HEADER LYASE 11-MAR-04 1UZD
TITLE CHLAMYDOMONAS,SPINACH CHIMERIC RUBISCO
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN;
COMPND 3 CHAIN: A, B, E, H, K, O, R, V;
COMPND 4 SYNONYM: RUBISCO LARGE SUBUNIT, RIBULOSE-1,5 BISPHOSPHATE
COMPND 5 CARBOXYLASE LARGE CHAIN;
COMPND 6 EC: 4.1.1.39;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1,
COMPND 9 RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 2;
COMPND 10 CHAIN: I, C, F, J, P, T, M, W;
COMPND 11 SYNONYM: RUBISCO SMALL SUBUNIT 1,CHLOROPLAST, RUBISCO
COMPND 12 SMALL SUBUNIT 2,OXYGENASE, RIBULOSE-1,5 BISPHOSPHATE
COMPND 13 CARBOXYLASE/OXYGENASE;
COMPND 14 EC: 4.1.1.39;
COMPND 15 OTHER_DETAILS: ONE LOOP OF CHLAMYDOMONAS RUBISCO, RESIDUES
COMPND 16 GLU46-ASN70 HAS BEEN REPLACED WITH THE CORRESPONDING LOOP
COMPND 17 FROM SPINACH RUBISCO, RESIDUES THR46 - GLY64
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CHLAMYDOMONAS REINHARDTII;
SOURCE 3 ORGANISM_TAXID: 3055;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: CHLAMYDOMONAS REINHARDTII, SPINACIA
SOURCE 6 OLERACEA
KEYWDS LYASE, RUBISCO, PHOTOSYNTHESIS, CARBON DIOXIDE FIXATION,
KEYWDS 2 PHOTORESPIRATION, OXIDOREDUCTASE, MONOOXYGENASE,
KEYWDS 3 CHLOROPLAST, TRANSIT PEPTIDE, MULTIGENE FAMILY
EXPDTA X-RAY DIFFRACTION
AUTHOR S.KARKEHABADI,R.J.SPREITZER,I.ANDERSSON
REVDAT 3 24-FEB-09 1UZD 1 VERSN
REVDAT 2 27-JUL-05 1UZD 1 JRNL
REVDAT 1 31-MAY-05 1UZD 0
JRNL AUTH S.KARKEHABADI,S.R.PEDDI,M.ANWARUZZAMAN,T.C.TAYLOR,
JRNL AUTH 2 A.CEDERLUND,T.GENKOV,I.ANDERSSON,R.J.SPREITZER
JRNL TITL CHIMERIC SMALL SUBUNITS INFLUENCE CATALYSIS
JRNL TITL 2 WITHOUT CAUSING GLOBAL CONFORMATIONAL CHANGES IN
JRNL TITL 3 THE CRYSTAL STRUCTURE OF RIBULOSE-1,5-BISPHOSPHATE
JRNL TITL 4 CARBOXYLASE/OXYGENASE
JRNL REF BIOCHEMISTRY V. 44 9851 2005
JRNL REFN ISSN 0006-2960
JRNL PMID 16026157
JRNL DOI 10.1021/BI050537V
REMARK 2
REMARK 2 RESOLUTION. 2.4 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.4
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.3
REMARK 3 NUMBER OF REFLECTIONS : 190692
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.1884
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 10097
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 37436
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 728
REMARK 3 SOLVENT ATOMS : 1891
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.921
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.93
REMARK 3 B22 (A**2) : 0.29
REMARK 3 B33 (A**2) : -1.22
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.540
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.264
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.197
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.838
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1UZD COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-MAR-04.
REMARK 100 THE PDBE ID CODE IS EBI-14773.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-AUG-03
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9762
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 215895
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.4
REMARK 200 DATA REDUNDANCY : 29.800
REMARK 200 R MERGE (I) : 0.18500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.90000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1GK8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS:
REMARK 280 50 MM HEPES PH 7.5, 8-12% PEG 4
REMARK 280 50 MM NAHCO3, 5 MM MGCL2, 50 UM 2-CABP, 18 DEG C, 10-15 MG
REMARK 280 PROTEIN
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 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+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 110.00700
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 112.03900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 110.00700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 112.03900
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 300
REMARK 300 DETAILS:FOR THE HETERO-ASSEMBLY DESCRIBED BY REMARK
REMARK 300 350
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 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXADECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXADECAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, H, K, O, R, V, I,
REMARK 350 AND CHAINS: C, F, J, P, T, M, W
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 400
REMARK 400 COMPOUND
REMARK 400 RUBISCO CATALYZES TWO REACTIONS: THE CARBOXYLATION OF D-
REMARK 400 RIBULOSE 1,5-BISPHOSPHATE, THE PRIMARY EVENT IN
REMARK 400 PHOTOSYNTHETIC CARBON DIOXIDE FIXATION, AS WELL AS THE
REMARK 400 OXIDATIVE FRAGMENTATION OF THE PENTOSE SUBSTRATE IN THE
REMARK 400 PHOTORESPIRATION PROCESS. BOTH REACTIONS OCCUR SIMULTANEOUSLY
REMARK 400 AND IN COMPETITION AT THE SAME ACTIVE SITE.
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 1
REMARK 465 VAL A 2
REMARK 465 PRO A 3
REMARK 465 GLN A 4
REMARK 465 THR A 5
REMARK 465 GLU A 6
REMARK 465 THR A 7
REMARK 465 LYS A 8
REMARK 465 ALA A 9
REMARK 465 GLY A 10
REMARK 465 MET B 1
REMARK 465 VAL B 2
REMARK 465 PRO B 3
REMARK 465 GLN B 4
REMARK 465 THR B 5
REMARK 465 GLU B 6
REMARK 465 THR B 7
REMARK 465 LYS B 8
REMARK 465 THR C 122
REMARK 465 ALA C 123
REMARK 465 ARG C 124
REMARK 465 ASP C 125
REMARK 465 PHE C 126
REMARK 465 MET E 1
REMARK 465 VAL E 2
REMARK 465 PRO E 3
REMARK 465 GLN E 4
REMARK 465 THR E 5
REMARK 465 GLU E 6
REMARK 465 THR E 7
REMARK 465 LYS E 8
REMARK 465 ALA E 9
REMARK 465 GLY E 10
REMARK 465 THR F 122
REMARK 465 ALA F 123
REMARK 465 ARG F 124
REMARK 465 ASP F 125
REMARK 465 PHE F 126
REMARK 465 MET H 1
REMARK 465 VAL H 2
REMARK 465 PRO H 3
REMARK 465 GLN H 4
REMARK 465 THR H 5
REMARK 465 GLU H 6
REMARK 465 THR I 122
REMARK 465 ALA I 123
REMARK 465 ARG I 124
REMARK 465 ASP I 125
REMARK 465 PHE I 126
REMARK 465 THR J 122
REMARK 465 ALA J 123
REMARK 465 ARG J 124
REMARK 465 ASP J 125
REMARK 465 PHE J 126
REMARK 465 MET K 1
REMARK 465 VAL K 2
REMARK 465 PRO K 3
REMARK 465 GLN K 4
REMARK 465 THR K 5
REMARK 465 GLU K 6
REMARK 465 THR M 122
REMARK 465 ALA M 123
REMARK 465 ARG M 124
REMARK 465 ASP M 125
REMARK 465 PHE M 126
REMARK 465 MET O 1
REMARK 465 VAL O 2
REMARK 465 PRO O 3
REMARK 465 GLN O 4
REMARK 465 THR O 5
REMARK 465 GLU O 6
REMARK 465 THR P 122
REMARK 465 ALA P 123
REMARK 465 ARG P 124
REMARK 465 ASP P 125
REMARK 465 PHE P 126
REMARK 465 MET R 1
REMARK 465 VAL R 2
REMARK 465 PRO R 3
REMARK 465 GLN R 4
REMARK 465 THR R 5
REMARK 465 GLU R 6
REMARK 465 THR R 7
REMARK 465 LYS R 8
REMARK 465 ALA R 9
REMARK 465 GLY R 10
REMARK 465 THR T 122
REMARK 465 ALA T 123
REMARK 465 ARG T 124
REMARK 465 ASP T 125
REMARK 465 PHE T 126
REMARK 465 MET V 1
REMARK 465 VAL V 2
REMARK 465 PRO V 3
REMARK 465 GLN V 4
REMARK 465 THR V 5
REMARK 465 GLU V 6
REMARK 465 THR V 7
REMARK 465 LYS V 8
REMARK 465 ALA V 9
REMARK 465 THR W 122
REMARK 465 ALA W 123
REMARK 465 ARG W 124
REMARK 465 ASP W 125
REMARK 465 PHE W 126
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O2P CAP H 1477 - O HOH H 2162 2.13
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 ASP A 324 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP A 351 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASN C 8 N - CA - C ANGL. DEV. = -16.4 DEGREES
REMARK 500 ASP C 63 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP E 33 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP E 160 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP E 351 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP H 286 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASN M 8 N - CA - C ANGL. DEV. = -16.7 DEGREES
REMARK 500 ASP M 47 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP O 160 CB - CG - OD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ASP R 86 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP R 160 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP R 202 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP R 286 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASN T 8 N - CA - C ANGL. DEV. = -16.9 DEGREES
REMARK 500 ASP V 86 CB - CG - OD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500 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 SER A 62 -78.15 -137.51
REMARK 500 THR A 65 -166.28 -129.29
REMARK 500 CYS A 172 130.18 -171.09
REMARK 500 ASN A 207 -87.70 -121.04
REMARK 500 MET A 212 113.86 -161.06
REMARK 500 MET A 297 -10.86 88.54
REMARK 500 VAL A 331 -52.27 73.29
REMARK 500 ASP A 357 88.90 -161.53
REMARK 500 SER B 62 -78.88 -138.48
REMARK 500 THR B 65 -166.85 -123.39
REMARK 500 CYS B 172 128.56 -171.79
REMARK 500 ASN B 207 -88.83 -119.81
REMARK 500 MET B 212 107.91 -163.44
REMARK 500 ALA B 296 133.71 -39.93
REMARK 500 MET B 297 -11.14 90.41
REMARK 500 VAL B 331 -51.88 71.52
REMARK 500 ASP B 357 91.85 -161.15
REMARK 500 PHE C 12 44.81 -140.50
REMARK 500 GLU C 13 -142.13 59.87
REMARK 500 PHE C 15 -3.48 84.03
REMARK 500 ASP C 47 -122.91 -121.76
REMARK 500 LYS C 71 -122.34 56.54
REMARK 500 GLN C 109 71.74 44.32
REMARK 500 PRO C 128 144.87 -39.51
REMARK 500 SER E 62 -82.56 -141.86
REMARK 500 CYS E 172 127.45 -173.03
REMARK 500 ASN E 207 -85.34 -121.63
REMARK 500 MET E 212 110.85 -162.62
REMARK 500 ALA E 296 135.84 -39.49
REMARK 500 MET E 297 -10.73 85.97
REMARK 500 VAL E 331 -52.51 71.67
REMARK 500 ASP E 357 92.19 -162.57
REMARK 500 ASN F 8 84.57 -13.63
REMARK 500 GLU F 13 -139.36 61.92
REMARK 500 PHE F 15 -6.60 88.79
REMARK 500 ASP F 47 -125.16 -121.25
REMARK 500 LYS F 71 -118.06 57.45
REMARK 500 SER H 62 -76.43 -138.27
REMARK 500 THR H 65 -169.70 -126.69
REMARK 500 THR H 75 -167.87 -129.77
REMARK 500 CYS H 172 127.89 -173.12
REMARK 500 ASN H 207 -88.53 -120.99
REMARK 500 MET H 297 -8.88 93.21
REMARK 500 VAL H 331 -48.88 68.93
REMARK 500 ASP H 357 94.59 -161.81
REMARK 500 ASN I 8 90.56 -36.25
REMARK 500 GLU I 13 -140.17 62.47
REMARK 500 PHE I 15 -0.77 80.92
REMARK 500 ASP I 47 -123.23 -119.47
REMARK 500 LYS I 71 -118.84 60.91
REMARK 500 PRO I 128 143.57 -39.93
REMARK 500 GLU J 13 -143.90 59.44
REMARK 500 PHE J 15 -3.98 85.60
REMARK 500 ASP J 47 -124.94 -119.37
REMARK 500 LYS J 71 -123.92 60.60
REMARK 500 GLN J 109 70.82 43.77
REMARK 500 SER K 62 -77.64 -140.14
REMARK 500 THR K 65 -169.81 -125.52
REMARK 500 CYS K 172 127.54 -174.43
REMARK 500 ASN K 207 -88.28 -120.71
REMARK 500 MET K 212 111.44 -164.33
REMARK 500 MET K 297 -10.23 90.35
REMARK 500 VAL K 331 -52.73 72.94
REMARK 500 LYS K 356 130.43 -39.57
REMARK 500 ASP K 357 93.44 -161.44
REMARK 500 GLU M 13 -142.05 60.67
REMARK 500 PHE M 15 -1.67 81.39
REMARK 500 ASP M 47 -124.66 -118.24
REMARK 500 LYS M 71 -122.08 62.23
REMARK 500 SER O 62 -78.53 -142.60
REMARK 500 THR O 65 -167.91 -122.54
REMARK 500 CYS O 172 126.51 -173.18
REMARK 500 ASN O 207 -90.12 -124.22
REMARK 500 MET O 212 109.19 -162.74
REMARK 500 ALA O 296 128.76 -34.95
REMARK 500 MET O 297 -6.96 90.55
REMARK 500 VAL O 331 -50.49 76.06
REMARK 500 ASP O 357 92.34 -161.21
REMARK 500 PHE P 12 43.19 -140.61
REMARK 500 GLU P 13 -140.90 62.33
REMARK 500 PHE P 15 -2.97 87.06
REMARK 500 ASP P 47 -121.99 -120.80
REMARK 500 LYS P 71 -118.24 59.79
REMARK 500 SER R 62 -77.61 -136.01
REMARK 500 THR R 65 -167.36 -125.60
REMARK 500 THR R 75 -168.75 -125.74
REMARK 500 CYS R 172 128.38 -174.00
REMARK 500 ASN R 207 -88.49 -122.38
REMARK 500 MET R 212 109.02 -161.42
REMARK 500 ALA R 296 131.27 -39.53
REMARK 500 MET R 297 -11.23 90.31
REMARK 500 VAL R 331 -50.69 70.41
REMARK 500 ASP R 357 88.99 -158.76
REMARK 500 GLU T 13 -140.96 64.13
REMARK 500 PHE T 15 -1.13 86.39
REMARK 500 ASP T 47 -122.43 -122.31
REMARK 500 LYS T 71 -120.09 60.23
REMARK 500 SER V 62 -79.44 -138.09
REMARK 500 CYS V 172 127.21 -175.34
REMARK 500 ASN V 207 -87.02 -124.38
REMARK 500 MET V 212 110.64 -165.11
REMARK 500 ALA V 296 129.82 -34.29
REMARK 500 MET V 297 -3.29 88.95
REMARK 500 VAL V 331 -52.66 71.90
REMARK 500 ASP V 357 90.16 -160.17
REMARK 500 GLU W 13 -144.94 60.61
REMARK 500 PHE W 15 -4.39 82.35
REMARK 500 ASP W 47 -122.34 -118.37
REMARK 500 LYS W 71 -120.89 59.48
REMARK 500 GLN W 109 73.06 42.65
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 VAL C 7 ASN C 8 -66.97
REMARK 500 VAL F 7 ASN F 8 -143.94
REMARK 500 VAL I 7 ASN I 8 -127.14
REMARK 500 VAL J 7 ASN J 8 -67.88
REMARK 500 VAL M 7 ASN M 8 -65.35
REMARK 500 VAL P 7 ASN P 8 -70.37
REMARK 500 VAL T 7 ASN T 8 -67.22
REMARK 500 VAL W 7 ASN W 8 -68.66
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 PHE O 345 25.0 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1476 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 203 OD1
REMARK 620 2 GLU A 204 OE1 94.5
REMARK 620 3 CAP A1477 O3 170.4 81.0
REMARK 620 4 CAP A1477 O6 104.7 90.4 83.9
REMARK 620 5 CAP A1477 O2 115.6 149.7 69.6 79.5
REMARK 620 6 KCX A 201 OQ2 91.7 90.4 80.0 163.5 91.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B1476 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAP B1477 O2
REMARK 620 2 KCX B 201 OQ2 98.0
REMARK 620 3 ASP B 203 OD1 116.1 88.2
REMARK 620 4 GLU B 204 OE1 151.8 90.8 90.8
REMARK 620 5 CAP B1477 O3 76.1 84.6 166.7 78.2
REMARK 620 6 CAP B1477 O6 81.1 172.0 99.3 86.4 87.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E1476 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAP E1477 O2
REMARK 620 2 CAP E1477 O3 74.4
REMARK 620 3 CAP E1477 O6 76.0 95.7
REMARK 620 4 KCX E 201 OQ2 88.5 77.5 164.3
REMARK 620 5 ASP E 203 OD1 105.4 164.4 99.3 86.9
REMARK 620 6 GLU E 204 OE1 158.3 84.3 102.6 90.9 96.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG H1476 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX H 201 OQ2
REMARK 620 2 ASP H 203 OD1 88.1
REMARK 620 3 CAP H1477 O2 90.0 107.3
REMARK 620 4 CAP H1477 O3 87.0 175.2 72.3
REMARK 620 5 CAP H1477 O6 166.3 96.3 76.3 88.3
REMARK 620 6 GLU H 204 OE1 95.8 92.3 159.7 88.5 97.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG K1476 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU K 204 OE1
REMARK 620 2 CAP K1477 O2 170.7
REMARK 620 3 CAP K1477 O3 94.2 78.5
REMARK 620 4 CAP K1477 O6 100.6 75.1 98.4
REMARK 620 5 KCX K 201 OQ1 108.1 72.9 57.2 142.9
REMARK 620 6 KCX K 201 OQ2 93.8 92.7 96.3 158.5 41.4
REMARK 620 7 ASP K 203 OD1 86.3 101.1 179.2 82.1 122.0 83.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG O1476 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU O 204 OE1
REMARK 620 2 CAP O1477 O3 82.5
REMARK 620 3 KCX O 201 OQ2 87.0 73.8
REMARK 620 4 ASP O 203 OD1 92.4 161.1 87.8
REMARK 620 5 CAP O1477 O2 152.1 69.9 89.0 115.1
REMARK 620 6 CAP O1477 O6 98.8 92.1 164.0 106.7 78.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG R1476 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX R 201 OQ2
REMARK 620 2 ASP R 203 OD1 93.3
REMARK 620 3 GLU R 204 OE1 94.6 94.5
REMARK 620 4 CAP R1477 O2 88.8 104.1 160.8
REMARK 620 5 CAP R1477 O6 163.8 99.9 93.6 79.0
REMARK 620 6 CAP R1477 O3 74.2 167.5 87.3 75.4 92.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG V1476 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP V 203 OD1
REMARK 620 2 CAP V1477 O2 110.6
REMARK 620 3 GLU V 204 OE1 97.6 149.1
REMARK 620 4 CAP V1477 O6 112.0 80.4 101.2
REMARK 620 5 KCX V 201 OQ2 87.0 84.7 84.2 159.0
REMARK 620 6 CAP V1477 O3 159.0 70.6 78.6 88.9 72.1
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG H1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG K1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG O1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG R1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG V1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP A1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1482
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1483
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP B1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1482
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1135
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1136
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP E1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1482
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F1135
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP H1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO I1135
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO J1135
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP K1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO K1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO K1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO K1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO K1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO K1482
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO M1135
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP O1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO O1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO O1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO O1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO O1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO O1482
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO O1483
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO P1135
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP R1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO R1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO R1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO R1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO R1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO R1482
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO R1483
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO R1484
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO T1135
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO T1136
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP V1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO V1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO V1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO V1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO V1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO V1482
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO V1483
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO W1135
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1GK8 RELATED DB: PDB
REMARK 900 RUBISCO FROM CHLAMYDOMONAS REINHARDTII
REMARK 900 RELATED ID: 1IR2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACTIVATED RIBULOSE-1,5
REMARK 900 -BISPHOSPHATECARBOXYLASE/OXYGENASE (RUBISCO) FROM
REMARK 900 GREEN ALGA,CHLAMYDOMONAS REINHARDTII COMPLEXED
REMARK 900 WITH 2-CARBOXYARABINITOL-1,5-BISPHOSPHATE
REMARK 900 (2-CABP)
REMARK 900 RELATED ID: 1UW9 RELATED DB: PDB
REMARK 900 L290F-A222T CHLAMYDOMONAS RUBISCO MUTANT
REMARK 900 RELATED ID: 1UWA RELATED DB: PDB
REMARK 900 L290F MUTANT RUBISCO FROM CHLAMYDOMONAS
REMARK 900 RELATED ID: 1UZH RELATED DB: PDB
REMARK 900 A CHIMERIC CHLAMYDOMONAS, SPINACH RUBISCO
REMARK 900 ENZYME
REMARK 900 RELATED ID: 1AA1 RELATED DB: PDB
REMARK 900 ACTIVATED SPINACH RUBISCO IN COMPLEX WITH
REMARK 900 THE PRODUCT 3-PHOSPHOGLYCERATE
REMARK 900 RELATED ID: 1AUS RELATED DB: PDB
REMARK 900 ACTIVATED UNLIGANDED SPINACH RUBISCO
REMARK 900 RELATED ID: 1IR1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF SPINACH RIBULOSE-1,5-
REMARK 900 BISPHOSPHATECARBOXYLASE/OXYGENASE (RUBISCO)
REMARK 900 COMPLEXED WITH CO2, MG2+AND 2-
REMARK 900 CARBOXYARABINITOL-1,5-BISPHOSPHATE
REMARK 900 RELATED ID: 1UPM RELATED DB: PDB
REMARK 900 ACTIVATED SPINACH RUBISCO COMPLEXED WITH 2-
REMARK 900 CARBOXYARABINITOL 2 BISPHOSPHAT AND CA2+.
REMARK 900 RELATED ID: 1UPP RELATED DB: PDB
REMARK 900 SPINACH RUBISCO IN COMPLEX WITH 2-
REMARK 900 CARBOXYARABINITOL 2 BISPHOSPHATE AND CALCIUM.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SMALL SUBUNIT LOOP BA-BB OF CHLAMYDOMONAS RUBISCO,
REMARK 999 (RESIDUES 46 - 70 ;EADKAYVSNESAIRFGSVSCLYYDN) IS 6 RESIDUES
REMARK 999 LONGER THAN THE CORRESPONDING LOOP OF SPINACH RUBISCO
REMARK 999 ( RESIDUES 46 - 64; TDHGFVYREHHNSPGYYDG. THE REPLACEMENT OF
REMARK 999 CHLMYDOMONAS RUBISCO LOOP WITH SPINACH
REMARK 999 RUBISCO LOOP AFFECTS THE NUMBERING OF THE SMALL SUBUNIT.
DBREF 1UZD A 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 1UZD B 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 1UZD E 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 1UZD H 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 1UZD K 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 1UZD O 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 1UZD R 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 1UZD V 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 1UZD I 1 45 UNP P00873 RBS1_CHLRE 46 90
DBREF 1UZD I 46 64 UNP Q43832 RBS2_SPIOL 103 121
DBREF 1UZD I 65 134 UNP P00873 RBS1_CHLRE 116 185
DBREF 1UZD C 1 45 UNP P00873 RBS1_CHLRE 46 90
DBREF 1UZD C 46 64 UNP Q43832 RBS2_SPIOL 103 121
DBREF 1UZD C 65 134 UNP P00873 RBS1_CHLRE 116 185
DBREF 1UZD F 1 45 UNP P00873 RBS1_CHLRE 46 90
DBREF 1UZD F 46 64 UNP Q43832 RBS2_SPIOL 103 121
DBREF 1UZD F 65 134 UNP P00873 RBS1_CHLRE 116 185
DBREF 1UZD J 1 45 UNP P00873 RBS1_CHLRE 46 90
DBREF 1UZD J 46 64 UNP Q43832 RBS2_SPIOL 103 121
DBREF 1UZD J 65 134 UNP P00873 RBS1_CHLRE 116 185
DBREF 1UZD P 1 45 UNP P00873 RBS1_CHLRE 46 90
DBREF 1UZD P 46 64 UNP Q43832 RBS2_SPIOL 103 121
DBREF 1UZD P 65 134 UNP P00873 RBS1_CHLRE 116 185
DBREF 1UZD T 1 45 UNP P00873 RBS1_CHLRE 46 90
DBREF 1UZD T 46 64 UNP Q43832 RBS2_SPIOL 103 121
DBREF 1UZD T 65 134 UNP P00873 RBS1_CHLRE 116 185
DBREF 1UZD M 1 45 UNP P00873 RBS1_CHLRE 46 90
DBREF 1UZD M 46 64 UNP Q43832 RBS2_SPIOL 103 121
DBREF 1UZD M 65 134 UNP P00873 RBS1_CHLRE 116 185
DBREF 1UZD W 1 45 UNP P00873 RBS1_CHLRE 46 90
DBREF 1UZD W 46 64 UNP Q43832 RBS2_SPIOL 103 121
DBREF 1UZD W 65 134 UNP P00873 RBS1_CHLRE 116 185
SEQADV 1UZD PRO A 46 UNP P00877 LEU 46 CONFLICT
SEQADV 1UZD PRO B 46 UNP P00877 LEU 46 CONFLICT
SEQADV 1UZD PRO E 46 UNP P00877 LEU 46 CONFLICT
SEQADV 1UZD PRO H 46 UNP P00877 LEU 46 CONFLICT
SEQADV 1UZD PRO K 46 UNP P00877 LEU 46 CONFLICT
SEQADV 1UZD PRO O 46 UNP P00877 LEU 46 CONFLICT
SEQADV 1UZD PRO R 46 UNP P00877 LEU 46 CONFLICT
SEQADV 1UZD PRO V 46 UNP P00877 LEU 46 CONFLICT
SEQRES 1 A 475 MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES 2 A 475 LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES 3 A 475 PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES 4 A 475 PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES 5 A 475 CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES 6 A 475 TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES 7 A 475 ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES 8 A 475 GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES 9 A 475 ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES 10 A 475 THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES 11 A 475 ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES 12 A 475 TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES 13 A 475 VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES 14 A 475 LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES 15 A 475 LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES 16 A 475 GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES 17 A 475 GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES 18 A 475 ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES 19 A 475 VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES 20 A 475 GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES 21 A 475 GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES 22 A 475 PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES 23 A 475 ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES 24 A 475 VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES 25 A 475 VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES 26 A 475 LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES 27 A 475 ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES 28 A 475 ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES 29 A 475 THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES 30 A 475 ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES 31 A 475 VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES 32 A 475 GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES 33 A 475 ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES 34 A 475 ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES 35 A 475 ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES 36 A 475 ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES 37 A 475 PHE ASP THR ILE ASP LYS LEU
SEQRES 1 B 475 MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES 2 B 475 LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES 3 B 475 PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES 4 B 475 PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES 5 B 475 CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES 6 B 475 TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES 7 B 475 ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES 8 B 475 GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES 9 B 475 ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES 10 B 475 THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES 11 B 475 ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES 12 B 475 TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES 13 B 475 VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES 14 B 475 LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES 15 B 475 LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES 16 B 475 GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES 17 B 475 GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES 18 B 475 ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES 19 B 475 VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES 20 B 475 GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES 21 B 475 GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES 22 B 475 PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES 23 B 475 ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES 24 B 475 VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES 25 B 475 VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES 26 B 475 LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES 27 B 475 ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES 28 B 475 ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES 29 B 475 THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES 30 B 475 ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES 31 B 475 VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES 32 B 475 GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES 33 B 475 ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES 34 B 475 ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES 35 B 475 ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES 36 B 475 ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES 37 B 475 PHE ASP THR ILE ASP LYS LEU
SEQRES 1 C 134 MET MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES 2 C 134 THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES 3 C 134 ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES 4 C 134 PRO CYS LEU GLU PHE ALA THR ASP HIS GLY PHE VAL TYR
SEQRES 5 C 134 ARG GLU HIS HIS ASN SER PRO GLY TYR TYR ASP GLY ARG
SEQRES 6 C 134 TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS ARG
SEQRES 7 C 134 ASP PRO MET GLN VAL LEU ARG GLU ILE VAL ALA CYS THR
SEQRES 8 C 134 LYS ALA PHE PRO ASP ALA TYR VAL ARG LEU VAL ALA PHE
SEQRES 9 C 134 ASP ASN GLN LYS GLN VAL GLN ILE MET GLY PHE LEU VAL
SEQRES 10 C 134 GLN ARG PRO LYS THR ALA ARG ASP PHE GLN PRO ALA ASN
SEQRES 11 C 134 LYS ARG SER VAL
SEQRES 1 E 475 MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES 2 E 475 LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES 3 E 475 PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES 4 E 475 PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES 5 E 475 CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES 6 E 475 TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES 7 E 475 ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES 8 E 475 GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES 9 E 475 ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES 10 E 475 THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES 11 E 475 ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES 12 E 475 TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES 13 E 475 VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES 14 E 475 LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES 15 E 475 LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES 16 E 475 GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES 17 E 475 GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES 18 E 475 ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES 19 E 475 VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES 20 E 475 GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES 21 E 475 GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES 22 E 475 PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES 23 E 475 ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES 24 E 475 VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES 25 E 475 VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES 26 E 475 LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES 27 E 475 ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES 28 E 475 ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES 29 E 475 THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES 30 E 475 ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES 31 E 475 VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES 32 E 475 GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES 33 E 475 ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES 34 E 475 ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES 35 E 475 ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES 36 E 475 ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES 37 E 475 PHE ASP THR ILE ASP LYS LEU
SEQRES 1 F 134 MET MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES 2 F 134 THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES 3 F 134 ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES 4 F 134 PRO CYS LEU GLU PHE ALA THR ASP HIS GLY PHE VAL TYR
SEQRES 5 F 134 ARG GLU HIS HIS ASN SER PRO GLY TYR TYR ASP GLY ARG
SEQRES 6 F 134 TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS ARG
SEQRES 7 F 134 ASP PRO MET GLN VAL LEU ARG GLU ILE VAL ALA CYS THR
SEQRES 8 F 134 LYS ALA PHE PRO ASP ALA TYR VAL ARG LEU VAL ALA PHE
SEQRES 9 F 134 ASP ASN GLN LYS GLN VAL GLN ILE MET GLY PHE LEU VAL
SEQRES 10 F 134 GLN ARG PRO LYS THR ALA ARG ASP PHE GLN PRO ALA ASN
SEQRES 11 F 134 LYS ARG SER VAL
SEQRES 1 H 475 MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES 2 H 475 LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES 3 H 475 PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES 4 H 475 PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES 5 H 475 CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES 6 H 475 TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES 7 H 475 ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES 8 H 475 GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES 9 H 475 ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES 10 H 475 THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES 11 H 475 ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES 12 H 475 TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES 13 H 475 VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES 14 H 475 LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES 15 H 475 LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES 16 H 475 GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES 17 H 475 GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES 18 H 475 ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES 19 H 475 VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES 20 H 475 GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES 21 H 475 GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES 22 H 475 PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES 23 H 475 ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES 24 H 475 VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES 25 H 475 VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES 26 H 475 LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES 27 H 475 ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES 28 H 475 ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES 29 H 475 THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES 30 H 475 ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES 31 H 475 VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES 32 H 475 GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES 33 H 475 ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES 34 H 475 ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES 35 H 475 ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES 36 H 475 ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES 37 H 475 PHE ASP THR ILE ASP LYS LEU
SEQRES 1 I 134 MET MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES 2 I 134 THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES 3 I 134 ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES 4 I 134 PRO CYS LEU GLU PHE ALA THR ASP HIS GLY PHE VAL TYR
SEQRES 5 I 134 ARG GLU HIS HIS ASN SER PRO GLY TYR TYR ASP GLY ARG
SEQRES 6 I 134 TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS ARG
SEQRES 7 I 134 ASP PRO MET GLN VAL LEU ARG GLU ILE VAL ALA CYS THR
SEQRES 8 I 134 LYS ALA PHE PRO ASP ALA TYR VAL ARG LEU VAL ALA PHE
SEQRES 9 I 134 ASP ASN GLN LYS GLN VAL GLN ILE MET GLY PHE LEU VAL
SEQRES 10 I 134 GLN ARG PRO LYS THR ALA ARG ASP PHE GLN PRO ALA ASN
SEQRES 11 I 134 LYS ARG SER VAL
SEQRES 1 J 134 MET MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES 2 J 134 THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES 3 J 134 ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES 4 J 134 PRO CYS LEU GLU PHE ALA THR ASP HIS GLY PHE VAL TYR
SEQRES 5 J 134 ARG GLU HIS HIS ASN SER PRO GLY TYR TYR ASP GLY ARG
SEQRES 6 J 134 TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS ARG
SEQRES 7 J 134 ASP PRO MET GLN VAL LEU ARG GLU ILE VAL ALA CYS THR
SEQRES 8 J 134 LYS ALA PHE PRO ASP ALA TYR VAL ARG LEU VAL ALA PHE
SEQRES 9 J 134 ASP ASN GLN LYS GLN VAL GLN ILE MET GLY PHE LEU VAL
SEQRES 10 J 134 GLN ARG PRO LYS THR ALA ARG ASP PHE GLN PRO ALA ASN
SEQRES 11 J 134 LYS ARG SER VAL
SEQRES 1 K 475 MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES 2 K 475 LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES 3 K 475 PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES 4 K 475 PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES 5 K 475 CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES 6 K 475 TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES 7 K 475 ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES 8 K 475 GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES 9 K 475 ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES 10 K 475 THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES 11 K 475 ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES 12 K 475 TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES 13 K 475 VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES 14 K 475 LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES 15 K 475 LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES 16 K 475 GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES 17 K 475 GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES 18 K 475 ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES 19 K 475 VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES 20 K 475 GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES 21 K 475 GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES 22 K 475 PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES 23 K 475 ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES 24 K 475 VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES 25 K 475 VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES 26 K 475 LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES 27 K 475 ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES 28 K 475 ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES 29 K 475 THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES 30 K 475 ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES 31 K 475 VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES 32 K 475 GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES 33 K 475 ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES 34 K 475 ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES 35 K 475 ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES 36 K 475 ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES 37 K 475 PHE ASP THR ILE ASP LYS LEU
SEQRES 1 M 134 MET MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES 2 M 134 THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES 3 M 134 ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES 4 M 134 PRO CYS LEU GLU PHE ALA THR ASP HIS GLY PHE VAL TYR
SEQRES 5 M 134 ARG GLU HIS HIS ASN SER PRO GLY TYR TYR ASP GLY ARG
SEQRES 6 M 134 TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS ARG
SEQRES 7 M 134 ASP PRO MET GLN VAL LEU ARG GLU ILE VAL ALA CYS THR
SEQRES 8 M 134 LYS ALA PHE PRO ASP ALA TYR VAL ARG LEU VAL ALA PHE
SEQRES 9 M 134 ASP ASN GLN LYS GLN VAL GLN ILE MET GLY PHE LEU VAL
SEQRES 10 M 134 GLN ARG PRO LYS THR ALA ARG ASP PHE GLN PRO ALA ASN
SEQRES 11 M 134 LYS ARG SER VAL
SEQRES 1 O 475 MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES 2 O 475 LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES 3 O 475 PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES 4 O 475 PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES 5 O 475 CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES 6 O 475 TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES 7 O 475 ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES 8 O 475 GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES 9 O 475 ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES 10 O 475 THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES 11 O 475 ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES 12 O 475 TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES 13 O 475 VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES 14 O 475 LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES 15 O 475 LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES 16 O 475 GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES 17 O 475 GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES 18 O 475 ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES 19 O 475 VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES 20 O 475 GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES 21 O 475 GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES 22 O 475 PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES 23 O 475 ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES 24 O 475 VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES 25 O 475 VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES 26 O 475 LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES 27 O 475 ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES 28 O 475 ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES 29 O 475 THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES 30 O 475 ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES 31 O 475 VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES 32 O 475 GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES 33 O 475 ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES 34 O 475 ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES 35 O 475 ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES 36 O 475 ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES 37 O 475 PHE ASP THR ILE ASP LYS LEU
SEQRES 1 P 134 MET MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES 2 P 134 THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES 3 P 134 ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES 4 P 134 PRO CYS LEU GLU PHE ALA THR ASP HIS GLY PHE VAL TYR
SEQRES 5 P 134 ARG GLU HIS HIS ASN SER PRO GLY TYR TYR ASP GLY ARG
SEQRES 6 P 134 TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS ARG
SEQRES 7 P 134 ASP PRO MET GLN VAL LEU ARG GLU ILE VAL ALA CYS THR
SEQRES 8 P 134 LYS ALA PHE PRO ASP ALA TYR VAL ARG LEU VAL ALA PHE
SEQRES 9 P 134 ASP ASN GLN LYS GLN VAL GLN ILE MET GLY PHE LEU VAL
SEQRES 10 P 134 GLN ARG PRO LYS THR ALA ARG ASP PHE GLN PRO ALA ASN
SEQRES 11 P 134 LYS ARG SER VAL
SEQRES 1 R 475 MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES 2 R 475 LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES 3 R 475 PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES 4 R 475 PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES 5 R 475 CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES 6 R 475 TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES 7 R 475 ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES 8 R 475 GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES 9 R 475 ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES 10 R 475 THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES 11 R 475 ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES 12 R 475 TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES 13 R 475 VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES 14 R 475 LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES 15 R 475 LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES 16 R 475 GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES 17 R 475 GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES 18 R 475 ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES 19 R 475 VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES 20 R 475 GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES 21 R 475 GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES 22 R 475 PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES 23 R 475 ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES 24 R 475 VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES 25 R 475 VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES 26 R 475 LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES 27 R 475 ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES 28 R 475 ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES 29 R 475 THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES 30 R 475 ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES 31 R 475 VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES 32 R 475 GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES 33 R 475 ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES 34 R 475 ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES 35 R 475 ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES 36 R 475 ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES 37 R 475 PHE ASP THR ILE ASP LYS LEU
SEQRES 1 T 134 MET MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES 2 T 134 THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES 3 T 134 ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES 4 T 134 PRO CYS LEU GLU PHE ALA THR ASP HIS GLY PHE VAL TYR
SEQRES 5 T 134 ARG GLU HIS HIS ASN SER PRO GLY TYR TYR ASP GLY ARG
SEQRES 6 T 134 TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS ARG
SEQRES 7 T 134 ASP PRO MET GLN VAL LEU ARG GLU ILE VAL ALA CYS THR
SEQRES 8 T 134 LYS ALA PHE PRO ASP ALA TYR VAL ARG LEU VAL ALA PHE
SEQRES 9 T 134 ASP ASN GLN LYS GLN VAL GLN ILE MET GLY PHE LEU VAL
SEQRES 10 T 134 GLN ARG PRO LYS THR ALA ARG ASP PHE GLN PRO ALA ASN
SEQRES 11 T 134 LYS ARG SER VAL
SEQRES 1 V 475 MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES 2 V 475 LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES 3 V 475 PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES 4 V 475 PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES 5 V 475 CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES 6 V 475 TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES 7 V 475 ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES 8 V 475 GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES 9 V 475 ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES 10 V 475 THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES 11 V 475 ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES 12 V 475 TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES 13 V 475 VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES 14 V 475 LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES 15 V 475 LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES 16 V 475 GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES 17 V 475 GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES 18 V 475 ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES 19 V 475 VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES 20 V 475 GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES 21 V 475 GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES 22 V 475 PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES 23 V 475 ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES 24 V 475 VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES 25 V 475 VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES 26 V 475 LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES 27 V 475 ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES 28 V 475 ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES 29 V 475 THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES 30 V 475 ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES 31 V 475 VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES 32 V 475 GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES 33 V 475 ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES 34 V 475 ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES 35 V 475 ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES 36 V 475 ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES 37 V 475 PHE ASP THR ILE ASP LYS LEU
SEQRES 1 W 134 MET MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES 2 W 134 THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES 3 W 134 ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES 4 W 134 PRO CYS LEU GLU PHE ALA THR ASP HIS GLY PHE VAL TYR
SEQRES 5 W 134 ARG GLU HIS HIS ASN SER PRO GLY TYR TYR ASP GLY ARG
SEQRES 6 W 134 TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS ARG
SEQRES 7 W 134 ASP PRO MET GLN VAL LEU ARG GLU ILE VAL ALA CYS THR
SEQRES 8 W 134 LYS ALA PHE PRO ASP ALA TYR VAL ARG LEU VAL ALA PHE
SEQRES 9 W 134 ASP ASN GLN LYS GLN VAL GLN ILE MET GLY PHE LEU VAL
SEQRES 10 W 134 GLN ARG PRO LYS THR ALA ARG ASP PHE GLN PRO ALA ASN
SEQRES 11 W 134 LYS ARG SER VAL
MODRES 1UZD HYP A 104 PRO 4-HYDROXYPROLINE
MODRES 1UZD HYP A 151 PRO 4-HYDROXYPROLINE
MODRES 1UZD HYP B 104 PRO 4-HYDROXYPROLINE
MODRES 1UZD HYP B 151 PRO 4-HYDROXYPROLINE
MODRES 1UZD HYP E 104 PRO 4-HYDROXYPROLINE
MODRES 1UZD HYP E 151 PRO 4-HYDROXYPROLINE
MODRES 1UZD HYP H 104 PRO 4-HYDROXYPROLINE
MODRES 1UZD HYP H 151 PRO 4-HYDROXYPROLINE
MODRES 1UZD HYP K 104 PRO 4-HYDROXYPROLINE
MODRES 1UZD HYP K 151 PRO 4-HYDROXYPROLINE
MODRES 1UZD HYP O 104 PRO 4-HYDROXYPROLINE
MODRES 1UZD HYP O 151 PRO 4-HYDROXYPROLINE
MODRES 1UZD HYP R 104 PRO 4-HYDROXYPROLINE
MODRES 1UZD HYP R 151 PRO 4-HYDROXYPROLINE
MODRES 1UZD HYP V 104 PRO 4-HYDROXYPROLINE
MODRES 1UZD HYP V 151 PRO 4-HYDROXYPROLINE
MODRES 1UZD KCX A 201 LYS LYSINE NZ- CARBOXYLIC ACID
MODRES 1UZD KCX B 201 LYS LYSINE NZ- CARBOXYLIC ACID
MODRES 1UZD KCX E 201 LYS LYSINE NZ- CARBOXYLIC ACID
MODRES 1UZD KCX H 201 LYS LYSINE NZ- CARBOXYLIC ACID
MODRES 1UZD KCX K 201 LYS LYSINE NZ- CARBOXYLIC ACID
MODRES 1UZD KCX O 201 LYS LYSINE NZ- CARBOXYLIC ACID
MODRES 1UZD KCX R 201 LYS LYSINE NZ- CARBOXYLIC ACID
MODRES 1UZD KCX V 201 LYS LYSINE NZ- CARBOXYLIC ACID
MODRES 1UZD SMC A 256 CYS S- METHYLCYSTEINE
MODRES 1UZD SMC A 369 CYS S- METHYLCYSTEINE
MODRES 1UZD SMC B 256 CYS S- METHYLCYSTEINE
MODRES 1UZD SMC B 369 CYS S- METHYLCYSTEINE
MODRES 1UZD SMC E 256 CYS S- METHYLCYSTEINE
MODRES 1UZD SMC E 369 CYS S- METHYLCYSTEINE
MODRES 1UZD SMC H 256 CYS S- METHYLCYSTEINE
MODRES 1UZD SMC H 369 CYS S- METHYLCYSTEINE
MODRES 1UZD SMC K 256 CYS S- METHYLCYSTEINE
MODRES 1UZD SMC K 369 CYS S- METHYLCYSTEINE
MODRES 1UZD SMC O 256 CYS S- METHYLCYSTEINE
MODRES 1UZD SMC O 369 CYS S- METHYLCYSTEINE
MODRES 1UZD SMC R 256 CYS S- METHYLCYSTEINE
MODRES 1UZD SMC R 369 CYS S- METHYLCYSTEINE
MODRES 1UZD SMC V 256 CYS S- METHYLCYSTEINE
MODRES 1UZD SMC V 369 CYS S- METHYLCYSTEINE
HET HYP A 104 8
HET HYP A 151 8
HET KCX A 201 12
HET SMC A 256 7
HET SMC A 369 7
HET HYP B 104 8
HET HYP B 151 8
HET KCX B 201 12
HET SMC B 256 7
HET SMC B 369 7
HET HYP E 104 8
HET HYP E 151 8
HET KCX E 201 12
HET SMC E 256 7
HET SMC E 369 7
HET HYP H 104 8
HET HYP H 151 8
HET KCX H 201 12
HET SMC H 256 7
HET SMC H 369 7
HET HYP K 104 8
HET HYP K 151 8
HET KCX K 201 12
HET SMC K 256 7
HET SMC K 369 7
HET HYP O 104 8
HET HYP O 151 8
HET KCX O 201 12
HET SMC O 256 7
HET SMC O 369 7
HET HYP R 104 8
HET HYP R 151 8
HET KCX R 201 12
HET SMC R 256 7
HET SMC R 369 7
HET HYP V 104 8
HET HYP V 151 8
HET KCX V 201 12
HET SMC V 256 7
HET SMC V 369 7
HET MG A1476 1
HET MG B1476 1
HET MG E1476 1
HET MG H1476 1
HET MG K1476 1
HET MG O1476 1
HET MG R1476 1
HET MG V1476 1
HET CAP A1477 21
HET EDO A1478 4
HET EDO A1479 4
HET EDO A1480 4
HET EDO A1481 4
HET EDO A1482 4
HET EDO A1483 4
HET CAP B1477 21
HET EDO B1478 4
HET EDO B1479 4
HET EDO B1480 4
HET EDO B1481 4
HET EDO B1482 4
HET EDO C1135 4
HET EDO C1136 4
HET CAP E1477 21
HET EDO E1478 4
HET EDO E1479 4
HET EDO E1480 4
HET EDO E1481 4
HET EDO E1482 4
HET EDO F1135 4
HET CAP H1477 21
HET EDO H1478 4
HET EDO H1479 4
HET EDO H1480 4
HET EDO H1481 4
HET EDO I1135 4
HET EDO J1135 4
HET CAP K1477 21
HET EDO K1478 4
HET EDO K1479 4
HET EDO K1480 4
HET EDO K1481 4
HET EDO K1482 4
HET EDO M1135 4
HET CAP O1477 21
HET EDO O1478 4
HET EDO O1479 4
HET EDO O1480 4
HET EDO O1481 4
HET EDO O1482 4
HET EDO O1483 4
HET EDO P1135 4
HET CAP R1477 21
HET EDO R1478 4
HET EDO R1479 4
HET EDO R1480 4
HET EDO R1481 4
HET EDO R1482 4
HET EDO R1483 4
HET EDO R1484 4
HET EDO T1135 4
HET EDO T1136 4
HET CAP V1477 21
HET EDO V1478 4
HET EDO V1479 4
HET EDO V1480 4
HET EDO V1481 4
HET EDO V1482 4
HET EDO V1483 4
HET EDO W1135 4
HETNAM HYP 4-HYDROXYPROLINE
HETNAM KCX LYSINE NZ-CARBOXYLIC ACID
HETNAM SMC S-METHYLCYSTEINE
HETNAM MG MAGNESIUM ION
HETNAM CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 HYP 16(C5 H9 N O3)
FORMUL 1 KCX 8(C7 H14 N2 O4)
FORMUL 1 SMC 16(C4 H9 N O2 S)
FORMUL 17 MG 8(MG 2+)
FORMUL 25 CAP 8(C6 H14 O13 P2)
FORMUL 26 EDO 54(C2 H6 O2)
FORMUL 87 HOH *1891(H2 O1)
HELIX 1 1 TYR A 20 TYR A 25 1 6
HELIX 2 2 PRO A 49 SER A 61 1 13
HELIX 3 3 VAL A 69 THR A 75 5 7
HELIX 4 4 SER A 76 LYS A 81 1 6
HELIX 5 5 SER A 112 GLY A 122 1 11
HELIX 6 6 ASN A 123 GLY A 126 5 4
HELIX 7 7 PRO A 141 LYS A 146 1 6
HELIX 8 8 GLY A 154 ASN A 163 1 10
HELIX 9 9 SER A 181 GLY A 195 1 15
HELIX 10 10 ARG A 213 GLY A 233 1 21
HELIX 11 11 THR A 246 VAL A 255 1 10
HELIX 12 12 TYR A 269 GLY A 288 1 20
HELIX 13 13 MET A 297 ARG A 303 1 7
HELIX 14 14 HIS A 310 GLY A 322 1 13
HELIX 15 15 GLU A 338 ASP A 351 1 14
HELIX 16 16 ARG A 358 GLY A 361 5 4
HELIX 17 17 HIS A 383 TRP A 385 5 3
HELIX 18 18 HIS A 386 GLY A 395 1 10
HELIX 19 19 GLY A 403 GLY A 408 1 6
HELIX 20 20 GLY A 412 GLU A 433 1 22
HELIX 21 21 ASP A 436 LYS A 463 1 28
HELIX 22 22 TYR B 20 TYR B 25 1 6
HELIX 23 23 PRO B 49 SER B 61 1 13
HELIX 24 24 VAL B 69 THR B 75 5 7
HELIX 25 25 SER B 76 LYS B 81 1 6
HELIX 26 26 SER B 112 GLY B 122 1 11
HELIX 27 27 ASN B 123 GLY B 126 5 4
HELIX 28 28 PRO B 141 LYS B 146 1 6
HELIX 29 29 GLY B 154 ASN B 163 1 10
HELIX 30 30 SER B 181 GLY B 195 1 15
HELIX 31 31 ARG B 213 GLY B 233 1 21
HELIX 32 32 THR B 246 VAL B 255 1 10
HELIX 33 33 TYR B 269 GLY B 288 1 20
HELIX 34 34 MET B 297 ARG B 303 1 7
HELIX 35 35 HIS B 310 GLY B 322 1 13
HELIX 36 36 GLU B 338 ASP B 351 1 14
HELIX 37 37 ARG B 358 GLY B 361 5 4
HELIX 38 38 HIS B 383 TRP B 385 5 3
HELIX 39 39 HIS B 386 GLY B 395 1 10
HELIX 40 40 GLY B 403 GLY B 408 1 6
HELIX 41 41 GLY B 412 GLU B 433 1 22
HELIX 42 42 ASP B 436 LYS B 463 1 28
HELIX 43 43 THR C 22 GLY C 37 1 16
HELIX 44 44 ASP C 79 PHE C 94 1 16
HELIX 45 45 TYR E 20 TYR E 25 1 6
HELIX 46 46 PRO E 49 SER E 61 1 13
HELIX 47 47 VAL E 69 THR E 75 5 7
HELIX 48 48 SER E 76 LYS E 81 1 6
HELIX 49 49 SER E 112 GLY E 122 1 11
HELIX 50 50 ASN E 123 GLY E 126 5 4
HELIX 51 51 PRO E 141 LYS E 146 1 6
HELIX 52 52 GLY E 154 ASN E 163 1 10
HELIX 53 53 SER E 181 GLY E 195 1 15
HELIX 54 54 ARG E 213 GLY E 233 1 21
HELIX 55 55 THR E 246 VAL E 255 1 10
HELIX 56 56 TYR E 269 GLY E 288 1 20
HELIX 57 57 MET E 297 ARG E 303 1 7
HELIX 58 58 HIS E 310 GLY E 322 1 13
HELIX 59 59 GLU E 338 ASP E 351 1 14
HELIX 60 60 ARG E 358 GLY E 361 5 4
HELIX 61 61 HIS E 383 TRP E 385 5 3
HELIX 62 62 HIS E 386 GLY E 395 1 10
HELIX 63 63 GLY E 403 GLY E 408 1 6
HELIX 64 64 GLY E 412 GLU E 433 1 22
HELIX 65 65 ASP E 436 LYS E 463 1 28
HELIX 66 66 THR F 22 GLY F 37 1 16
HELIX 67 67 ASP F 79 PHE F 94 1 16
HELIX 68 68 TYR H 20 TYR H 25 1 6
HELIX 69 69 PRO H 49 SER H 61 1 13
HELIX 70 70 VAL H 69 THR H 75 5 7
HELIX 71 71 SER H 76 LYS H 81 1 6
HELIX 72 72 SER H 112 VAL H 121 1 10
HELIX 73 73 ASN H 123 GLY H 126 5 4
HELIX 74 74 PRO H 141 LYS H 146 1 6
HELIX 75 75 GLY H 154 ASN H 163 1 10
HELIX 76 76 SER H 181 GLY H 195 1 15
HELIX 77 77 ARG H 213 GLY H 233 1 21
HELIX 78 78 THR H 246 VAL H 255 1 10
HELIX 79 79 TYR H 269 GLY H 288 1 20
HELIX 80 80 MET H 297 ARG H 303 1 7
HELIX 81 81 HIS H 310 GLY H 322 1 13
HELIX 82 82 GLU H 338 ASP H 351 1 14
HELIX 83 83 ARG H 358 GLY H 361 5 4
HELIX 84 84 HIS H 383 TRP H 385 5 3
HELIX 85 85 HIS H 386 GLY H 395 1 10
HELIX 86 86 GLY H 403 GLY H 408 1 6
HELIX 87 87 GLY H 412 GLU H 433 1 22
HELIX 88 88 ASP H 436 LYS H 463 1 28
HELIX 89 89 THR I 22 GLY I 37 1 16
HELIX 90 90 ASP I 79 PHE I 94 1 16
HELIX 91 91 THR J 22 GLY J 37 1 16
HELIX 92 92 ASP J 79 PHE J 94 1 16
HELIX 93 93 TYR K 20 TYR K 25 1 6
HELIX 94 94 PRO K 49 SER K 61 1 13
HELIX 95 95 VAL K 69 THR K 75 5 7
HELIX 96 96 SER K 76 LYS K 81 1 6
HELIX 97 97 SER K 112 GLY K 122 1 11
HELIX 98 98 ASN K 123 GLY K 126 5 4
HELIX 99 99 PRO K 141 LYS K 146 1 6
HELIX 100 100 GLY K 154 ASN K 163 1 10
HELIX 101 101 SER K 181 GLY K 195 1 15
HELIX 102 102 ARG K 213 GLY K 233 1 21
HELIX 103 103 THR K 246 VAL K 255 1 10
HELIX 104 104 TYR K 269 GLY K 288 1 20
HELIX 105 105 MET K 297 ARG K 303 1 7
HELIX 106 106 HIS K 310 GLY K 322 1 13
HELIX 107 107 GLU K 338 ASP K 351 1 14
HELIX 108 108 ARG K 358 GLY K 361 5 4
HELIX 109 109 HIS K 383 TRP K 385 5 3
HELIX 110 110 HIS K 386 GLY K 395 1 10
HELIX 111 111 GLY K 403 GLY K 408 1 6
HELIX 112 112 GLY K 412 GLU K 433 1 22
HELIX 113 113 ASP K 436 LYS K 463 1 28
HELIX 114 114 THR M 22 ASN M 36 1 15
HELIX 115 115 ASP M 79 PHE M 94 1 16
HELIX 116 116 TYR O 20 TYR O 25 1 6
HELIX 117 117 PRO O 49 SER O 61 1 13
HELIX 118 118 VAL O 69 THR O 75 5 7
HELIX 119 119 SER O 76 LYS O 81 1 6
HELIX 120 120 SER O 112 GLY O 122 1 11
HELIX 121 121 ASN O 123 GLY O 126 5 4
HELIX 122 122 PRO O 141 LYS O 146 1 6
HELIX 123 123 GLY O 154 ASN O 163 1 10
HELIX 124 124 SER O 181 GLY O 195 1 15
HELIX 125 125 ARG O 213 GLY O 233 1 21
HELIX 126 126 THR O 246 VAL O 255 1 10
HELIX 127 127 TYR O 269 GLY O 288 1 20
HELIX 128 128 MET O 297 ARG O 303 1 7
HELIX 129 129 HIS O 310 GLY O 322 1 13
HELIX 130 130 GLU O 338 ASP O 351 1 14
HELIX 131 131 ARG O 358 GLY O 361 5 4
HELIX 132 132 HIS O 383 TRP O 385 5 3
HELIX 133 133 HIS O 386 GLY O 395 1 10
HELIX 134 134 GLY O 403 GLY O 408 1 6
HELIX 135 135 GLY O 412 GLU O 433 1 22
HELIX 136 136 ASP O 436 LYS O 463 1 28
HELIX 137 137 THR P 22 GLY P 37 1 16
HELIX 138 138 ASP P 79 PHE P 94 1 16
HELIX 139 139 TYR R 20 TYR R 25 1 6
HELIX 140 140 PRO R 49 SER R 61 1 13
HELIX 141 141 VAL R 69 THR R 75 5 7
HELIX 142 142 SER R 76 LYS R 81 1 6
HELIX 143 143 SER R 112 VAL R 121 1 10
HELIX 144 144 ASN R 123 GLY R 126 5 4
HELIX 145 145 PRO R 141 LYS R 146 1 6
HELIX 146 146 GLY R 154 ASN R 163 1 10
HELIX 147 147 SER R 181 GLY R 195 1 15
HELIX 148 148 ARG R 213 GLY R 233 1 21
HELIX 149 149 THR R 246 VAL R 255 1 10
HELIX 150 150 TYR R 269 GLY R 288 1 20
HELIX 151 151 MET R 297 ARG R 303 1 7
HELIX 152 152 HIS R 310 GLY R 322 1 13
HELIX 153 153 GLU R 338 ASP R 351 1 14
HELIX 154 154 ARG R 358 GLY R 361 5 4
HELIX 155 155 HIS R 383 TRP R 385 5 3
HELIX 156 156 HIS R 386 GLY R 395 1 10
HELIX 157 157 GLY R 403 GLY R 408 1 6
HELIX 158 158 GLY R 412 GLU R 433 1 22
HELIX 159 159 ASP R 436 LYS R 463 1 28
HELIX 160 160 THR T 22 GLY T 37 1 16
HELIX 161 161 ASP T 79 PHE T 94 1 16
HELIX 162 162 TYR V 20 TYR V 25 1 6
HELIX 163 163 PRO V 49 SER V 61 1 13
HELIX 164 164 VAL V 69 THR V 75 5 7
HELIX 165 165 SER V 76 LYS V 81 1 6
HELIX 166 166 SER V 112 GLY V 122 1 11
HELIX 167 167 ASN V 123 GLY V 126 5 4
HELIX 168 168 PRO V 141 LYS V 146 1 6
HELIX 169 169 GLY V 154 ASN V 163 1 10
HELIX 170 170 SER V 181 GLY V 195 1 15
HELIX 171 171 ARG V 213 GLY V 233 1 21
HELIX 172 172 THR V 246 VAL V 255 1 10
HELIX 173 173 TYR V 269 GLY V 288 1 20
HELIX 174 174 MET V 297 ARG V 303 1 7
HELIX 175 175 HIS V 310 GLY V 322 1 13
HELIX 176 176 GLU V 338 ASP V 351 1 14
HELIX 177 177 ARG V 358 GLY V 361 5 4
HELIX 178 178 HIS V 383 TRP V 385 5 3
HELIX 179 179 HIS V 386 GLY V 395 1 10
HELIX 180 180 GLY V 403 GLY V 408 1 6
HELIX 181 181 GLY V 412 GLU V 433 1 22
HELIX 182 182 ASP V 436 LYS V 463 1 28
HELIX 183 183 THR W 22 GLY W 37 1 16
HELIX 184 184 ASP W 79 PHE W 94 1 16
SHEET 1 AA 5 ARG A 83 PRO A 89 0
SHEET 2 AA 5 TYR A 97 TYR A 103 -1 O ILE A 98 N GLU A 88
SHEET 3 AA 5 ILE A 36 PRO A 44 -1 O ILE A 36 N TYR A 103
SHEET 4 AA 5 LEU A 130 ARG A 139 -1 N ARG A 131 O THR A 43
SHEET 5 AA 5 GLY A 308 ILE A 309 1 O GLY A 308 N LEU A 135
SHEET 1 AB 7 LEU A 169 GLY A 171 0
SHEET 2 AB 7 CYS A 399 GLN A 401 1 O LEU A 400 N GLY A 171
SHEET 3 AB 7 MET A 375 SER A 379 1 O PRO A 376 N CYS A 399
SHEET 4 AB 7 HIS A 325 HIS A 327 1 O LEU A 326 N VAL A 377
SHEET 5 AB 7 LEU A 290 HIS A 294 1 O ILE A 293 N HIS A 327
SHEET 6 AB 7 ILE A 264 ASP A 268 1 O ILE A 265 N HIS A 292
SHEET 7 AB 7 LEU A 240 ASN A 241 1 O LEU A 240 N MET A 266
SHEET 1 AC 2 PHE A 199 THR A 200 0
SHEET 2 AC 2 GLY A 237 HIS A 238 1 O GLY A 237 N THR A 200
SHEET 1 AD 2 TYR A 353 VAL A 354 0
SHEET 2 AD 2 GLN A 366 ASP A 367 -1 O GLN A 366 N VAL A 354
SHEET 1 BA 5 ARG B 83 PRO B 89 0
SHEET 2 BA 5 TYR B 97 TYR B 103 -1 O ILE B 98 N GLU B 88
SHEET 3 BA 5 ILE B 36 PRO B 44 -1 O ILE B 36 N TYR B 103
SHEET 4 BA 5 LEU B 130 ARG B 139 -1 N ARG B 131 O THR B 43
SHEET 5 BA 5 GLY B 308 ILE B 309 1 O GLY B 308 N LEU B 135
SHEET 1 BB 7 LEU B 169 GLY B 171 0
SHEET 2 BB 7 CYS B 399 GLN B 401 1 O LEU B 400 N GLY B 171
SHEET 3 BB 7 MET B 375 SER B 379 1 O PRO B 376 N CYS B 399
SHEET 4 BB 7 HIS B 325 HIS B 327 1 O LEU B 326 N VAL B 377
SHEET 5 BB 7 LEU B 290 HIS B 294 1 O ILE B 293 N HIS B 327
SHEET 6 BB 7 ILE B 264 ASP B 268 1 O ILE B 265 N HIS B 292
SHEET 7 BB 7 LEU B 240 ASN B 241 1 O LEU B 240 N MET B 266
SHEET 1 BC 2 PHE B 199 THR B 200 0
SHEET 2 BC 2 GLY B 237 HIS B 238 1 O GLY B 237 N THR B 200
SHEET 1 BD 2 TYR B 353 VAL B 354 0
SHEET 2 BD 2 GLN B 366 ASP B 367 -1 O GLN B 366 N VAL B 354
SHEET 1 CA 4 THR C 68 TRP C 70 0
SHEET 2 CA 4 ILE C 39 ALA C 45 -1 O LEU C 42 N TRP C 70
SHEET 3 CA 4 TYR C 98 ASP C 105 -1 O TYR C 98 N ALA C 45
SHEET 4 CA 4 VAL C 110 GLN C 118 -1 O VAL C 110 N ASP C 105
SHEET 1 EA 5 ARG E 83 PRO E 89 0
SHEET 2 EA 5 TYR E 97 TYR E 103 -1 O ILE E 98 N GLU E 88
SHEET 3 EA 5 ILE E 36 PRO E 44 -1 O ILE E 36 N TYR E 103
SHEET 4 EA 5 LEU E 130 ARG E 139 -1 N ARG E 131 O THR E 43
SHEET 5 EA 5 GLY E 308 ILE E 309 1 O GLY E 308 N LEU E 135
SHEET 1 EB 7 LEU E 169 GLY E 171 0
SHEET 2 EB 7 CYS E 399 GLN E 401 1 O LEU E 400 N GLY E 171
SHEET 3 EB 7 MET E 375 SER E 379 1 O PRO E 376 N CYS E 399
SHEET 4 EB 7 HIS E 325 HIS E 327 1 O LEU E 326 N VAL E 377
SHEET 5 EB 7 LEU E 290 HIS E 294 1 O ILE E 293 N HIS E 327
SHEET 6 EB 7 ILE E 264 ASP E 268 1 O ILE E 265 N HIS E 292
SHEET 7 EB 7 LEU E 240 ASN E 241 1 O LEU E 240 N MET E 266
SHEET 1 EC 2 PHE E 199 THR E 200 0
SHEET 2 EC 2 GLY E 237 HIS E 238 1 O GLY E 237 N THR E 200
SHEET 1 ED 2 TYR E 353 VAL E 354 0
SHEET 2 ED 2 GLN E 366 ASP E 367 -1 O GLN E 366 N VAL E 354
SHEET 1 FA 4 THR F 68 TRP F 70 0
SHEET 2 FA 4 ILE F 39 ALA F 45 -1 O LEU F 42 N TRP F 70
SHEET 3 FA 4 TYR F 98 ASP F 105 -1 O TYR F 98 N ALA F 45
SHEET 4 FA 4 VAL F 110 GLN F 118 -1 O VAL F 110 N ASP F 105
SHEET 1 HA 5 ARG H 83 PRO H 89 0
SHEET 2 HA 5 TYR H 97 TYR H 103 -1 O ILE H 98 N GLU H 88
SHEET 3 HA 5 ILE H 36 PRO H 44 -1 O ILE H 36 N TYR H 103
SHEET 4 HA 5 LEU H 130 ARG H 139 -1 N ARG H 131 O THR H 43
SHEET 5 HA 5 GLY H 308 ILE H 309 1 O GLY H 308 N LEU H 135
SHEET 1 HB 7 LEU H 169 GLY H 171 0
SHEET 2 HB 7 CYS H 399 GLN H 401 1 O LEU H 400 N GLY H 171
SHEET 3 HB 7 MET H 375 SER H 379 1 O PRO H 376 N CYS H 399
SHEET 4 HB 7 HIS H 325 HIS H 327 1 O LEU H 326 N VAL H 377
SHEET 5 HB 7 LEU H 290 HIS H 294 1 O ILE H 293 N HIS H 327
SHEET 6 HB 7 ILE H 264 ASP H 268 1 O ILE H 265 N HIS H 292
SHEET 7 HB 7 LEU H 240 ASN H 241 1 O LEU H 240 N MET H 266
SHEET 1 HC 2 PHE H 199 THR H 200 0
SHEET 2 HC 2 GLY H 237 HIS H 238 1 O GLY H 237 N THR H 200
SHEET 1 HD 2 TYR H 353 VAL H 354 0
SHEET 2 HD 2 GLN H 366 ASP H 367 -1 O GLN H 366 N VAL H 354
SHEET 1 IA 4 THR I 68 TRP I 70 0
SHEET 2 IA 4 ILE I 39 ALA I 45 -1 O LEU I 42 N TRP I 70
SHEET 3 IA 4 TYR I 98 ASP I 105 -1 O TYR I 98 N ALA I 45
SHEET 4 IA 4 VAL I 110 GLN I 118 -1 O VAL I 110 N ASP I 105
SHEET 1 JA 4 THR J 68 TRP J 70 0
SHEET 2 JA 4 ILE J 39 ALA J 45 -1 O LEU J 42 N TRP J 70
SHEET 3 JA 4 TYR J 98 ASP J 105 -1 O TYR J 98 N ALA J 45
SHEET 4 JA 4 VAL J 110 GLN J 118 -1 O VAL J 110 N ASP J 105
SHEET 1 KA 5 ARG K 83 PRO K 89 0
SHEET 2 KA 5 TYR K 97 TYR K 103 -1 O ILE K 98 N GLU K 88
SHEET 3 KA 5 ILE K 36 PRO K 44 -1 O ILE K 36 N TYR K 103
SHEET 4 KA 5 LEU K 130 ARG K 139 -1 N ARG K 131 O THR K 43
SHEET 5 KA 5 GLY K 308 ILE K 309 1 O GLY K 308 N LEU K 135
SHEET 1 KB 7 LEU K 169 GLY K 171 0
SHEET 2 KB 7 CYS K 399 GLN K 401 1 O LEU K 400 N GLY K 171
SHEET 3 KB 7 MET K 375 SER K 379 1 O PRO K 376 N CYS K 399
SHEET 4 KB 7 HIS K 325 HIS K 327 1 O LEU K 326 N VAL K 377
SHEET 5 KB 7 LEU K 290 HIS K 294 1 O ILE K 293 N HIS K 327
SHEET 6 KB 7 ILE K 264 ASP K 268 1 O ILE K 265 N HIS K 292
SHEET 7 KB 7 LEU K 240 ASN K 241 1 O LEU K 240 N MET K 266
SHEET 1 KC 2 PHE K 199 THR K 200 0
SHEET 2 KC 2 GLY K 237 HIS K 238 1 O GLY K 237 N THR K 200
SHEET 1 KD 2 TYR K 353 VAL K 354 0
SHEET 2 KD 2 GLN K 366 ASP K 367 -1 O GLN K 366 N VAL K 354
SHEET 1 MA 4 THR M 68 TRP M 70 0
SHEET 2 MA 4 ILE M 39 ALA M 45 -1 O LEU M 42 N TRP M 70
SHEET 3 MA 4 TYR M 98 ASP M 105 -1 O TYR M 98 N ALA M 45
SHEET 4 MA 4 VAL M 110 GLN M 118 -1 O VAL M 110 N ASP M 105
SHEET 1 OA 5 ARG O 83 PRO O 89 0
SHEET 2 OA 5 TYR O 97 TYR O 103 -1 O ILE O 98 N GLU O 88
SHEET 3 OA 5 ILE O 36 PRO O 44 -1 O ILE O 36 N TYR O 103
SHEET 4 OA 5 LEU O 130 ARG O 139 -1 N ARG O 131 O THR O 43
SHEET 5 OA 5 GLY O 308 ILE O 309 1 O GLY O 308 N LEU O 135
SHEET 1 OB 7 LEU O 169 GLY O 171 0
SHEET 2 OB 7 CYS O 399 GLN O 401 1 O LEU O 400 N GLY O 171
SHEET 3 OB 7 MET O 375 SER O 379 1 O PRO O 376 N CYS O 399
SHEET 4 OB 7 HIS O 325 HIS O 327 1 O LEU O 326 N VAL O 377
SHEET 5 OB 7 LEU O 290 HIS O 294 1 O ILE O 293 N HIS O 327
SHEET 6 OB 7 ILE O 264 ASP O 268 1 O ILE O 265 N HIS O 292
SHEET 7 OB 7 LEU O 240 ASN O 241 1 O LEU O 240 N MET O 266
SHEET 1 OC 2 PHE O 199 THR O 200 0
SHEET 2 OC 2 GLY O 237 HIS O 238 1 O GLY O 237 N THR O 200
SHEET 1 OD 2 TYR O 353 VAL O 354 0
SHEET 2 OD 2 GLN O 366 ASP O 367 -1 O GLN O 366 N VAL O 354
SHEET 1 PA 4 THR P 68 TRP P 70 0
SHEET 2 PA 4 ILE P 39 ALA P 45 -1 O LEU P 42 N TRP P 70
SHEET 3 PA 4 TYR P 98 ASP P 105 -1 O TYR P 98 N ALA P 45
SHEET 4 PA 4 VAL P 110 GLN P 118 -1 O VAL P 110 N ASP P 105
SHEET 1 RA 5 ARG R 83 PRO R 89 0
SHEET 2 RA 5 TYR R 97 TYR R 103 -1 O ILE R 98 N GLU R 88
SHEET 3 RA 5 ILE R 36 PRO R 44 -1 O ILE R 36 N TYR R 103
SHEET 4 RA 5 LEU R 130 ARG R 139 -1 N ARG R 131 O THR R 43
SHEET 5 RA 5 GLY R 308 ILE R 309 1 O GLY R 308 N LEU R 135
SHEET 1 RB 7 LEU R 169 GLY R 171 0
SHEET 2 RB 7 CYS R 399 GLN R 401 1 O LEU R 400 N GLY R 171
SHEET 3 RB 7 MET R 375 SER R 379 1 O PRO R 376 N CYS R 399
SHEET 4 RB 7 HIS R 325 HIS R 327 1 O LEU R 326 N VAL R 377
SHEET 5 RB 7 LEU R 290 HIS R 294 1 O ILE R 293 N HIS R 327
SHEET 6 RB 7 ILE R 264 ASP R 268 1 O ILE R 265 N HIS R 292
SHEET 7 RB 7 LEU R 240 ASN R 241 1 O LEU R 240 N MET R 266
SHEET 1 RC 2 PHE R 199 THR R 200 0
SHEET 2 RC 2 GLY R 237 HIS R 238 1 O GLY R 237 N THR R 200
SHEET 1 RD 2 TYR R 353 VAL R 354 0
SHEET 2 RD 2 GLN R 366 ASP R 367 -1 O GLN R 366 N VAL R 354
SHEET 1 TA 4 THR T 68 TRP T 70 0
SHEET 2 TA 4 ILE T 39 ALA T 45 -1 O LEU T 42 N TRP T 70
SHEET 3 TA 4 TYR T 98 ASP T 105 -1 O TYR T 98 N ALA T 45
SHEET 4 TA 4 VAL T 110 GLN T 118 -1 O VAL T 110 N ASP T 105
SHEET 1 VA 5 ARG V 83 PRO V 89 0
SHEET 2 VA 5 TYR V 97 TYR V 103 -1 O ILE V 98 N GLU V 88
SHEET 3 VA 5 ILE V 36 PRO V 44 -1 O ILE V 36 N TYR V 103
SHEET 4 VA 5 LEU V 130 ARG V 139 -1 N ARG V 131 O THR V 43
SHEET 5 VA 5 GLY V 308 ILE V 309 1 O GLY V 308 N LEU V 135
SHEET 1 VB 7 LEU V 169 GLY V 171 0
SHEET 2 VB 7 CYS V 399 GLN V 401 1 O LEU V 400 N GLY V 171
SHEET 3 VB 7 MET V 375 SER V 379 1 O PRO V 376 N CYS V 399
SHEET 4 VB 7 HIS V 325 HIS V 327 1 O LEU V 326 N VAL V 377
SHEET 5 VB 7 LEU V 290 HIS V 294 1 O ILE V 293 N HIS V 327
SHEET 6 VB 7 ILE V 264 ASP V 268 1 O ILE V 265 N HIS V 292
SHEET 7 VB 7 LEU V 240 ASN V 241 1 O LEU V 240 N MET V 266
SHEET 1 VC 2 PHE V 199 THR V 200 0
SHEET 2 VC 2 GLY V 237 HIS V 238 1 O GLY V 237 N THR V 200
SHEET 1 VD 2 TYR V 353 VAL V 354 0
SHEET 2 VD 2 GLN V 366 ASP V 367 -1 O GLN V 366 N VAL V 354
SHEET 1 WA 4 THR W 68 TRP W 70 0
SHEET 2 WA 4 ILE W 39 ALA W 45 -1 O LEU W 42 N TRP W 70
SHEET 3 WA 4 TYR W 98 ASP W 105 -1 O TYR W 98 N ALA W 45
SHEET 4 WA 4 VAL W 110 GLN W 118 -1 O VAL W 110 N ASP W 105
SSBOND 1 CYS A 247 CYS B 247 1555 1555 2.09
SSBOND 2 CYS E 247 CYS K 247 1555 1555 2.10
SSBOND 3 CYS H 247 CYS R 247 1555 1555 2.09
SSBOND 4 CYS O 247 CYS V 247 1555 1555 2.10
LINK C TYR A 103 N HYP A 104 1555 1555 1.32
LINK C HYP A 104 N ILE A 105 1555 1555 1.32
LINK C GLY A 150 N HYP A 151 1555 1555 1.34
LINK C HYP A 151 N PRO A 152 1555 1555 1.34
LINK C THR A 200 N KCX A 201 1555 1555 1.32
LINK C KCX A 201 N ASP A 202 1555 1555 1.33
LINK OQ2 KCX A 201 MG MG A1476 1555 1555 2.05
LINK C VAL A 255 N SMC A 256 1555 1555 1.33
LINK C SMC A 256 N ALA A 257 1555 1555 1.34
LINK C TRP A 368 N SMC A 369 1555 1555 1.33
LINK C SMC A 369 N SER A 370 1555 1555 1.33
LINK MG MG A1476 OD1 ASP A 203 1555 1555 1.77
LINK MG MG A1476 OE1 GLU A 204 1555 1555 2.18
LINK MG MG A1476 O3 CAP A1477 1555 1555 2.16
LINK MG MG A1476 O6 CAP A1477 1555 1555 2.19
LINK MG MG A1476 O2 CAP A1477 1555 1555 2.28
LINK C TYR B 103 N HYP B 104 1555 1555 1.33
LINK C HYP B 104 N ILE B 105 1555 1555 1.33
LINK C GLY B 150 N HYP B 151 1555 1555 1.32
LINK C HYP B 151 N PRO B 152 1555 1555 1.33
LINK C THR B 200 N KCX B 201 1555 1555 1.32
LINK C KCX B 201 N ASP B 202 1555 1555 1.33
LINK OQ2 KCX B 201 MG MG B1476 1555 1555 1.91
LINK C VAL B 255 N SMC B 256 1555 1555 1.32
LINK C SMC B 256 N ALA B 257 1555 1555 1.34
LINK C TRP B 368 N SMC B 369 1555 1555 1.33
LINK C SMC B 369 N SER B 370 1555 1555 1.35
LINK MG MG B1476 O6 CAP B1477 1555 1555 1.76
LINK MG MG B1476 O2 CAP B1477 1555 1555 2.35
LINK MG MG B1476 OD1 ASP B 203 1555 1555 1.84
LINK MG MG B1476 OE1 GLU B 204 1555 1555 2.31
LINK MG MG B1476 O3 CAP B1477 1555 1555 2.23
LINK C TYR E 103 N HYP E 104 1555 1555 1.33
LINK C HYP E 104 N ILE E 105 1555 1555 1.32
LINK C GLY E 150 N HYP E 151 1555 1555 1.33
LINK C HYP E 151 N PRO E 152 1555 1555 1.33
LINK C THR E 200 N KCX E 201 1555 1555 1.33
LINK C KCX E 201 N ASP E 202 1555 1555 1.33
LINK C VAL E 255 N SMC E 256 1555 1555 1.33
LINK C SMC E 256 N ALA E 257 1555 1555 1.33
LINK C TRP E 368 N SMC E 369 1555 1555 1.35
LINK C SMC E 369 N SER E 370 1555 1555 1.33
LINK MG MG E1476 O2 CAP E1477 1555 1555 2.31
LINK MG MG E1476 O3 CAP E1477 1555 1555 2.03
LINK MG MG E1476 O6 CAP E1477 1555 1555 1.98
LINK MG MG E1476 OQ2 KCX E 201 1555 1555 2.12
LINK MG MG E1476 OD1 ASP E 203 1555 1555 1.88
LINK MG MG E1476 OE1 GLU E 204 1555 1555 2.09
LINK C TYR H 103 N HYP H 104 1555 1555 1.33
LINK C HYP H 104 N ILE H 105 1555 1555 1.32
LINK C GLY H 150 N HYP H 151 1555 1555 1.33
LINK C HYP H 151 N PRO H 152 1555 1555 1.33
LINK C THR H 200 N KCX H 201 1555 1555 1.32
LINK C KCX H 201 N ASP H 202 1555 1555 1.34
LINK OQ2 KCX H 201 MG MG H1476 1555 1555 1.99
LINK C VAL H 255 N SMC H 256 1555 1555 1.33
LINK C SMC H 256 N ALA H 257 1555 1555 1.33
LINK C TRP H 368 N SMC H 369 1555 1555 1.34
LINK C SMC H 369 N SER H 370 1555 1555 1.34
LINK MG MG H1476 OD1 ASP H 203 1555 1555 1.99
LINK MG MG H1476 OE1 GLU H 204 1555 1555 2.09
LINK MG MG H1476 O6 CAP H1477 1555 1555 1.91
LINK MG MG H1476 O3 CAP H1477 1555 1555 2.19
LINK MG MG H1476 O2 CAP H1477 1555 1555 2.54
LINK C TYR K 103 N HYP K 104 1555 1555 1.32
LINK C HYP K 104 N ILE K 105 1555 1555 1.33
LINK C GLY K 150 N HYP K 151 1555 1555 1.33
LINK C HYP K 151 N PRO K 152 1555 1555 1.33
LINK C THR K 200 N KCX K 201 1555 1555 1.32
LINK OQ2 KCX K 201 MG MG K1476 1555 1555 1.98
LINK C KCX K 201 N ASP K 202 1555 1555 1.33
LINK C VAL K 255 N SMC K 256 1555 1555 1.32
LINK C SMC K 256 N ALA K 257 1555 1555 1.33
LINK C TRP K 368 N SMC K 369 1555 1555 1.34
LINK C SMC K 369 N SER K 370 1555 1555 1.33
LINK MG MG K1476 OD1 ASP K 203 1555 1555 2.21
LINK MG MG K1476 O6 CAP K1477 1555 1555 1.84
LINK MG MG K1476 O3 CAP K1477 1555 1555 1.85
LINK MG MG K1476 O2 CAP K1477 1555 1555 2.23
LINK MG MG K1476 OE1 GLU K 204 1555 1555 2.06
LINK MG MG K1476 OQ1 KCX K 201 1555 1555 3.15
LINK C TYR O 103 N HYP O 104 1555 1555 1.32
LINK C HYP O 104 N ILE O 105 1555 1555 1.34
LINK C GLY O 150 N HYP O 151 1555 1555 1.32
LINK C HYP O 151 N PRO O 152 1555 1555 1.32
LINK C THR O 200 N KCX O 201 1555 1555 1.32
LINK C KCX O 201 N ASP O 202 1555 1555 1.34
LINK C VAL O 255 N SMC O 256 1555 1555 1.34
LINK C SMC O 256 N ALA O 257 1555 1555 1.33
LINK C TRP O 368 N SMC O 369 1555 1555 1.32
LINK C SMC O 369 N SER O 370 1555 1555 1.34
LINK MG MG O1476 O6 CAP O1477 1555 1555 1.95
LINK MG MG O1476 OD1 ASP O 203 1555 1555 1.76
LINK MG MG O1476 O2 CAP O1477 1555 1555 2.10
LINK MG MG O1476 OQ2 KCX O 201 1555 1555 2.14
LINK MG MG O1476 O3 CAP O1477 1555 1555 2.23
LINK MG MG O1476 OE1 GLU O 204 1555 1555 2.15
LINK C TYR R 103 N HYP R 104 1555 1555 1.32
LINK C HYP R 104 N ILE R 105 1555 1555 1.33
LINK C GLY R 150 N HYP R 151 1555 1555 1.33
LINK C HYP R 151 N PRO R 152 1555 1555 1.33
LINK C THR R 200 N KCX R 201 1555 1555 1.33
LINK OQ2 KCX R 201 MG MG R1476 1555 1555 2.01
LINK C KCX R 201 N ASP R 202 1555 1555 1.33
LINK C VAL R 255 N SMC R 256 1555 1555 1.32
LINK C SMC R 256 N ALA R 257 1555 1555 1.33
LINK C TRP R 368 N SMC R 369 1555 1555 1.33
LINK C SMC R 369 N SER R 370 1555 1555 1.34
LINK MG MG R1476 O3 CAP R1477 1555 1555 2.18
LINK MG MG R1476 O6 CAP R1477 1555 1555 2.28
LINK MG MG R1476 OD1 ASP R 203 1555 1555 1.86
LINK MG MG R1476 OE1 GLU R 204 1555 1555 1.99
LINK MG MG R1476 O2 CAP R1477 1555 1555 2.15
LINK C TYR V 103 N HYP V 104 1555 1555 1.34
LINK C HYP V 104 N ILE V 105 1555 1555 1.32
LINK C GLY V 150 N HYP V 151 1555 1555 1.34
LINK C HYP V 151 N PRO V 152 1555 1555 1.33
LINK C THR V 200 N KCX V 201 1555 1555 1.33
LINK C KCX V 201 N ASP V 202 1555 1555 1.33
LINK C VAL V 255 N SMC V 256 1555 1555 1.34
LINK C SMC V 256 N ALA V 257 1555 1555 1.33
LINK C TRP V 368 N SMC V 369 1555 1555 1.34
LINK C SMC V 369 N SER V 370 1555 1555 1.34
LINK MG MG V1476 O3 CAP V1477 1555 1555 2.38
LINK MG MG V1476 OQ2 KCX V 201 1555 1555 2.18
LINK MG MG V1476 O6 CAP V1477 1555 1555 1.80
LINK MG MG V1476 OE1 GLU V 204 1555 1555 2.10
LINK MG MG V1476 O2 CAP V1477 1555 1555 2.32
LINK MG MG V1476 OD1 ASP V 203 1555 1555 1.70
CISPEP 1 LYS A 175 PRO A 176 0 -2.39
CISPEP 2 LYS B 175 PRO B 176 0 2.45
CISPEP 3 LYS E 175 PRO E 176 0 -0.67
CISPEP 4 LYS H 175 PRO H 176 0 -2.13
CISPEP 5 LYS K 175 PRO K 176 0 -1.13
CISPEP 6 LYS O 175 PRO O 176 0 -0.80
CISPEP 7 LYS R 175 PRO R 176 0 0.99
CISPEP 8 LYS V 175 PRO V 176 0 -4.23
SITE 1 AC1 5 LYS A 177 KCX A 201 ASP A 203 GLU A 204
SITE 2 AC1 5 CAP A1477
SITE 1 AC2 4 KCX B 201 ASP B 203 GLU B 204 CAP B1477
SITE 1 AC3 5 LYS E 177 KCX E 201 ASP E 203 GLU E 204
SITE 2 AC3 5 CAP E1477
SITE 1 AC4 5 LYS H 177 KCX H 201 ASP H 203 GLU H 204
SITE 2 AC4 5 CAP H1477
SITE 1 AC5 4 KCX K 201 ASP K 203 GLU K 204 CAP K1477
SITE 1 AC6 5 LYS O 177 KCX O 201 ASP O 203 GLU O 204
SITE 2 AC6 5 CAP O1477
SITE 1 AC7 5 LYS R 177 KCX R 201 ASP R 203 GLU R 204
SITE 2 AC7 5 CAP R1477
SITE 1 AC8 5 LYS V 177 KCX V 201 ASP V 203 GLU V 204
SITE 2 AC8 5 CAP V1477
SITE 1 AC9 29 THR A 173 LYS A 175 LYS A 177 KCX A 201
SITE 2 AC9 29 ASP A 203 GLU A 204 HIS A 294 ARG A 295
SITE 3 AC9 29 HIS A 327 LYS A 334 LEU A 335 SER A 379
SITE 4 AC9 29 GLY A 380 GLY A 381 GLY A 403 GLY A 404
SITE 5 AC9 29 MG A1476 HOH A2103 HOH A2134 HOH A2135
SITE 6 AC9 29 HOH A2143 HOH A2172 HOH A2173 HOH A2174
SITE 7 AC9 29 GLU B 60 THR B 65 TRP B 66 ASN B 123
SITE 8 AC9 29 HOH B2028
SITE 1 BC1 7 TYR A 24 THR A 68 VAL A 69 ASP A 72
SITE 2 BC1 7 EDO A1479 HOH A2024 HOH A2175
SITE 1 BC2 9 VAL A 17 LYS A 18 THR A 65 TRP A 66
SITE 2 BC2 9 THR A 67 THR A 68 EDO A1478 HOH A2004
SITE 3 BC2 9 HOH A2175
SITE 1 BC3 2 TYR A 20 GLU A 52
SITE 1 BC4 4 LYS A 466 GLU A 468 PHE A 469 HOH B2200
SITE 1 BC5 4 ASP A 302 GLU A 336 ASP A 473 HOH A2177
SITE 1 BC6 4 LEU A 270 HOH A2178 LEU B 270 HOH B2111
SITE 1 BC7 29 GLU A 60 THR A 65 TRP A 66 ASN A 123
SITE 2 BC7 29 HOH A2021 HOH A2022 HOH A2047 THR B 173
SITE 3 BC7 29 LYS B 175 LYS B 177 KCX B 201 ASP B 203
SITE 4 BC7 29 GLU B 204 HIS B 294 ARG B 295 HIS B 327
SITE 5 BC7 29 LYS B 334 LEU B 335 SER B 379 GLY B 380
SITE 6 BC7 29 GLY B 381 GLY B 403 GLY B 404 MG B1476
SITE 7 BC7 29 HOH B2159 HOH B2194 HOH B2195 HOH B2196
SITE 8 BC7 29 HOH B2197
SITE 1 BC8 6 TYR B 24 THR B 68 VAL B 69 ASP B 72
SITE 2 BC8 6 HOH B2031 HOH B2198
SITE 1 BC9 7 VAL B 17 LYS B 18 TRP B 66 THR B 67
SITE 2 BC9 7 THR B 68 HOH B2198 HOH B2199
SITE 1 CC1 3 TYR B 20 GLU B 52 HOH B2200
SITE 1 CC2 3 LYS B 466 PHE B 467 GLU B 468
SITE 1 CC3 7 ARG B 295 SER B 328 GLY B 329 GLU B 336
SITE 2 CC3 7 GLY B 337 ASP B 473 HOH B2140
SITE 1 CC4 3 TYR C 52 GLU C 54 HOH C2055
SITE 1 CC5 4 GLY C 37 ILE C 39 PHE C 75 GLY C 76
SITE 1 CC6 28 THR E 173 LYS E 175 LYS E 177 KCX E 201
SITE 2 CC6 28 ASP E 203 GLU E 204 HIS E 294 ARG E 295
SITE 3 CC6 28 HIS E 327 LYS E 334 LEU E 335 SER E 379
SITE 4 CC6 28 GLY E 380 GLY E 381 GLY E 403 GLY E 404
SITE 5 CC6 28 MG E1476 HOH E2079 HOH E2149 HOH E2150
SITE 6 CC6 28 HOH E2183 HOH E2184 HOH E2185 GLU K 60
SITE 7 CC6 28 THR K 65 TRP K 66 ASN K 123 HOH K2057
SITE 1 CC7 7 TYR E 24 GLY E 64 THR E 68 VAL E 69
SITE 2 CC7 7 ASP E 72 EDO E1479 HOH E2037
SITE 1 CC8 8 LYS E 18 TYR E 20 THR E 65 TRP E 66
SITE 2 CC8 8 THR E 67 THR E 68 EDO E1478 HOH E2014
SITE 1 CC9 5 TYR E 20 GLU E 52 ALA E 129 HOH E2015
SITE 2 CC9 5 HOH E2186
SITE 1 DC1 4 LYS E 466 PHE E 467 GLU E 468 EDO K1480
SITE 1 DC2 4 LEU E 270 GLY E 273 PHE E 274 LEU K 270
SITE 1 DC3 4 GLY F 37 TRP F 38 ILE F 39 GLY F 76
SITE 1 DC4 27 THR H 173 LYS H 175 LYS H 177 KCX H 201
SITE 2 DC4 27 ASP H 203 GLU H 204 HIS H 294 ARG H 295
SITE 3 DC4 27 HIS H 327 LYS H 334 LEU H 335 SER H 379
SITE 4 DC4 27 GLY H 380 GLY H 381 GLY H 403 GLY H 404
SITE 5 DC4 27 MG H1476 HOH H2144 HOH H2162 HOH H2163
SITE 6 DC4 27 HOH H2164 HOH H2165 GLU R 60 THR R 65
SITE 7 DC4 27 TRP R 66 ASN R 123 HOH R2022
SITE 1 DC5 8 TYR H 24 THR H 68 VAL H 69 ASP H 72
SITE 2 DC5 8 LEU H 77 EDO H1479 HOH H2030 HOH H2166
SITE 1 DC6 9 LYS H 18 TYR H 20 THR H 65 TRP H 66
SITE 2 DC6 9 THR H 67 THR H 68 EDO H1478 HOH H2010
SITE 3 DC6 9 HOH H2166
SITE 1 DC7 4 TYR H 20 GLU H 52 ALA H 129 HOH H2024
SITE 1 DC8 4 ARG H 295 GLU H 336 ASP H 473 HOH H2125
SITE 1 DC9 3 GLY I 37 ILE I 39 GLY I 76
SITE 1 EC1 4 GLY J 37 ILE J 39 PHE J 75 GLY J 76
SITE 1 EC2 28 GLU E 60 THR E 65 TRP E 66 ASN E 123
SITE 2 EC2 28 HOH E2033 THR K 173 LYS K 175 LYS K 177
SITE 3 EC2 28 KCX K 201 ASP K 203 GLU K 204 HIS K 294
SITE 4 EC2 28 ARG K 295 HIS K 327 LYS K 334 LEU K 335
SITE 5 EC2 28 SER K 379 GLY K 380 GLY K 381 GLY K 403
SITE 6 EC2 28 GLY K 404 MG K1476 HOH K2125 HOH K2183
SITE 7 EC2 28 HOH K2184 HOH K2185 HOH K2186 HOH K2187
SITE 1 EC3 9 TYR K 24 GLY K 64 THR K 68 VAL K 69
SITE 2 EC3 9 ASP K 72 LEU K 77 HOH K2027 HOH K2188
SITE 3 EC3 9 HOH K2189
SITE 1 EC4 6 LYS K 18 TRP K 66 THR K 67 THR K 68
SITE 2 EC4 6 HOH K2027 HOH K2190
SITE 1 EC5 2 EDO E1481 GLU K 52
SITE 1 EC6 4 LYS K 466 PHE K 467 GLU K 468 HOH K2191
SITE 1 EC7 2 GLU K 336 ASP K 473
SITE 1 EC8 4 GLY M 37 ILE M 39 GLY M 76 CYS M 77
SITE 1 EC9 29 THR O 173 LYS O 175 LYS O 177 KCX O 201
SITE 2 EC9 29 ASP O 203 GLU O 204 HIS O 294 ARG O 295
SITE 3 EC9 29 HIS O 327 LYS O 334 LEU O 335 SER O 379
SITE 4 EC9 29 GLY O 380 GLY O 381 GLY O 403 GLY O 404
SITE 5 EC9 29 MG O1476 HOH O2108 HOH O2144 HOH O2184
SITE 6 EC9 29 HOH O2185 HOH O2186 GLU V 60 THR V 65
SITE 7 EC9 29 TRP V 66 ASN V 123 HOH V2026 HOH V2028
SITE 8 EC9 29 HOH V2059
SITE 1 FC1 8 TYR O 24 THR O 68 VAL O 69 ASP O 72
SITE 2 FC1 8 LEU O 77 EDO O1479 HOH O2024 HOH O2188
SITE 1 FC2 7 LYS O 18 THR O 65 TRP O 66 THR O 67
SITE 2 FC2 7 EDO O1478 HOH O2187 HOH O2188
SITE 1 FC3 2 GLU O 52 EDO V1482
SITE 1 FC4 4 LYS O 466 PHE O 467 GLU O 468 PHE O 469
SITE 1 FC5 4 ARG O 295 GLU O 336 ASP O 473 HOH O2111
SITE 1 FC6 6 TYR M 52 HIS M 55 ASP M 63 HOH M2018
SITE 2 FC6 6 GLU O 223 LYS O 227
SITE 1 FC7 7 GLY P 37 TRP P 38 ILE P 39 PHE P 75
SITE 2 FC7 7 GLY P 76 CYS P 77 HOH P2051
SITE 1 FC8 28 GLU H 60 THR H 65 TRP H 66 ASN H 123
SITE 2 FC8 28 THR R 173 LYS R 175 LYS R 177 KCX R 201
SITE 3 FC8 28 ASP R 203 GLU R 204 HIS R 294 ARG R 295
SITE 4 FC8 28 HIS R 327 LYS R 334 LEU R 335 SER R 379
SITE 5 FC8 28 GLY R 380 GLY R 381 GLY R 403 GLY R 404
SITE 6 FC8 28 MG R1476 HOH R2066 HOH R2110 HOH R2138
SITE 7 FC8 28 HOH R2179 HOH R2180 HOH R2181 HOH R2182
SITE 1 FC9 8 TYR R 24 GLY R 64 THR R 68 VAL R 69
SITE 2 FC9 8 ASP R 72 HOH R2023 HOH R2027 HOH R2183
SITE 1 GC1 7 LYS R 18 THR R 65 TRP R 66 THR R 67
SITE 2 GC1 7 THR R 68 HOH R2013 HOH R2183
SITE 1 GC2 4 TYR R 20 GLU R 52 EDO R1484 HOH R2010
SITE 1 GC3 4 LYS R 466 PHE R 467 GLU R 468 PHE R 469
SITE 1 GC4 7 TYR P 52 HIS P 55 ASP P 63 HOH P2023
SITE 2 GC4 7 GLU R 223 TYR R 226 LYS R 227
SITE 1 GC5 5 LEU H 270 GLY H 273 PHE H 274 LEU R 270
SITE 2 GC5 5 THR R 271
SITE 1 GC6 3 ARG B 439 LYS H 466 EDO R1480
SITE 1 GC7 6 TYR A 226 ALA A 230 HIS T 48 TYR T 52
SITE 2 GC7 6 GLU T 54 HIS T 55
SITE 1 GC8 5 GLY T 37 TRP T 38 ILE T 39 GLY T 76
SITE 2 GC8 5 HOH T2048
SITE 1 GC9 29 GLU O 60 THR O 65 TRP O 66 ASN O 123
SITE 2 GC9 29 HOH O2021 HOH O2049 THR V 173 LYS V 175
SITE 3 GC9 29 LYS V 177 KCX V 201 ASP V 203 GLU V 204
SITE 4 GC9 29 HIS V 294 ARG V 295 HIS V 327 LYS V 334
SITE 5 GC9 29 LEU V 335 SER V 379 GLY V 380 GLY V 381
SITE 6 GC9 29 GLY V 403 GLY V 404 MG V1476 HOH V2078
SITE 7 GC9 29 HOH V2122 HOH V2123 HOH V2190 HOH V2191
SITE 8 GC9 29 HOH V2192
SITE 1 HC1 3 LEU O 270 LEU V 270 PHE V 274
SITE 1 HC2 7 TYR V 24 THR V 68 VAL V 69 ASP V 72
SITE 2 HC2 7 LEU V 77 EDO V1480 HOH V2193
SITE 1 HC3 7 LYS V 18 TYR V 20 THR V 65 TRP V 66
SITE 2 HC3 7 THR V 67 EDO V1479 HOH V2194
SITE 1 HC4 2 PHE O 469 GLU V 52
SITE 1 HC5 6 ARG E 439 EDO O1480 LYS V 466 PHE V 467
SITE 2 HC5 6 GLU V 468 PHE V 469
SITE 1 HC6 3 ARG V 295 GLU V 336 ASP V 473
SITE 1 HC7 5 GLY W 37 TRP W 38 GLY W 76 CYS W 77
SITE 2 HC7 5 HOH W2034
CRYST1 220.014 224.078 111.725 90.00 90.00 90.00 P 21 21 2 32
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 0.004545 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004463 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008950 0.00000
MTRIX1 1 0.944700 0.319800 0.072140 -13.04000 1
MTRIX2 1 0.319800 -0.947400 0.011780 67.49000 1
MTRIX3 1 0.072110 0.011940 -0.997300 51.69000 1
MTRIX1 2 -0.320800 0.947100 0.003269 43.13000 1
MTRIX2 2 0.947100 0.320800 0.003249 -31.23000 1
MTRIX3 2 0.002028 0.004139 -1.000000 56.75000 1
MTRIX1 3 -0.947200 -0.320300 0.010540 141.89999 1
MTRIX2 3 -0.320300 0.944900 -0.067150 25.25000 1
MTRIX3 3 0.011550 -0.066980 -0.997700 59.24000 1
MTRIX1 4 -0.001938 0.997600 -0.068640 22.02000 1
MTRIX2 4 -0.999900 -0.002908 -0.014030 111.60000 1
MTRIX3 4 -0.014200 0.068600 0.997500 -2.15400 1
MTRIX1 5 0.008612 -0.999900 -0.014900 111.10000 1
MTRIX2 5 0.997600 0.007575 0.068280 -22.13000 1
MTRIX3 5 -0.068160 -0.015460 0.997600 5.26800 1
MTRIX1 6 -0.996500 -0.006193 -0.083820 133.39999 1
MTRIX2 6 0.001507 -0.998400 0.055850 89.54000 1
MTRIX3 6 -0.084040 0.055530 0.994900 3.15800 1
MTRIX1 7 0.321900 -0.943500 0.079110 85.28000 1
MTRIX2 7 -0.943300 -0.326700 -0.057750 124.00000 1
MTRIX3 7 0.080330 -0.056040 -0.995200 54.15000 1
MTRIX1 8 0.942400 0.326500 0.072810 -13.24000 1
MTRIX2 8 0.326800 -0.945100 0.008759 67.14000 1
MTRIX3 8 0.071670 0.015540 -0.997300 51.56000 1
MTRIX1 9 -0.322700 0.946500 0.002013 43.32000 1
MTRIX2 9 0.946500 0.322700 0.000834 -31.17000 1
MTRIX3 9 0.000140 0.002175 -1.000000 56.90000 1
MTRIX1 10 -0.946400 -0.322700 0.015480 141.89999 1
MTRIX2 10 -0.322900 0.943900 -0.069000 25.55000 1
MTRIX3 10 0.007651 -0.070300 -0.997500 59.76000 1
MTRIX1 11 -0.000736 0.997500 -0.070390 22.04000 1
MTRIX2 11 -0.999900 -0.001476 -0.010460 111.40000 1
MTRIX3 11 -0.010540 0.070380 0.997500 -2.44600 1
MTRIX1 12 0.002121 -0.999900 -0.015480 111.50000 1
MTRIX2 12 0.997400 0.000993 0.072470 -21.92000 1
MTRIX3 12 -0.072450 -0.015590 0.997300 5.54500 1
MTRIX1 13 -0.996700 -0.001846 -0.081380 133.10001 1
MTRIX2 13 -0.002854 -0.998300 0.057590 89.83000 1
MTRIX3 13 -0.081350 0.057630 0.995000 2.80300 1
MTRIX1 14 0.322500 -0.943300 0.078780 85.22000 1
MTRIX2 14 -0.943200 -0.327200 -0.057430 124.10000 1
MTRIX3 14 0.079950 -0.055790 -0.995200 54.20000 1
(ATOM LINES ARE NOT SHOWN.)
END
