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1SJJ.pdb
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1SJJ.pdb
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HEADER CONTRACTILE PROTEIN 03-MAR-04 1SJJ
TITLE CRYO-EM STRUCTURE OF CHICKEN GIZZARD SMOOTH MUSCLE ALPHA-
TITLE 2 ACTININ
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACTININ;
COMPND 3 CHAIN: A, B
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 OTHER_DETAILS: PROTEIN ISOLATED FROM CHICKEN GIZZARDS
KEYWDS 3-HELIX BUNDLE, CALPONIN HOMOLOGY DOMAIN, CALMODULIN-LIKE
KEYWDS 2 DOMAIN, ACTIN BINDING PROTEIN
EXPDTA CRYO-ELECTRON MICROSCOPY
AUTHOR J.LIU,D.W.TAYLOR,K.A.TAYLOR
REVDAT 2 13-APR-04 1SJJ 1 JRNL
REVDAT 1 23-MAR-04 1SJJ 0
JRNL AUTH J.LIU,D.W.TAYLOR,K.A.TAYLOR
JRNL TITL A 3-D RECONSTRUCTION OF SMOOTH MUSCLE
JRNL TITL 2 ALPHA-ACTININ BY CRYOEM REVEALS TWO DIFFERENT
JRNL TITL 3 CONFORMATIONS AT THE ACTIN-BINDING REGION.
JRNL REF J.MOL.BIOL. V. 338 115 2004
JRNL REFN ASTM JMOBAK UK ISSN 0022-2836
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.A.TAYLOR,D.W.TAYLOR
REMARK 1 TITL PROJECTION IMAGE OF SMOOTH MUSCLE ALPHA-ACTININ
REMARK 1 TITL 2 FROM TWO-DIMENSIONAL CRYSTALS FORMED ON POSITIVELY
REMARK 1 TITL 3 CHARGED LIPID LAYERS
REMARK 1 REF J.MOL.BIOL. V. 230 196 1993
REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.TANG,D. W.TAYLOR,K. A.TAYLOR
REMARK 1 TITL THE THREE-DIMENSIONAL STRUCTURE OF ALPHA-ACTININ
REMARK 1 TITL 2 OBTAINED BY CRYOELECTRON MICROSCOPY SUGGESTS A
REMARK 1 TITL 3 MODEL FOR CA(2+)-DEPENDENT ACTIN BINDING
REMARK 1 REF J.MOL.BIOL. V. 310 845 2001
REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836
REMARK 1 REFERENCE 3
REMARK 1 AUTH K. A.TAYLOR,D. W.TAYLOR,F.SCHACHAT
REMARK 1 TITL ISOFORMS OF ALPHA-ACTININ FROM CARDIAC, SMOOTH AND
REMARK 1 TITL 2 SKELETAL MUSCLE FORM POLAR ARRAYS OF ACTIN
REMARK 1 TITL 3 FILAMENTS
REMARK 1 REF J.CELL BIOL. V. 149 635 2000
REMARK 1 REFN ASTM JCLBA3 US ISSN 0021-9525
REMARK 2
REMARK 2 RESOLUTION. 20.00ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : RSREF
REMARK 3 RECONSTRUCTION SCHEMA : 2-D CRYSTALLOGRAPHY
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : 1DXX, 1HCI, 1CFD
REMARK 3 REFINEMENT SPACE : REAL
REMARK 3 REFINEMENT PROTOCOL : RIGID BODY
REMARK 3 REFINEMENT TARGET : HIGHEST CROSS CORRELATION
REMARK 3 COEFFICIENT AND LOWEST
REMARK 3 INTERATOM CONFLICTS
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : NULL
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : 5.000
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : 5.000
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 20.000
REMARK 3 NUMBER OF PARTICLES : NULL
REMARK 3 CTF CORRECTION METHOD : CORRECTION OF PHASES ONLY
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: UNIT CELL
REMARK 3 CALIBRATED USING THE AXIAL REPEAT OF TOBACCO MOSAIC VIRUS
REMARK 3
REMARK 3 OTHER_DETAILS: FOURIER TRANSFORMS OF IMAGES WERE MERGED USING
REMARK 3 STANDARD 2-D CRYSTAL PROGRAMS WITH AMPLITUDES AND PHASES
REMARK 3 DERIVED FROM IMAGES ALONE.
REMARK 4
REMARK 4 1SJJ COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAR-2004.
REMARK 100 THE RCSB ID CODE IS RCSB021764.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 EXPERIMENT TYPE : CRYO-ELECTRON MICROSCOPY
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE AGGREGATION STATE : 2D-CRYSTAL
REMARK 245 NAME OF SAMPLE : ALPHA-ACTININ
REMARK 245 SAMPLE CONCENTRATION : 0.75
REMARK 245 SAMPLE SUPPORT DETAILS : SAMPLES WERE RECOVERED FROM
REMARK 245 THE LIPID MONOLAYER USING
REMARK 245 RETICULATED CARBON FILMS,
REMARK 245 PLUNGE FROZEN IN LIQUID
REMARK 245 ETHANE, AND STORED FOR UP TO
REMARK 245 A MONTH BEFORE USE.
REMARK 245 SAMPLE VITRIFICATION DETAILS : PLUNGE FROZEN IN LIQUID
REMARK 245 ETHANE
REMARK 245 SAMPLE BUFFER : PHOSPHATE BUFFERED KCL
REMARK 245 PH : 7.00
REMARK 245 SAMPLE DETAILS: THE SAMPLE WAS FORMED ON A POSITIVELY CHARGED
REMARK 245 LIPID MONOLAYER COMPOSED OF DILAURYL PHOSPHATIDYL CHOLINE AND
REMARK 245 DIDODECYLDIMETHYL AMMONIUM BROMIDE
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : 100.00
REMARK 245 MICROSCOPE MODEL : FEI/PHILIPS CM300FEG/T
REMARK 245 DETECTOR TYPE : KODAK SO163 FILM
REMARK 245 MINIMUM DEFOCUS (NM) : 2000.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 6000.00
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : 0.00
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : 68.00
REMARK 245 NOMINAL CS : 2.00
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : NULL
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : 24000
REMARK 245 CALIBRATED MAGNIFICATION : NULL
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 300
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 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 1 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
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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS A PORTION OF THE BIOLOGICALLY
REMARK 300 SIGNIFICANT MULTIMER. SEE REMARK 350 FOR INFORMATION
REMARK 300 ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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: A, 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 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 CB ASN A 864 CZ ARG B 845 1665 0.31
REMARK 500 CE LYS A 836 CB SER B 828 1665 0.32
REMARK 500 CD2 HIS A 89 O SER A 813 1445 0.48
REMARK 500 CB PRO B 81 NH2 ARG B 301 2555 0.68
REMARK 500 CD PRO B 81 NH1 ARG B 301 2555 0.68
REMARK 500 O ARG A 866 O THR B 840 1665 0.70
REMARK 500 CA TYR A 863 C GLU B 847 1665 0.71
REMARK 500 CB PRO B 352 CA GLU B 358 2555 0.75
REMARK 500 CD PRO B 352 CB GLU B 358 2555 0.77
REMARK 500 O PRO A 81 C ALA A 817 1445 0.79
REMARK 500 CD1 TYR A 863 N GLU B 847 1665 0.83
REMARK 500 CE2 TYR A 863 O GLU B 843 1665 0.83
REMARK 500 NE2 HIS A 89 C SER A 813 1445 0.90
REMARK 500 CG1 VAL A 869 CA LEU B 832 1665 0.92
REMARK 500 CG PRO B 81 CZ ARG B 301 2555 0.94
REMARK 500 CG PRO B 352 CA GLU B 358 2555 0.99
REMARK 500 CB TYR A 863 C GLU B 847 1665 1.02
REMARK 500 CA TYR A 863 N LEU B 848 1665 1.04
REMARK 500 CG TYR A 863 CA GLU B 847 1665 1.04
REMARK 500 CA PRO A 81 CB ASP A 818 1445 1.07
REMARK 500 CG ASP A 874 CG PRO B 849 1665 1.07
REMARK 500 CB ASN A 864 NH2 ARG B 845 1665 1.10
REMARK 500 C TYR A 863 N LEU B 848 1665 1.12
REMARK 500 O ASN A 864 CB ALA B 853 1665 1.12
REMARK 500 CG PRO B 352 CB GLU B 358 2555 1.14
REMARK 500 CB PRO A 81 CB ASP A 818 1445 1.16
REMARK 500 NZ LYS A 836 CB SER B 828 1665 1.16
REMARK 500 N TYR A 863 O GLU B 847 1665 1.16
REMARK 500 CG PRO B 81 NH2 ARG B 301 2555 1.16
REMARK 500 CB ALA A 868 CB GLU B 843 1665 1.18
REMARK 500 NE2 HIS A 89 O SER A 813 1445 1.19
REMARK 500 NZ LYS A 836 CA SER B 828 1665 1.20
REMARK 500 OD2 ASP A 867 CD2 LEU B 844 1665 1.23
REMARK 500 CB PRO B 81 CZ ARG B 301 2555 1.24
REMARK 500 NE ARG A 866 CD2 LEU B 873 1665 1.25
REMARK 500 CG HIS A 89 O SER A 813 1445 1.26
REMARK 500 CA TYR A 863 O GLU B 847 1665 1.26
REMARK 500 CB TYR A 863 CA GLU B 847 1665 1.27
REMARK 500 O ALA A 868 O LEU B 832 1665 1.27
REMARK 500 CB PRO B 352 N GLU B 358 2555 1.28
REMARK 500 CG TYR A 863 N GLU B 847 1665 1.29
REMARK 500 CG TYR A 863 CB GLU B 847 1665 1.29
REMARK 500 CG PRO B 81 NH1 ARG B 301 2555 1.29
REMARK 500 C ARG A 866 O THR B 840 1665 1.32
REMARK 500 CB ASN A 864 NH1 ARG B 845 1665 1.33
REMARK 500 NH2 ARG B 83 N TRP B 382 2555 1.34
REMARK 500 N PRO B 352 CB GLU B 358 2555 1.34
REMARK 500 CD PRO B 352 CG GLU B 358 2555 1.35
REMARK 500 CD1 TYR A 863 CA GLU B 847 1665 1.36
REMARK 500 CZ TYR A 838 CD1 LEU B 832 1665 1.37
REMARK 500 O GLY A 865 O VAL B 841 1665 1.37
REMARK 500 CD ARG A 866 CD2 LEU B 873 1665 1.38
REMARK 500 CA ASN A 864 NH2 ARG B 845 1665 1.39
REMARK 500 O PRO A 81 CA ALA A 817 1445 1.42
REMARK 500 CE LYS A 836 OG SER B 828 1665 1.42
REMARK 500 O GLY A 865 N ARG B 845 1665 1.42
REMARK 500 CA ALA A 872 OE1 GLU B 847 1665 1.42
REMARK 500 CG1 VAL A 869 N LEU B 832 1665 1.43
REMARK 500 CG1 VAL A 88 NE ARG A 814 1445 1.44
REMARK 500 N PRO B 352 CG GLU B 358 2555 1.44
REMARK 500 CG ASN A 864 CZ ARG B 845 1665 1.45
REMARK 500 CB PRO A 81 CA ASP A 818 1445 1.46
REMARK 500 CD2 HIS A 89 C SER A 813 1445 1.48
REMARK 500 N TYR A 863 C GLU B 847 1665 1.48
REMARK 500 O TYR A 863 N LEU B 848 1665 1.48
REMARK 500 CZ TYR A 863 O GLU B 843 1665 1.49
REMARK 500 O PRO A 81 N ASP A 818 1445 1.50
REMARK 500 CG ASN A 864 NH2 ARG B 845 1665 1.50
REMARK 500 N ALA A 872 OE1 GLU B 847 1665 1.50
REMARK 500 CB ALA A 872 OE1 GLU B 847 1665 1.50
REMARK 500 CG GLU A 82 CB ALA A 817 1445 1.53
REMARK 500 ND1 HIS A 89 CG ARG A 814 1445 1.53
REMARK 500 CG PRO A 81 CB ASP A 818 1445 1.54
REMARK 500 N GLY A 865 CA ARG B 845 1665 1.54
REMARK 500 NE1 TRP A 30 O ARG A 233 2345 1.55
REMARK 500 CB TYR A 863 N LEU B 848 1665 1.55
REMARK 500 CG ASN A 864 NE ARG B 845 1665 1.55
REMARK 500 N ARG A 866 CG LEU B 844 1665 1.55
REMARK 500 CB TYR A 863 CB GLU B 847 1665 1.57
REMARK 500 CG PRO B 352 C GLU B 358 2555 1.57
REMARK 500 NH1 ARG A 866 CG MET B 860 1665 1.58
REMARK 500 N PRO B 81 NH1 ARG B 301 2555 1.59
REMARK 500 N ASN A 864 O LEU B 848 1665 1.61
REMARK 500 CB ASN A 864 NE ARG B 845 1665 1.61
REMARK 500 CB PRO B 352 CB GLU B 358 2555 1.62
REMARK 500 C ALA A 868 O LEU B 832 1665 1.63
REMARK 500 OD1 ASP A 874 CG PRO B 849 1665 1.63
REMARK 500 CG ASP A 867 CD2 LEU B 844 1665 1.64
REMARK 500 CB ASP A 874 CG PRO B 849 1665 1.65
REMARK 500 CE1 HIS A 89 CB ARG A 814 1445 1.66
REMARK 500 CD LYS A 836 CB SER B 828 1665 1.66
REMARK 500 OD1 ASN A 864 NE ARG B 845 1665 1.66
REMARK 500 CD PRO B 81 CZ ARG B 301 2555 1.67
REMARK 500 N PRO A 81 CB ASP A 818 1445 1.68
REMARK 500 CE1 TYR A 863 N GLU B 847 1665 1.68
REMARK 500 CA PRO B 81 CZ ARG B 301 2555 1.68
REMARK 500 CG1 VAL A 88 CD ARG A 814 1445 1.69
REMARK 500 NH1 ARG A 866 SD MET B 860 1665 1.69
REMARK 500 N ASN A 864 NH2 ARG B 845 1665 1.70
REMARK 500 CA PRO A 81 CA ASP A 818 1445 1.71
REMARK 500 CE1 HIS A 89 CG ARG A 814 1445 1.72
REMARK 500 CA ASN A 864 CZ ARG B 845 1665 1.72
REMARK 500 NE2 HIS A 89 N ARG A 814 1445 1.73
REMARK 500 C GLY A 865 N ARG B 845 1665 1.73
REMARK 500 N ASP A 867 CB LEU B 844 1665 1.73
REMARK 500 O PRO A 81 O ALA A 817 1445 1.74
REMARK 500 NH2 ARG A 83 CG ASP A 820 1445 1.74
REMARK 500 CB ALA A 253 CB ALA A 253 2345 1.75
REMARK 500 OH TYR A 838 CD1 LEU B 832 1665 1.76
REMARK 500 N ASP A 867 CG LEU B 844 1665 1.77
REMARK 500 CE LYS A 836 CA SER B 828 1665 1.78
REMARK 500 ND2 ASN A 864 NH2 ARG B 845 1665 1.78
REMARK 500 C PRO A 81 C ALA A 817 1445 1.79
REMARK 500 C TYR A 863 CA LEU B 848 1665 1.80
REMARK 500 N GLY A 865 N ARG B 845 1665 1.80
REMARK 500 OD2 ASP A 867 CG LEU B 844 1665 1.80
REMARK 500 N PRO B 81 CZ ARG B 301 2555 1.81
REMARK 500 CA PRO B 352 CB GLU B 358 2555 1.81
REMARK 500 NH2 ARG A 83 CB ASP A 820 1445 1.84
REMARK 500 O ARG A 866 C THR B 840 1665 1.85
REMARK 500 CE1 HIS A 89 O SER A 813 1445 1.87
REMARK 500 CA ALA A 29 OD2 ASP A 235 2345 1.89
REMARK 500 CB ALA A 868 CA GLU B 843 1665 1.89
REMARK 500 CZ ARG B 83 N TRP B 382 2555 1.89
REMARK 500 CA ASP A 867 CG1 ILE B 839 1665 1.90
REMARK 500 CE1 HIS A 89 CA ARG A 814 1445 1.91
REMARK 500 CB ASP A 867 CD1 ILE B 839 1665 1.91
REMARK 500 CB ASP A 874 CD PRO B 849 1665 1.91
REMARK 500 OH TYR A 838 O SER B 828 1665 1.92
REMARK 500 CA TYR A 863 CA LEU B 848 1665 1.92
REMARK 500 N ARG A 866 CD1 LEU B 844 1665 1.92
REMARK 500 OD2 ASP A 874 CG PRO B 849 1665 1.92
REMARK 500 O TYR A 863 O LEU B 844 1665 1.93
REMARK 500 N ASP A 867 CD2 LEU B 844 1665 1.93
REMARK 500 CA PRO B 81 NE ARG B 301 2555 1.93
REMARK 500 OE2 GLU B 82 CA GLY B 378 2555 1.93
REMARK 500 ND1 HIS A 89 O SER A 813 1445 1.94
REMARK 500 NE2 HIS A 89 CA SER A 813 1445 1.94
REMARK 500 CE2 TYR A 838 CD1 LEU B 832 1665 1.94
REMARK 500 O TYR A 863 CA LEU B 848 1665 1.94
REMARK 500 OE2 GLU B 82 O LYS B 377 2555 1.94
REMARK 500 CE1 HIS A 89 C SER A 813 1445 1.95
REMARK 500 CE1 HIS A 89 N ARG A 814 1445 1.95
REMARK 500 O TYR A 863 CB LEU B 848 1665 1.95
REMARK 500 CD1 TYR A 863 C ARG B 846 1665 1.95
REMARK 500 CE2 TYR A 863 C GLU B 843 1665 1.95
REMARK 500 O ASP A 867 CD1 ILE B 839 1665 1.95
REMARK 500 N VAL A 869 O LEU B 832 1665 1.95
REMARK 500 CG PRO B 352 N GLY B 359 2555 1.96
REMARK 500 NZ LYS A 836 C SER B 828 1665 1.98
REMARK 500 CG PRO B 352 CG GLU B 358 2555 1.98
REMARK 500 NZ LYS A 836 OG SER B 828 1665 1.99
REMARK 500 NE ARG B 83 N TRP B 382 2555 1.99
REMARK 500 CA PRO A 81 N ASP A 818 1445 2.00
REMARK 500 CD PRO A 81 CB ASP A 818 1445 2.00
REMARK 500 NH1 ARG A 83 O THR A 816 1445 2.01
REMARK 500 C PRO A 862 O GLU B 847 1665 2.01
REMARK 500 CB PRO B 81 NE ARG B 301 2555 2.01
REMARK 500 CE1 TYR A 863 CB ARG B 846 1665 2.02
REMARK 500 CB ARG A 866 CA VAL B 841 1665 2.03
REMARK 500 C ARG B 351 CG GLU B 358 2555 2.03
REMARK 500 CB PRO A 81 N ASP A 818 1445 2.04
REMARK 500 C TYR A 863 C GLU B 847 1665 2.04
REMARK 500 CD2 TYR A 863 CB GLU B 847 1665 2.04
REMARK 500 CZ ARG A 866 CD2 LEU B 873 1665 2.05
REMARK 500 CG1 VAL A 869 CB LEU B 832 1665 2.05
REMARK 500 C TYR A 863 O LEU B 848 1665 2.06
REMARK 500 O GLY A 865 CA ARG B 845 1665 2.06
REMARK 500 O LYS A 80 OD1 ASP A 818 1445 2.07
REMARK 500 CB TYR A 863 O GLU B 847 1665 2.07
REMARK 500 CA ARG A 866 O THR B 840 1665 2.07
REMARK 500 CG TYR A 863 C GLU B 847 1665 2.08
REMARK 500 OH TYR A 863 O GLU B 843 1665 2.08
REMARK 500 CB PRO A 81 O ALA A 817 1445 2.09
REMARK 500 OE1 GLN A 254 NE2 GLN A 254 2345 2.09
REMARK 500 CA ARG A 866 CA VAL B 841 1665 2.09
REMARK 500 CA ASP A 867 CD1 ILE B 839 1665 2.09
REMARK 500 CB VAL A 88 CD ARG A 814 1445 2.10
REMARK 500 CB ALA A 868 CG GLU B 843 1665 2.11
REMARK 500 NH2 ARG B 83 C GLU B 381 2555 2.11
REMARK 500 CA PRO A 81 CG ASP A 818 1445 2.13
REMARK 500 CD PRO B 352 CD GLU B 358 2555 2.13
REMARK 500 N PRO A 81 CG ASP A 818 1445 2.14
REMARK 500 CD2 TYR A 863 O LEU B 844 1665 2.14
REMARK 500 CA GLY A 865 N ARG B 845 1665 2.14
REMARK 500 CB ARG A 866 N VAL B 841 1665 2.14
REMARK 500 C ASP A 867 CD1 ILE B 839 1665 2.14
REMARK 500 CA PRO B 81 NH2 ARG B 301 2555 2.14
REMARK 500 CA PRO B 352 CA GLU B 358 2555 2.14
REMARK 500 CB PRO A 81 C ASP A 818 1445 2.15
REMARK 500 CD2 TYR A 863 O GLU B 843 1665 2.15
REMARK 500 C GLY A 865 O VAL B 841 1665 2.15
REMARK 500 O GLY A 865 CB ARG B 845 1665 2.15
REMARK 500 C ALA A 872 OE1 GLU B 847 1665 2.15
REMARK 500 NH2 ARG B 83 N GLU B 381 2555 2.15
REMARK 500 CH2 TRP A 129 O LYS A 237 2345 2.16
REMARK 500 CD1 TYR A 863 CB GLU B 847 1665 2.16
REMARK 500 CD2 TYR A 863 N GLU B 847 1665 2.16
REMARK 500 CG PRO B 81 NE ARG B 301 2555 2.16
REMARK 500 CA TYR A 863 CA GLU B 847 1665 2.17
REMARK 500 NH2 ARG A 866 O CYS B 856 1665 2.17
REMARK 500 CE1 TYR A 838 CD1 LEU B 832 1665 2.18
REMARK 500 C ASN A 864 CB ALA B 853 1665 2.18
REMARK 500 OD1 ASN A 864 CZ ARG B 845 1665 2.18
REMARK 500 OD2 ASP A 867 CD1 LEU B 844 1665 2.18
REMARK 500 O PRO A 28 CA ASP A 235 2345 2.19
REMARK 500 O PRO A 81 CB ALA A 817 1445 2.19
REMARK 500 CB VAL A 869 CA LEU B 832 1665 2.19
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),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 149 CD GLU A 149 OE2 0.113
REMARK 500 GLU B 149 CD GLU B 149 OE2 0.114
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 VAL A 142 CB - CA - C ANGL. DEV. = 18.8 DEGREES
REMARK 500 GLU A 149 CB - CA - C ANGL. DEV. =-25.7 DEGREES
REMARK 500 CYS B 264 C - N - CA ANGL. DEV. = 16.6 DEGREES
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 M RES CSSEQI PSI PHI
REMARK 500 SER A 110 -45.50 135.01
REMARK 500 LYS A 148 60.34 133.43
REMARK 500 SER A 251 68.79 5.12
REMARK 500 ALA A 268 -44.98 142.11
REMARK 500 GLU A 299 -49.26 65.65
REMARK 500 ARG A 389 -68.28 78.01
REMARK 500 ARG A 392 -68.80 146.07
REMARK 500 MET A 587 129.72 72.02
REMARK 500 ILE A 657 -38.20 52.79
REMARK 500 ASP B 59 -38.92 70.85
REMARK 500 GLU B 82 134.85 104.83
REMARK 500 ALA B 249 -80.57 62.54
REMARK 500 SER B 349 -67.66 94.25
REMARK 500 ASN B 350 72.54 104.57
REMARK 500 ILE B 657 -64.27 72.21
REMARK 500 THR B 710 167.46 78.00
REMARK 500 ARG B 799 56.18 136.67
REMARK 500 ASN B 864 -52.65 54.17
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 LEU A 26 ASP A 27 -131.98
REMARK 500 ASP A 27 PRO A 28 -149.74
REMARK 500 ILE A 56 GLU A 57 147.43
REMARK 500 GLU A 58 ASP A 59 -120.97
REMARK 500 ASP A 118 GLY A 119 119.03
REMARK 500 ALA A 136 ILE A 137 146.46
REMARK 500 SER A 141 VAL A 142 -52.63
REMARK 500 LYS A 148 GLU A 149 -32.45
REMARK 500 ALA A 256 GLU A 257 135.61
REMARK 500 GLU A 257 THR A 258 48.22
REMARK 500 ALA A 624 ARG A 625 143.95
REMARK 500 SER A 745 GLN A 746 -125.90
REMARK 500 PHE A 759 ASP A 760 145.50
REMARK 500 TYR A 863 ASN A 864 -149.28
REMARK 500 LEU B 26 ASP B 27 -128.37
REMARK 500 ASP B 27 PRO B 28 -147.64
REMARK 500 GLU B 58 ASP B 59 133.16
REMARK 500 ASP B 118 GLY B 119 142.39
REMARK 500 LYS B 199 ASP B 200 148.21
REMARK 500 VAL B 229 GLY B 230 -149.44
REMARK 500 MET B 355 PRO B 356 -136.49
REMARK 500 GLU B 376 LYS B 377 -146.14
REMARK 500 GLU B 660 MET B 661 -142.00
REMARK 500 ASN B 730 GLU B 731 143.08
REMARK 500 THR B 738 ARG B 739 126.71
REMARK 500 SER B 745 GLN B 746 106.13
REMARK 500 GLY B 780 TYR B 781 -147.29
REMARK 500 TYR B 781 ASN B 782 144.55
REMARK 500 ASP B 818 THR B 819 138.87
REMARK 500 THR B 819 ASP B 820 -140.41
REMARK 500 SER B 886 ASP B 887 140.71
REMARK 500 ASP B 887 LEU B 888 133.39
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HCI RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE ROD DOMAIN OF ALPHA-ACTININ
REMARK 900 RELATED ID: 1AOA RELATED DB: PDB
REMARK 900 N-TERMINAL ACTIN-CROSSLINKING DOMAIN FROM HUMAN FIMBRIN
REMARK 900 RELATED ID: 1DXX RELATED DB: PDB
REMARK 900 N-TERMINAL ACTIN-BINDING DOMAIN OF HUMAN DYSTROPHIN
REMARK 900 RELATED ID: 1QAG RELATED DB: PDB
REMARK 900 ACTIN BINDING REGION OF THE DYSTROPHIN HOMOLOGUE UTROPHIN
REMARK 900 RELATED ID: 1CFD RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF CALMODULIN OBTAINED BY NMR
DBREF 1SJJ A 26 888 GB 211077 AAA48567 26 888
DBREF 1SJJ B 26 888 GB 211077 AAA48567 26 888
SEQRES 1 A 863 LEU ASP PRO ALA TRP GLU LYS GLN GLN ARG LYS THR PHE
SEQRES 2 A 863 THR ALA TRP CYS ASN SER HIS LEU ARG LYS ALA GLY THR
SEQRES 3 A 863 GLN ILE GLU ASN ILE GLU GLU ASP PHE ARG ASP GLY LEU
SEQRES 4 A 863 LYS LEU MET LEU LEU LEU GLU VAL ILE SER GLY GLU ARG
SEQRES 5 A 863 LEU ALA LYS PRO GLU ARG GLY LYS MET ARG VAL HIS LYS
SEQRES 6 A 863 ILE SER ASN VAL ASN LYS ALA LEU ASP PHE ILE ALA SER
SEQRES 7 A 863 LYS GLY VAL LYS LEU VAL SER ILE GLY ALA GLU GLU ILE
SEQRES 8 A 863 VAL ASP GLY ASN VAL LYS MET THR LEU GLY MET ILE TRP
SEQRES 9 A 863 THR ILE ILE LEU ARG PHE ALA ILE GLN ASP ILE SER VAL
SEQRES 10 A 863 GLU GLU THR SER ALA LYS GLU GLY LEU LEU LEU TRP TYR
SEQRES 11 A 863 GLN ARG LYS THR ALA PRO TYR LYS ASN VAL ASN ILE GLN
SEQRES 12 A 863 ASN PHE HIS ILE SER TRP LYS ASP GLY LEU GLY PHE CYS
SEQRES 13 A 863 ALA LEU ILE HIS ARG HIS ARG PRO GLU LEU ILE ASP TYR
SEQRES 14 A 863 GLY LYS LEU ARG LYS ASP ASP PRO LEU THR ASN LEU ASN
SEQRES 15 A 863 THR ALA PHE ASP VAL ALA GLU LYS TYR LEU ASP ILE PRO
SEQRES 16 A 863 LYS MET LEU ASP ALA GLU ASP ILE VAL GLY THR ALA ARG
SEQRES 17 A 863 PRO ASP GLU LYS ALA ILE MET THR TYR VAL SER SER PHE
SEQRES 18 A 863 TYR HIS ALA PHE SER GLY ALA GLN LYS ALA GLU THR ALA
SEQRES 19 A 863 ALA ASN ARG ILE CYS LYS VAL LEU ALA VAL ASN GLN GLU
SEQRES 20 A 863 ASN GLU GLN LEU MET GLU ASP TYR GLU LYS LEU ALA SER
SEQRES 21 A 863 ASP LEU LEU GLU TRP ILE ARG ARG THR ILE PRO TRP LEU
SEQRES 22 A 863 GLU ASN ARG ALA PRO GLU ASN THR MET GLN ALA MET GLN
SEQRES 23 A 863 GLN LYS LEU GLU ASP PHE ARG ASP TYR ARG ARG LEU HIS
SEQRES 24 A 863 LYS PRO PRO LYS VAL GLN GLU LYS CYS GLN LEU GLU ILE
SEQRES 25 A 863 ASN PHE ASN THR LEU GLN THR LYS LEU ARG LEU SER ASN
SEQRES 26 A 863 ARG PRO ALA PHE MET PRO SER GLU GLY LYS MET VAL SER
SEQRES 27 A 863 ASP ILE ASN ASN ALA TRP GLY GLY LEU GLU GLN ALA GLU
SEQRES 28 A 863 LYS GLY TYR GLU GLU TRP LEU LEU ASN GLU ILE ARG ARG
SEQRES 29 A 863 LEU GLU ARG LEU ASP HIS LEU ALA GLU LYS PHE ARG GLN
SEQRES 30 A 863 LYS ALA SER ILE HIS GLU SER TRP THR ASP GLY LYS GLU
SEQRES 31 A 863 ALA MET LEU GLN GLN LYS ASP TYR GLU THR ALA THR LEU
SEQRES 32 A 863 SER GLU ILE LYS ALA LEU LEU LYS LYS HIS GLU ALA PHE
SEQRES 33 A 863 GLU SER ASP LEU ALA ALA HIS GLN ASP ARG VAL GLU GLN
SEQRES 34 A 863 ILE ALA ALA ILE ALA GLN GLU LEU ASN GLU LEU ASP TYR
SEQRES 35 A 863 TYR ASP SER PRO SER VAL ASN ALA ARG CYS GLN LYS ILE
SEQRES 36 A 863 CYS ASP GLN TRP ASP ASN LEU GLY ALA LEU THR GLN LYS
SEQRES 37 A 863 ARG ARG GLU ALA LEU GLU ARG THR GLU LYS LEU LEU GLU
SEQRES 38 A 863 THR ILE ASP GLN LEU TYR LEU GLU TYR ALA LYS ARG ALA
SEQRES 39 A 863 ALA PRO PHE ASN ASN TRP MET GLU GLY ALA MET GLU ASP
SEQRES 40 A 863 LEU GLN ASP THR PHE ILE VAL HIS THR ILE GLU GLU ILE
SEQRES 41 A 863 GLN GLY LEU THR THR ALA HIS GLU GLN PHE LYS ALA THR
SEQRES 42 A 863 LEU PRO ASP ALA ASP LYS GLU ARG GLN ALA ILE LEU GLY
SEQRES 43 A 863 ILE HIS ASN GLU VAL SER LYS ILE VAL GLN THR TYR HIS
SEQRES 44 A 863 VAL ASN MET ALA GLY THR ASN PRO TYR THR THR ILE THR
SEQRES 45 A 863 PRO GLN GLU ILE ASN GLY LYS TRP GLU HIS VAL ARG GLN
SEQRES 46 A 863 LEU VAL PRO ARG ARG ASP GLN ALA LEU MET GLU GLU HIS
SEQRES 47 A 863 ALA ARG GLN GLN GLN ASN GLU ARG LEU ARG LYS GLN PHE
SEQRES 48 A 863 GLY ALA GLN ALA ASN VAL ILE GLY PRO TRP ILE GLN THR
SEQRES 49 A 863 LYS MET GLU GLU ILE GLY ARG ILE SER ILE GLU MET HIS
SEQRES 50 A 863 GLY THR LEU GLU ASP GLN LEU ASN HIS LEU ARG GLN TYR
SEQRES 51 A 863 GLU LYS SER ILE VAL ASN TYR LYS PRO LYS ILE ASP GLN
SEQRES 52 A 863 LEU GLU GLY ASP HIS GLN GLN ILE GLN GLU ALA LEU ILE
SEQRES 53 A 863 PHE ASP ASN LYS HIS THR ASN TYR THR MET GLU HIS ILE
SEQRES 54 A 863 ARG VAL GLY TRP GLU GLN LEU LEU THR THR ILE ALA ARG
SEQRES 55 A 863 THR ILE ASN GLU VAL GLU ASN GLN ILE LEU THR ARG ASP
SEQRES 56 A 863 ALA LYS GLY ILE SER GLN GLU GLN MET ASN GLU PHE ARG
SEQRES 57 A 863 ALA SER PHE ASN HIS PHE ASP ARG LYS LYS THR GLY MET
SEQRES 58 A 863 MET ASP CYS GLU ASP PHE ARG ALA CYS LEU ILE SER MET
SEQRES 59 A 863 GLY TYR ASN MET GLY GLU ALA GLU PHE ALA ARG ILE MET
SEQRES 60 A 863 SER ILE VAL ASP PRO ASN ARG MET GLY VAL VAL THR PHE
SEQRES 61 A 863 GLN ALA PHE ILE ASP PHE MET SER ARG GLU THR ALA ASP
SEQRES 62 A 863 THR ASP THR ALA ASP GLN VAL MET ALA SER PHE LYS ILE
SEQRES 63 A 863 LEU ALA GLY ASP LYS ASN TYR ILE THR VAL ASP GLU LEU
SEQRES 64 A 863 ARG ARG GLU LEU PRO PRO ASP GLN ALA GLU TYR CYS ILE
SEQRES 65 A 863 ALA ARG MET ALA PRO TYR ASN GLY ARG ASP ALA VAL PRO
SEQRES 66 A 863 GLY ALA LEU ASP TYR MET SER PHE SER THR ALA LEU TYR
SEQRES 67 A 863 GLY GLU SER ASP LEU
SEQRES 1 B 863 LEU ASP PRO ALA TRP GLU LYS GLN GLN ARG LYS THR PHE
SEQRES 2 B 863 THR ALA TRP CYS ASN SER HIS LEU ARG LYS ALA GLY THR
SEQRES 3 B 863 GLN ILE GLU ASN ILE GLU GLU ASP PHE ARG ASP GLY LEU
SEQRES 4 B 863 LYS LEU MET LEU LEU LEU GLU VAL ILE SER GLY GLU ARG
SEQRES 5 B 863 LEU ALA LYS PRO GLU ARG GLY LYS MET ARG VAL HIS LYS
SEQRES 6 B 863 ILE SER ASN VAL ASN LYS ALA LEU ASP PHE ILE ALA SER
SEQRES 7 B 863 LYS GLY VAL LYS LEU VAL SER ILE GLY ALA GLU GLU ILE
SEQRES 8 B 863 VAL ASP GLY ASN VAL LYS MET THR LEU GLY MET ILE TRP
SEQRES 9 B 863 THR ILE ILE LEU ARG PHE ALA ILE GLN ASP ILE SER VAL
SEQRES 10 B 863 GLU GLU THR SER ALA LYS GLU GLY LEU LEU LEU TRP TYR
SEQRES 11 B 863 GLN ARG LYS THR ALA PRO TYR LYS ASN VAL ASN ILE GLN
SEQRES 12 B 863 ASN PHE HIS ILE SER TRP LYS ASP GLY LEU GLY PHE CYS
SEQRES 13 B 863 ALA LEU ILE HIS ARG HIS ARG PRO GLU LEU ILE ASP TYR
SEQRES 14 B 863 GLY LYS LEU ARG LYS ASP ASP PRO LEU THR ASN LEU ASN
SEQRES 15 B 863 THR ALA PHE ASP VAL ALA GLU LYS TYR LEU ASP ILE PRO
SEQRES 16 B 863 LYS MET LEU ASP ALA GLU ASP ILE VAL GLY THR ALA ARG
SEQRES 17 B 863 PRO ASP GLU LYS ALA ILE MET THR TYR VAL SER SER PHE
SEQRES 18 B 863 TYR HIS ALA PHE SER GLY ALA GLN LYS ALA GLU THR ALA
SEQRES 19 B 863 ALA ASN ARG ILE CYS LYS VAL LEU ALA VAL ASN GLN GLU
SEQRES 20 B 863 ASN GLU GLN LEU MET GLU ASP TYR GLU LYS LEU ALA SER
SEQRES 21 B 863 ASP LEU LEU GLU TRP ILE ARG ARG THR ILE PRO TRP LEU
SEQRES 22 B 863 GLU ASN ARG ALA PRO GLU ASN THR MET GLN ALA MET GLN
SEQRES 23 B 863 GLN LYS LEU GLU ASP PHE ARG ASP TYR ARG ARG LEU HIS
SEQRES 24 B 863 LYS PRO PRO LYS VAL GLN GLU LYS CYS GLN LEU GLU ILE
SEQRES 25 B 863 ASN PHE ASN THR LEU GLN THR LYS LEU ARG LEU SER ASN
SEQRES 26 B 863 ARG PRO ALA PHE MET PRO SER GLU GLY LYS MET VAL SER
SEQRES 27 B 863 ASP ILE ASN ASN ALA TRP GLY GLY LEU GLU GLN ALA GLU
SEQRES 28 B 863 LYS GLY TYR GLU GLU TRP LEU LEU ASN GLU ILE ARG ARG
SEQRES 29 B 863 LEU GLU ARG LEU ASP HIS LEU ALA GLU LYS PHE ARG GLN
SEQRES 30 B 863 LYS ALA SER ILE HIS GLU SER TRP THR ASP GLY LYS GLU
SEQRES 31 B 863 ALA MET LEU GLN GLN LYS ASP TYR GLU THR ALA THR LEU
SEQRES 32 B 863 SER GLU ILE LYS ALA LEU LEU LYS LYS HIS GLU ALA PHE
SEQRES 33 B 863 GLU SER ASP LEU ALA ALA HIS GLN ASP ARG VAL GLU GLN
SEQRES 34 B 863 ILE ALA ALA ILE ALA GLN GLU LEU ASN GLU LEU ASP TYR
SEQRES 35 B 863 TYR ASP SER PRO SER VAL ASN ALA ARG CYS GLN LYS ILE
SEQRES 36 B 863 CYS ASP GLN TRP ASP ASN LEU GLY ALA LEU THR GLN LYS
SEQRES 37 B 863 ARG ARG GLU ALA LEU GLU ARG THR GLU LYS LEU LEU GLU
SEQRES 38 B 863 THR ILE ASP GLN LEU TYR LEU GLU TYR ALA LYS ARG ALA
SEQRES 39 B 863 ALA PRO PHE ASN ASN TRP MET GLU GLY ALA MET GLU ASP
SEQRES 40 B 863 LEU GLN ASP THR PHE ILE VAL HIS THR ILE GLU GLU ILE
SEQRES 41 B 863 GLN GLY LEU THR THR ALA HIS GLU GLN PHE LYS ALA THR
SEQRES 42 B 863 LEU PRO ASP ALA ASP LYS GLU ARG GLN ALA ILE LEU GLY
SEQRES 43 B 863 ILE HIS ASN GLU VAL SER LYS ILE VAL GLN THR TYR HIS
SEQRES 44 B 863 VAL ASN MET ALA GLY THR ASN PRO TYR THR THR ILE THR
SEQRES 45 B 863 PRO GLN GLU ILE ASN GLY LYS TRP GLU HIS VAL ARG GLN
SEQRES 46 B 863 LEU VAL PRO ARG ARG ASP GLN ALA LEU MET GLU GLU HIS
SEQRES 47 B 863 ALA ARG GLN GLN GLN ASN GLU ARG LEU ARG LYS GLN PHE
SEQRES 48 B 863 GLY ALA GLN ALA ASN VAL ILE GLY PRO TRP ILE GLN THR
SEQRES 49 B 863 LYS MET GLU GLU ILE GLY ARG ILE SER ILE GLU MET HIS
SEQRES 50 B 863 GLY THR LEU GLU ASP GLN LEU ASN HIS LEU ARG GLN TYR
SEQRES 51 B 863 GLU LYS SER ILE VAL ASN TYR LYS PRO LYS ILE ASP GLN
SEQRES 52 B 863 LEU GLU GLY ASP HIS GLN GLN ILE GLN GLU ALA LEU ILE
SEQRES 53 B 863 PHE ASP ASN LYS HIS THR ASN TYR THR MET GLU HIS ILE
SEQRES 54 B 863 ARG VAL GLY TRP GLU GLN LEU LEU THR THR ILE ALA ARG
SEQRES 55 B 863 THR ILE ASN GLU VAL GLU ASN GLN ILE LEU THR ARG ASP
SEQRES 56 B 863 ALA LYS GLY ILE SER GLN GLU GLN MET ASN GLU PHE ARG
SEQRES 57 B 863 ALA SER PHE ASN HIS PHE ASP ARG LYS LYS THR GLY MET
SEQRES 58 B 863 MET ASP CYS GLU ASP PHE ARG ALA CYS LEU ILE SER MET
SEQRES 59 B 863 GLY TYR ASN MET GLY GLU ALA GLU PHE ALA ARG ILE MET
SEQRES 60 B 863 SER ILE VAL ASP PRO ASN ARG MET GLY VAL VAL THR PHE
SEQRES 61 B 863 GLN ALA PHE ILE ASP PHE MET SER ARG GLU THR ALA ASP
SEQRES 62 B 863 THR ASP THR ALA ASP GLN VAL MET ALA SER PHE LYS ILE
SEQRES 63 B 863 LEU ALA GLY ASP LYS ASN TYR ILE THR VAL ASP GLU LEU
SEQRES 64 B 863 ARG ARG GLU LEU PRO PRO ASP GLN ALA GLU TYR CYS ILE
SEQRES 65 B 863 ALA ARG MET ALA PRO TYR ASN GLY ARG ASP ALA VAL PRO
SEQRES 66 B 863 GLY ALA LEU ASP TYR MET SER PHE SER THR ALA LEU TYR
SEQRES 67 B 863 GLY GLU SER ASP LEU
HELIX 1 1 TRP A 30 GLY A 50 1 21
HELIX 2 2 GLY A 63 ILE A 73 1 11
HELIX 3 3 MET A 86 LYS A 104 1 19
HELIX 4 4 ALA A 113 ASP A 118 1 6
HELIX 5 5 ASN A 120 LEU A 133 1 14
HELIX 6 6 LEU A 151 ALA A 160 1 10
HELIX 7 7 HIS A 171 LYS A 175 5 5
HELIX 8 8 GLY A 177 ARG A 186 1 10
HELIX 9 9 TYR A 194 LYS A 199 5 6
HELIX 10 10 PRO A 202 LEU A 206 5 5
HELIX 11 11 ASN A 207 ASP A 218 1 12
HELIX 12 12 ASP A 224 VAL A 229 1 6
HELIX 13 13 ASP A 235 PHE A 246 1 12
HELIX 14 14 VAL A 269 ILE A 295 1 27
HELIX 15 15 PRO A 296 LEU A 298 5 3
HELIX 16 16 THR A 306 LEU A 323 1 18
HELIX 17 17 LYS A 325 ASN A 338 1 14
HELIX 18 18 ASN A 340 LEU A 346 1 7
HELIX 19 19 MET A 361 SER A 363 5 3
HELIX 20 20 ASP A 364 LYS A 377 1 14
HELIX 21 21 TYR A 379 ILE A 387 1 9
HELIX 22 22 LEU A 390 GLN A 420 1 31
HELIX 23 23 THR A 427 ALA A 446 1 20
HELIX 24 24 ALA A 447 LEU A 465 1 19
HELIX 25 25 ASP A 469 ALA A 519 1 51
HELIX 26 26 PHE A 522 ASP A 535 1 14
HELIX 27 27 ILE A 542 GLU A 544 5 3
HELIX 28 28 ILE A 545 ALA A 557 1 13
HELIX 29 29 THR A 558 THR A 582 1 25
HELIX 30 30 THR A 597 MET A 620 1 24
HELIX 31 31 GLU A 622 ILE A 654 1 33
HELIX 32 32 LEU A 665 ASN A 681 1 17
HELIX 33 33 TYR A 682 PRO A 684 5 3
HELIX 34 34 LYS A 685 GLU A 698 1 14
HELIX 35 35 MET A 711 ARG A 739 1 29
HELIX 36 36 SER A 745 ASN A 757 1 13
HELIX 37 37 ASP A 771 GLY A 780 1 10
HELIX 38 38 GLU A 785 ASP A 796 1 12
HELIX 39 39 GLN A 806 PHE A 811 1 6
HELIX 40 40 PHE A 811 THR A 816 1 6
HELIX 41 41 ALA A 822 ILE A 831 1 10
HELIX 42 42 LEU A 832 GLY A 834 5 3
HELIX 43 43 VAL A 841 LEU A 848 1 8
HELIX 44 44 PRO A 849 MET A 860 1 12
HELIX 45 45 TYR A 875 TYR A 883 1 9
HELIX 46 46 ARG B 35 GLY B 50 1 16
HELIX 47 47 GLY B 63 VAL B 72 1 10
HELIX 48 48 MET B 86 SER B 103 1 18
HELIX 49 49 ALA B 113 ASP B 118 1 6
HELIX 50 50 ASN B 120 ARG B 134 1 15
HELIX 51 51 ILE B 137 VAL B 142 1 6
HELIX 52 52 ALA B 147 ALA B 160 1 14
HELIX 53 53 HIS B 171 LYS B 175 5 5
HELIX 54 54 GLY B 177 ARG B 188 1 12
HELIX 55 55 PRO B 189 ILE B 192 5 4
HELIX 56 56 ASP B 193 ARG B 198 1 6
HELIX 57 57 PRO B 202 LEU B 206 5 5
HELIX 58 58 ASN B 207 TYR B 216 1 10
HELIX 59 59 ASP B 224 VAL B 229 1 6
HELIX 60 60 ASP B 235 SER B 244 1 10
HELIX 61 61 SER B 245 HIS B 248 5 4
HELIX 62 62 GLN B 271 ASN B 300 1 30
HELIX 63 63 THR B 306 HIS B 324 1 19
HELIX 64 64 HIS B 324 LEU B 346 1 23
HELIX 65 65 ASP B 364 GLU B 376 1 13
HELIX 66 66 GLY B 378 TRP B 410 1 33
HELIX 67 67 GLY B 413 GLN B 419 1 7
HELIX 68 68 THR B 427 ALA B 446 1 20
HELIX 69 69 ALA B 447 GLU B 464 1 18
HELIX 70 70 ASP B 469 ALA B 519 1 51
HELIX 71 71 ASN B 523 LEU B 533 1 11
HELIX 72 72 THR B 541 THR B 558 1 18
HELIX 73 73 THR B 558 THR B 582 1 25
HELIX 74 74 THR B 597 ALA B 624 1 28
HELIX 75 75 ARG B 625 ILE B 654 1 30
HELIX 76 76 LEU B 665 LYS B 683 1 19
HELIX 77 77 LYS B 683 GLU B 698 1 16
HELIX 78 78 THR B 710 ILE B 729 1 20
HELIX 79 79 GLU B 731 ILE B 736 1 6
HELIX 80 80 GLN B 746 ASP B 760 1 15
HELIX 81 81 CYS B 769 GLY B 780 1 12
HELIX 82 82 GLU B 787 MET B 792 1 6
HELIX 83 83 SER B 793 VAL B 795 5 3
HELIX 84 84 THR B 804 ALA B 817 1 14
HELIX 85 85 ALA B 822 GLY B 834 1 13
HELIX 86 86 VAL B 841 LEU B 848 1 8
HELIX 87 87 GLN B 852 ALA B 858 1 7
HELIX 88 88 TYR B 875 THR B 880 1 6
SHEET 1 A 2 MET A 766 ASP A 768 0
SHEET 2 A 2 VAL A 802 THR A 804 -1 O VAL A 803 N MET A 767
SHEET 1 B 3 TYR A 838 THR A 840 0
SHEET 2 B 3 ALA A 872 ASP A 874 -1 O LEU A 873 N ILE A 839
SHEET 3 B 3 ALA A 861 PRO A 862 -1 N ALA A 861 O ASP A 874
SHEET 1 C 2 MET B 767 ASP B 768 0
SHEET 2 C 2 VAL B 802 VAL B 803 -1 O VAL B 803 N MET B 767
SHEET 1 D 3 TYR B 838 THR B 840 0
SHEET 2 D 3 ALA B 872 ASP B 874 -1 O LEU B 873 N ILE B 839
SHEET 3 D 3 ALA B 861 PRO B 862 -1 N ALA B 861 O ASP B 874
CISPEP 1 GLU A 82 ARG A 83 0 -0.18
CISPEP 2 ASP A 139 ILE A 140 0 1.33
CISPEP 3 VAL A 142 GLU A 143 0 -23.92
CISPEP 4 GLU A 143 GLU A 144 0 1.73
CISPEP 5 GLU A 144 THR A 145 0 -12.25
CISPEP 6 THR A 145 SER A 146 0 21.30
CISPEP 7 GLU A 149 GLY A 150 0 8.50
CISPEP 8 PHE A 250 SER A 251 0 15.20
CISPEP 9 SER A 251 GLY A 252 0 -3.97
CISPEP 10 ALA A 253 GLN A 254 0 6.72
CISPEP 11 ALA A 259 ALA A 260 0 19.78
CISPEP 12 ALA A 741 LYS A 742 0 2.91
CISPEP 13 GLU B 82 ARG B 83 0 13.33
CISPEP 14 GLU B 144 THR B 145 0 -6.54
CISPEP 15 THR B 145 SER B 146 0 -1.51
CISPEP 16 ARG B 262 ILE B 263 0 16.42
CISPEP 17 ILE B 263 CYS B 264 0 -3.32
CISPEP 18 ALA B 268 VAL B 269 0 -25.39
CRYST1 263.100 203.700 100.000 90.00 90.00 107.10 P 1 1 2 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.003801 0.001169 0.000000 0.00000
SCALE2 0.000000 0.005136 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010000 0.00000
ATOM 1912 N LYS A 265 -216.616-115.541 5.892 1.00 50.00 N
ATOM 1913 CA LYS A 265 -215.284-116.120 5.805 1.00 50.00 C
ATOM 1914 C LYS A 265 -215.134-116.928 7.076 1.00 50.00 C
ATOM 1915 O LYS A 265 -215.761-117.981 7.240 1.00 50.00 O
ATOM 1916 CB LYS A 265 -214.132-115.099 5.571 1.00 50.00 C
ATOM 1917 CG LYS A 265 -214.224-114.318 4.238 1.00 50.00 C
ATOM 1918 CD LYS A 265 -213.384-114.885 3.065 1.00 50.00 C
ATOM 1919 CE LYS A 265 -213.685-116.350 2.695 1.00 50.00 C
ATOM 1920 NZ LYS A 265 -213.013-116.751 1.436 1.00 50.00 N
ATOM 1921 N VAL A 266 -214.332-116.440 8.058 1.00 50.00 N
ATOM 1922 CA VAL A 266 -214.263-117.107 9.350 1.00 50.00 C
ATOM 1923 C VAL A 266 -214.365-116.072 10.465 1.00 50.00 C
ATOM 1924 O VAL A 266 -213.890-114.943 10.339 1.00 50.00 O
ATOM 1925 CB VAL A 266 -213.011-117.982 9.523 1.00 50.00 C
ATOM 1926 CG1 VAL A 266 -213.287-119.189 10.434 1.00 50.00 C
ATOM 1927 CG2 VAL A 266 -212.472-118.489 8.175 1.00 50.00 C
ATOM 1928 N LEU A 267 -214.952-116.409 11.631 1.00 50.00 N
ATOM 1929 CA LEU A 267 -214.697-115.715 12.887 1.00 50.00 C
ATOM 1930 C LEU A 267 -213.570-116.574 13.448 1.00 50.00 C
ATOM 1931 O LEU A 267 -213.739-117.781 13.608 1.00 50.00 O
ATOM 1932 CB LEU A 267 -215.964-115.630 13.788 1.00 50.00 C
ATOM 1933 CG LEU A 267 -215.943-114.748 15.068 1.00 50.00 C
ATOM 1934 CD1 LEU A 267 -214.817-115.103 16.056 1.00 50.00 C
ATOM 1935 CD2 LEU A 267 -215.944-113.246 14.758 1.00 50.00 C
ATOM 1936 N ALA A 268 -212.369-115.982 13.574 1.00 50.00 N
ATOM 1937 CA ALA A 268 -211.076-116.655 13.559 1.00 50.00 C
ATOM 1938 C ALA A 268 -210.114-115.756 12.814 1.00 50.00 C
ATOM 1939 O ALA A 268 -209.018-115.510 13.309 1.00 50.00 O
ATOM 1940 CB ALA A 268 -210.994-118.045 12.889 1.00 50.00 C
ATOM 1941 N VAL A 269 -210.561-115.202 11.649 1.00 50.00 N
ATOM 1942 CA VAL A 269 -209.958-114.137 10.819 1.00 50.00 C
ATOM 1943 C VAL A 269 -209.588-112.898 11.627 1.00 50.00 C
ATOM 1944 O VAL A 269 -208.899-111.968 11.232 1.00 50.00 O
ATOM 1945 CB VAL A 269 -210.950-113.741 9.721 1.00 50.00 C
ATOM 1946 CG1 VAL A 269 -210.574-112.463 8.937 1.00 50.00 C
ATOM 1947 CG2 VAL A 269 -211.018-114.903 8.724 1.00 50.00 C
ATOM 1948 N ASN A 270 -210.075-112.851 12.860 1.00 50.00 N
ATOM 1949 CA ASN A 270 -210.007-111.753 13.782 1.00 50.00 C
ATOM 1950 C ASN A 270 -208.624-111.564 14.376 1.00 50.00 C
ATOM 1951 O ASN A 270 -208.173-110.435 14.539 1.00 50.00 O
ATOM 1952 CB ASN A 270 -211.080-111.997 14.866 1.00 50.00 C
ATOM 1953 CG ASN A 270 -212.405-112.100 14.122 1.00 50.00 C
ATOM 1954 OD1 ASN A 270 -212.752-113.141 13.540 1.00 50.00 O
ATOM 1955 ND2 ASN A 270 -213.076-110.932 13.990 1.00 50.00 N
ATOM 1956 N GLN A 271 -207.873-112.649 14.669 1.00 50.00 N
ATOM 1957 CA GLN A 271 -206.604-112.552 15.373 1.00 50.00 C
ATOM 1958 C GLN A 271 -205.561-111.916 14.488 1.00 50.00 C
ATOM 1959 O GLN A 271 -204.729-111.140 14.944 1.00 50.00 O
ATOM 1960 CB GLN A 271 -206.051-113.904 15.898 1.00 50.00 C
ATOM 1961 CG GLN A 271 -207.089-115.032 16.097 1.00 50.00 C
ATOM 1962 CD GLN A 271 -208.174-114.836 17.157 1.00 50.00 C
ATOM 1963 OE1 GLN A 271 -208.843-113.805 17.255 1.00 50.00 O
ATOM 1964 NE2 GLN A 271 -208.389-115.915 17.951 1.00 50.00 N
ATOM 1965 N GLU A 272 -205.613-112.204 13.177 1.00 50.00 N
ATOM 1966 CA GLU A 272 -204.942-111.387 12.205 1.00 50.00 C
ATOM 1967 C GLU A 272 -205.524-109.986 12.136 1.00 50.00 C
ATOM 1968 O GLU A 272 -204.860-108.988 12.408 1.00 50.00 O
ATOM 1969 CB GLU A 272 -204.761-112.079 10.815 1.00 50.00 C
ATOM 1970 CG GLU A 272 -205.995-112.526 9.998 1.00 50.00 C
ATOM 1971 CD GLU A 272 -206.501-113.903 10.395 1.00 50.00 C
ATOM 1972 OE1 GLU A 272 -206.823-114.112 11.593 1.00 50.00 O
ATOM 1973 OE2 GLU A 272 -206.602-114.795 9.517 1.00 50.00 O
ATOM 1974 N ASN A 273 -206.810-109.844 11.795 1.00 50.00 N
ATOM 1975 CA ASN A 273 -207.332-108.672 11.133 1.00 50.00 C
ATOM 1976 C ASN A 273 -207.552-107.430 11.986 1.00 50.00 C
ATOM 1977 O ASN A 273 -207.328-106.304 11.542 1.00 50.00 O
ATOM 1978 CB ASN A 273 -208.603-109.155 10.437 1.00 50.00 C
ATOM 1979 CG ASN A 273 -209.009-108.384 9.219 1.00 50.00 C
ATOM 1980 OD1 ASN A 273 -210.125-108.588 8.737 1.00 50.00 O
ATOM 1981 ND2 ASN A 273 -208.146-107.542 8.632 1.00 50.00 N
ATOM 1982 N GLU A 274 -207.920-107.583 13.270 1.00 50.00 N
ATOM 1983 CA GLU A 274 -208.103-106.493 14.212 1.00 50.00 C
ATOM 1984 C GLU A 274 -206.801-106.267 14.998 1.00 50.00 C
ATOM 1985 O GLU A 274 -206.613-105.304 15.742 1.00 50.00 O
ATOM 1986 CB GLU A 274 -209.360-106.760 15.072 1.00 50.00 C
ATOM 1987 CG GLU A 274 -210.706-106.536 14.307 1.00 50.00 C
ATOM 1988 CD GLU A 274 -211.079-107.545 13.230 1.00 50.00 C
ATOM 1989 OE1 GLU A 274 -211.720-108.588 13.535 1.00 50.00 O
ATOM 1990 OE2 GLU A 274 -210.836-107.324 12.012 1.00 50.00 O
ATOM 1991 N GLN A 275 -205.781-107.094 14.687 1.00 50.00 N
ATOM 1992 CA GLN A 275 -204.398-106.737 14.942 1.00 50.00 C
ATOM 1993 C GLN A 275 -203.776-105.904 13.821 1.00 50.00 C
ATOM 1994 O GLN A 275 -202.931-105.062 14.110 1.00 50.00 O
ATOM 1995 CB GLN A 275 -203.498-107.952 15.178 1.00 50.00 C
ATOM 1996 CG GLN A 275 -203.436-108.458 16.633 1.00 50.00 C
ATOM 1997 CD GLN A 275 -202.287-109.461 16.698 1.00 50.00 C
ATOM 1998 OE1 GLN A 275 -201.146-109.134 16.394 1.00 50.00 O
ATOM 1999 NE2 GLN A 275 -202.596-110.739 16.982 1.00 50.00 N
ATOM 2000 N LEU A 276 -204.143-106.065 12.521 1.00 50.00 N
ATOM 2001 CA LEU A 276 -203.779-105.067 11.497 1.00 50.00 C
ATOM 2002 C LEU A 276 -204.221-103.654 11.951 1.00 50.00 C
ATOM 2003 O LEU A 276 -203.466-102.687 12.020 1.00 50.00 O
ATOM 2004 CB LEU A 276 -204.313-105.382 10.055 1.00 50.00 C
ATOM 2005 CG LEU A 276 -203.557-106.463 9.225 1.00 50.00 C
ATOM 2006 CD1 LEU A 276 -203.682-107.898 9.735 1.00 50.00 C
ATOM 2007 CD2 LEU A 276 -203.934-106.480 7.734 1.00 50.00 C
ATOM 2008 N MET A 277 -205.467-103.541 12.426 1.00 50.00 N
ATOM 2009 CA MET A 277 -205.993-102.428 13.203 1.00 50.00 C
ATOM 2010 C MET A 277 -205.195-101.956 14.464 1.00 50.00 C
ATOM 2011 O MET A 277 -205.201-100.772 14.804 1.00 50.00 O
ATOM 2012 CB MET A 277 -207.425-102.873 13.574 1.00 50.00 C
ATOM 2013 CG MET A 277 -208.392-101.778 14.024 1.00 50.00 C
ATOM 2014 SD MET A 277 -209.914-102.423 14.776 1.00 50.00 S
ATOM 2015 CE MET A 277 -209.148-102.800 16.380 1.00 50.00 C
ATOM 2016 N GLU A 278 -204.473-102.839 15.200 1.00 50.00 N
ATOM 2017 CA GLU A 278 -203.658-102.473 16.373 1.00 50.00 C
ATOM 2018 C GLU A 278 -202.234-102.082 15.986 1.00 50.00 C
ATOM 2019 O GLU A 278 -201.672-101.124 16.505 1.00 50.00 O
ATOM 2020 CB GLU A 278 -203.617-103.594 17.456 1.00 50.00 C
ATOM 2021 CG GLU A 278 -203.588-103.079 18.936 1.00 50.00 C
ATOM 2022 CD GLU A 278 -202.389-102.227 19.362 1.00 50.00 C
ATOM 2023 OE1 GLU A 278 -201.281-102.799 19.557 1.00 50.00 O
ATOM 2024 OE2 GLU A 278 -202.547-100.982 19.538 1.00 50.00 O
ATOM 2025 N ASP A 279 -201.623-102.801 15.022 1.00 50.00 N
ATOM 2026 CA ASP A 279 -200.292-102.619 14.474 1.00 50.00 C
ATOM 2027 C ASP A 279 -200.036-101.199 13.989 1.00 50.00 C
ATOM 2028 O ASP A 279 -199.084-100.548 14.404 1.00 50.00 O
ATOM 2029 CB ASP A 279 -200.138-103.629 13.309 1.00 50.00 C
ATOM 2030 CG ASP A 279 -198.699-104.028 13.043 1.00 50.00 C
ATOM 2031 OD1 ASP A 279 -198.391-105.231 13.256 1.00 50.00 O
ATOM 2032 OD2 ASP A 279 -197.894-103.184 12.605 1.00 50.00 O
ATOM 2033 N TYR A 280 -200.930-100.655 13.148 1.00 50.00 N
ATOM 2034 CA TYR A 280 -200.978 -99.248 12.786 1.00 50.00 C
ATOM 2035 C TYR A 280 -200.981 -98.339 14.022 1.00 50.00 C
ATOM 2036 O TYR A 280 -200.219 -97.373 14.107 1.00 50.00 O
ATOM 2037 CB TYR A 280 -202.227 -98.998 11.889 1.00 50.00 C
ATOM 2038 CG TYR A 280 -202.304 -97.576 11.383 1.00 50.00 C
ATOM 2039 CD1 TYR A 280 -202.786 -96.554 12.220 1.00 50.00 C
ATOM 2040 CD2 TYR A 280 -201.810 -97.234 10.113 1.00 50.00 C
ATOM 2041 CE1 TYR A 280 -202.696 -95.213 11.835 1.00 50.00 C
ATOM 2042 CE2 TYR A 280 -201.747 -95.889 9.712 1.00 50.00 C
ATOM 2043 CZ TYR A 280 -202.171 -94.880 10.585 1.00 50.00 C
ATOM 2044 OH TYR A 280 -202.032 -93.523 10.244 1.00 50.00 O
ATOM 2045 N GLU A 281 -201.815 -98.640 15.034 1.00 50.00 N
ATOM 2046 CA GLU A 281 -201.858 -97.900 16.289 1.00 50.00 C
ATOM 2047 C GLU A 281 -200.538 -97.856 17.076 1.00 50.00 C
ATOM 2048 O GLU A 281 -199.960 -96.782 17.261 1.00 50.00 O
ATOM 2049 CB GLU A 281 -203.041 -98.373 17.176 1.00 50.00 C
ATOM 2050 CG GLU A 281 -204.285 -97.477 17.027 1.00 50.00 C
ATOM 2051 CD GLU A 281 -203.960 -96.121 17.582 1.00 50.00 C
ATOM 2052 OE1 GLU A 281 -203.859 -95.129 16.815 1.00 50.00 O
ATOM 2053 OE2 GLU A 281 -203.721 -96.009 18.818 1.00 50.00 O
ATOM 2054 N LYS A 282 -200.006 -98.992 17.543 1.00 50.00 N
ATOM 2055 CA LYS A 282 -198.676 -99.179 18.123 1.00 50.00 C
ATOM 2056 C LYS A 282 -197.549 -98.553 17.305 1.00 50.00 C
ATOM 2057 O LYS A 282 -196.822 -97.685 17.803 1.00 50.00 O
ATOM 2058 CB LYS A 282 -198.448-100.703 18.290 1.00 50.00 C
ATOM 2059 CG LYS A 282 -197.010-101.269 18.337 1.00 50.00 C
ATOM 2060 CD LYS A 282 -196.940-102.398 17.294 1.00 50.00 C
ATOM 2061 CE LYS A 282 -195.587-103.069 17.104 1.00 50.00 C
ATOM 2062 NZ LYS A 282 -195.809-104.270 16.299 1.00 50.00 N
ATOM 2063 N LEU A 283 -197.389 -98.941 16.022 1.00 50.00 N
ATOM 2064 CA LEU A 283 -196.308 -98.498 15.137 1.00 50.00 C
ATOM 2065 C LEU A 283 -196.304 -96.997 14.961 1.00 50.00 C
ATOM 2066 O LEU A 283 -195.320 -96.291 15.201 1.00 50.00 O
ATOM 2067 CB LEU A 283 -196.410 -99.154 13.728 1.00 50.00 C
ATOM 2068 CG LEU A 283 -195.178 -99.003 12.809 1.00 50.00 C
ATOM 2069 CD1 LEU A 283 -193.981 -99.764 13.391 1.00 50.00 C
ATOM 2070 CD2 LEU A 283 -195.475 -99.520 11.388 1.00 50.00 C
ATOM 2071 N ALA A 284 -197.474 -96.410 14.604 1.00 50.00 N
ATOM 2072 CA ALA A 284 -197.641 -94.972 14.490 1.00 50.00 C
ATOM 2073 C ALA A 284 -197.349 -94.221 15.775 1.00 50.00 C
ATOM 2074 O ALA A 284 -196.916 -93.067 15.764 1.00 50.00 O
ATOM 2075 CB ALA A 284 -199.077 -94.610 14.063 1.00 50.00 C
ATOM 2076 N SER A 285 -197.580 -94.874 16.936 1.00 50.00 N
ATOM 2077 CA SER A 285 -197.256 -94.284 18.230 1.00 50.00 C
ATOM 2078 C SER A 285 -195.787 -93.994 18.396 1.00 50.00 C
ATOM 2079 O SER A 285 -195.459 -92.919 18.876 1.00 50.00 O
ATOM 2080 CB SER A 285 -197.758 -95.071 19.472 1.00 50.00 C
ATOM 2081 OG SER A 285 -198.893 -94.408 20.038 1.00 50.00 O
ATOM 2082 N ASP A 286 -194.864 -94.867 17.970 1.00 50.00 N
ATOM 2083 CA ASP A 286 -193.430 -94.640 18.031 1.00 50.00 C
ATOM 2084 C ASP A 286 -192.929 -93.637 17.016 1.00 50.00 C
ATOM 2085 O ASP A 286 -192.092 -92.771 17.294 1.00 50.00 O
ATOM 2086 CB ASP A 286 -192.674 -95.961 17.790 1.00 50.00 C
ATOM 2087 CG ASP A 286 -191.960 -96.272 19.072 1.00 50.00 C
ATOM 2088 OD1 ASP A 286 -190.729 -96.007 19.213 1.00 50.00 O
ATOM 2089 OD2 ASP A 286 -192.677 -96.788 19.972 1.00 50.00 O
ATOM 2090 N LEU A 287 -193.450 -93.696 15.773 1.00 50.00 N
ATOM 2091 CA LEU A 287 -193.038 -92.777 14.726 1.00 50.00 C
ATOM 2092 C LEU A 287 -193.421 -91.338 15.071 1.00 50.00 C
ATOM 2093 O LEU A 287 -192.653 -90.383 14.935 1.00 50.00 O
ATOM 2094 CB LEU A 287 -193.658 -93.218 13.378 1.00 50.00 C
ATOM 2095 CG LEU A 287 -193.166 -92.427 12.153 1.00 50.00 C
ATOM 2096 CD1 LEU A 287 -191.675 -92.652 11.875 1.00 50.00 C
ATOM 2097 CD2 LEU A 287 -193.975 -92.816 10.913 1.00 50.00 C
ATOM 2098 N LEU A 288 -194.628 -91.150 15.633 1.00 50.00 N
ATOM 2099 CA LEU A 288 -195.085 -89.876 16.144 1.00 50.00 C
ATOM 2100 C LEU A 288 -194.496 -89.496 17.493 1.00 50.00 C
ATOM 2101 O LEU A 288 -194.380 -88.307 17.793 1.00 50.00 O
ATOM 2102 CB LEU A 288 -196.622 -89.889 16.222 1.00 50.00 C
ATOM 2103 CG LEU A 288 -197.290 -89.980 14.836 1.00 50.00 C
ATOM 2104 CD1 LEU A 288 -198.798 -90.225 14.981 1.00 50.00 C
ATOM 2105 CD2 LEU A 288 -197.020 -88.699 14.036 1.00 50.00 C
ATOM 2106 N GLU A 289 -194.090 -90.472 18.341 1.00 50.00 N
ATOM 2107 CA GLU A 289 -193.289 -90.216 19.527 1.00 50.00 C
ATOM 2108 C GLU A 289 -191.961 -89.618 19.100 1.00 50.00 C
ATOM 2109 O GLU A 289 -191.643 -88.492 19.467 1.00 50.00 O
ATOM 2110 CB GLU A 289 -193.102 -91.487 20.404 1.00 50.00 C
ATOM 2111 CG GLU A 289 -192.416 -91.288 21.785 1.00 50.00 C
ATOM 2112 CD GLU A 289 -190.923 -91.049 21.673 1.00 50.00 C
ATOM 2113 OE1 GLU A 289 -190.252 -91.883 21.026 1.00 50.00 O
ATOM 2114 OE2 GLU A 289 -190.405 -90.037 22.202 1.00 50.00 O
ATOM 2115 N TRP A 290 -191.201 -90.302 18.225 1.00 50.00 N
ATOM 2116 CA TRP A 290 -189.886 -89.872 17.770 1.00 50.00 C
ATOM 2117 C TRP A 290 -189.782 -88.470 17.140 1.00 50.00 C
ATOM 2118 O TRP A 290 -188.904 -87.692 17.515 1.00 50.00 O
ATOM 2119 CB TRP A 290 -189.248 -90.939 16.842 1.00 50.00 C
ATOM 2120 CG TRP A 290 -187.807 -90.623 16.479 1.00 50.00 C
ATOM 2121 CD1 TRP A 290 -186.730 -90.514 17.316 1.00 50.00 C
ATOM 2122 CD2 TRP A 290 -187.380 -90.133 15.195 1.00 50.00 C
ATOM 2123 NE1 TRP A 290 -185.654 -89.995 16.627 1.00 50.00 N
ATOM 2124 CE2 TRP A 290 -186.030 -89.754 15.329 1.00 50.00 C
ATOM 2125 CE3 TRP A 290 -188.052 -89.976 13.987 1.00 50.00 C
ATOM 2126 CZ2 TRP A 290 -185.328 -89.218 14.259 1.00 50.00 C
ATOM 2127 CZ3 TRP A 290 -187.344 -89.420 12.908 1.00 50.00 C
ATOM 2128 CH2 TRP A 290 -185.999 -89.053 13.040 1.00 50.00 C
ATOM 2129 N ILE A 291 -190.651 -88.080 16.167 1.00 50.00 N
ATOM 2130 CA ILE A 291 -190.564 -86.733 15.585 1.00 50.00 C
ATOM 2131 C ILE A 291 -191.140 -85.620 16.467 1.00 50.00 C
ATOM 2132 O ILE A 291 -190.808 -84.454 16.266 1.00 50.00 O
ATOM 2133 CB ILE A 291 -191.109 -86.583 14.160 1.00 50.00 C
ATOM 2134 CG1 ILE A 291 -192.615 -86.876 14.024 1.00 50.00 C
ATOM 2135 CG2 ILE A 291 -190.258 -87.440 13.201 1.00 50.00 C
ATOM 2136 CD1 ILE A 291 -193.143 -86.578 12.617 1.00 50.00 C
ATOM 2137 N ARG A 292 -191.974 -85.925 17.480 1.00 50.00 N
ATOM 2138 CA ARG A 292 -192.455 -84.940 18.444 1.00 50.00 C
ATOM 2139 C ARG A 292 -191.384 -84.667 19.497 1.00 50.00 C
ATOM 2140 O ARG A 292 -191.345 -83.633 20.167 1.00 50.00 O