HEADER IMMUNE SYSTEM 23-JUN-14 3J7E
TITLE ELECTRON CRYO-MICROSCOPY OF HUMAN PAPILLOMAVIRUS 16 AND H16.V5 FAB
TITLE 2 FRAGMENTS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: H16.V5 FAB LIGHT CHAIN;
COMPND 3 CHAIN: L, A, C, E;
COMPND 4 FRAGMENT: VARIABLE DOMAIN;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: H16.V5 FAB HEAVY CHAIN;
COMPND 7 CHAIN: H, B, D, F;
COMPND 8 FRAGMENT: VARIABLE DOMAIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 CELL: HYBRIDOMA;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 8 ORGANISM_COMMON: MOUSE;
SOURCE 9 ORGANISM_TAXID: 10090;
SOURCE 10 CELL: HYBRIDOMA
KEYWDS HPV16.V5 FAB VARIABLE DOMAIN, HI AND FG LOOPS, HPV16 CAPSID, VIRUS-
KEYWDS 2 FAB COMPLEX, NEUTRALIZATION ANTIBODY, MATURATION, IMMUNE SYSTEM
EXPDTA ELECTRON MICROSCOPY
AUTHOR H.LEE,S.A.BRENDLE,S.M.BYWATERS,N.D.CHRISTENSEN,S.HAFENSTEIN
REVDAT 4 18-JUL-18 3J7E 1 REMARK
REVDAT 3 18-MAR-15 3J7E 1 JRNL
REVDAT 2 03-DEC-14 3J7E 1 JRNL
REVDAT 1 26-NOV-14 3J7E 0
JRNL AUTH H.LEE,S.A.BRENDLE,S.M.BYWATERS,J.GUAN,R.E.ASHLEY,J.D.YODER,
JRNL AUTH 2 A.M.MAKHOV,J.F.CONWAY,N.D.CHRISTENSEN,S.HAFENSTEIN
JRNL TITL A CRYO-ELECTRON MICROSCOPY STUDY IDENTIFIES THE COMPLETE
JRNL TITL 2 H16.V5 EPITOPE AND REVEALS GLOBAL CONFORMATIONAL CHANGES
JRNL TITL 3 INITIATED BY BINDING OF THE NEUTRALIZING ANTIBODY FRAGMENT.
JRNL REF J.VIROL. V. 89 1428 2015
JRNL REFN ISSN 0022-538X
JRNL PMID 25392224
JRNL DOI 10.1128/JVI.02898-14
REMARK 2
REMARK 2 RESOLUTION. 13.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : SITUS, UCSF CHIMERA, AUTO3DEM, EMAN
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : NULL
REMARK 3 REFINEMENT SPACE : REAL
REMARK 3 REFINEMENT PROTOCOL : FLEXIBLE FIT
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : REFINEMENT PROTOCOL--FLEXIBLE
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : 1.480
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 13.60
REMARK 3 NUMBER OF PARTICLES : 2075
REMARK 3 CTF CORRECTION METHOD : NULL
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: SEMI-AUTOMATIC PARTICLE SELECTION WAS PERFORMED
REMARK 3 USING E2BOXER.PY TO OBTAIN THE PARTICLE COORDINATES, FOLLOWED BY
REMARK 3 PARTICLE BOXING, LINEARIZATION, NORMALIZATION, AND APODIZATION
REMARK 3 OF THE IMAGES USING ROBEM. DEFOCUS AND ASTIGMATISM VALUES TO
REMARK 3 PERFORM CONTRAST TRANSFER FUNCTION (CTF) CORRECTION WERE
REMARK 3 ASSESSED USING ROBEM FOR THE EXTRACTED PARTICLES. THE
REMARK 3 ICOSAHEDRALLY AVERAGED RECONSTRUCTIONS WERE INITIATED USING A
REMARK 3 RANDOM MODEL GENERATED WITH SETUP_RMC AND REACHED 14 A
REMARK 3 RESOLUTION ESTIMATED AT A FOURIER SHELL CORRELATION (FSC) OF
REMARK 3 0.5. FOR THE LAST STEP OF REFINEMENT, THE FINAL MAPS WERE CTF-
REMARK 3 CORRECTED USING A B FACTOR OF 200 A2. (SINGLE PARTICLE--APPLIED
REMARK 3 SYMMETRY: I)
REMARK 4
REMARK 4 3J7E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUL-14.
REMARK 100 THE DEPOSITION ID IS D_1000160344.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE
REMARK 245 SPECIMEN TYPE : VITREOUS ICE (CRYO EM)
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : PARTICLE
REMARK 245 PARTICLE TYPE : POINT
REMARK 245 NAME OF SAMPLE : MATURE HPV16 QUASIVIRUS CAPSID
REMARK 245 COMPLEXED WITH H16.V5 FABS;
REMARK 245 HUMAN PAPILLOMAVIRUS 16; H16.V5
REMARK 245 FAB
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 1.00
REMARK 245 SAMPLE SUPPORT DETAILS : GLOW-DISCHARGED HOLEY CARBON
REMARK 245 QUANTIFOIL GRIDS
REMARK 245 SAMPLE VITRIFICATION DETAILS : BLOT FOR 0.7 SECONDS BEFORE
REMARK 245 PLUNGING INTO LIQUID ETHANE
REMARK 245 (GATAN CRYOPLUNGE 3).
REMARK 245 SAMPLE BUFFER : 137 MM NACL, 2.7 MM KCL, 10 MM
REMARK 245 NA2HPO4, 1.8 MM KH2PO4
REMARK 245 PH : 7.40
REMARK 245 SAMPLE DETAILS : THREE HUNDRED H16.V5 FABS BIND
REMARK 245 TO ONE HPV16 CAPSID
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : 30-OCT-13
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : 95.00
REMARK 245 MICROSCOPE MODEL : JEOL 2100
REMARK 245 DETECTOR TYPE : GATAN ULTRASCAN 4000 (4K X
REMARK 245 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 690.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 3990.00
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : 0.00
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : 0.00
REMARK 245 NOMINAL CS : 2.00
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 15.00
REMARK 245 ILLUMINATION MODE : SPOT SCAN
REMARK 245 NOMINAL MAGNIFICATION : 80000
REMARK 245 CALIBRATED MAGNIFICATION : NULL
REMARK 245 SOURCE : LAB6
REMARK 245 ACCELERATION VOLTAGE (KV) : 200
REMARK 245 IMAGING DETAILS : NULL
REMARK 247
REMARK 247 ELECTRON MICROSCOPY
REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON
REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE
REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES
REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION
REMARK 247 OF THE STRUCTURE FACTORS.
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 300 THE ASSEMBLY REPRESENTED IN THIS ENTRY HAS REGULAR
REMARK 300 ICOSAHEDRAL POINT SYMMETRY (SCHOENFLIES SYMBOL = I).
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 APPLY THE FOLLOWING TO CHAINS: L, H, A, B, C, D, E, F
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 0.309017 0.500000 -0.809017 0.00000
REMARK 350 BIOMT2 2 -0.500000 0.809017 0.309017 0.00000
REMARK 350 BIOMT3 2 0.809017 0.309017 0.500000 0.00000
REMARK 350 BIOMT1 3 -0.809017 0.309017 -0.500000 0.00000
REMARK 350 BIOMT2 3 -0.309017 0.500000 0.809017 0.00000
REMARK 350 BIOMT3 3 0.500000 0.809017 -0.309017 0.00000
REMARK 350 BIOMT1 4 -0.809017 -0.309017 0.500000 0.00000
REMARK 350 BIOMT2 4 0.309017 0.500000 0.809017 0.00000
REMARK 350 BIOMT3 4 -0.500000 0.809017 -0.309017 0.00000
REMARK 350 BIOMT1 5 0.309017 -0.500000 0.809017 0.00000
REMARK 350 BIOMT2 5 0.500000 0.809017 0.309017 0.00000
REMARK 350 BIOMT3 5 -0.809017 0.309017 0.500000 0.00000
REMARK 350 BIOMT1 6 -0.500000 0.809017 0.309017 0.00000
REMARK 350 BIOMT2 6 0.809017 0.309017 0.500000 0.00000
REMARK 350 BIOMT3 6 0.309017 0.500000 -0.809017 0.00000
REMARK 350 BIOMT1 7 -0.309017 0.500000 0.809017 0.00000
REMARK 350 BIOMT2 7 0.500000 0.809017 -0.309017 0.00000
REMARK 350 BIOMT3 7 -0.809017 0.309017 -0.500000 0.00000
REMARK 350 BIOMT1 8 0.309017 0.500000 0.809017 0.00000
REMARK 350 BIOMT2 8 -0.500000 0.809017 -0.309017 0.00000
REMARK 350 BIOMT3 8 -0.809017 -0.309017 0.500000 0.00000
REMARK 350 BIOMT1 9 0.500000 0.809017 0.309017 0.00000
REMARK 350 BIOMT2 9 -0.809017 0.309017 0.500000 0.00000
REMARK 350 BIOMT3 9 0.309017 -0.500000 0.809017 0.00000
REMARK 350 BIOMT1 10 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 10 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT3 10 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT1 11 0.309017 -0.500000 -0.809017 0.00000
REMARK 350 BIOMT2 11 -0.500000 -0.809017 0.309017 0.00000
REMARK 350 BIOMT3 11 -0.809017 0.309017 -0.500000 0.00000
REMARK 350 BIOMT1 12 -0.309017 -0.500000 -0.809017 0.00000
REMARK 350 BIOMT2 12 0.500000 -0.809017 0.309017 0.00000
REMARK 350 BIOMT3 12 -0.809017 -0.309017 0.500000 0.00000
REMARK 350 BIOMT1 13 -0.500000 -0.809017 -0.309017 0.00000
REMARK 350 BIOMT2 13 0.809017 -0.309017 -0.500000 0.00000
REMARK 350 BIOMT3 13 0.309017 -0.500000 0.809017 0.00000
REMARK 350 BIOMT1 14 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 14 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT3 14 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT1 15 0.500000 -0.809017 -0.309017 0.00000
REMARK 350 BIOMT2 15 -0.809017 -0.309017 -0.500000 0.00000
REMARK 350 BIOMT3 15 0.309017 0.500000 -0.809017 0.00000
REMARK 350 BIOMT1 16 -0.809017 -0.309017 0.500000 0.00000
REMARK 350 BIOMT2 16 -0.309017 -0.500000 -0.809017 0.00000
REMARK 350 BIOMT3 16 0.500000 -0.809017 0.309017 0.00000
REMARK 350 BIOMT1 17 0.309017 -0.500000 0.809017 0.00000
REMARK 350 BIOMT2 17 -0.500000 -0.809017 -0.309017 0.00000
REMARK 350 BIOMT3 17 0.809017 -0.309017 -0.500000 0.00000
REMARK 350 BIOMT1 18 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 18 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 18 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 19 0.309017 0.500000 -0.809017 0.00000
REMARK 350 BIOMT2 19 0.500000 -0.809017 -0.309017 0.00000
REMARK 350 BIOMT3 19 -0.809017 -0.309017 -0.500000 0.00000
REMARK 350 BIOMT1 20 -0.809017 0.309017 -0.500000 0.00000
REMARK 350 BIOMT2 20 0.309017 -0.500000 -0.809017 0.00000
REMARK 350 BIOMT3 20 -0.500000 -0.809017 0.309017 0.00000
REMARK 350 BIOMT1 21 -0.500000 0.809017 -0.309017 0.00000
REMARK 350 BIOMT2 21 -0.809017 -0.309017 0.500000 0.00000
REMARK 350 BIOMT3 21 0.309017 0.500000 0.809017 0.00000
REMARK 350 BIOMT1 22 -0.809017 0.309017 0.500000 0.00000
REMARK 350 BIOMT2 22 0.309017 -0.500000 0.809017 0.00000
REMARK 350 BIOMT3 22 0.500000 0.809017 0.309017 0.00000
REMARK 350 BIOMT1 23 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT2 23 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 23 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT1 24 0.809017 0.309017 0.500000 0.00000
REMARK 350 BIOMT2 24 0.309017 0.500000 -0.809017 0.00000
REMARK 350 BIOMT3 24 -0.500000 0.809017 0.309017 0.00000
REMARK 350 BIOMT1 25 0.500000 0.809017 -0.309017 0.00000
REMARK 350 BIOMT2 25 -0.809017 0.309017 -0.500000 0.00000
REMARK 350 BIOMT3 25 -0.309017 0.500000 0.809017 0.00000
REMARK 350 BIOMT1 26 0.809017 -0.309017 0.500000 0.00000
REMARK 350 BIOMT2 26 0.309017 -0.500000 -0.809017 0.00000
REMARK 350 BIOMT3 26 0.500000 0.809017 -0.309017 0.00000
REMARK 350 BIOMT1 27 0.809017 0.309017 -0.500000 0.00000
REMARK 350 BIOMT2 27 -0.309017 -0.500000 -0.809017 0.00000
REMARK 350 BIOMT3 27 -0.500000 0.809017 -0.309017 0.00000
REMARK 350 BIOMT1 28 -0.309017 0.500000 -0.809017 0.00000
REMARK 350 BIOMT2 28 -0.500000 -0.809017 -0.309017 0.00000
REMARK 350 BIOMT3 28 -0.809017 0.309017 0.500000 0.00000
REMARK 350 BIOMT1 29 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 29 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 29 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 30 -0.309017 -0.500000 0.809017 0.00000
REMARK 350 BIOMT2 30 0.500000 -0.809017 -0.309017 0.00000
REMARK 350 BIOMT3 30 0.809017 0.309017 0.500000 0.00000
REMARK 350 BIOMT1 31 -0.309017 -0.500000 0.809017 0.00000
REMARK 350 BIOMT2 31 -0.500000 0.809017 0.309017 0.00000
REMARK 350 BIOMT3 31 -0.809017 -0.309017 -0.500000 0.00000
REMARK 350 BIOMT1 32 0.809017 -0.309017 0.500000 0.00000
REMARK 350 BIOMT2 32 -0.309017 0.500000 0.809017 0.00000
REMARK 350 BIOMT3 32 -0.500000 -0.809017 0.309017 0.00000
REMARK 350 BIOMT1 33 0.809017 0.309017 -0.500000 0.00000
REMARK 350 BIOMT2 33 0.309017 0.500000 0.809017 0.00000
REMARK 350 BIOMT3 33 0.500000 -0.809017 0.309017 0.00000
REMARK 350 BIOMT1 34 -0.309017 0.500000 -0.809017 0.00000
REMARK 350 BIOMT2 34 0.500000 0.809017 0.309017 0.00000
REMARK 350 BIOMT3 34 0.809017 -0.309017 -0.500000 0.00000
REMARK 350 BIOMT1 35 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 35 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 35 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 36 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT2 36 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 36 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT1 37 -0.809017 -0.309017 -0.500000 0.00000
REMARK 350 BIOMT2 37 0.309017 0.500000 -0.809017 0.00000
REMARK 350 BIOMT3 37 0.500000 -0.809017 -0.309017 0.00000
REMARK 350 BIOMT1 38 -0.500000 -0.809017 0.309017 0.00000
REMARK 350 BIOMT2 38 -0.809017 0.309017 -0.500000 0.00000
REMARK 350 BIOMT3 38 0.309017 -0.500000 -0.809017 0.00000
REMARK 350 BIOMT1 39 0.500000 -0.809017 0.309017 0.00000
REMARK 350 BIOMT2 39 -0.809017 -0.309017 0.500000 0.00000
REMARK 350 BIOMT3 39 -0.309017 -0.500000 -0.809017 0.00000
REMARK 350 BIOMT1 40 0.809017 -0.309017 -0.500000 0.00000
REMARK 350 BIOMT2 40 0.309017 -0.500000 0.809017 0.00000
REMARK 350 BIOMT3 40 -0.500000 -0.809017 -0.309017 0.00000
REMARK 350 BIOMT1 41 -0.500000 -0.809017 0.309017 0.00000
REMARK 350 BIOMT2 41 0.809017 -0.309017 0.500000 0.00000
REMARK 350 BIOMT3 41 -0.309017 0.500000 0.809017 0.00000
REMARK 350 BIOMT1 42 0.500000 -0.809017 0.309017 0.00000
REMARK 350 BIOMT2 42 0.809017 0.309017 -0.500000 0.00000
REMARK 350 BIOMT3 42 0.309017 0.500000 0.809017 0.00000
REMARK 350 BIOMT1 43 0.809017 -0.309017 -0.500000 0.00000
REMARK 350 BIOMT2 43 -0.309017 0.500000 -0.809017 0.00000
REMARK 350 BIOMT3 43 0.500000 0.809017 0.309017 0.00000
REMARK 350 BIOMT1 44 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT2 44 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 44 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT1 45 -0.809017 -0.309017 -0.500000 0.00000
REMARK 350 BIOMT2 45 -0.309017 -0.500000 0.809017 0.00000
REMARK 350 BIOMT3 45 -0.500000 0.809017 0.309017 0.00000
REMARK 350 BIOMT1 46 -0.309017 -0.500000 -0.809017 0.00000
REMARK 350 BIOMT2 46 -0.500000 0.809017 -0.309017 0.00000
REMARK 350 BIOMT3 46 0.809017 0.309017 -0.500000 0.00000
REMARK 350 BIOMT1 47 -0.500000 -0.809017 -0.309017 0.00000
REMARK 350 BIOMT2 47 -0.809017 0.309017 0.500000 0.00000
REMARK 350 BIOMT3 47 -0.309017 0.500000 -0.809017 0.00000
REMARK 350 BIOMT1 48 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 48 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT3 48 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT1 49 0.500000 -0.809017 -0.309017 0.00000
REMARK 350 BIOMT2 49 0.809017 0.309017 0.500000 0.00000
REMARK 350 BIOMT3 49 -0.309017 -0.500000 0.809017 0.00000
REMARK 350 BIOMT1 50 0.309017 -0.500000 -0.809017 0.00000
REMARK 350 BIOMT2 50 0.500000 0.809017 -0.309017 0.00000
REMARK 350 BIOMT3 50 0.809017 -0.309017 0.500000 0.00000
REMARK 350 BIOMT1 51 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 51 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT3 51 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT1 52 -0.500000 0.809017 0.309017 0.00000
REMARK 350 BIOMT2 52 -0.809017 -0.309017 -0.500000 0.00000
REMARK 350 BIOMT3 52 -0.309017 -0.500000 0.809017 0.00000
REMARK 350 BIOMT1 53 -0.309017 0.500000 0.809017 0.00000
REMARK 350 BIOMT2 53 -0.500000 -0.809017 0.309017 0.00000
REMARK 350 BIOMT3 53 0.809017 -0.309017 0.500000 0.00000
REMARK 350 BIOMT1 54 0.309017 0.500000 0.809017 0.00000
REMARK 350 BIOMT2 54 0.500000 -0.809017 0.309017 0.00000
REMARK 350 BIOMT3 54 0.809017 0.309017 -0.500000 0.00000
REMARK 350 BIOMT1 55 0.500000 0.809017 0.309017 0.00000
REMARK 350 BIOMT2 55 0.809017 -0.309017 -0.500000 0.00000
REMARK 350 BIOMT3 55 -0.309017 0.500000 -0.809017 0.00000
REMARK 350 BIOMT1 56 0.809017 0.309017 0.500000 0.00000
REMARK 350 BIOMT2 56 -0.309017 -0.500000 0.809017 0.00000
REMARK 350 BIOMT3 56 0.500000 -0.809017 -0.309017 0.00000
REMARK 350 BIOMT1 57 0.500000 0.809017 -0.309017 0.00000
REMARK 350 BIOMT2 57 0.809017 -0.309017 0.500000 0.00000
REMARK 350 BIOMT3 57 0.309017 -0.500000 -0.809017 0.00000
REMARK 350 BIOMT1 58 -0.500000 0.809017 -0.309017 0.00000
REMARK 350 BIOMT2 58 0.809017 0.309017 -0.500000 0.00000
REMARK 350 BIOMT3 58 -0.309017 -0.500000 -0.809017 0.00000
REMARK 350 BIOMT1 59 -0.809017 0.309017 0.500000 0.00000
REMARK 350 BIOMT2 59 -0.309017 0.500000 -0.809017 0.00000
REMARK 350 BIOMT3 59 -0.500000 -0.809017 -0.309017 0.00000
REMARK 350 BIOMT1 60 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT2 60 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 60 0.000000 -1.000000 0.000000 0.00000
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 SER H 122 C SER H 122 O -0.125
REMARK 500 GLN H 229 CD GLN H 229 OE1 0.170
REMARK 500 SER B 122 C SER B 122 O -0.125
REMARK 500 GLN B 229 CD GLN B 229 OE1 0.171
REMARK 500 SER D 122 C SER D 122 O -0.123
REMARK 500 GLN D 229 CD GLN D 229 OE1 0.170
REMARK 500 SER F 122 C SER F 122 O -0.125
REMARK 500 GLN F 229 CD GLN F 229 OE1 0.170
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 MET L 13 CG - SD - CE ANGL. DEV. = -39.6 DEGREES
REMARK 500 PHE L 56 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 VAL L 84 CG1 - CB - CG2 ANGL. DEV. = 22.4 DEGREES
REMARK 500 VAL L 84 CA - CB - CG1 ANGL. DEV. = -12.3 DEGREES
REMARK 500 VAL L 84 CA - CB - CG2 ANGL. DEV. = -15.0 DEGREES
REMARK 500 HIS L 97 CG - ND1 - CE1 ANGL. DEV. = -8.0 DEGREES
REMARK 500 HIS L 97 ND1 - CE1 - NE2 ANGL. DEV. = 10.4 DEGREES
REMARK 500 THR L 103 CA - CB - CG2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 LEU L 112 N - CA - CB ANGL. DEV. = -14.0 DEGREES
REMARK 500 LEU L 112 CA - CB - CG ANGL. DEV. = -15.7 DEGREES
REMARK 500 GLN H 121 CA - C - N ANGL. DEV. = 14.1 DEGREES
REMARK 500 GLN H 121 O - C - N ANGL. DEV. = -21.0 DEGREES
REMARK 500 THR H 221 CA - CB - CG2 ANGL. DEV. = 10.5 DEGREES
REMARK 500 GLN H 229 OE1 - CD - NE2 ANGL. DEV. = -14.6 DEGREES
REMARK 500 GLN H 229 CG - CD - NE2 ANGL. DEV. = 15.1 DEGREES
REMARK 500 MET A 13 CG - SD - CE ANGL. DEV. = -39.6 DEGREES
REMARK 500 PHE A 56 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 VAL A 84 CG1 - CB - CG2 ANGL. DEV. = 22.4 DEGREES
REMARK 500 VAL A 84 CA - CB - CG1 ANGL. DEV. = -12.2 DEGREES
REMARK 500 VAL A 84 CA - CB - CG2 ANGL. DEV. = -14.9 DEGREES
REMARK 500 HIS A 97 CG - ND1 - CE1 ANGL. DEV. = -8.0 DEGREES
REMARK 500 HIS A 97 ND1 - CE1 - NE2 ANGL. DEV. = 10.5 DEGREES
REMARK 500 THR A 103 CA - CB - CG2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 LEU A 112 N - CA - CB ANGL. DEV. = -14.1 DEGREES
REMARK 500 LEU A 112 CA - CB - CG ANGL. DEV. = -15.8 DEGREES
REMARK 500 GLN B 121 CA - C - N ANGL. DEV. = 14.1 DEGREES
REMARK 500 GLN B 121 O - C - N ANGL. DEV. = -20.9 DEGREES
REMARK 500 THR B 221 CA - CB - CG2 ANGL. DEV. = 10.5 DEGREES
REMARK 500 GLN B 229 OE1 - CD - NE2 ANGL. DEV. = -14.6 DEGREES
REMARK 500 GLN B 229 CG - CD - NE2 ANGL. DEV. = 15.1 DEGREES
REMARK 500 MET C 13 CG - SD - CE ANGL. DEV. = -39.6 DEGREES
REMARK 500 PHE C 56 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 VAL C 84 CG1 - CB - CG2 ANGL. DEV. = 22.5 DEGREES
REMARK 500 VAL C 84 CA - CB - CG1 ANGL. DEV. = -12.2 DEGREES
REMARK 500 VAL C 84 CA - CB - CG2 ANGL. DEV. = -15.0 DEGREES
REMARK 500 HIS C 97 CG - ND1 - CE1 ANGL. DEV. = -7.9 DEGREES
REMARK 500 HIS C 97 ND1 - CE1 - NE2 ANGL. DEV. = 10.3 DEGREES
REMARK 500 THR C 103 CA - CB - CG2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 LEU C 112 N - CA - CB ANGL. DEV. = -14.0 DEGREES
REMARK 500 LEU C 112 CA - CB - CG ANGL. DEV. = -15.6 DEGREES
REMARK 500 GLN D 121 CA - C - N ANGL. DEV. = 14.1 DEGREES
REMARK 500 GLN D 121 O - C - N ANGL. DEV. = -21.0 DEGREES
REMARK 500 THR D 221 CA - CB - CG2 ANGL. DEV. = 10.5 DEGREES
REMARK 500 GLN D 229 OE1 - CD - NE2 ANGL. DEV. = -14.5 DEGREES
REMARK 500 GLN D 229 CG - CD - NE2 ANGL. DEV. = 15.0 DEGREES
REMARK 500 MET E 13 CG - SD - CE ANGL. DEV. = -39.5 DEGREES
REMARK 500 PHE E 56 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 VAL E 84 CG1 - CB - CG2 ANGL. DEV. = 22.4 DEGREES
REMARK 500 VAL E 84 CA - CB - CG1 ANGL. DEV. = -12.2 DEGREES
REMARK 500 VAL E 84 CA - CB - CG2 ANGL. DEV. = -15.0 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 60 ANGLE DEVIATIONS.
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 ARG L 33 -39.66 -141.31
REMARK 500 GLN L 35 71.00 68.71
REMARK 500 TYR L 38 77.07 -101.26
REMARK 500 PHE L 56 -145.90 63.96
REMARK 500 ALA L 90 168.07 178.73
REMARK 500 ALA H 131 -160.48 -100.70
REMARK 500 ALA H 207 -174.73 177.72
REMARK 500 TYR H 216 4.32 -159.36
REMARK 500 TYR H 217 -179.26 -67.11
REMARK 500 TYR H 218 -35.69 93.51
REMARK 500 THR H 220 -151.69 -133.51
REMARK 500 TYR H 222 71.39 -67.62
REMARK 500 ARG A 33 -39.74 -141.25
REMARK 500 GLN A 35 71.00 68.75
REMARK 500 TYR A 38 77.27 -101.35
REMARK 500 PHE A 56 -145.91 64.07
REMARK 500 ALA A 90 168.06 178.76
REMARK 500 ALA B 131 -160.53 -100.73
REMARK 500 ALA B 207 -174.67 177.79
REMARK 500 TYR B 216 4.27 -159.32
REMARK 500 TYR B 217 -179.18 -67.11
REMARK 500 TYR B 218 -35.92 93.60
REMARK 500 THR B 220 -151.65 -133.51
REMARK 500 TYR B 222 71.36 -67.49
REMARK 500 ARG C 33 -39.74 -141.30
REMARK 500 GLN C 35 71.00 68.71
REMARK 500 TYR C 38 77.02 -101.27
REMARK 500 PHE C 56 -146.04 63.96
REMARK 500 ALA C 90 168.07 178.78
REMARK 500 ALA D 131 -160.50 -100.62
REMARK 500 ALA D 207 -174.70 177.72
REMARK 500 TYR D 216 4.30 -159.32
REMARK 500 TYR D 217 -179.23 -67.06
REMARK 500 TYR D 218 -35.86 93.63
REMARK 500 THR D 220 -151.74 -133.48
REMARK 500 TYR D 222 71.46 -67.65
REMARK 500 ARG E 33 -39.66 -141.28
REMARK 500 GLN E 35 70.99 68.76
REMARK 500 TYR E 38 77.05 -101.33
REMARK 500 PHE E 56 -145.89 64.06
REMARK 500 ALA E 90 168.15 178.76
REMARK 500 ALA F 131 -160.50 -100.61
REMARK 500 ALA F 207 -174.74 177.75
REMARK 500 TYR F 216 4.18 -159.32
REMARK 500 TYR F 217 -179.28 -66.99
REMARK 500 TYR F 218 -35.81 93.58
REMARK 500 THR F 220 -151.68 -133.56
REMARK 500 TYR F 222 71.36 -67.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 HIS L 97 0.15 SIDE CHAIN
REMARK 500 HIS A 97 0.15 SIDE CHAIN
REMARK 500 HIS C 97 0.15 SIDE CHAIN
REMARK 500 HIS E 97 0.15 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 GLN H 121 -27.27
REMARK 500 SER H 122 17.40
REMARK 500 GLN B 121 -27.35
REMARK 500 SER B 122 17.41
REMARK 500 GLN D 121 -27.38
REMARK 500 SER D 122 17.45
REMARK 500 GLN F 121 -27.41
REMARK 500 SER F 122 17.42
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-5991 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-5992 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-5993 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-5994 RELATED DB: EMDB
REMARK 900 RELATED ID: 3J7G RELATED DB: PDB
DBREF 3J7E L 1 115 PDB 3J7E 3J7E 1 115
DBREF 3J7E A 1 115 PDB 3J7E 3J7E 1 115
DBREF 3J7E C 1 115 PDB 3J7E 3J7E 1 115
DBREF 3J7E E 1 115 PDB 3J7E 3J7E 1 115
DBREF 3J7E H 116 236 PDB 3J7E 3J7E 116 236
DBREF 3J7E B 116 236 PDB 3J7E 3J7E 116 236
DBREF 3J7E D 116 236 PDB 3J7E 3J7E 116 236
DBREF 3J7E F 116 236 PDB 3J7E 3J7E 116 236
SEQRES 1 L 115 ASP ILE VAL MET THR GLN SER PRO SER SER LEU ALA MET
SEQRES 2 L 115 SER VAL GLY GLN LYS VAL THR MET SER CYS LYS SER SER
SEQRES 3 L 115 GLN SER LEU LEU ASP SER ARG ASN GLN LYS ASN TYR LEU
SEQRES 4 L 115 ALA TRP TYR GLN GLN LYS PRO GLY GLN SER PRO LYS LEU
SEQRES 5 L 115 LEU VAL TYR PHE ALA SER THR ARG GLU SER GLY VAL PRO
SEQRES 6 L 115 ASP ARG PHE ILE GLY SER GLY SER GLY THR ASP PHE THR
SEQRES 7 L 115 LEU THR ILE SER SER VAL GLN ALA GLU ASP LEU ALA ASP
SEQRES 8 L 115 TYR PHE CYS GLN GLN HIS TYR SER THR PRO LEU THR PHE
SEQRES 9 L 115 GLY ALA GLY THR LYS LEU GLU LEU LYS ARG ALA
SEQRES 1 H 121 GLU VAL LYS LEU GLU GLN SER GLY ALA GLU LEU ALA ARG
SEQRES 2 H 121 PRO GLY ALA SER VAL LYS LEU SER CYS LYS ALA SER GLY
SEQRES 3 H 121 TYR THR PHE ALA SER TYR TRP MET GLN TRP VAL LYS GLN
SEQRES 4 H 121 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY ALA ILE TYR
SEQRES 5 H 121 PRO GLY ASP GLY ASP THR TRP TYR THR GLN LYS PHE LYS
SEQRES 6 H 121 GLY LYS ALA THR LEU THR ALA ASP LYS SER SER SER THR
SEQRES 7 H 121 ALA TYR MET GLN LEU SER SER LEU ALA SER GLU ASP SER
SEQRES 8 H 121 ALA VAL TYR TYR CYS ALA ARG PRO PRO TYR TYR TYR GLY
SEQRES 9 H 121 THR THR TYR TYR PHE ASP TYR TRP GLY GLN GLY THR THR
SEQRES 10 H 121 LEU THR VAL SER
SEQRES 1 A 115 ASP ILE VAL MET THR GLN SER PRO SER SER LEU ALA MET
SEQRES 2 A 115 SER VAL GLY GLN LYS VAL THR MET SER CYS LYS SER SER
SEQRES 3 A 115 GLN SER LEU LEU ASP SER ARG ASN GLN LYS ASN TYR LEU
SEQRES 4 A 115 ALA TRP TYR GLN GLN LYS PRO GLY GLN SER PRO LYS LEU
SEQRES 5 A 115 LEU VAL TYR PHE ALA SER THR ARG GLU SER GLY VAL PRO
SEQRES 6 A 115 ASP ARG PHE ILE GLY SER GLY SER GLY THR ASP PHE THR
SEQRES 7 A 115 LEU THR ILE SER SER VAL GLN ALA GLU ASP LEU ALA ASP
SEQRES 8 A 115 TYR PHE CYS GLN GLN HIS TYR SER THR PRO LEU THR PHE
SEQRES 9 A 115 GLY ALA GLY THR LYS LEU GLU LEU LYS ARG ALA
SEQRES 1 B 121 GLU VAL LYS LEU GLU GLN SER GLY ALA GLU LEU ALA ARG
SEQRES 2 B 121 PRO GLY ALA SER VAL LYS LEU SER CYS LYS ALA SER GLY
SEQRES 3 B 121 TYR THR PHE ALA SER TYR TRP MET GLN TRP VAL LYS GLN
SEQRES 4 B 121 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY ALA ILE TYR
SEQRES 5 B 121 PRO GLY ASP GLY ASP THR TRP TYR THR GLN LYS PHE LYS
SEQRES 6 B 121 GLY LYS ALA THR LEU THR ALA ASP LYS SER SER SER THR
SEQRES 7 B 121 ALA TYR MET GLN LEU SER SER LEU ALA SER GLU ASP SER
SEQRES 8 B 121 ALA VAL TYR TYR CYS ALA ARG PRO PRO TYR TYR TYR GLY
SEQRES 9 B 121 THR THR TYR TYR PHE ASP TYR TRP GLY GLN GLY THR THR
SEQRES 10 B 121 LEU THR VAL SER
SEQRES 1 C 115 ASP ILE VAL MET THR GLN SER PRO SER SER LEU ALA MET
SEQRES 2 C 115 SER VAL GLY GLN LYS VAL THR MET SER CYS LYS SER SER
SEQRES 3 C 115 GLN SER LEU LEU ASP SER ARG ASN GLN LYS ASN TYR LEU
SEQRES 4 C 115 ALA TRP TYR GLN GLN LYS PRO GLY GLN SER PRO LYS LEU
SEQRES 5 C 115 LEU VAL TYR PHE ALA SER THR ARG GLU SER GLY VAL PRO
SEQRES 6 C 115 ASP ARG PHE ILE GLY SER GLY SER GLY THR ASP PHE THR
SEQRES 7 C 115 LEU THR ILE SER SER VAL GLN ALA GLU ASP LEU ALA ASP
SEQRES 8 C 115 TYR PHE CYS GLN GLN HIS TYR SER THR PRO LEU THR PHE
SEQRES 9 C 115 GLY ALA GLY THR LYS LEU GLU LEU LYS ARG ALA
SEQRES 1 D 121 GLU VAL LYS LEU GLU GLN SER GLY ALA GLU LEU ALA ARG
SEQRES 2 D 121 PRO GLY ALA SER VAL LYS LEU SER CYS LYS ALA SER GLY
SEQRES 3 D 121 TYR THR PHE ALA SER TYR TRP MET GLN TRP VAL LYS GLN
SEQRES 4 D 121 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY ALA ILE TYR
SEQRES 5 D 121 PRO GLY ASP GLY ASP THR TRP TYR THR GLN LYS PHE LYS
SEQRES 6 D 121 GLY LYS ALA THR LEU THR ALA ASP LYS SER SER SER THR
SEQRES 7 D 121 ALA TYR MET GLN LEU SER SER LEU ALA SER GLU ASP SER
SEQRES 8 D 121 ALA VAL TYR TYR CYS ALA ARG PRO PRO TYR TYR TYR GLY
SEQRES 9 D 121 THR THR TYR TYR PHE ASP TYR TRP GLY GLN GLY THR THR
SEQRES 10 D 121 LEU THR VAL SER
SEQRES 1 E 115 ASP ILE VAL MET THR GLN SER PRO SER SER LEU ALA MET
SEQRES 2 E 115 SER VAL GLY GLN LYS VAL THR MET SER CYS LYS SER SER
SEQRES 3 E 115 GLN SER LEU LEU ASP SER ARG ASN GLN LYS ASN TYR LEU
SEQRES 4 E 115 ALA TRP TYR GLN GLN LYS PRO GLY GLN SER PRO LYS LEU
SEQRES 5 E 115 LEU VAL TYR PHE ALA SER THR ARG GLU SER GLY VAL PRO
SEQRES 6 E 115 ASP ARG PHE ILE GLY SER GLY SER GLY THR ASP PHE THR
SEQRES 7 E 115 LEU THR ILE SER SER VAL GLN ALA GLU ASP LEU ALA ASP
SEQRES 8 E 115 TYR PHE CYS GLN GLN HIS TYR SER THR PRO LEU THR PHE
SEQRES 9 E 115 GLY ALA GLY THR LYS LEU GLU LEU LYS ARG ALA
SEQRES 1 F 121 GLU VAL LYS LEU GLU GLN SER GLY ALA GLU LEU ALA ARG
SEQRES 2 F 121 PRO GLY ALA SER VAL LYS LEU SER CYS LYS ALA SER GLY
SEQRES 3 F 121 TYR THR PHE ALA SER TYR TRP MET GLN TRP VAL LYS GLN
SEQRES 4 F 121 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY ALA ILE TYR
SEQRES 5 F 121 PRO GLY ASP GLY ASP THR TRP TYR THR GLN LYS PHE LYS
SEQRES 6 F 121 GLY LYS ALA THR LEU THR ALA ASP LYS SER SER SER THR
SEQRES 7 F 121 ALA TYR MET GLN LEU SER SER LEU ALA SER GLU ASP SER
SEQRES 8 F 121 ALA VAL TYR TYR CYS ALA ARG PRO PRO TYR TYR TYR GLY
SEQRES 9 F 121 THR THR TYR TYR PHE ASP TYR TRP GLY GLN GLY THR THR
SEQRES 10 F 121 LEU THR VAL SER
HELIX 1 1 GLN L 85 LEU L 89 5 5
HELIX 2 2 THR H 143 TYR H 147 5 5
HELIX 3 3 GLN H 177 LYS H 180 5 4
HELIX 4 4 ALA H 202 SER H 206 5 5
HELIX 5 5 TYR H 216 THR H 220 5 5
HELIX 6 6 GLN A 85 LEU A 89 5 5
HELIX 7 7 THR B 143 TYR B 147 5 5
HELIX 8 8 GLN B 177 LYS B 180 5 4
HELIX 9 9 ALA B 202 SER B 206 5 5
HELIX 10 10 TYR B 216 THR B 220 5 5
HELIX 11 11 GLN C 85 LEU C 89 5 5
HELIX 12 12 THR D 143 TYR D 147 5 5
HELIX 13 13 GLN D 177 LYS D 180 5 4
HELIX 14 14 ALA D 202 SER D 206 5 5
HELIX 15 15 TYR D 216 THR D 220 5 5
HELIX 16 16 GLN E 85 LEU E 89 5 5
HELIX 17 17 THR F 143 TYR F 147 5 5
HELIX 18 18 GLN F 177 LYS F 180 5 4
HELIX 19 19 ALA F 202 SER F 206 5 5
HELIX 20 20 TYR F 216 THR F 220 5 5
SHEET 1 A 4 MET L 4 SER L 7 0
SHEET 2 A 4 VAL L 19 SER L 25 -1 O LYS L 24 N THR L 5
SHEET 3 A 4 ASP L 76 ILE L 81 -1 O PHE L 77 N CYS L 23
SHEET 4 A 4 PHE L 68 SER L 73 -1 N SER L 71 O THR L 78
SHEET 1 B 6 SER L 10 SER L 14 0
SHEET 2 B 6 THR L 108 LYS L 113 1 O GLU L 111 N LEU L 11
SHEET 3 B 6 ALA L 90 GLN L 96 -1 N ALA L 90 O LEU L 110
SHEET 4 B 6 LEU L 39 GLN L 44 -1 N TYR L 42 O PHE L 93
SHEET 5 B 6 LYS L 51 TYR L 55 -1 O LEU L 53 N TRP L 41
SHEET 6 B 6 THR L 59 ARG L 60 -1 O THR L 59 N TYR L 55
SHEET 1 C 4 SER L 10 SER L 14 0
SHEET 2 C 4 THR L 108 LYS L 113 1 O GLU L 111 N LEU L 11
SHEET 3 C 4 ALA L 90 GLN L 96 -1 N ALA L 90 O LEU L 110
SHEET 4 C 4 THR L 103 PHE L 104 -1 O THR L 103 N GLN L 96
SHEET 1 D 4 LYS H 118 GLU H 120 0
SHEET 2 D 4 VAL H 133 SER H 140 -1 O LYS H 138 N GLU H 120
SHEET 3 D 4 THR H 193 LEU H 198 -1 O MET H 196 N LEU H 135
SHEET 4 D 4 ALA H 183 ASP H 188 -1 N THR H 186 O TYR H 195
SHEET 1 E 6 ALA H 124 ALA H 127 0
SHEET 2 E 6 THR H 231 VAL H 235 1 O THR H 234 N ALA H 127
SHEET 3 E 6 ALA H 207 ARG H 213 -1 N ALA H 207 O LEU H 233
SHEET 4 E 6 MET H 149 ARG H 155 -1 N VAL H 152 O TYR H 210
SHEET 5 E 6 GLY H 159 TYR H 167 -1 O GLU H 161 N LYS H 153
SHEET 6 E 6 ASP H 172 TYR H 175 -1 O TRP H 174 N ALA H 165
SHEET 1 F 4 ALA H 124 ALA H 127 0
SHEET 2 F 4 THR H 231 VAL H 235 1 O THR H 234 N ALA H 127
SHEET 3 F 4 ALA H 207 ARG H 213 -1 N ALA H 207 O LEU H 233
SHEET 4 F 4 TYR H 226 TRP H 227 -1 O TYR H 226 N ARG H 213
SHEET 1 G 4 MET A 4 SER A 7 0
SHEET 2 G 4 VAL A 19 SER A 25 -1 O LYS A 24 N THR A 5
SHEET 3 G 4 ASP A 76 ILE A 81 -1 O PHE A 77 N CYS A 23
SHEET 4 G 4 PHE A 68 SER A 73 -1 N SER A 71 O THR A 78
SHEET 1 H 6 SER A 10 SER A 14 0
SHEET 2 H 6 THR A 108 LYS A 113 1 O GLU A 111 N LEU A 11
SHEET 3 H 6 ALA A 90 GLN A 96 -1 N ALA A 90 O LEU A 110
SHEET 4 H 6 LEU A 39 GLN A 44 -1 N TYR A 42 O PHE A 93
SHEET 5 H 6 LYS A 51 TYR A 55 -1 O LEU A 53 N TRP A 41
SHEET 6 H 6 THR A 59 ARG A 60 -1 O THR A 59 N TYR A 55
SHEET 1 I 4 SER A 10 SER A 14 0
SHEET 2 I 4 THR A 108 LYS A 113 1 O GLU A 111 N LEU A 11
SHEET 3 I 4 ALA A 90 GLN A 96 -1 N ALA A 90 O LEU A 110
SHEET 4 I 4 THR A 103 PHE A 104 -1 O THR A 103 N GLN A 96
SHEET 1 J 4 LYS B 118 GLU B 120 0
SHEET 2 J 4 VAL B 133 SER B 140 -1 O LYS B 138 N GLU B 120
SHEET 3 J 4 THR B 193 LEU B 198 -1 O MET B 196 N LEU B 135
SHEET 4 J 4 ALA B 183 ASP B 188 -1 N THR B 186 O TYR B 195
SHEET 1 K 6 ALA B 124 ALA B 127 0
SHEET 2 K 6 THR B 231 VAL B 235 1 O THR B 234 N ALA B 127
SHEET 3 K 6 ALA B 207 ARG B 213 -1 N ALA B 207 O LEU B 233
SHEET 4 K 6 MET B 149 ARG B 155 -1 N VAL B 152 O TYR B 210
SHEET 5 K 6 GLY B 159 TYR B 167 -1 O GLU B 161 N LYS B 153
SHEET 6 K 6 ASP B 172 TYR B 175 -1 O TRP B 174 N ALA B 165
SHEET 1 L 4 ALA B 124 ALA B 127 0
SHEET 2 L 4 THR B 231 VAL B 235 1 O THR B 234 N ALA B 127
SHEET 3 L 4 ALA B 207 ARG B 213 -1 N ALA B 207 O LEU B 233
SHEET 4 L 4 TYR B 226 TRP B 227 -1 O TYR B 226 N ARG B 213
SHEET 1 M 4 MET C 4 SER C 7 0
SHEET 2 M 4 VAL C 19 SER C 25 -1 O LYS C 24 N THR C 5
SHEET 3 M 4 ASP C 76 ILE C 81 -1 O PHE C 77 N CYS C 23
SHEET 4 M 4 PHE C 68 SER C 73 -1 N SER C 71 O THR C 78
SHEET 1 N 6 SER C 10 SER C 14 0
SHEET 2 N 6 THR C 108 LYS C 113 1 O GLU C 111 N LEU C 11
SHEET 3 N 6 ALA C 90 GLN C 96 -1 N ALA C 90 O LEU C 110
SHEET 4 N 6 LEU C 39 GLN C 44 -1 N TYR C 42 O PHE C 93
SHEET 5 N 6 LYS C 51 TYR C 55 -1 O LEU C 53 N TRP C 41
SHEET 6 N 6 THR C 59 ARG C 60 -1 O THR C 59 N TYR C 55
SHEET 1 O 4 SER C 10 SER C 14 0
SHEET 2 O 4 THR C 108 LYS C 113 1 O GLU C 111 N LEU C 11
SHEET 3 O 4 ALA C 90 GLN C 96 -1 N ALA C 90 O LEU C 110
SHEET 4 O 4 THR C 103 PHE C 104 -1 O THR C 103 N GLN C 96
SHEET 1 P 4 LYS D 118 GLU D 120 0
SHEET 2 P 4 VAL D 133 SER D 140 -1 O LYS D 138 N GLU D 120
SHEET 3 P 4 THR D 193 LEU D 198 -1 O MET D 196 N LEU D 135
SHEET 4 P 4 ALA D 183 ASP D 188 -1 N THR D 186 O TYR D 195
SHEET 1 Q 6 ALA D 124 ALA D 127 0
SHEET 2 Q 6 THR D 231 VAL D 235 1 O THR D 234 N ALA D 127
SHEET 3 Q 6 ALA D 207 ARG D 213 -1 N ALA D 207 O LEU D 233
SHEET 4 Q 6 MET D 149 ARG D 155 -1 N VAL D 152 O TYR D 210
SHEET 5 Q 6 GLY D 159 TYR D 167 -1 O GLU D 161 N LYS D 153
SHEET 6 Q 6 ASP D 172 TYR D 175 -1 O TRP D 174 N ALA D 165
SHEET 1 R 4 ALA D 124 ALA D 127 0
SHEET 2 R 4 THR D 231 VAL D 235 1 O THR D 234 N ALA D 127
SHEET 3 R 4 ALA D 207 ARG D 213 -1 N ALA D 207 O LEU D 233
SHEET 4 R 4 TYR D 226 TRP D 227 -1 O TYR D 226 N ARG D 213
SHEET 1 S 4 MET E 4 SER E 7 0
SHEET 2 S 4 VAL E 19 SER E 25 -1 O LYS E 24 N THR E 5
SHEET 3 S 4 ASP E 76 ILE E 81 -1 O PHE E 77 N CYS E 23
SHEET 4 S 4 PHE E 68 SER E 73 -1 N SER E 71 O THR E 78
SHEET 1 T 6 SER E 10 SER E 14 0
SHEET 2 T 6 THR E 108 LYS E 113 1 O GLU E 111 N LEU E 11
SHEET 3 T 6 ALA E 90 GLN E 96 -1 N ALA E 90 O LEU E 110
SHEET 4 T 6 LEU E 39 GLN E 44 -1 N TYR E 42 O PHE E 93
SHEET 5 T 6 LYS E 51 TYR E 55 -1 O LEU E 53 N TRP E 41
SHEET 6 T 6 THR E 59 ARG E 60 -1 O THR E 59 N TYR E 55
SHEET 1 U 4 SER E 10 SER E 14 0
SHEET 2 U 4 THR E 108 LYS E 113 1 O GLU E 111 N LEU E 11
SHEET 3 U 4 ALA E 90 GLN E 96 -1 N ALA E 90 O LEU E 110
SHEET 4 U 4 THR E 103 PHE E 104 -1 O THR E 103 N GLN E 96
SHEET 1 V 4 LYS F 118 GLU F 120 0
SHEET 2 V 4 VAL F 133 SER F 140 -1 O LYS F 138 N GLU F 120
SHEET 3 V 4 THR F 193 LEU F 198 -1 O MET F 196 N LEU F 135
SHEET 4 V 4 ALA F 183 ASP F 188 -1 N THR F 186 O TYR F 195
SHEET 1 W 6 ALA F 124 ALA F 127 0
SHEET 2 W 6 THR F 231 VAL F 235 1 O THR F 234 N ALA F 127
SHEET 3 W 6 ALA F 207 ARG F 213 -1 N ALA F 207 O LEU F 233
SHEET 4 W 6 MET F 149 ARG F 155 -1 N VAL F 152 O TYR F 210
SHEET 5 W 6 GLY F 159 TYR F 167 -1 O GLU F 161 N LYS F 153
SHEET 6 W 6 ASP F 172 TYR F 175 -1 O TRP F 174 N ALA F 165
SHEET 1 X 4 ALA F 124 ALA F 127 0
SHEET 2 X 4 THR F 231 VAL F 235 1 O THR F 234 N ALA F 127
SHEET 3 X 4 ALA F 207 ARG F 213 -1 N ALA F 207 O LEU F 233
SHEET 4 X 4 TYR F 226 TRP F 227 -1 O TYR F 226 N ARG F 213
SSBOND 1 CYS L 23 CYS L 94 1555 1555 2.59
SSBOND 2 CYS H 137 CYS H 211 1555 1555 2.59
SSBOND 3 CYS A 23 CYS A 94 1555 1555 2.59
SSBOND 4 CYS B 137 CYS B 211 1555 1555 2.59
SSBOND 5 CYS C 23 CYS C 94 1555 1555 2.59
SSBOND 6 CYS D 137 CYS D 211 1555 1555 2.59
SSBOND 7 CYS E 23 CYS E 94 1555 1555 2.59
SSBOND 8 CYS F 137 CYS F 211 1555 1555 2.59
CISPEP 1 SER L 7 PRO L 8 0 -3.48
CISPEP 2 THR L 100 PRO L 101 0 -0.47
CISPEP 3 SER A 7 PRO A 8 0 -3.41
CISPEP 4 THR A 100 PRO A 101 0 -0.39
CISPEP 5 SER C 7 PRO C 8 0 -3.46
CISPEP 6 THR C 100 PRO C 101 0 -0.39
CISPEP 7 SER E 7 PRO E 8 0 -3.58
CISPEP 8 THR E 100 PRO E 101 0 -0.37
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
