455
REMARK 465 MET C 0
REMARK 465 GLN C 441
REMARK 465 HIS C 442
REMARK 465 ARG C 443
REMARK 465 SER C 444
REMARK 465 HIS C 445
REMARK 465 ARG C 446
REMARK 465 GLN C 447
REMARK 465 LEU C 448
REMARK 465 GLU C 449
REMARK 465 HIS C 450
REMARK 465 HIS C 451
REMARK 465 HIS C 452
REMARK 465 HIS C 453
REMARK 465 HIS C 454
REMARK 465 HIS C 455
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 9 -131.49 55.95
REMARK 500 PRO A 33 49.50 -105.62
REMARK 500 GLN A 66 65.22 -119.44
REMARK 500 SER A 98 -117.94 51.09
REMARK 500 THR A 176 -82.60 -116.14
REMARK 500 TYR A 206 35.22 -90.43
REMARK 500 PRO A 256 -168.99 -79.78
REMARK 500 ASN B 9 -124.25 54.60
REMARK 500 PRO B 33 49.51 -105.76
REMARK 500 ARG B 59 135.55 -38.38
REMARK 500 GLN B 66 65.18 -119.25
REMARK 500 SER B 98 -127.10 58.30
REMARK 500 THR B 176 -78.74 -125.34
REMARK 500 PRO B 256 -169.03 -79.71
REMARK 500 ASN C 9 -124.13 54.51
REMARK 500 PRO C 33 49.36 -105.88
REMARK 500 GLN C 66 65.20 -119.51
REMARK 500 SER C 98 -117.92 51.13
REMARK 500 THR C 176 -88.23 -118.52
REMARK 500 TYR C 206 35.42 -90.46
REMARK 500 PRO C 219 135.75 -38.86
REMARK 500 PRO C 256 -168.98 -79.82
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3VDX RELATED DB: PDB
REMARK 900 RELATED ID: 4D9J RELATED DB: PDB
REMARK 900 RELATED ID: 4IQ4 RELATED DB: PDB
REMARK 900 RELATED ID: 4ITV RELATED DB: PDB
DBREF 4IVJ A 0 277 UNP P29715 BPOA2_STRAU 1 278
DBREF 4IVJ A 286 448 UNP P03485 M1_I34A1 3 165
DBREF 4IVJ B 0 277 UNP P29715 BPOA2_STRAU 1 278
DBREF 4IVJ B 286 448 UNP P03485 M1_I34A1 3 165
DBREF 4IVJ C 0 277 UNP P29715 BPOA2_STRAU 1 278
DBREF 4IVJ C 286 448 UNP P03485 M1_I34A1 3 165
SEQADV 4IVJ THR A 24 UNP P29715 GLN 25 ENGINEERED MUTATION
SEQADV 4IVJ ALA A 118 UNP P29715 LYS 119 ENGINEERED MUTATION
SEQADV 4IVJ ALA A 278 UNP P03485 LINKER
SEQADV 4IVJ GLN A 279 UNP P03485 LINKER
SEQADV 4IVJ GLU A 280 UNP P03485 LINKER
SEQADV 4IVJ ALA A 281 UNP P03485 LINKER
SEQADV 4IVJ GLN A 282 UNP P03485 LINKER
SEQADV 4IVJ LYS A 283 UNP P03485 LINKER
SEQADV 4IVJ GLN A 284 UNP P03485 LINKER
SEQADV 4IVJ LYS A 285 UNP P03485 LINKER
SEQADV 4IVJ LEU A 448 UNP P03485 EXPRESSION TAG
SEQADV 4IVJ GLU A 449 UNP P03485 EXPRESSION TAG
SEQADV 4IVJ HIS A 450 UNP P03485 EXPRESSION TAG
SEQADV 4IVJ HIS A 451 UNP P03485 EXPRESSION TAG
SEQADV 4IVJ HIS A 452 UNP P03485 EXPRESSION TAG
SEQADV 4IVJ HIS A 453 UNP P03485 EXPRESSION TAG
SEQADV 4IVJ HIS A 454 UNP P03485 EXPRESSION TAG
SEQADV 4IVJ HIS A 455 UNP P03485 EXPRESSION TAG
SEQADV 4IVJ THR B 24 UNP P29715 GLN 25 ENGINEERED MUTATION
SEQADV 4IVJ ALA B 118 UNP P29715 LYS 119 ENGINEERED MUTATION
SEQADV 4IVJ ALA B 278 UNP P03485 LINKER
SEQADV 4IVJ GLN B 279 UNP P03485 LINKER
SEQADV 4IVJ GLU B 280 UNP P03485 LINKER
SEQADV 4IVJ ALA B 281 UNP P03485 LINKER
SEQADV 4IVJ GLN B 282 UNP P03485 LINKER
SEQADV 4IVJ LYS B 283 UNP P03485 LINKER
SEQADV 4IVJ GLN B 284 UNP P03485 LINKER
SEQADV 4IVJ LYS B 285 UNP P03485 LINKER
SEQADV 4IVJ LEU B 448 UNP P03485 EXPRESSION TAG
SEQADV 4IVJ GLU B 449 UNP P03485 EXPRESSION TAG
SEQADV 4IVJ HIS B 450 UNP P03485 EXPRESSION TAG
SEQADV 4IVJ HIS B 451 UNP P03485 EXPRESSION TAG
SEQADV 4IVJ HIS B 452 UNP P03485 EXPRESSION TAG
SEQADV 4IVJ HIS B 453 UNP P03485 EXPRESSION TAG
SEQADV 4IVJ HIS B 454 UNP P03485 EXPRESSION TAG
SEQADV 4IVJ HIS B 455 UNP P03485 EXPRESSION TAG
SEQADV 4IVJ THR C 24 UNP P29715 GLN 25 ENGINEERED MUTATION
SEQADV 4IVJ ALA C 118 UNP P29715 LYS 119 ENGINEERED MUTATION
SEQADV 4IVJ ALA C 278 UNP P03485 LINKER
SEQADV 4IVJ GLN C 279 UNP P03485 LINKER
SEQADV 4IVJ GLU C 280 UNP P03485 LINKER
SEQADV 4IVJ ALA C 281 UNP P03485 LINKER
SEQADV 4IVJ GLN C 282 UNP P03485 LINKER
SEQADV 4IVJ LYS C 283 UNP P03485 LINKER
SEQADV 4IVJ GLN C 284 UNP P03485 LINKER
SEQADV 4IVJ LYS C 285 UNP P03485 LINKER
SEQADV 4IVJ LEU C 448 UNP P03485 EXPRESSION TAG
SEQADV 4IVJ GLU C 449 UNP P03485 EXPRESSION TAG
SEQADV 4IVJ HIS C 450 UNP P03485 EXPRESSION TAG
SEQADV 4IVJ HIS C 451 UNP P03485 EXPRESSION TAG
SEQADV 4IVJ HIS C 452 UNP P03485 EXPRESSION TAG
SEQADV 4IVJ HIS C 453 UNP P03485 EXPRESSION TAG
SEQADV 4IVJ HIS C 454 UNP P03485 EXPRESSION TAG
SEQADV 4IVJ HIS C 455 UNP P03485 EXPRESSION TAG
SEQRES 1 A 456 MET PRO PHE ILE THR VAL GLY GLN GLU ASN SER THR SER
SEQRES 2 A 456 ILE ASP LEU TYR TYR GLU ASP HIS GLY THR GLY THR PRO
SEQRES 3 A 456 VAL VAL LEU ILE HIS GLY PHE PRO LEU SER GLY HIS SER
SEQRES 4 A 456 TRP GLU ARG GLN SER ALA ALA LEU LEU ASP ALA GLY TYR
SEQRES 5 A 456 ARG VAL ILE THR TYR ASP ARG ARG GLY PHE GLY GLN SER
SEQRES 6 A 456 SER GLN PRO THR THR GLY TYR ASP TYR ASP THR PHE ALA
SEQRES 7 A 456 ALA ASP LEU ASN THR VAL LEU GLU THR LEU ASP LEU GLN
SEQRES 8 A 456 ASP ALA VAL LEU VAL GLY PHE SER MET GLY THR GLY GLU
SEQRES 9 A 456 VAL ALA ARG TYR VAL SER SER TYR GLY THR ALA ARG ILE
SEQRES 10 A 456 ALA ALA VAL ALA PHE LEU ALA SER LEU GLU PRO PHE LEU
SEQRES 11 A 456 LEU LYS THR ASP ASP ASN PRO ASP GLY ALA ALA PRO GLN
SEQRES 12 A 456 GLU PHE PHE ASP GLY ILE VAL ALA ALA VAL LYS ALA ASP
SEQRES 13 A 456 ARG TYR ALA PHE TYR THR GLY PHE PHE ASN ASP PHE TYR
SEQRES 14 A 456 ASN LEU ASP GLU ASN LEU GLY THR ARG ILE SER GLU GLU
SEQRES 15 A 456 ALA VAL ARG ASN SER TRP ASN THR ALA ALA SER GLY GLY
SEQRES 16 A 456 PHE PHE ALA ALA ALA ALA ALA PRO THR THR TRP TYR THR
SEQRES 17 A 456 ASP PHE ARG ALA ASP ILE PRO ARG ILE ASP VAL PRO ALA
SEQRES 18 A 456 LEU ILE LEU HIS GLY THR GLY ASP ARG THR LEU PRO ILE
SEQRES 19 A 456 GLU ASN THR ALA ARG VAL PHE HIS LYS ALA LEU PRO SER
SEQRES 20 A 456 ALA GLU TYR VAL GLU VAL GLU GLY ALA PRO HIS GLY LEU
SEQRES 21 A 456 LEU TRP THR HIS ALA GLU GLU VAL ASN THR ALA LEU LEU
SEQRES 22 A 456 ALA PHE LEU ALA LYS ALA GLN GLU ALA GLN LYS GLN LYS
SEQRES 23 A 456 LEU LEU THR GLU VAL GLU THR TYR VAL LEU SER ILE ILE
SEQRES 24 A 456 PRO SER GLY PRO LEU LYS ALA GLU ILE ALA GLN ARG LEU
SEQRES 25 A 456 GLU ASP VAL PHE ALA GLY LYS ASN THR ASP LEU GLU VAL
SEQRES 26 A 456 LEU MET GLU TRP LEU LYS THR ARG PRO ILE LEU SER PRO
SEQRES 27 A 456 LEU THR LYS GLY ILE LEU GLY PHE VAL PHE THR LEU THR
SEQRES 28 A 456 VAL PRO SER GLU ARG GLY LEU GLN ARG ARG ARG PHE VAL
SEQRES 29 A 456 GLN ASN ALA LEU ASN GLY ASN GLY ASP PRO ASN ASN MET
SEQRES 30 A 456 ASP LYS ALA VAL LYS LEU TYR ARG LYS LEU LYS ARG GLU
SEQRES 31 A 456 ILE THR PHE HIS GLY ALA LYS GLU ILE SER LEU SER TYR
SEQRES 32 A 456 SER ALA GLY ALA LEU ALA SER CYS MET GLY LEU ILE TYR
SEQRES 33 A 456 ASN ARG MET GLY ALA VAL THR THR GLU VAL ALA PHE GLY
SEQRES 34 A 456 LEU VAL CYS ALA THR CYS GLU GLN ILE ALA ASP SER GLN
SEQRES 35 A 456 HIS ARG SER HIS ARG GLN LEU GLU HIS HIS HIS HIS HIS
SEQRES 36 A 456 HIS
SEQRES 1 B 456 MET PRO PHE ILE THR VAL GLY GLN GLU ASN SER THR SER
SEQRES 2 B 456 ILE ASP LEU TYR TYR GLU ASP HIS GLY THR GLY THR PRO
SEQRES 3 B 456 VAL VAL LEU ILE HIS GLY PHE PRO LEU SER GLY HIS SER
SEQRES 4 B 456 TRP GLU ARG GLN SER ALA ALA LEU LEU ASP ALA GLY TYR
SEQRES 5 B 456 ARG VAL ILE THR TYR ASP ARG ARG GLY PHE GLY GLN SER
SEQRES 6 B 456 SER GLN PRO THR THR GLY TYR ASP TYR ASP THR PHE ALA
SEQRES 7 B 456 ALA ASP LEU ASN THR VAL LEU GLU THR LEU ASP LEU GLN
SEQRES 8 B 456 ASP ALA VAL LEU VAL GLY PHE SER MET GLY THR GLY GLU
SEQRES 9 B 456 VAL ALA ARG TYR VAL SER SER TYR GLY THR ALA ARG ILE
SEQRES 10 B 456 ALA ALA VAL ALA PHE LEU ALA SER LEU GLU PRO PHE LEU
SEQRES 11 B 456 LEU LYS THR ASP ASP ASN PRO ASP GLY ALA ALA PRO GLN
SEQRES 12 B 456 GLU PHE PHE ASP GLY ILE VAL ALA ALA VAL LYS ALA ASP
SEQRES 13 B 456 ARG TYR ALA PHE TYR THR GLY PHE PHE ASN ASP PHE TYR
SEQRES 14 B 456 ASN LEU ASP GLU ASN LEU GLY THR ARG ILE SER GLU GLU
SEQRES 15 B 456 ALA VAL ARG ASN SER TRP ASN THR ALA ALA SER GLY GLY
SEQRES 16 B 456 PHE PHE ALA ALA ALA ALA ALA PRO THR THR TRP TYR THR
SEQRES 17 B 456 ASP PHE ARG ALA ASP ILE PRO ARG ILE ASP VAL PRO ALA
SEQRES 18 B 456 LEU ILE LEU HIS GLY THR GLY ASP ARG THR LEU PRO ILE
SEQRES 19 B 456 GLU ASN THR ALA ARG VAL PHE HIS LYS ALA LEU PRO SER
SEQRES 20 B 456 ALA GLU TYR VAL GLU VAL GLU GLY ALA PRO HIS GLY LEU
SEQRES 21 B 456 LEU TRP THR HIS ALA GLU GLU VAL ASN THR ALA LEU LEU
SEQRES 22 B 456 ALA PHE LEU ALA LYS ALA GLN GLU ALA GLN LYS GLN LYS
SEQRES 23 B 456 LEU LEU THR GLU VAL GLU THR TYR VAL LEU SER ILE ILE
SEQRES 24 B 456 PRO SER GLY PRO LEU LYS ALA GLU ILE ALA GLN ARG LEU
SEQRES 25 B 456 GLU ASP VAL PHE ALA GLY LYS ASN THR ASP LEU GLU VAL
SEQRES 26 B 456 LEU MET GLU TRP LEU LYS THR ARG PRO ILE LEU SER PRO
SEQRES 27 B 456 LEU THR LYS GLY ILE LEU GLY PHE VAL PHE THR LEU THR
SEQRES 28 B 456 VAL PRO SER GLU ARG GLY LEU GLN ARG ARG ARG PHE VAL
SEQRES 29 B 456 GLN ASN ALA LEU ASN GLY ASN GLY ASP PRO ASN ASN MET
SEQRES 30 B 456 ASP LYS ALA VAL LYS LEU TYR ARG LYS LEU LYS ARG GLU
SEQRES 31 B 456 ILE THR PHE HIS GLY ALA LYS GLU ILE SER LEU SER TYR
SEQRES 32 B 456 SER ALA GLY ALA LEU ALA SER CYS MET GLY LEU ILE TYR
SEQRES 33 B 456 ASN ARG MET GLY ALA VAL THR THR GLU VAL ALA PHE GLY
SEQRES 34 B 456 LEU VAL CYS ALA THR CYS GLU GLN ILE ALA ASP SER GLN
SEQRES 35 B 456 HIS ARG SER HIS ARG GLN LEU GLU HIS HIS HIS HIS HIS
SEQRES 36 B 456 HIS
SEQRES 1 C 456 MET PRO PHE ILE THR VAL GLY GLN GLU ASN SER THR SER
SEQRES 2 C 456 ILE ASP LEU TYR TYR GLU ASP HIS GLY THR GLY THR PRO
SEQRES 3 C 456 VAL VAL LEU ILE HIS GLY PHE PRO LEU SER GLY HIS SER
SEQRES 4 C 456 TRP GLU ARG GLN SER ALA ALA LEU LEU ASP ALA GLY TYR
SEQRES 5 C 456 ARG VAL ILE THR TYR ASP ARG ARG GLY PHE GLY GLN SER
SEQRES 6 C 456 SER GLN PRO THR THR GLY TYR ASP TYR ASP THR PHE ALA
SEQRES 7 C 456 ALA ASP LEU ASN THR VAL LEU GLU THR LEU ASP LEU GLN
SEQRES 8 C 456 ASP ALA VAL LEU VAL GLY PHE SER MET GLY THR GLY GLU
SEQRES 9 C 456 VAL ALA ARG TYR VAL SER SER TYR GLY THR ALA ARG ILE
SEQRES 10 C 456 ALA ALA VAL ALA PHE LEU ALA SER LEU GLU PRO PHE LEU
SEQRES 11 C 456 LEU LYS THR ASP ASP ASN PRO ASP GLY ALA ALA PRO GLN
SEQRES 12 C 456 GLU PHE PHE ASP GLY ILE VAL ALA ALA VAL LYS ALA ASP
SEQRES 13 C 456 ARG TYR ALA PHE TYR THR GLY PHE PHE ASN ASP PHE TYR
SEQRES 14 C 456 ASN LEU ASP GLU ASN LEU GLY THR ARG ILE SER GLU GLU
SEQRES 15 C 456 ALA VAL ARG ASN SER TRP ASN THR ALA ALA SER GLY GLY
SEQRES 16 C 456 PHE PHE ALA ALA ALA ALA ALA PRO THR THR TRP TYR THR
SEQRES 17 C 456 ASP PHE ARG ALA ASP ILE PRO ARG ILE ASP VAL PRO ALA
SEQRES 18 C 456 LEU ILE LEU HIS GLY THR GLY ASP ARG THR LEU PRO ILE
SEQRES 19 C 456 GLU ASN THR ALA ARG VAL PHE HIS LYS ALA LEU PRO SER
SEQRES 20 C 456 ALA GLU TYR VAL GLU VAL GLU GLY ALA PRO HIS GLY LEU
SEQRES 21 C 456 LEU TRP THR HIS ALA GLU GLU VAL ASN THR ALA LEU LEU
SEQRES 22 C 456 ALA PHE LEU ALA LYS ALA GLN GLU ALA GLN LYS GLN LYS
SEQRES 23 C 456 LEU LEU THR GLU VAL GLU THR TYR VAL LEU SER ILE ILE
SEQRES 24 C 456 PRO SER GLY PRO LEU LYS ALA GLU ILE ALA GLN ARG LEU
SEQRES 25 C 456 GLU ASP VAL PHE ALA GLY LYS ASN THR ASP LEU GLU VAL
SEQRES 26 C 456 LEU MET GLU TRP LEU LYS THR ARG PRO ILE LEU SER PRO
SEQRES 27 C 456 LEU THR LYS GLY ILE LEU GLY PHE VAL PHE THR LEU THR
SEQRES 28 C 456 VAL PRO SER GLU ARG GLY LEU GLN ARG ARG ARG PHE VAL
SEQRES 29 C 456 GLN ASN ALA LEU ASN GLY ASN GLY ASP PRO ASN ASN MET
SEQRES 30 C 456 ASP LYS ALA VAL LYS LEU TYR ARG LYS LEU LYS ARG GLU
SEQRES 31 C 456 ILE THR PHE HIS GLY ALA LYS GLU ILE SER LEU SER TYR
SEQRES 32 C 456 SER ALA GLY ALA LEU ALA SER CYS MET GLY LEU ILE TYR
SEQRES 33 C 456 ASN ARG MET GLY ALA VAL THR THR GLU VAL ALA PHE GLY
SEQRES 34 C 456 LEU VAL CYS ALA THR CYS GLU GLN ILE ALA ASP SER GLN
SEQRES 35 C 456 HIS ARG SER HIS ARG GLN LEU GLU HIS HIS HIS HIS HIS
SEQRES 36 C 456 HIS
HELIX 1 1 SER A 35 SER A 38 5 4
HELIX 2 2 TRP A 39 ALA A 49 1 11
HELIX 3 3 ASP A 72 ASP A 88 1 17
HELIX 4 4 MET A 99 GLY A 112 1 14
HELIX 5 5 PRO A 141 ASP A 155 1 15
HELIX 6 6 ASP A 155 ASN A 169 1 15
HELIX 7 7 ASN A 169 LEU A 174 1 6
HELIX 8 8 SER A 179 SER A 192 1 14
HELIX 9 9 GLY A 194 TRP A 205 1 12
HELIX 10 10 ASP A 212 ILE A 216 5 5
HELIX 11 11 PRO A 232 LEU A 244 1 13
HELIX 12 12 GLY A 258 HIS A 263 1 6
HELIX 13 13 HIS A 263 SER A 296 1 34
HELIX 14 14 GLY A 301 ALA A 316 1 16
HELIX 15 15 ASP A 321 THR A 331 1 11
HELIX 16 16 SER A 336 VAL A 351 1 16
HELIX 17 17 ARG A 360 LEU A 367 1 8
HELIX 18 18 ASN A 368 GLY A 371 5 4
HELIX 19 19 ASP A 372 LYS A 387 1 16
HELIX 20 20 THR A 391 LEU A 400 1 10
HELIX 21 21 SER A 403 ASN A 416 1 14
HELIX 22 22 THR A 422 SER A 440 1 19
HELIX 23 23 SER B 35 SER B 38 5 4
HELIX 24 24 TRP B 39 GLY B 50 1 12
HELIX 25 25 ASP B 72 ASP B 88 1 17
HELIX 26 26 MET B 99 GLY B 112 1 14
HELIX 27 27 PRO B 141 ASP B 155 1 15
HELIX 28 28 ASP B 155 ASN B 169 1 15
HELIX 29 29 ASN B 169 LEU B 174 1 6
HELIX 30 30 SER B 179 SER B 192 1 14
HELIX 31 31 GLY B 194 TRP B 205 1 12
HELIX 32 32 ALA B 211 ILE B 216 1 6
HELIX 33 33 THR B 236 LEU B 244 1 9
HELIX 34 34 GLY B 258 SER B 296 1 39
HELIX 35 35 GLY B 301 ALA B 316 1 16
HELIX 36 36 ASP B 321 THR B 331 1 11
HELIX 37 37 SER B 336 VAL B 351 1 16
HELIX 38 38 ARG B 360 LEU B 367 1 8
HELIX 39 39 ASN B 368 GLY B 371 5 4
HELIX 40 40 ASP B 372 LYS B 387 1 16
HELIX 41 41 THR B 391 LEU B 400 1 10
HELIX 42 42 SER B 403 ASN B 416 1 14
HELIX 43 43 THR B 422 SER B 440 1 19
HELIX 44 44 SER C 35 SER C 38 5 4
HELIX 45 45 TRP C 39 GLY C 50 1 12
HELIX 46 46 ASP C 72 ASP C 88 1 17
HELIX 47 47 MET C 99 GLY C 112 1 14
HELIX 48 48 PRO C 141 ASP C 155 1 15
HELIX 49 49 ASP C 155 ASN C 169 1 15
HELIX 50 50 ASN C 169 LEU C 174 1 6
HELIX 51 51 SER C 179 SER C 192 1 14
HELIX 52 52 GLY C 194 TRP C 205 1 12
HELIX 53 53 ASP C 212 ILE C 216 5 5
HELIX 54 54 PRO C 232 LEU C 244 1 13
HELIX 55 55 GLY C 258 HIS C 263 1 6
HELIX 56 56 HIS C 263 SER C 296 1 34
HELIX 57 57 GLY C 301 ALA C 316 1 16
HELIX 58 58 ASP C 321 THR C 331 1 11
HELIX 59 59 SER C 336 VAL C 351 1 16
HELIX 60 60 ARG C 360 LEU C 367 1 8
HELIX 61 61 ASN C 368 GLY C 371 5 4
HELIX 62 62 ASP C 372 LYS C 387 1 16
HELIX 63 63 THR C 391 LEU C 400 1 10
HELIX 64 64 SER C 403 ASN C 416 1 14
HELIX 65 65 THR C 422 SER C 440 1 19
SHEET 1 A 8 PHE A 2 GLU A 8 0
SHEET 2 A 8 THR A 11 HIS A 20 -1 O LEU A 15 N ILE A 3
SHEET 3 A 8 ARG A 52 TYR A 56 -1 O VAL A 53 N HIS A 20
SHEET 4 A 8 PRO A 25 ILE A 29 1 N VAL A 26 O ILE A 54
SHEET 5 A 8 ALA A 92 PHE A 97 1 O VAL A 93 N VAL A 27
SHEET 6 A 8 ILE A 116 LEU A 122 1 O ALA A 117 N ALA A 92
SHEET 7 A 8 ALA A 220 GLY A 225 1 O LEU A 223 N PHE A 121
SHEET 8 A 8 GLU A 248 VAL A 252 1 O VAL A 252 N HIS A 224
SHEET 1 B 8 PHE B 2 GLU B 8 0
SHEET 2 B 8 THR B 11 HIS B 20 -1 O LEU B 15 N ILE B 3
SHEET 3 B 8 TYR B 51 TYR B 56 -1 O VAL B 53 N HIS B 20
SHEET 4 B 8 THR B 24 ILE B 29 1 N VAL B 26 O ILE B 54
SHEET 5 B 8 ALA B 92 PHE B 97 1 O VAL B 93 N VAL B 27
SHEET 6 B 8 ILE B 116 LEU B 122 1 O ALA B 120 N LEU B 94
SHEET 7 B 8 ALA B 220 GLY B 225 1 O LEU B 221 N PHE B 121
SHEET 8 B 8 GLU B 248 VAL B 252 1 O VAL B 252 N HIS B 224
SHEET 1 C 8 PHE C 2 GLU C 8 0
SHEET 2 C 8 THR C 11 HIS C 20 -1 O LEU C 15 N ILE C 3
SHEET 3 C 8 ARG C 52 TYR C 56 -1 O VAL C 53 N HIS C 20
SHEET 4 C 8 PRO C 25 ILE C 29 1 N VAL C 26 O ILE C 54
SHEET 5 C 8 ALA C 92 PHE C 97 1 O VAL C 93 N VAL C 27
SHEET 6 C 8 ILE C 116 LEU C 122 1 O ALA C 117 N ALA C 92
SHEET 7 C 8 ALA C 220 GLY C 225 1 O LEU C 223 N PHE C 121
SHEET 8 C 8 GLU C 248 VAL C 252 1 O VAL C 252 N HIS C 224
CISPEP 1 PHE A 32 PRO A 33 0 -3.90
CISPEP 2 GLU A 126 PRO A 127 0 -12.19
CISPEP 3 PHE B 32 PRO B 33 0 -3.65
CISPEP 4 GLU B 126 PRO B 127 0 -2.94
CISPEP 5 PHE C 32 PRO C 33 0 -3.53
CISPEP 6 GLU C 126 PRO C 127 0 -11.00
CRYST1 129.670 160.980 167.630 90.00 90.00 90.00 I 2 2 2 24
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 0.007712 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006212 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005966 0.00000
TER 3399 SER A 440
TER 6798 SER B 440
TER 10197 SER C 440
MASTER 408 0 0 65 24 0 0 610194 3 0 108
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