HEADER AMIDOTRANSFERASE 14-APR-98 1A9X
TITLE CARBAMOYL PHOSPHATE SYNTHETASE: CAUGHT IN THE ACT OF GLUTAMINE
TITLE 2 HYDROLYSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBAMOYL PHOSPHATE SYNTHETASE (LARGE CHAIN);
COMPND 3 CHAIN: A, C, E, G;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: CARBAMOYL PHOSPHATE SYNTHETASE (SMALL CHAIN);
COMPND 7 CHAIN: B, D, F, H;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 8 ORGANISM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS AMIDOTRANSFERASE, THIOESTER
EXPDTA X-RAY DIFFRACTION
AUTHOR J.THODEN,H.HOLDEN
REVDAT 3 13-JUL-11 1A9X 1 VERSN
REVDAT 2 24-FEB-09 1A9X 1 VERSN
REVDAT 1 21-OCT-98 1A9X 0
JRNL AUTH J.B.THODEN,S.G.MIRAN,J.C.PHILLIPS,A.J.HOWARD,F.M.RAUSHEL,
JRNL AUTH 2 H.M.HOLDEN
JRNL TITL CARBAMOYL PHOSPHATE SYNTHETASE: CAUGHT IN THE ACT OF
JRNL TITL 2 GLUTAMINE HYDROLYSIS.
JRNL REF BIOCHEMISTRY V. 37 8825 1998
JRNL REFN ISSN 0006-2960
JRNL PMID 9636022
JRNL DOI 10.1021/BI9807761
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT V. 5-E
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.0
REMARK 3 NUMBER OF REFLECTIONS : 700998
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 USING ALL DATA, NO SIGMA CUTOFF.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.1910
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.1910
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 700998
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 44248
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 435
REMARK 3 SOLVENT ATOMS : 4528
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : 0.014 ; 6.000 ; 45467
REMARK 3 BOND ANGLES (DEGREES) : 2.520 ; 10.000; 61307
REMARK 3 TORSION ANGLES (DEGREES) : 17.700; 0.000 ; 27421
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : 0.008 ; 18.000; 1229
REMARK 3 GENERAL PLANES (A) : 0.010 ; 50.000; 6579
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : 0.000 ; 0.000 ; 49310
REMARK 3 NON-BONDED CONTACTS (A) : 0.032 ; NULL ; 367
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : TNT
REMARK 3 KSOL : 0.99
REMARK 3 BSOL : 290.80
REMARK 3
REMARK 3 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : TNT PROTGEO
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1A9X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NOV-97
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.20
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : BRUKER
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SAINT 2000
REMARK 200 DATA SCALING SOFTWARE : XCALIBRE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 700998
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.0
REMARK 200 DATA REDUNDANCY : 2.400
REMARK 200 R MERGE (I) : 0.06500
REMARK 200 R SYM (I) : 0.06500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.88
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.27500
REMARK 200 R SYM FOR SHELL (I) : 0.27500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 1JDB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.65M NET4CL 8% PEG 8000 100MM KCL
REMARK 280 2.5MM MNCL2 2.5MM ADP 2.5MM ORNITHINE 5MM GLUTAMINE 25MM HEPES PH
REMARK 280 7.4 THEN SOAKED INTO: 1.4M NET4CL 8% PEG 8000 250MM KCL 2.5MM
REMARK 280 MNCL2 2.5MM ADP 2.5MM ORNITHINE 5MM GLUTAMINE 25MM HEPES PH 7.4
REMARK 280 7.5% ETHYLENE GLYCOL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 76.05000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 166.15000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 82.20000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 166.15000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 76.05000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 82.20000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 8760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 46650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -77.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 8710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 46880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -76.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 8740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 46920 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 8640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 46700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -72.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 SER A 717
REMARK 465 TYR A 718
REMARK 465 VAL A 719
REMARK 465 LEU A 720
REMARK 465 GLY A 721
REMARK 465 GLY A 722
REMARK 465 ARG A 723
REMARK 465 VAL A 742
REMARK 465 SER A 743
REMARK 465 VAL A 744
REMARK 465 SER A 745
REMARK 465 ASN A 746
REMARK 465 ASP A 747
REMARK 465 ALA A 748
REMARK 465 PRO A 749
REMARK 465 SER C 2717
REMARK 465 TYR C 2718
REMARK 465 VAL C 2719
REMARK 465 LEU C 2720
REMARK 465 GLY C 2721
REMARK 465 GLY C 2722
REMARK 465 ARG C 2723
REMARK 465 VAL C 2742
REMARK 465 SER C 2743
REMARK 465 VAL C 2744
REMARK 465 SER C 2745
REMARK 465 ASN C 2746
REMARK 465 ASP C 2747
REMARK 465 ALA C 2748
REMARK 465 PRO C 2749
REMARK 465 SER E 4717
REMARK 465 TYR E 4718
REMARK 465 VAL E 4719
REMARK 465 LEU E 4720
REMARK 465 GLY E 4721
REMARK 465 GLY E 4722
REMARK 465 ARG E 4723
REMARK 465 VAL E 4742
REMARK 465 SER E 4743
REMARK 465 VAL E 4744
REMARK 465 SER E 4745
REMARK 465 ASN E 4746
REMARK 465 ASP E 4747
REMARK 465 ALA E 4748
REMARK 465 PRO E 4749
REMARK 465 SER G 6717
REMARK 465 TYR G 6718
REMARK 465 VAL G 6719
REMARK 465 LEU G 6720
REMARK 465 GLY G 6721
REMARK 465 GLY G 6722
REMARK 465 ARG G 6723
REMARK 465 VAL G 6742
REMARK 465 SER G 6743
REMARK 465 VAL G 6744
REMARK 465 SER G 6745
REMARK 465 ASN G 6746
REMARK 465 ASP G 6747
REMARK 465 ALA G 6748
REMARK 465 PRO G 6749
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 O HOH C 4116 O HOH C 4492 1.91
REMARK 500 O HOH E 6352 O HOH E 6811 1.94
REMARK 500 O HOH E 6438 O HOH E 6638 2.00
REMARK 500 O HOH E 6324 O HOH E 6779 2.01
REMARK 500 O HOH A 2423 O HOH A 2827 2.02
REMARK 500 O HOH A 2153 O HOH A 2154 2.02
REMARK 500 O HOH G 903 O HOH G 907 2.07
REMARK 500 O MET E 4001 OE2 GLU E 4334 2.08
REMARK 500 O HOH D 4018 O HOH D 4044 2.11
REMARK 500 O HOH D 4199 O HOH D 4200 2.12
REMARK 500 O HOH A 2608 O HOH A 2883 2.14
REMARK 500 O HOH C 4679 O HOH C 4680 2.15
REMARK 500 O HOH C 4028 O HOH C 4029 2.16
REMARK 500 O HOH E 6046 O HOH E 6662 2.17
REMARK 500 O HOH E 6829 O HOH E 6830 2.18
REMARK 500 OE1 GLU G 6467 O HOH G 295 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH D 4245 O HOH H 947 3554 2.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 72 CD GLU A 72 OE2 0.075
REMARK 500 GLU A 79 CD GLU A 79 OE1 0.067
REMARK 500 LYS A 80 CE LYS A 80 NZ 0.189
REMARK 500 GLU A 109 CD GLU A 109 OE1 0.070
REMARK 500 GLU A 110 CD GLU A 110 OE1 0.089
REMARK 500 GLU A 153 CD GLU A 153 OE1 0.070
REMARK 500 GLU A 186 CD GLU A 186 OE2 0.073
REMARK 500 GLU A 217 CD GLU A 217 OE2 0.082
REMARK 500 GLU A 260 CD GLU A 260 OE2 0.071
REMARK 500 GLU A 299 CD GLU A 299 OE2 0.070
REMARK 500 GLU A 334 CD GLU A 334 OE2 0.067
REMARK 500 GLU A 393 CD GLU A 393 OE1 0.071
REMARK 500 GLU A 403 CD GLU A 403 OE2 0.075
REMARK 500 GLU A 419 CD GLU A 419 OE1 0.073
REMARK 500 GLU A 474 CD GLU A 474 OE1 0.069
REMARK 500 GLU A 478 CD GLU A 478 OE1 0.082
REMARK 500 GLU A 512 CD GLU A 512 OE1 0.092
REMARK 500 GLU A 535 CD GLU A 535 OE1 0.070
REMARK 500 GLU A 549 CD GLU A 549 OE2 0.081
REMARK 500 GLU A 560 CD GLU A 560 OE1 0.069
REMARK 500 GLU A 604 CD GLU A 604 OE1 0.074
REMARK 500 GLU A 633 CD GLU A 633 OE1 0.069
REMARK 500 GLU A 655 CD GLU A 655 OE2 0.083
REMARK 500 GLU A 676 CD GLU A 676 OE2 0.067
REMARK 500 GLU A 683 CD GLU A 683 OE2 0.069
REMARK 500 GLU A 699 CD GLU A 699 OE1 0.075
REMARK 500 GLU A 703 CD GLU A 703 OE2 0.080
REMARK 500 GLU A 707 CD GLU A 707 OE1 0.070
REMARK 500 GLU A 731 CD GLU A 731 OE1 0.067
REMARK 500 GLU A 761 CD GLU A 761 OE1 0.083
REMARK 500 GLU A 771 CD GLU A 771 OE1 0.085
REMARK 500 GLU A 876 CD GLU A 876 OE2 0.068
REMARK 500 GLU A 910 CD GLU A 910 OE2 0.070
REMARK 500 GLU A 926 CD GLU A 926 OE1 0.071
REMARK 500 GLU A 951 CD GLU A 951 OE2 0.067
REMARK 500 GLU A1009 CD GLU A1009 OE1 0.072
REMARK 500 GLU A1024 CD GLU A1024 OE1 0.078
REMARK 500 GLU A1067 CD GLU A1067 OE1 0.074
REMARK 500 GLU B1510 CD GLU B1510 OE1 0.067
REMARK 500 GLU B1541 CD GLU B1541 OE1 0.066
REMARK 500 GLU B1645 CD GLU B1645 OE1 0.085
REMARK 500 GLU B1666 CD GLU B1666 OE2 0.081
REMARK 500 GLU B1687 CD GLU B1687 OE1 0.072
REMARK 500 GLU B1726 CD GLU B1726 OE1 0.074
REMARK 500 GLU B1818 CD GLU B1818 OE2 0.081
REMARK 500 GLU B1872 CD GLU B1872 OE2 0.073
REMARK 500 GLU C2059 CD GLU C2059 OE1 0.077
REMARK 500 GLU C2067 CD GLU C2067 OE1 0.067
REMARK 500 GLU C2079 CD GLU C2079 OE1 0.067
REMARK 500 GLU C2109 CD GLU C2109 OE1 0.081
REMARK 500
REMARK 500 THIS ENTRY HAS 191 BOND DEVIATIONS.
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 6 CB - CG - OD1 ANGL. DEV. = -8.0 DEGREES
REMARK 500 ASP A 6 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP A 27 CB - CG - OD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ASP A 121 CB - CG - OD1 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ASP A 124 CB - CG - OD1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ASP A 124 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ARG A 129 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 131 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 MET A 136 CG - SD - CE ANGL. DEV. = 9.8 DEGREES
REMARK 500 ASP A 161 CB - CG - OD1 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ARG A 194 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG A 194 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 LEU A 204 CB - CA - C ANGL. DEV. = -13.3 DEGREES
REMARK 500 ASP A 223 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP A 223 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ASP A 226 CB - CG - OD1 ANGL. DEV. = -5.6 DEGREES
REMARK 500 VAL A 297 CA - CB - CG1 ANGL. DEV. = -9.1 DEGREES
REMARK 500 ARG A 361 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ASP A 372 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ARG A 400 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG A 400 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ASP A 410 CB - CG - OD1 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ASP A 416 CB - CG - OD1 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ASP A 416 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ASP A 441 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG A 444 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG A 444 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ASP A 459 CB - CG - OD1 ANGL. DEV. = -7.4 DEGREES
REMARK 500 ASP A 459 CB - CG - OD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ARG A 460 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG A 460 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ASP A 487 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG A 517 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG A 517 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ASP A 530 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP A 539 CB - CG - OD1 ANGL. DEV. = -6.7 DEGREES
REMARK 500 GLU A 560 N - CA - CB ANGL. DEV. = 11.2 DEGREES
REMARK 500 ARG A 571 CD - NE - CZ ANGL. DEV. = -9.1 DEGREES
REMARK 500 ASP A 579 CB - CG - OD1 ANGL. DEV. = -7.6 DEGREES
REMARK 500 ASP A 579 CB - CG - OD2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 ASP A 609 CB - CG - OD1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ASP A 609 CB - CG - OD2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 ASP A 611 CB - CG - OD1 ANGL. DEV. = -6.9 DEGREES
REMARK 500 ASP A 611 CB - CG - OD2 ANGL. DEV. = 7.1 DEGREES
REMARK 500 ARG A 615 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ASP A 625 CB - CG - OD1 ANGL. DEV. = -7.1 DEGREES
REMARK 500 ASP A 625 CB - CG - OD2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 ASP A 667 CB - CG - OD2 ANGL. DEV. = 7.6 DEGREES
REMARK 500 ASP A 670 CB - CG - OD1 ANGL. DEV. = -8.1 DEGREES
REMARK 500 ASP A 670 CB - CG - OD2 ANGL. DEV. = 7.0 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 377 ANGLE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLN A 22 88.58 -152.97
REMARK 500 ALA A 23 -150.89 -119.94
REMARK 500 ALA A 52 25.86 -77.50
REMARK 500 ARG A 82 71.54 46.35
REMARK 500 ASP A 226 7.45 83.22
REMARK 500 THR A 279 57.08 -140.86
REMARK 500 ASN A 292 14.20 -150.43
REMARK 500 ARG A 303 -176.13 -177.31
REMARK 500 VAL A 328 30.03 -97.63
REMARK 500 ASN A 363 40.78 -152.22
REMARK 500 ALA A 368 -87.90 -26.57
REMARK 500 THR A 375 -156.82 -148.24
REMARK 500 ASP A 530 5.47 -152.50
REMARK 500 THR A 531 -14.60 72.68
REMARK 500 ALA A 541 72.62 -104.96
REMARK 500 GLU A 549 -73.29 -72.98
REMARK 500 ASN A 554 58.75 38.82
REMARK 500 CYS A 601 27.60 -141.56
REMARK 500 THR A 646 -72.40 -47.44
REMARK 500 ALA A 693 135.97 -175.10
REMARK 500 THR A 800 -15.93 -143.29
REMARK 500 PRO A 844 44.90 -73.19
REMARK 500 HIS A 975 -82.35 -26.20
REMARK 500 ARG A1020 -54.26 -27.05
REMARK 500 THR B1671 30.23 -142.46
REMARK 500 CYG B1769 -106.06 59.29
REMARK 500 PHE B1788 -15.71 -140.94
REMARK 500 ASN B1811 81.36 -164.56
REMARK 500 ALA B1856 -120.38 52.47
REMARK 500 SER B1857 70.71 53.26
REMARK 500 PRO C2002 -154.64 -84.02
REMARK 500 ALA C2023 -150.55 -122.22
REMARK 500 ALA C2052 43.98 -85.95
REMARK 500 THR C2279 63.38 -150.62
REMARK 500 PRO C2302 43.65 -77.88
REMARK 500 THR C2340 36.08 -91.88
REMARK 500 ASN C2363 37.68 -152.55
REMARK 500 ALA C2368 -68.42 -20.16
REMARK 500 THR C2531 -17.69 74.61
REMARK 500 ALA C2541 76.71 -104.25
REMARK 500 GLU C2548 -166.53 -107.03
REMARK 500 LYS C2686 61.16 61.25
REMARK 500 ILE C2698 -70.76 -55.10
REMARK 500 ARG C2736 -46.22 -28.31
REMARK 500 TYR C2737 -71.91 -66.46
REMARK 500 PHE C2738 -32.32 -37.79
REMARK 500 THR C2800 16.62 -142.80
REMARK 500 HIS C2995 20.48 -76.47
REMARK 500 ASN D3591 132.99 -174.84
REMARK 500 CYG D3769 -98.38 62.12
REMARK 500
REMARK 500 THIS ENTRY HAS 108 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 MET A 55 24.1 L L OUTSIDE RANGE
REMARK 500 GLU A 127 22.6 L L OUTSIDE RANGE
REMARK 500 PHE A 172 23.7 L L OUTSIDE RANGE
REMARK 500 ASP A 197 24.4 L L OUTSIDE RANGE
REMARK 500 ILE A 339 23.2 L L OUTSIDE RANGE
REMARK 500 ARG A 435 20.2 L L OUTSIDE RANGE
REMARK 500 ALA A 651 23.5 L L OUTSIDE RANGE
REMARK 500 GLU A 726 3.0 L L EXPECTING SP3
REMARK 500 TYR A 729 24.4 L L OUTSIDE RANGE
REMARK 500 TYR A 799 24.7 L L OUTSIDE RANGE
REMARK 500 GLN A 821 24.3 L L OUTSIDE RANGE
REMARK 500 VAL A 850 24.2 L L OUTSIDE RANGE
REMARK 500 LYS A 954 23.1 L L OUTSIDE RANGE
REMARK 500 HIS A 975 14.1 L L OUTSIDE RANGE
REMARK 500 VAL A 994 24.9 L L OUTSIDE RANGE
REMARK 500 ASN A1007 24.1 L L OUTSIDE RANGE
REMARK 500 TYR A1036 23.6 L L OUTSIDE RANGE
REMARK 500 TYR B1548 24.0 L L OUTSIDE RANGE
REMARK 500 PRO B1558 24.2 L L OUTSIDE RANGE
REMARK 500 GLU B1571 23.1 L L OUTSIDE RANGE
REMARK 500 ASP B1612 21.1 L L OUTSIDE RANGE
REMARK 500 ASP B1636 22.5 L L OUTSIDE RANGE
REMARK 500 ASN B1704 24.6 L L OUTSIDE RANGE
REMARK 500 GLN B1722 20.8 L L OUTSIDE RANGE
REMARK 500 SER B1739 23.9 L L OUTSIDE RANGE
REMARK 500 VAL B1804 24.7 L L OUTSIDE RANGE
REMARK 500 LYS C2003 21.7 L L OUTSIDE RANGE
REMARK 500 CYS C2024 24.7 L L OUTSIDE RANGE
REMARK 500 ARG C2129 23.1 L L OUTSIDE RANGE
REMARK 500 ILE C2339 17.3 L L OUTSIDE RANGE
REMARK 500 SER C2414 24.9 L L OUTSIDE RANGE
REMARK 500 ARG C2435 24.5 L L OUTSIDE RANGE
REMARK 500 GLU C2478 24.5 L L OUTSIDE RANGE
REMARK 500 VAL C2479 23.3 L L OUTSIDE RANGE
REMARK 500 ALA C2534 24.6 L L OUTSIDE RANGE
REMARK 500 LEU C2861 21.9 L L OUTSIDE RANGE
REMARK 500 MET C2869 22.2 L L OUTSIDE RANGE
REMARK 500 ILE C2884 19.3 L L OUTSIDE RANGE
REMARK 500 HIS C2975 24.6 L L OUTSIDE RANGE
REMARK 500 ILE C3014 24.9 L L OUTSIDE RANGE
REMARK 500 TYR C3036 18.9 L L OUTSIDE RANGE
REMARK 500 ALA D3505 24.1 L L OUTSIDE RANGE
REMARK 500 ASP D3569 21.4 L L OUTSIDE RANGE
REMARK 500 ASP D3636 22.6 L L OUTSIDE RANGE
REMARK 500 SER D3674 18.6 L L OUTSIDE RANGE
REMARK 500 ARG D3712 24.8 L L OUTSIDE RANGE
REMARK 500 SER D3739 24.4 L L OUTSIDE RANGE
REMARK 500 ASP D3862 23.7 L L OUTSIDE RANGE
REMARK 500 THR E4005 22.7 L L OUTSIDE RANGE
REMARK 500 ALA E4023 22.8 L L OUTSIDE RANGE
REMARK 500
REMARK 500 THIS ENTRY HAS 93 CHIRALITY DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2028 DISTANCE = 5.22 ANGSTROMS
REMARK 525 HOH A2097 DISTANCE = 6.37 ANGSTROMS
REMARK 525 HOH A2207 DISTANCE = 5.49 ANGSTROMS
REMARK 525 HOH A2241 DISTANCE = 5.43 ANGSTROMS
REMARK 525 HOH A2254 DISTANCE = 5.36 ANGSTROMS
REMARK 525 HOH A2263 DISTANCE = 5.18 ANGSTROMS
REMARK 525 HOH A2264 DISTANCE = 5.07 ANGSTROMS
REMARK 525 HOH A2276 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH A2277 DISTANCE = 5.27 ANGSTROMS
REMARK 525 HOH A2402 DISTANCE = 5.10 ANGSTROMS
REMARK 525 HOH A2403 DISTANCE = 5.31 ANGSTROMS
REMARK 525 HOH A2412 DISTANCE = 5.10 ANGSTROMS
REMARK 525 HOH A2414 DISTANCE = 6.23 ANGSTROMS
REMARK 525 HOH A2443 DISTANCE = 5.50 ANGSTROMS
REMARK 525 HOH A2488 DISTANCE = 7.15 ANGSTROMS
REMARK 525 HOH A2490 DISTANCE = 5.26 ANGSTROMS
REMARK 525 HOH A2498 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH A2500 DISTANCE = 5.66 ANGSTROMS
REMARK 525 HOH A2506 DISTANCE = 5.03 ANGSTROMS
REMARK 525 HOH A2543 DISTANCE = 5.91 ANGSTROMS
REMARK 525 HOH A2635 DISTANCE = 5.16 ANGSTROMS
REMARK 525 HOH A2637 DISTANCE = 5.47 ANGSTROMS
REMARK 525 HOH A2639 DISTANCE = 6.22 ANGSTROMS
REMARK 525 HOH A2664 DISTANCE = 5.46 ANGSTROMS
REMARK 525 HOH A2667 DISTANCE = 6.51 ANGSTROMS
REMARK 525 HOH A2697 DISTANCE = 5.30 ANGSTROMS
REMARK 525 HOH A2725 DISTANCE = 5.80 ANGSTROMS
REMARK 525 HOH A2767 DISTANCE = 5.46 ANGSTROMS
REMARK 525 HOH A2787 DISTANCE = 7.38 ANGSTROMS
REMARK 525 HOH A2821 DISTANCE = 5.03 ANGSTROMS
REMARK 525 HOH A2836 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH B2048 DISTANCE = 5.12 ANGSTROMS
REMARK 525 HOH B2095 DISTANCE = 6.08 ANGSTROMS
REMARK 525 HOH B2109 DISTANCE = 5.08 ANGSTROMS
REMARK 525 HOH B2125 DISTANCE = 5.43 ANGSTROMS
REMARK 525 HOH B2132 DISTANCE = 5.36 ANGSTROMS
REMARK 525 HOH B2146 DISTANCE = 5.33 ANGSTROMS
REMARK 525 HOH B2157 DISTANCE = 5.91 ANGSTROMS
REMARK 525 HOH C4027 DISTANCE = 5.26 ANGSTROMS
REMARK 525 HOH C4095 DISTANCE = 6.30 ANGSTROMS
REMARK 525 HOH C4100 DISTANCE = 5.21 ANGSTROMS
REMARK 525 HOH C4250 DISTANCE = 5.36 ANGSTROMS
REMARK 525 HOH C4259 DISTANCE = 5.15 ANGSTROMS
REMARK 525 HOH C4260 DISTANCE = 5.99 ANGSTROMS
REMARK 525 HOH C4270 DISTANCE = 6.97 ANGSTROMS
REMARK 525 HOH C4410 DISTANCE = 5.06 ANGSTROMS
REMARK 525 HOH C4441 DISTANCE = 5.32 ANGSTROMS
REMARK 525 HOH C4481 DISTANCE = 7.42 ANGSTROMS
REMARK 525 HOH C4482 DISTANCE = 6.23 ANGSTROMS
REMARK 525 HOH C4490 DISTANCE = 5.75 ANGSTROMS
REMARK 525 HOH C4491 DISTANCE = 5.61 ANGSTROMS
REMARK 525 HOH C4493 DISTANCE = 5.12 ANGSTROMS
REMARK 525 HOH C4536 DISTANCE = 5.20 ANGSTROMS
REMARK 525 HOH C4568 DISTANCE = 5.15 ANGSTROMS
REMARK 525 HOH C4603 DISTANCE = 5.66 ANGSTROMS
REMARK 525 HOH C4621 DISTANCE = 7.32 ANGSTROMS
REMARK 525 HOH C4630 DISTANCE = 5.49 ANGSTROMS
REMARK 525 HOH C4645 DISTANCE = 8.14 ANGSTROMS
REMARK 525 HOH C4653 DISTANCE = 6.49 ANGSTROMS
REMARK 525 HOH C4654 DISTANCE = 5.62 ANGSTROMS
REMARK 525 HOH C4657 DISTANCE = 9.05 ANGSTROMS
REMARK 525 HOH C4658 DISTANCE = 5.02 ANGSTROMS
REMARK 525 HOH C4683 DISTANCE = 6.79 ANGSTROMS
REMARK 525 HOH C4686 DISTANCE = 5.70 ANGSTROMS
REMARK 525 HOH C4688 DISTANCE = 5.03 ANGSTROMS
REMARK 525 HOH C4705 DISTANCE = 6.59 ANGSTROMS
REMARK 525 HOH C4732 DISTANCE = 5.20 ANGSTROMS
REMARK 525 HOH C4781 DISTANCE = 5.22 ANGSTROMS
REMARK 525 HOH C4784 DISTANCE = 7.26 ANGSTROMS
REMARK 525 HOH C4786 DISTANCE = 5.09 ANGSTROMS
REMARK 525 HOH C4787 DISTANCE = 5.74 ANGSTROMS
REMARK 525 HOH C4794 DISTANCE = 5.08 ANGSTROMS
REMARK 525 HOH C4819 DISTANCE = 7.41 ANGSTROMS
REMARK 525 HOH C4823 DISTANCE = 5.30 ANGSTROMS
REMARK 525 HOH C4830 DISTANCE = 5.76 ANGSTROMS
REMARK 525 HOH D3957 DISTANCE = 6.10 ANGSTROMS
REMARK 525 HOH D3982 DISTANCE = 5.02 ANGSTROMS
REMARK 525 HOH D4047 DISTANCE = 5.17 ANGSTROMS
REMARK 525 HOH D4099 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH D4109 DISTANCE = 5.36 ANGSTROMS
REMARK 525 HOH D4181 DISTANCE = 5.37 ANGSTROMS
REMARK 525 HOH D4182 DISTANCE = 7.16 ANGSTROMS
REMARK 525 HOH D4218 DISTANCE = 6.20 ANGSTROMS
REMARK 525 HOH D4219 DISTANCE = 6.06 ANGSTROMS
REMARK 525 HOH D4252 DISTANCE = 5.65 ANGSTROMS
REMARK 525 HOH E5983 DISTANCE = 6.13 ANGSTROMS
REMARK 525 HOH E6030 DISTANCE = 5.06 ANGSTROMS
REMARK 525 HOH E6099 DISTANCE = 6.35 ANGSTROMS
REMARK 525 HOH E6105 DISTANCE = 5.14 ANGSTROMS
REMARK 525 HOH E6158 DISTANCE = 5.49 ANGSTROMS
REMARK 525 HOH E6162 DISTANCE = 5.03 ANGSTROMS
REMARK 525 HOH E6244 DISTANCE = 5.28 ANGSTROMS
REMARK 525 HOH E6257 DISTANCE = 5.20 ANGSTROMS
REMARK 525 HOH E6265 DISTANCE = 5.08 ANGSTROMS
REMARK 525 HOH E6278 DISTANCE = 6.83 ANGSTROMS
REMARK 525 HOH E6279 DISTANCE = 5.27 ANGSTROMS
REMARK 525 HOH E6414 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH E6416 DISTANCE = 5.66 ANGSTROMS
REMARK 525 HOH E6438 DISTANCE = 5.23 ANGSTROMS
REMARK 525 HOH E6448 DISTANCE = 5.52 ANGSTROMS
REMARK 525 HOH E6455 DISTANCE = 5.09 ANGSTROMS
REMARK 525 HOH E6487 DISTANCE = 5.19 ANGSTROMS
REMARK 525 HOH E6494 DISTANCE = 5.53 ANGSTROMS
REMARK 525 HOH E6495 DISTANCE = 5.21 ANGSTROMS
REMARK 525 HOH E6504 DISTANCE = 6.14 ANGSTROMS
REMARK 525 HOH E6539 DISTANCE = 5.16 ANGSTROMS
REMARK 525 HOH E6549 DISTANCE = 5.30 ANGSTROMS
REMARK 525 HOH E6587 DISTANCE = 5.08 ANGSTROMS
REMARK 525 HOH E6615 DISTANCE = 5.48 ANGSTROMS
REMARK 525 HOH E6639 DISTANCE = 5.05 ANGSTROMS
REMARK 525 HOH E6640 DISTANCE = 7.40 ANGSTROMS
REMARK 525 HOH E6659 DISTANCE = 7.75 ANGSTROMS
REMARK 525 HOH E6683 DISTANCE = 6.60 ANGSTROMS
REMARK 525 HOH E6715 DISTANCE = 5.38 ANGSTROMS
REMARK 525 HOH E6728 DISTANCE = 5.42 ANGSTROMS
REMARK 525 HOH E6789 DISTANCE = 5.47 ANGSTROMS
REMARK 525 HOH E6797 DISTANCE = 5.32 ANGSTROMS
REMARK 525 HOH E6872 DISTANCE = 5.37 ANGSTROMS
REMARK 525 HOH E6873 DISTANCE = 6.91 ANGSTROMS
REMARK 525 HOH E6874 DISTANCE = 8.12 ANGSTROMS
REMARK 525 HOH E6875 DISTANCE = 6.95 ANGSTROMS
REMARK 525 HOH F2361 DISTANCE = 6.36 ANGSTROMS
REMARK 525 HOH F2721 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH F2747 DISTANCE = 5.51 ANGSTROMS
REMARK 525 HOH F3055 DISTANCE = 5.50 ANGSTROMS
REMARK 525 HOH F3056 DISTANCE = 6.59 ANGSTROMS
REMARK 525 HOH F3235 DISTANCE = 7.83 ANGSTROMS
REMARK 525 HOH F3286 DISTANCE = 5.64 ANGSTROMS
REMARK 525 HOH G 112 DISTANCE = 6.55 ANGSTROMS
REMARK 525 HOH G 120 DISTANCE = 5.15 ANGSTROMS
REMARK 525 HOH G 278 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH G 291 DISTANCE = 5.80 ANGSTROMS
REMARK 525 HOH G 306 DISTANCE = 6.48 ANGSTROMS
REMARK 525 HOH G 315 DISTANCE = 6.41 ANGSTROMS
REMARK 525 HOH G 316 DISTANCE = 5.47 ANGSTROMS
REMARK 525 HOH G 451 DISTANCE = 5.32 ANGSTROMS
REMARK 525 HOH G 537 DISTANCE = 6.59 ANGSTROMS
REMARK 525 HOH G 539 DISTANCE = 5.25 ANGSTROMS
REMARK 525 HOH G 643 DISTANCE = 5.33 ANGSTROMS
REMARK 525 HOH G 646 DISTANCE = 5.35 ANGSTROMS
REMARK 525 HOH G 674 DISTANCE = 5.67 ANGSTROMS
REMARK 525 HOH G 676 DISTANCE = 6.88 ANGSTROMS
REMARK 525 HOH G 688 DISTANCE = 5.78 ANGSTROMS
REMARK 525 HOH G 698 DISTANCE = 5.52 ANGSTROMS
REMARK 525 HOH G 700 DISTANCE = 5.03 ANGSTROMS
REMARK 525 HOH G 758 DISTANCE = 5.08 ANGSTROMS
REMARK 525 HOH G 765 DISTANCE = 5.74 ANGSTROMS
REMARK 525 HOH G 847 DISTANCE = 6.37 ANGSTROMS
REMARK 525 HOH G 852 DISTANCE = 5.30 ANGSTROMS
REMARK 525 HOH G 919 DISTANCE = 6.01 ANGSTROMS
REMARK 525 HOH H 532 DISTANCE = 5.15 ANGSTROMS
REMARK 525 HOH H 818 DISTANCE = 8.25 ANGSTROMS
REMARK 525 HOH H 832 DISTANCE = 5.36 ANGSTROMS
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 MN A1902 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP A1900 O1A
REMARK 620 2 GLU A 299 OE2 84.6
REMARK 620 3 ADP A1900 O1B 88.6 99.0
REMARK 620 4 GLN A 285 OE1 96.0 72.8 170.1
REMARK 620 5 PO4 A1906 O2 168.8 86.3 86.3 87.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A1901 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A2674 O
REMARK 620 2 GLU A 299 OE1 92.5
REMARK 620 3 GLU A 299 OE2 147.1 54.6
REMARK 620 4 ADP A1900 O3B 91.4 82.3 84.4
REMARK 620 5 ASN A 301 OD1 87.1 91.3 93.4 173.4
REMARK 620 6 PO4 A1906 O1 118.5 148.5 94.3 100.9 85.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A1903 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 215 OE1
REMARK 620 2 ALA A 239 O 92.5
REMARK 620 3 ILE A 242 O 83.2 85.9
REMARK 620 4 ASN A 236 OD1 85.9 150.4 123.1
REMARK 620 5 ASP A 238 O 123.8 67.7 141.4 88.8
REMARK 620 6 SER A 247 OG 138.4 116.6 70.9 82.0 95.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A1904 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 127 OE2
REMARK 620 2 HOH A2081 O 144.1
REMARK 620 3 HOH A2085 O 70.0 118.2
REMARK 620 4 HOH A2674 O 64.7 150.9 57.8
REMARK 620 5 ALA A 126 O 92.9 54.8 88.1 143.4
REMARK 620 6 MET A 300 O 95.9 68.7 163.9 124.0 84.8
REMARK 620 7 GLU A 299 OE1 130.9 82.4 106.6 72.7 136.1 88.3
REMARK 620 8 ASN A 301 OD1 76.2 124.3 110.9 53.4 152.4 71.4 58.9
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A1911 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 829 OE1
REMARK 620 2 GLU A 841 OE2 87.0
REMARK 620 3 ADP A1910 O3B 177.0 93.6
REMARK 620 4 ADP A1910 O2A 88.4 85.1 88.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A1912 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 841 OE2
REMARK 620 2 ADP A1910 O3B 60.5
REMARK 620 3 HOH A2561 O 87.4 46.8
REMARK 620 4 ADP A1910 O2B 79.9 43.0 81.3
REMARK 620 5 HOH A2791 O 143.1 89.3 85.9 63.2
REMARK 620 6 GLU A 841 OE1 46.6 88.8 130.7 75.0 118.7
REMARK 620 7 ASN A 843 OD1 76.1 134.3 122.6 144.6 136.4 69.6
REMARK 620 8 HOH A2789 O 133.0 161.4 115.8 140.5 81.9 109.9 56.9
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A1913 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 783 O
REMARK 620 2 GLN A 784 O 66.4
REMARK 620 3 VAL A 787 O 138.0 84.3
REMARK 620 4 SER A 792 OG 98.3 124.8 73.7
REMARK 620 5 GLU A 761 OE1 132.4 94.9 76.9 126.5
REMARK 620 6 HIS A 781 ND1 94.1 145.7 124.9 84.2 77.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A1940 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 84 O
REMARK 620 2 GLY A 112 O 81.2
REMARK 620 3 THR A 114 N 47.8 69.7
REMARK 620 4 THR A 114 OG1 86.3 104.2 49.2
REMARK 620 5 HOH A2426 O 90.0 166.4 111.6 85.3
REMARK 620 6 HOH A2615 O 129.5 149.3 129.2 82.0 40.3
REMARK 620 7 HOH A2628 O 148.1 83.0 100.5 71.0 109.5 70.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A1942 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 283 OD1
REMARK 620 2 GLN A 285 OE1 75.1
REMARK 620 3 PO4 A1906 O2 91.1 58.5
REMARK 620 4 HOH A2124 O 87.2 134.0 80.2
REMARK 620 5 GLU A 217 OE1 95.7 127.1 172.2 96.2
REMARK 620 6 THR A 244 OG1 169.1 95.8 89.1 103.6 85.0
REMARK 620 7 HOH A2125 O 145.0 133.8 91.1 58.9 81.1 45.9
REMARK 620 8 ASN A 283 ND2 38.2 106.3 126.4 81.0 59.3 144.3 119.9
REMARK 620 9 SER A 307 OG 100.6 170.3 130.8 53.3 44.0 87.5 53.7 66.7
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A1943 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A2479 O
REMARK 620 2 THR A 143 OG1 121.3
REMARK 620 3 ALA A 144 O 81.2 69.9
REMARK 620 4 HOH A2478 O 57.8 63.6 57.3
REMARK 620 5 THR A 143 O 143.2 62.3 65.4 110.5
REMARK 620 6 HOH A2477 O 145.2 75.9 133.2 130.0 70.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B1941 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B1612 O
REMARK 620 2 HOH A2417 O 75.5
REMARK 620 3 HIS B1516 O 101.0 119.8
REMARK 620 4 HOH A2288 O 114.7 76.4 143.9
REMARK 620 5 HOH B1977 O 147.9 136.6 64.5 81.7
REMARK 620 6 HOH B1984 O 143.7 75.8 74.9 79.2 63.5
REMARK 620 7 HOH B2143 O 94.3 149.1 90.6 82.0 59.2 121.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN C3902 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP C3900 O1A
REMARK 620 2 GLU C2299 OE2 89.6
REMARK 620 3 GLN C2285 OE1 103.9 70.5
REMARK 620 4 PO4 C3906 O2 164.0 83.3 87.3
REMARK 620 5 ADP C3900 O1B 84.2 101.7 168.4 83.2
REMARK 620 6 HOH C4661 O 92.7 164.0 93.6 98.1 94.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN C3901 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C4447 O
REMARK 620 2 ASN C2301 OD1 84.2
REMARK 620 3 PO4 C3906 O1 107.1 93.2
REMARK 620 4 GLU C2299 OE2 153.5 85.7 97.9
REMARK 620 5 GLU C2299 OE1 96.1 82.7 155.9 58.3
REMARK 620 6 ADP C3900 O3B 90.8 167.6 99.1 93.9 86.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K C3903 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C2238 O
REMARK 620 2 ALA C2239 O 67.9
REMARK 620 3 GLU C2215 OE1 122.0 94.3
REMARK 620 4 ASN C2236 OD1 90.6 150.4 79.7
REMARK 620 5 SER C2247 OG 96.3 118.8 137.4 82.3
REMARK 620 6 ILE C2242 O 143.4 86.3 84.0 121.3 73.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K C3904 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA C2126 O
REMARK 620 2 GLU C2127 OE2 87.9
REMARK 620 3 GLU C2299 OE1 140.0 131.3
REMARK 620 4 MET C2300 O 83.4 95.7 97.8
REMARK 620 5 HOH C4079 O 54.6 139.3 88.8 67.5
REMARK 620 6 HOH C4632 O 61.9 95.2 101.1 143.1 81.4
REMARK 620 7 HOH C4083 O 90.7 67.5 97.2 162.5 121.7 40.5
REMARK 620 8 HOH C4447 O 139.4 67.8 67.4 129.2 151.3 87.5 50.5
REMARK 620 9 ASN C2301 OD1 154.5 80.6 58.5 75.3 125.9 141.4 105.4 55.2
REMARK 620 10 MN C3901 MN 168.8 95.9 35.4 106.6 124.0 107.2 81.1 35.9
REMARK 620 36.6
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 620 9
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN C3911 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C2841 OE2
REMARK 620 2 ADP C3910 O3B 101.3
REMARK 620 3 GLN C2829 OE1 87.8 160.0
REMARK 620 4 GLN C2829 NE2 73.8 148.0 51.7
REMARK 620 5 HOH C4825 O 86.8 97.0 101.4 51.7
REMARK 620 6 ADP C3910 O2A 90.9 83.3 78.7 127.7 177.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K C3912 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C2841 OE1
REMARK 620 2 GLU C2841 OE2 42.1
REMARK 620 3 ASN C2843 OD1 67.2 63.0
REMARK 620 4 ADP C3910 O3B 79.0 56.1 116.5
REMARK 620 5 ADP C3910 O2B 81.0 90.1 147.7 48.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K C3913 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL C2787 O
REMARK 620 2 HIS C2781 ND1 123.7
REMARK 620 3 GLU C2761 OE1 79.0 79.8
REMARK 620 4 GLU C2783 O 135.7 96.1 131.6
REMARK 620 5 GLN C2784 O 82.7 149.3 91.8 67.5
REMARK 620 6 SER C2792 OG 70.5 86.2 130.9 96.4 120.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K C3940 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR C2114 OG1
REMARK 620 2 HOH C4424 O 68.6
REMARK 620 3 ASP C2084 O 87.5 111.4
REMARK 620 4 GLY C2112 O 104.2 168.6 76.3
REMARK 620 5 THR C2114 N 53.5 113.3 44.3 65.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K C3942 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN C2283 ND2
REMARK 620 2 HOH C4123 O 113.8
REMARK 620 3 PO4 C3906 O2 130.4 92.4
REMARK 620 4 GLN C2285 OE1 114.5 130.2 64.7
REMARK 620 5 HOH C4122 O 74.4 60.5 84.7 146.5
REMARK 620 6 THR C2244 OG1 142.8 39.7 83.6 91.9 98.2
REMARK 620 7 ASN C2283 OD1 40.3 154.0 107.5 74.7 103.8 156.0
REMARK 620 8 GLU C2217 OE1 65.4 75.8 163.8 114.7 98.5 80.2 87.3
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K C3943 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR C2143 O
REMARK 620 2 HOH C4473 O 73.2
REMARK 620 3 HOH C4648 O 111.4 109.9
REMARK 620 4 THR C2143 OG1 64.7 74.2 173.8
REMARK 620 5 HOH C4640 O 134.6 86.7 113.7 70.8
REMARK 620 6 HOH C4475 O 135.3 151.4 62.1 116.7 73.7
REMARK 620 7 ALA C2144 O 61.2 130.4 104.1 69.8 111.4 77.1
REMARK 620 8 HOH C4474 O 104.8 128.3 117.9 60.2 57.6 56.6 54.4
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K D3941 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D3516 O
REMARK 620 2 HOH C4414 O 104.3
REMARK 620 3 HOH D3986 O 70.5 77.3
REMARK 620 4 ASP D3612 O 86.7 93.5 152.0
REMARK 620 5 HOH C4283 O 145.2 85.7 79.7 126.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN E5901 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E4299 OE1
REMARK 620 2 GLU E4299 OE2 54.8
REMARK 620 3 HOH E6698 O 93.5 148.3
REMARK 620 4 ADP E5900 O3B 83.5 85.4 91.5
REMARK 620 5 PO4 E5906 O1 148.3 95.2 115.9 106.2
REMARK 620 6 ASN E4301 OD1 84.7 90.5 85.9 167.7 85.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN E5902 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP E5900 O1A
REMARK 620 2 PO4 E5906 O2 169.3
REMARK 620 3 GLU E4299 OE2 85.0 87.9
REMARK 620 4 GLN E4285 OE1 98.2 87.3 72.7
REMARK 620 5 ADP E5900 O1B 89.1 84.2 99.8 169.0
REMARK 620 6 HOH E6707 O 90.2 98.5 166.3 95.3 92.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K E5903 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E4238 O
REMARK 620 2 ALA E4239 O 68.0
REMARK 620 3 SER E4247 OG 96.7 121.9
REMARK 620 4 GLU E4215 OE1 130.4 94.9 129.8
REMARK 620 5 ASN E4236 OD1 92.9 152.5 78.3 82.6
REMARK 620 6 ILE E4242 O 139.8 88.6 67.6 81.8 117.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K E5904 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E4127 OE2
REMARK 620 2 GLU E4299 OE1 132.3
REMARK 620 3 HOH E6087 O 71.0 106.0
REMARK 620 4 ALA E4126 O 88.2 139.1 79.0
REMARK 620 5 HOH E6083 O 143.3 84.1 107.3 56.4
REMARK 620 6 ASN E4301 OD1 82.4 55.4 115.9 158.1 126.4
REMARK 620 7 HOH E6698 O 67.3 69.0 64.5 140.8 146.9 51.5
REMARK 620 8 MET E4300 O 99.2 87.9 166.1 91.2 74.5 71.0 121.6
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN E5911 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN E4829 OE1
REMARK 620 2 ADP E5910 O3B 169.1
REMARK 620 3 GLU E4841 OE2 86.9 82.4
REMARK 620 4 ADP E5910 O2A 91.0 91.3 92.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K E5912 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E4841 OE1
REMARK 620 2 GLU E4841 OE2 45.6
REMARK 620 3 ADP E5910 O2B 87.7 83.6
REMARK 620 4 ADP E5910 O3B 86.8 52.3 46.6
REMARK 620 5 ASN E4843 OD1 64.4 71.5 151.0 119.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K E5913 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E4781 ND1
REMARK 620 2 GLU E4783 O 94.4
REMARK 620 3 SER E4792 OG 83.2 103.4
REMARK 620 4 GLU E4761 OE1 78.4 123.2 130.6
REMARK 620 5 GLN E4784 O 145.9 64.6 126.2 90.7
REMARK 620 6 VAL E4787 O 120.7 142.7 71.4 79.5 88.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K E5940 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR E4114 N
REMARK 620 2 THR E4114 OG1 49.0
REMARK 620 3 HOH E6628 O 132.9 159.1
REMARK 620 4 HOH E6431 O 119.0 82.6 80.2
REMARK 620 5 GLY E4112 O 67.7 110.6 84.7 163.5
REMARK 620 6 ASP E4084 O 49.2 82.6 88.0 97.9 74.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K E5942 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN E4283 OD1
REMARK 620 2 ASN E4283 ND2 38.0
REMARK 620 3 HOH E6128 O 83.0 76.1
REMARK 620 4 THR E4244 OG1 172.6 143.0 104.4
REMARK 620 5 GLN E4285 OE1 80.1 110.7 136.6 94.3
REMARK 620 6 MN E5902 MN 101.7 139.1 113.4 75.7 34.6
REMARK 620 7 PO4 E5906 O2 97.0 130.0 78.4 84.9 64.5 35.1
REMARK 620 8 GLU E4217 OE1 97.8 61.3 92.8 81.8 128.9 148.8 161.7
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K E5943 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR E4143 OG1
REMARK 620 2 HOH E6485 O 127.4
REMARK 620 3 HOH E6483 O 75.1 151.3
REMARK 620 4 ALA E4144 O 75.9 79.5 127.4
REMARK 620 5 THR E4143 O 65.0 139.1 62.5 65.6
REMARK 620 6 HOH E6484 O 68.4 60.4 142.8 49.3 105.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K F5941 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH E6291 O
REMARK 620 2 ASP F5612 O 117.6
REMARK 620 3 HOH E6419 O 76.3 81.4
REMARK 620 4 HIS F5516 O 147.2 94.1 119.6
REMARK 620 5 HOH F2588 O 78.4 153.8 82.9 75.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN G7901 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP G7900 O3B
REMARK 620 2 PO4 G7906 O1 106.8
REMARK 620 3 ASN G6301 OD1 166.0 87.0
REMARK 620 4 GLU G6299 OE2 90.1 93.3 86.4
REMARK 620 5 GLU G6299 OE1 78.3 148.7 88.6 55.5
REMARK 620 6 HOH G 851 O 87.8 124.6 86.4 141.0 86.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN G7902 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP G7900 O1B
REMARK 620 2 HOH G 874 O 98.9
REMARK 620 3 ADP G7900 O1A 87.7 100.8
REMARK 620 4 PO4 G7906 O2 84.1 87.8 168.9
REMARK 620 5 GLU G6299 OE2 96.3 162.6 88.1 85.6
REMARK 620 6 GLN G6285 OE1 173.7 81.0 98.5 89.7 82.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K G7903 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA G6239 O
REMARK 620 2 ASN G6236 OD1 151.5
REMARK 620 3 SER G6247 OG 120.0 83.7
REMARK 620 4 GLU G6215 OE1 90.0 81.4 135.6
REMARK 620 5 ASP G6238 O 67.8 94.9 98.4 124.3
REMARK 620 6 ILE G6242 O 85.9 120.4 65.3 87.2 137.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K G7904 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH G 96 O
REMARK 620 2 GLU G6127 OE2 136.7
REMARK 620 3 MET G6300 O 68.6 94.2
REMARK 620 4 GLU G6299 OE1 87.8 134.1 93.3
REMARK 620 5 ASN G6301 OD1 125.0 82.0 72.0 57.7
REMARK 620 6 HOH G 851 O 153.6 67.1 129.4 73.3 59.4
REMARK 620 7 ALA G6126 O 53.7 86.3 84.4 139.5 152.7 136.4
REMARK 620 8 HOH G 100 O 118.2 71.4 164.7 100.5 109.9 50.5 89.3
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN G7911 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP G7910 O3B
REMARK 620 2 ADP G7910 O2A 87.4
REMARK 620 3 GLU G6841 OE2 85.8 80.9
REMARK 620 4 GLN G6829 OE1 159.8 87.9 74.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K G7912 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU G6841 OE2
REMARK 620 2 ADP G7910 O3B 53.0
REMARK 620 3 GLU G6841 OE1 43.9 83.5
REMARK 620 4 ADP G7910 O2B 81.8 47.7 79.6
REMARK 620 5 ASN G6843 OD1 77.8 126.1 72.9 152.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K G7913 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER G6792 OG
REMARK 620 2 GLN G6784 O 125.0
REMARK 620 3 VAL G6787 O 67.0 84.3
REMARK 620 4 GLU G6783 O 98.1 68.5 133.4
REMARK 620 5 GLU G6761 OE1 125.2 93.0 81.7 134.6
REMARK 620 6 HIS G6781 ND1 83.2 149.7 120.6 99.5 75.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K G7940 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR G6114 OG1
REMARK 620 2 GLY G6112 O 108.7
REMARK 620 3 HOH G 835 O 165.6 81.7
REMARK 620 4 ASP G6084 O 78.5 77.5 94.7
REMARK 620 5 HOH G 626 O 75.5 166.7 96.6 115.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K G7942 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH G 143 O
REMARK 620 2 THR G6244 OG1 108.4
REMARK 620 3 HOH G 144 O 65.1 44.9
REMARK 620 4 ASN G6283 OD1 92.7 158.8 155.3
REMARK 620 5 GLN G6285 OE1 144.8 84.5 127.0 77.4
REMARK 620 6 PO4 G7906 O2 86.1 87.0 95.4 93.7 61.3
REMARK 620 7 HOH G 874 O 123.6 43.9 80.7 122.6 46.7 52.6
REMARK 620 8 SER G6307 OG 56.0 89.9 56.1 103.2 159.0 138.6 133.4
REMARK 620 9 ASN G6283 ND2 88.1 140.3 125.5 38.0 102.7 131.0 147.1 69.4
REMARK 620 10 GLU G6217 OE1 103.4 79.8 79.3 96.5 111.3 165.7 113.1 47.8
REMARK 620 61.0
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 620 9
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K G7943 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH G 677 O
REMARK 620 2 HOH G 678 O 126.2
REMARK 620 3 HOH G 679 O 154.4 51.4
REMARK 620 4 ALA G6144 O 128.2 56.1 74.2
REMARK 620 5 THR G6143 O 68.9 111.3 136.7 65.3
REMARK 620 6 THR G6143 OG1 71.3 61.6 113.1 69.5 66.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K H7941 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP H7612 O
REMARK 620 2 HIS H7516 O 86.5
REMARK 620 3 HOH G 549 O 89.5 122.5
REMARK 620 4 HOH H 468 O 151.7 79.0 78.2
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ADP BINDING SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ADP BINDING SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: OR1
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ORNITHINE BINDING SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: CY1
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR GLUTAMYL THIOESTERMEDIATE IN
REMARK 800 SMALL SUBUNIT.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ADP BINDING SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ADP BINDING SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: OR2
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ORNITHINE BINDING SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: CY2
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR GLUTAMYL THIOESTERMEDIATE IN
REMARK 800 SMALL SUBUNIT.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ADP BINDING SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ADP BINDING SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: OR3
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ORNITHINE BINDING SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: CY3
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR GLUTAMYL THIOESTERMEDIATE IN
REMARK 800 SMALL SUBUNIT.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ADP BINDING SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ADP BINDING SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: OR4
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ORNITHINE BINDING SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: CY4
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR GLUTAMYL THIOESTERMEDIATE IN
REMARK 800 SMALL SUBUNIT.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN G 7901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN G 7902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 7903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 7904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 G 7906
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN G 7911
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 7912
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 7913
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 7930
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 7931
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 7932
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL H 7933
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 7934
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 7935
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 7936
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 7940
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K H 7941
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 7942
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 7943
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1981
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1982
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 3901
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 3902
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 3903
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 3904
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 3906
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 3911
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 3912
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 3913
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 3930
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 3931
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 3932
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 3933
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 3934
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 3935
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 3936
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 3940
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K D 3941
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 3942
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 3943
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 3980
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 3981
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 3982
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 5901
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 5902
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 5903
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 5904
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 E 5906
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 5911
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 5912
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 5913
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 5930
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 5931
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 5932
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL F 5933
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 5934
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 5935
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 5936
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 5940
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K F 5941
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 5942
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 5943
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 E 5980
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 E 5981
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 G 7980
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 G 7981
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 G 7982
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 1901
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 1902
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 1903
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 1904
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1906
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 1911
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 1912
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 1913
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1930
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1931
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1932
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 1933
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1934
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1935
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1936
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 1940
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 1941
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 1942
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 1943
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP G 7900
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP G 7910
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORN G 7920
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NET G 7950
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 3900
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 3910
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORN C 3920
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NET C 3950
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP E 5900
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP E 5910
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORN E 5920
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NET E 5950
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 1900
REMARK 800
REMARK 800 SITE_IDENTIFIER: LC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 1910
REMARK 800
REMARK 800 SITE_IDENTIFIER: LC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORN A 1920
REMARK 800
REMARK 800 SITE_IDENTIFIER: LC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NET A 1950
DBREF 1A9X A 2 1073 UNP P00968 CARB_ECOLI 1 1072
DBREF 1A9X B 1502 1880 UNP P00907 CARA_ECOLI 2 380
DBREF 1A9X C 2002 3073 UNP P00968 CARB_ECOLI 1 1072
DBREF 1A9X D 3502 3880 UNP P00907 CARA_ECOLI 2 380
DBREF 1A9X E 4002 5073 UNP P00968 CARB_ECOLI 1 1072
DBREF 1A9X F 5502 5880 UNP P00907 CARA_ECOLI 2 380
DBREF 1A9X G 6002 7073 UNP P00968 CARB_ECOLI 1 1072
DBREF 1A9X H 7502 7880 UNP P00907 CARA_ECOLI 2 380
SEQADV 1A9X ASN A 46 UNP P00968 LEU 45 CONFLICT
SEQADV 1A9X ALA A 716 UNP P00968 PRO 715 CONFLICT
SEQADV 1A9X GLN B 1683 UNP P00907 GLU 183 CONFLICT
SEQADV 1A9X CYG B 1769 UNP P00907 CYS 269 MODIFIED
SEQADV 1A9X ASN B 1853 UNP P00907 HIS 353 MUTATION
SEQADV 1A9X ASN C 2046 UNP P00968 LEU 45 CONFLICT
SEQADV 1A9X ALA C 2716 UNP P00968 PRO 715 CONFLICT
SEQADV 1A9X GLN D 3683 UNP P00907 GLU 183 CONFLICT
SEQADV 1A9X CYG D 3769 UNP P00907 CYS 269 MODIFIED
SEQADV 1A9X ASN D 3853 UNP P00907 HIS 353 MUTATION
SEQADV 1A9X ASN E 4046 UNP P00968 LEU 45 CONFLICT
SEQADV 1A9X ALA E 4716 UNP P00968 PRO 715 CONFLICT
SEQADV 1A9X GLN F 5683 UNP P00907 GLU 183 CONFLICT
SEQADV 1A9X CYG F 5769 UNP P00907 CYS 269 MODIFIED
SEQADV 1A9X ASN F 5853 UNP P00907 HIS 353 MUTATION
SEQADV 1A9X ASN G 6046 UNP P00968 LEU 45 CONFLICT
SEQADV 1A9X ALA G 6716 UNP P00968 PRO 715 CONFLICT
SEQADV 1A9X GLN H 7683 UNP P00907 GLU 183 CONFLICT
SEQADV 1A9X CYG H 7769 UNP P00907 CYS 269 MODIFIED
SEQADV 1A9X ASN H 7853 UNP P00907 HIS 353 MUTATION
SEQRES 1 A 1073 MET PRO LYS ARG THR ASP ILE LYS SER ILE LEU ILE LEU
SEQRES 2 A 1073 GLY ALA GLY PRO ILE VAL ILE GLY GLN ALA CYS GLU PHE
SEQRES 3 A 1073 ASP TYR SER GLY ALA GLN ALA CYS LYS ALA LEU ARG GLU
SEQRES 4 A 1073 GLU GLY TYR ARG VAL ILE ASN VAL ASN SER ASN PRO ALA
SEQRES 5 A 1073 THR ILE MET THR ASP PRO GLU MET ALA ASP ALA THR TYR
SEQRES 6 A 1073 ILE GLU PRO ILE HIS TRP GLU VAL VAL ARG LYS ILE ILE
SEQRES 7 A 1073 GLU LYS GLU ARG PRO ASP ALA VAL LEU PRO THR MET GLY
SEQRES 8 A 1073 GLY GLN THR ALA LEU ASN CYS ALA LEU GLU LEU GLU ARG
SEQRES 9 A 1073 GLN GLY VAL LEU GLU GLU PHE GLY VAL THR MET ILE GLY
SEQRES 10 A 1073 ALA THR ALA ASP ALA ILE ASP LYS ALA GLU ASP ARG ARG
SEQRES 11 A 1073 ARG PHE ASP VAL ALA MET LYS LYS ILE GLY LEU GLU THR
SEQRES 12 A 1073 ALA ARG SER GLY ILE ALA HIS THR MET GLU GLU ALA LEU
SEQRES 13 A 1073 ALA VAL ALA ALA ASP VAL GLY PHE PRO CYS ILE ILE ARG
SEQRES 14 A 1073 PRO SER PHE THR MET GLY GLY SER GLY GLY GLY ILE ALA
SEQRES 15 A 1073 TYR ASN ARG GLU GLU PHE GLU GLU ILE CYS ALA ARG GLY
SEQRES 16 A 1073 LEU ASP LEU SER PRO THR LYS GLU LEU LEU ILE ASP GLU
SEQRES 17 A 1073 SER LEU ILE GLY TRP LYS GLU TYR GLU MET GLU VAL VAL
SEQRES 18 A 1073 ARG ASP LYS ASN ASP ASN CYS ILE ILE VAL CYS SER ILE
SEQRES 19 A 1073 GLU ASN PHE ASP ALA MET GLY ILE HIS THR GLY ASP SER
SEQRES 20 A 1073 ILE THR VAL ALA PRO ALA GLN THR LEU THR ASP LYS GLU
SEQRES 21 A 1073 TYR GLN ILE MET ARG ASN ALA SER MET ALA VAL LEU ARG
SEQRES 22 A 1073 GLU ILE GLY VAL GLU THR GLY GLY SER ASN VAL GLN PHE
SEQRES 23 A 1073 ALA VAL ASN PRO LYS ASN GLY ARG LEU ILE VAL ILE GLU
SEQRES 24 A 1073 MET ASN PRO ARG VAL SER ARG SER SER ALA LEU ALA SER
SEQRES 25 A 1073 LYS ALA THR GLY PHE PRO ILE ALA LYS VAL ALA ALA LYS
SEQRES 26 A 1073 LEU ALA VAL GLY TYR THR LEU ASP GLU LEU MET ASN ASP
SEQRES 27 A 1073 ILE THR GLY GLY ARG THR PRO ALA SER PHE GLU PRO SER
SEQRES 28 A 1073 ILE ASP TYR VAL VAL THR LYS ILE PRO ARG PHE ASN PHE
SEQRES 29 A 1073 GLU LYS PHE ALA GLY ALA ASN ASP ARG LEU THR THR GLN
SEQRES 30 A 1073 MET LYS SER VAL GLY GLU VAL MET ALA ILE GLY ARG THR
SEQRES 31 A 1073 GLN GLN GLU SER LEU GLN LYS ALA LEU ARG GLY LEU GLU
SEQRES 32 A 1073 VAL GLY ALA THR GLY PHE ASP PRO LYS VAL SER LEU ASP
SEQRES 33 A 1073 ASP PRO GLU ALA LEU THR LYS ILE ARG ARG GLU LEU LYS
SEQRES 34 A 1073 ASP ALA GLY ALA ASP ARG ILE TRP TYR ILE ALA ASP ALA
SEQRES 35 A 1073 PHE ARG ALA GLY LEU SER VAL ASP GLY VAL PHE ASN LEU
SEQRES 36 A 1073 THR ASN ILE ASP ARG TRP PHE LEU VAL GLN ILE GLU GLU
SEQRES 37 A 1073 LEU VAL ARG LEU GLU GLU LYS VAL ALA GLU VAL GLY ILE
SEQRES 38 A 1073 THR GLY LEU ASN ALA ASP PHE LEU ARG GLN LEU LYS ARG
SEQRES 39 A 1073 LYS GLY PHE ALA ASP ALA ARG LEU ALA LYS LEU ALA GLY
SEQRES 40 A 1073 VAL ARG GLU ALA GLU ILE ARG LYS LEU ARG ASP GLN TYR
SEQRES 41 A 1073 ASP LEU HIS PRO VAL TYR LYS ARG VAL ASP THR CYS ALA
SEQRES 42 A 1073 ALA GLU PHE ALA THR ASP THR ALA TYR MET TYR SER THR
SEQRES 43 A 1073 TYR GLU GLU GLU CYS GLU ALA ASN PRO SER THR ASP ARG
SEQRES 44 A 1073 GLU LYS ILE MET VAL LEU GLY GLY GLY PRO ASN ARG ILE
SEQRES 45 A 1073 GLY GLN GLY ILE GLU PHE ASP TYR CYS CYS VAL HIS ALA
SEQRES 46 A 1073 SER LEU ALA LEU ARG GLU ASP GLY TYR GLU THR ILE MET
SEQRES 47 A 1073 VAL ASN CYS ASN PRO GLU THR VAL SER THR ASP TYR ASP
SEQRES 48 A 1073 THR SER ASP ARG LEU TYR PHE GLU PRO VAL THR LEU GLU
SEQRES 49 A 1073 ASP VAL LEU GLU ILE VAL ARG ILE GLU LYS PRO LYS GLY
SEQRES 50 A 1073 VAL ILE VAL GLN TYR GLY GLY GLN THR PRO LEU LYS LEU
SEQRES 51 A 1073 ALA ARG ALA LEU GLU ALA ALA GLY VAL PRO VAL ILE GLY
SEQRES 52 A 1073 THR SER PRO ASP ALA ILE ASP ARG ALA GLU ASP ARG GLU
SEQRES 53 A 1073 ARG PHE GLN HIS ALA VAL GLU ARG LEU LYS LEU LYS GLN
SEQRES 54 A 1073 PRO ALA ASN ALA THR VAL THR ALA ILE GLU MET ALA VAL
SEQRES 55 A 1073 GLU LYS ALA LYS GLU ILE GLY TYR PRO LEU VAL VAL ARG
SEQRES 56 A 1073 ALA SER TYR VAL LEU GLY GLY ARG ALA MET GLU ILE VAL
SEQRES 57 A 1073 TYR ASP GLU ALA ASP LEU ARG ARG TYR PHE GLN THR ALA
SEQRES 58 A 1073 VAL SER VAL SER ASN ASP ALA PRO VAL LEU LEU ASP HIS
SEQRES 59 A 1073 PHE LEU ASP ASP ALA VAL GLU VAL ASP VAL ASP ALA ILE
SEQRES 60 A 1073 CYS ASP GLY GLU MET VAL LEU ILE GLY GLY ILE MET GLU
SEQRES 61 A 1073 HIS ILE GLU GLN ALA GLY VAL HIS SER GLY ASP SER ALA
SEQRES 62 A 1073 CYS SER LEU PRO ALA TYR THR LEU SER GLN GLU ILE GLN
SEQRES 63 A 1073 ASP VAL MET ARG GLN GLN VAL GLN LYS LEU ALA PHE GLU
SEQRES 64 A 1073 LEU GLN VAL ARG GLY LEU MET ASN VAL GLN PHE ALA VAL
SEQRES 65 A 1073 LYS ASN ASN GLU VAL TYR LEU ILE GLU VAL ASN PRO ARG
SEQRES 66 A 1073 ALA ALA ARG THR VAL PRO PHE VAL SER LYS ALA THR GLY
SEQRES 67 A 1073 VAL PRO LEU ALA LYS VAL ALA ALA ARG VAL MET ALA GLY
SEQRES 68 A 1073 LYS SER LEU ALA GLU GLN GLY VAL THR LYS GLU VAL ILE
SEQRES 69 A 1073 PRO PRO TYR TYR SER VAL LYS GLU VAL VAL LEU PRO PHE
SEQRES 70 A 1073 ASN LYS PHE PRO GLY VAL ASP PRO LEU LEU GLY PRO GLU
SEQRES 71 A 1073 MET ARG SER THR GLY GLU VAL MET GLY VAL GLY ARG THR
SEQRES 72 A 1073 PHE ALA GLU ALA PHE ALA LYS ALA GLN LEU GLY SER ASN
SEQRES 73 A 1073 SER THR MET LYS LYS HIS GLY ARG ALA LEU LEU SER VAL
SEQRES 74 A 1073 ARG GLU GLY ASP LYS GLU ARG VAL VAL ASP LEU ALA ALA
SEQRES 75 A 1073 LYS LEU LEU LYS GLN GLY PHE GLU LEU ASP ALA THR HIS
SEQRES 76 A 1073 GLY THR ALA ILE VAL LEU GLY GLU ALA GLY ILE ASN PRO
SEQRES 77 A 1073 ARG LEU VAL ASN LYS VAL HIS GLU GLY ARG PRO HIS ILE
SEQRES 78 A 1073 GLN ASP ARG ILE LYS ASN GLY GLU TYR THR TYR ILE ILE
SEQRES 79 A 1073 ASN THR THR SER GLY ARG ARG ALA ILE GLU ASP SER ARG
SEQRES 80 A 1073 VAL ILE ARG ARG SER ALA LEU GLN TYR LYS VAL HIS TYR
SEQRES 81 A 1073 ASP THR THR LEU ASN GLY GLY PHE ALA THR ALA MET ALA
SEQRES 82 A 1073 LEU ASN ALA ASP ALA THR GLU LYS VAL ILE SER VAL GLN
SEQRES 83 A 1073 GLU MET HIS ALA GLN ILE LYS
SEQRES 1 B 379 ILE LYS SER ALA LEU LEU VAL LEU GLU ASP GLY THR GLN
SEQRES 2 B 379 PHE HIS GLY ARG ALA ILE GLY ALA THR GLY SER ALA VAL
SEQRES 3 B 379 GLY GLU VAL VAL PHE ASN THR SER MET THR GLY TYR GLN
SEQRES 4 B 379 GLU ILE LEU THR ASP PRO SER TYR SER ARG GLN ILE VAL
SEQRES 5 B 379 THR LEU THR TYR PRO HIS ILE GLY ASN VAL GLY THR ASN
SEQRES 6 B 379 ASP ALA ASP GLU GLU SER SER GLN VAL HIS ALA GLN GLY
SEQRES 7 B 379 LEU VAL ILE ARG ASP LEU PRO LEU ILE ALA SER ASN PHE
SEQRES 8 B 379 ARG ASN THR GLU ASP LEU SER SER TYR LEU LYS ARG HIS
SEQRES 9 B 379 ASN ILE VAL ALA ILE ALA ASP ILE ASP THR ARG LYS LEU
SEQRES 10 B 379 THR ARG LEU LEU ARG GLU LYS GLY ALA GLN ASN GLY CYS
SEQRES 11 B 379 ILE ILE ALA GLY ASP ASN PRO ASP ALA ALA LEU ALA LEU
SEQRES 12 B 379 GLU LYS ALA ARG ALA PHE PRO GLY LEU ASN GLY MET ASP
SEQRES 13 B 379 LEU ALA LYS GLU VAL THR THR ALA GLU ALA TYR SER TRP
SEQRES 14 B 379 THR GLN GLY SER TRP THR LEU THR GLY GLY LEU PRO GLN
SEQRES 15 B 379 ALA LYS LYS GLU ASP GLU LEU PRO PHE HIS VAL VAL ALA
SEQRES 16 B 379 TYR ASP PHE GLY ALA LYS ARG ASN ILE LEU ARG MET LEU
SEQRES 17 B 379 VAL ASP ARG GLY CYS ARG LEU THR ILE VAL PRO ALA GLN
SEQRES 18 B 379 THR SER ALA GLU ASP VAL LEU LYS MET ASN PRO ASP GLY
SEQRES 19 B 379 ILE PHE LEU SER ASN GLY PRO GLY ASP PRO ALA PRO CYS
SEQRES 20 B 379 ASP TYR ALA ILE THR ALA ILE GLN LYS PHE LEU GLU THR
SEQRES 21 B 379 ASP ILE PRO VAL PHE GLY ILE CYG LEU GLY HIS GLN LEU
SEQRES 22 B 379 LEU ALA LEU ALA SER GLY ALA LYS THR VAL LYS MET LYS
SEQRES 23 B 379 PHE GLY HIS HIS GLY GLY ASN HIS PRO VAL LYS ASP VAL
SEQRES 24 B 379 GLU LYS ASN VAL VAL MET ILE THR ALA GLN ASN HIS GLY
SEQRES 25 B 379 PHE ALA VAL ASP GLU ALA THR LEU PRO ALA ASN LEU ARG
SEQRES 26 B 379 VAL THR HIS LYS SER LEU PHE ASP GLY THR LEU GLN GLY
SEQRES 27 B 379 ILE HIS ARG THR ASP LYS PRO ALA PHE SER PHE GLN GLY
SEQRES 28 B 379 ASN PRO GLU ALA SER PRO GLY PRO HIS ASP ALA ALA PRO
SEQRES 29 B 379 LEU PHE ASP HIS PHE ILE GLU LEU ILE GLU GLN TYR ARG
SEQRES 30 B 379 LYS THR
SEQRES 1 C 1073 MET PRO LYS ARG THR ASP ILE LYS SER ILE LEU ILE LEU
SEQRES 2 C 1073 GLY ALA GLY PRO ILE VAL ILE GLY GLN ALA CYS GLU PHE
SEQRES 3 C 1073 ASP TYR SER GLY ALA GLN ALA CYS LYS ALA LEU ARG GLU
SEQRES 4 C 1073 GLU GLY TYR ARG VAL ILE ASN VAL ASN SER ASN PRO ALA
SEQRES 5 C 1073 THR ILE MET THR ASP PRO GLU MET ALA ASP ALA THR TYR
SEQRES 6 C 1073 ILE GLU PRO ILE HIS TRP GLU VAL VAL ARG LYS ILE ILE
SEQRES 7 C 1073 GLU LYS GLU ARG PRO ASP ALA VAL LEU PRO THR MET GLY
SEQRES 8 C 1073 GLY GLN THR ALA LEU ASN CYS ALA LEU GLU LEU GLU ARG
SEQRES 9 C 1073 GLN GLY VAL LEU GLU GLU PHE GLY VAL THR MET ILE GLY
SEQRES 10 C 1073 ALA THR ALA ASP ALA ILE ASP LYS ALA GLU ASP ARG ARG
SEQRES 11 C 1073 ARG PHE ASP VAL ALA MET LYS LYS ILE GLY LEU GLU THR
SEQRES 12 C 1073 ALA ARG SER GLY ILE ALA HIS THR MET GLU GLU ALA LEU
SEQRES 13 C 1073 ALA VAL ALA ALA ASP VAL GLY PHE PRO CYS ILE ILE ARG
SEQRES 14 C 1073 PRO SER PHE THR MET GLY GLY SER GLY GLY GLY ILE ALA
SEQRES 15 C 1073 TYR ASN ARG GLU GLU PHE GLU GLU ILE CYS ALA ARG GLY
SEQRES 16 C 1073 LEU ASP LEU SER PRO THR LYS GLU LEU LEU ILE ASP GLU
SEQRES 17 C 1073 SER LEU ILE GLY TRP LYS GLU TYR GLU MET GLU VAL VAL
SEQRES 18 C 1073 ARG ASP LYS ASN ASP ASN CYS ILE ILE VAL CYS SER ILE
SEQRES 19 C 1073 GLU ASN PHE ASP ALA MET GLY ILE HIS THR GLY ASP SER
SEQRES 20 C 1073 ILE THR VAL ALA PRO ALA GLN THR LEU THR ASP LYS GLU
SEQRES 21 C 1073 TYR GLN ILE MET ARG ASN ALA SER MET ALA VAL LEU ARG
SEQRES 22 C 1073 GLU ILE GLY VAL GLU THR GLY GLY SER ASN VAL GLN PHE
SEQRES 23 C 1073 ALA VAL ASN PRO LYS ASN GLY ARG LEU ILE VAL ILE GLU
SEQRES 24 C 1073 MET ASN PRO ARG VAL SER ARG SER SER ALA LEU ALA SER
SEQRES 25 C 1073 LYS ALA THR GLY PHE PRO ILE ALA LYS VAL ALA ALA LYS
SEQRES 26 C 1073 LEU ALA VAL GLY TYR THR LEU ASP GLU LEU MET ASN ASP
SEQRES 27 C 1073 ILE THR GLY GLY ARG THR PRO ALA SER PHE GLU PRO SER
SEQRES 28 C 1073 ILE ASP TYR VAL VAL THR LYS ILE PRO ARG PHE ASN PHE
SEQRES 29 C 1073 GLU LYS PHE ALA GLY ALA ASN ASP ARG LEU THR THR GLN
SEQRES 30 C 1073 MET LYS SER VAL GLY GLU VAL MET ALA ILE GLY ARG THR
SEQRES 31 C 1073 GLN GLN GLU SER LEU GLN LYS ALA LEU ARG GLY LEU GLU
SEQRES 32 C 1073 VAL GLY ALA THR GLY PHE ASP PRO LYS VAL SER LEU ASP
SEQRES 33 C 1073 ASP PRO GLU ALA LEU THR LYS ILE ARG ARG GLU LEU LYS
SEQRES 34 C 1073 ASP ALA GLY ALA ASP ARG ILE TRP TYR ILE ALA ASP ALA
SEQRES 35 C 1073 PHE ARG ALA GLY LEU SER VAL ASP GLY VAL PHE ASN LEU
SEQRES 36 C 1073 THR ASN ILE ASP ARG TRP PHE LEU VAL GLN ILE GLU GLU
SEQRES 37 C 1073 LEU VAL ARG LEU GLU GLU LYS VAL ALA GLU VAL GLY ILE
SEQRES 38 C 1073 THR GLY LEU ASN ALA ASP PHE LEU ARG GLN LEU LYS ARG
SEQRES 39 C 1073 LYS GLY PHE ALA ASP ALA ARG LEU ALA LYS LEU ALA GLY
SEQRES 40 C 1073 VAL ARG GLU ALA GLU ILE ARG LYS LEU ARG ASP GLN TYR
SEQRES 41 C 1073 ASP LEU HIS PRO VAL TYR LYS ARG VAL ASP THR CYS ALA
SEQRES 42 C 1073 ALA GLU PHE ALA THR ASP THR ALA TYR MET TYR SER THR
SEQRES 43 C 1073 TYR GLU GLU GLU CYS GLU ALA ASN PRO SER THR ASP ARG
SEQRES 44 C 1073 GLU LYS ILE MET VAL LEU GLY GLY GLY PRO ASN ARG ILE
SEQRES 45 C 1073 GLY GLN GLY ILE GLU PHE ASP TYR CYS CYS VAL HIS ALA
SEQRES 46 C 1073 SER LEU ALA LEU ARG GLU ASP GLY TYR GLU THR ILE MET
SEQRES 47 C 1073 VAL ASN CYS ASN PRO GLU THR VAL SER THR ASP TYR ASP
SEQRES 48 C 1073 THR SER ASP ARG LEU TYR PHE GLU PRO VAL THR LEU GLU
SEQRES 49 C 1073 ASP VAL LEU GLU ILE VAL ARG ILE GLU LYS PRO LYS GLY
SEQRES 50 C 1073 VAL ILE VAL GLN TYR GLY GLY GLN THR PRO LEU LYS LEU
SEQRES 51 C 1073 ALA ARG ALA LEU GLU ALA ALA GLY VAL PRO VAL ILE GLY
SEQRES 52 C 1073 THR SER PRO ASP ALA ILE ASP ARG ALA GLU ASP ARG GLU
SEQRES 53 C 1073 ARG PHE GLN HIS ALA VAL GLU ARG LEU LYS LEU LYS GLN
SEQRES 54 C 1073 PRO ALA ASN ALA THR VAL THR ALA ILE GLU MET ALA VAL
SEQRES 55 C 1073 GLU LYS ALA LYS GLU ILE GLY TYR PRO LEU VAL VAL ARG
SEQRES 56 C 1073 ALA SER TYR VAL LEU GLY GLY ARG ALA MET GLU ILE VAL
SEQRES 57 C 1073 TYR ASP GLU ALA ASP LEU ARG ARG TYR PHE GLN THR ALA
SEQRES 58 C 1073 VAL SER VAL SER ASN ASP ALA PRO VAL LEU LEU ASP HIS
SEQRES 59 C 1073 PHE LEU ASP ASP ALA VAL GLU VAL ASP VAL ASP ALA ILE
SEQRES 60 C 1073 CYS ASP GLY GLU MET VAL LEU ILE GLY GLY ILE MET GLU
SEQRES 61 C 1073 HIS ILE GLU GLN ALA GLY VAL HIS SER GLY ASP SER ALA
SEQRES 62 C 1073 CYS SER LEU PRO ALA TYR THR LEU SER GLN GLU ILE GLN
SEQRES 63 C 1073 ASP VAL MET ARG GLN GLN VAL GLN LYS LEU ALA PHE GLU
SEQRES 64 C 1073 LEU GLN VAL ARG GLY LEU MET ASN VAL GLN PHE ALA VAL
SEQRES 65 C 1073 LYS ASN ASN GLU VAL TYR LEU ILE GLU VAL ASN PRO ARG
SEQRES 66 C 1073 ALA ALA ARG THR VAL PRO PHE VAL SER LYS ALA THR GLY
SEQRES 67 C 1073 VAL PRO LEU ALA LYS VAL ALA ALA ARG VAL MET ALA GLY
SEQRES 68 C 1073 LYS SER LEU ALA GLU GLN GLY VAL THR LYS GLU VAL ILE
SEQRES 69 C 1073 PRO PRO TYR TYR SER VAL LYS GLU VAL VAL LEU PRO PHE
SEQRES 70 C 1073 ASN LYS PHE PRO GLY VAL ASP PRO LEU LEU GLY PRO GLU
SEQRES 71 C 1073 MET ARG SER THR GLY GLU VAL MET GLY VAL GLY ARG THR
SEQRES 72 C 1073 PHE ALA GLU ALA PHE ALA LYS ALA GLN LEU GLY SER ASN
SEQRES 73 C 1073 SER THR MET LYS LYS HIS GLY ARG ALA LEU LEU SER VAL
SEQRES 74 C 1073 ARG GLU GLY ASP LYS GLU ARG VAL VAL ASP LEU ALA ALA
SEQRES 75 C 1073 LYS LEU LEU LYS GLN GLY PHE GLU LEU ASP ALA THR HIS
SEQRES 76 C 1073 GLY THR ALA ILE VAL LEU GLY GLU ALA GLY ILE ASN PRO
SEQRES 77 C 1073 ARG LEU VAL ASN LYS VAL HIS GLU GLY ARG PRO HIS ILE
SEQRES 78 C 1073 GLN ASP ARG ILE LYS ASN GLY GLU TYR THR TYR ILE ILE
SEQRES 79 C 1073 ASN THR THR SER GLY ARG ARG ALA ILE GLU ASP SER ARG
SEQRES 80 C 1073 VAL ILE ARG ARG SER ALA LEU GLN TYR LYS VAL HIS TYR
SEQRES 81 C 1073 ASP THR THR LEU ASN GLY GLY PHE ALA THR ALA MET ALA
SEQRES 82 C 1073 LEU ASN ALA ASP ALA THR GLU LYS VAL ILE SER VAL GLN
SEQRES 83 C 1073 GLU MET HIS ALA GLN ILE LYS
SEQRES 1 D 379 ILE LYS SER ALA LEU LEU VAL LEU GLU ASP GLY THR GLN
SEQRES 2 D 379 PHE HIS GLY ARG ALA ILE GLY ALA THR GLY SER ALA VAL
SEQRES 3 D 379 GLY GLU VAL VAL PHE ASN THR SER MET THR GLY TYR GLN
SEQRES 4 D 379 GLU ILE LEU THR ASP PRO SER TYR SER ARG GLN ILE VAL
SEQRES 5 D 379 THR LEU THR TYR PRO HIS ILE GLY ASN VAL GLY THR ASN
SEQRES 6 D 379 ASP ALA ASP GLU GLU SER SER GLN VAL HIS ALA GLN GLY
SEQRES 7 D 379 LEU VAL ILE ARG ASP LEU PRO LEU ILE ALA SER ASN PHE
SEQRES 8 D 379 ARG ASN THR GLU ASP LEU SER SER TYR LEU LYS ARG HIS
SEQRES 9 D 379 ASN ILE VAL ALA ILE ALA ASP ILE ASP THR ARG LYS LEU
SEQRES 10 D 379 THR ARG LEU LEU ARG GLU LYS GLY ALA GLN ASN GLY CYS
SEQRES 11 D 379 ILE ILE ALA GLY ASP ASN PRO ASP ALA ALA LEU ALA LEU
SEQRES 12 D 379 GLU LYS ALA ARG ALA PHE PRO GLY LEU ASN GLY MET ASP
SEQRES 13 D 379 LEU ALA LYS GLU VAL THR THR ALA GLU ALA TYR SER TRP
SEQRES 14 D 379 THR GLN GLY SER TRP THR LEU THR GLY GLY LEU PRO GLN
SEQRES 15 D 379 ALA LYS LYS GLU ASP GLU LEU PRO PHE HIS VAL VAL ALA
SEQRES 16 D 379 TYR ASP PHE GLY ALA LYS ARG ASN ILE LEU ARG MET LEU
SEQRES 17 D 379 VAL ASP ARG GLY CYS ARG LEU THR ILE VAL PRO ALA GLN
SEQRES 18 D 379 THR SER ALA GLU ASP VAL LEU LYS MET ASN PRO ASP GLY
SEQRES 19 D 379 ILE PHE LEU SER ASN GLY PRO GLY ASP PRO ALA PRO CYS
SEQRES 20 D 379 ASP TYR ALA ILE THR ALA ILE GLN LYS PHE LEU GLU THR
SEQRES 21 D 379 ASP ILE PRO VAL PHE GLY ILE CYG LEU GLY HIS GLN LEU
SEQRES 22 D 379 LEU ALA LEU ALA SER GLY ALA LYS THR VAL LYS MET LYS
SEQRES 23 D 379 PHE GLY HIS HIS GLY GLY ASN HIS PRO VAL LYS ASP VAL
SEQRES 24 D 379 GLU LYS ASN VAL VAL MET ILE THR ALA GLN ASN HIS GLY
SEQRES 25 D 379 PHE ALA VAL ASP GLU ALA THR LEU PRO ALA ASN LEU ARG
SEQRES 26 D 379 VAL THR HIS LYS SER LEU PHE ASP GLY THR LEU GLN GLY
SEQRES 27 D 379 ILE HIS ARG THR ASP LYS PRO ALA PHE SER PHE GLN GLY
SEQRES 28 D 379 ASN PRO GLU ALA SER PRO GLY PRO HIS ASP ALA ALA PRO
SEQRES 29 D 379 LEU PHE ASP HIS PHE ILE GLU LEU ILE GLU GLN TYR ARG
SEQRES 30 D 379 LYS THR
SEQRES 1 E 1073 MET PRO LYS ARG THR ASP ILE LYS SER ILE LEU ILE LEU
SEQRES 2 E 1073 GLY ALA GLY PRO ILE VAL ILE GLY GLN ALA CYS GLU PHE
SEQRES 3 E 1073 ASP TYR SER GLY ALA GLN ALA CYS LYS ALA LEU ARG GLU
SEQRES 4 E 1073 GLU GLY TYR ARG VAL ILE ASN VAL ASN SER ASN PRO ALA
SEQRES 5 E 1073 THR ILE MET THR ASP PRO GLU MET ALA ASP ALA THR TYR
SEQRES 6 E 1073 ILE GLU PRO ILE HIS TRP GLU VAL VAL ARG LYS ILE ILE
SEQRES 7 E 1073 GLU LYS GLU ARG PRO ASP ALA VAL LEU PRO THR MET GLY
SEQRES 8 E 1073 GLY GLN THR ALA LEU ASN CYS ALA LEU GLU LEU GLU ARG
SEQRES 9 E 1073 GLN GLY VAL LEU GLU GLU PHE GLY VAL THR MET ILE GLY
SEQRES 10 E 1073 ALA THR ALA ASP ALA ILE ASP LYS ALA GLU ASP ARG ARG
SEQRES 11 E 1073 ARG PHE ASP VAL ALA MET LYS LYS ILE GLY LEU GLU THR
SEQRES 12 E 1073 ALA ARG SER GLY ILE ALA HIS THR MET GLU GLU ALA LEU
SEQRES 13 E 1073 ALA VAL ALA ALA ASP VAL GLY PHE PRO CYS ILE ILE ARG
SEQRES 14 E 1073 PRO SER PHE THR MET GLY GLY SER GLY GLY GLY ILE ALA
SEQRES 15 E 1073 TYR ASN ARG GLU GLU PHE GLU GLU ILE CYS ALA ARG GLY
SEQRES 16 E 1073 LEU ASP LEU SER PRO THR LYS GLU LEU LEU ILE ASP GLU
SEQRES 17 E 1073 SER LEU ILE GLY TRP LYS GLU TYR GLU MET GLU VAL VAL
SEQRES 18 E 1073 ARG ASP LYS ASN ASP ASN CYS ILE ILE VAL CYS SER ILE
SEQRES 19 E 1073 GLU ASN PHE ASP ALA MET GLY ILE HIS THR GLY ASP SER
SEQRES 20 E 1073 ILE THR VAL ALA PRO ALA GLN THR LEU THR ASP LYS GLU
SEQRES 21 E 1073 TYR GLN ILE MET ARG ASN ALA SER MET ALA VAL LEU ARG
SEQRES 22 E 1073 GLU ILE GLY VAL GLU THR GLY GLY SER ASN VAL GLN PHE
SEQRES 23 E 1073 ALA VAL ASN PRO LYS ASN GLY ARG LEU ILE VAL ILE GLU
SEQRES 24 E 1073 MET ASN PRO ARG VAL SER ARG SER SER ALA LEU ALA SER
SEQRES 25 E 1073 LYS ALA THR GLY PHE PRO ILE ALA LYS VAL ALA ALA LYS
SEQRES 26 E 1073 LEU ALA VAL GLY TYR THR LEU ASP GLU LEU MET ASN ASP
SEQRES 27 E 1073 ILE THR GLY GLY ARG THR PRO ALA SER PHE GLU PRO SER
SEQRES 28 E 1073 ILE ASP TYR VAL VAL THR LYS ILE PRO ARG PHE ASN PHE
SEQRES 29 E 1073 GLU LYS PHE ALA GLY ALA ASN ASP ARG LEU THR THR GLN
SEQRES 30 E 1073 MET LYS SER VAL GLY GLU VAL MET ALA ILE GLY ARG THR
SEQRES 31 E 1073 GLN GLN GLU SER LEU GLN LYS ALA LEU ARG GLY LEU GLU
SEQRES 32 E 1073 VAL GLY ALA THR GLY PHE ASP PRO LYS VAL SER LEU ASP
SEQRES 33 E 1073 ASP PRO GLU ALA LEU THR LYS ILE ARG ARG GLU LEU LYS
SEQRES 34 E 1073 ASP ALA GLY ALA ASP ARG ILE TRP TYR ILE ALA ASP ALA
SEQRES 35 E 1073 PHE ARG ALA GLY LEU SER VAL ASP GLY VAL PHE ASN LEU
SEQRES 36 E 1073 THR ASN ILE ASP ARG TRP PHE LEU VAL GLN ILE GLU GLU
SEQRES 37 E 1073 LEU VAL ARG LEU GLU GLU LYS VAL ALA GLU VAL GLY ILE
SEQRES 38 E 1073 THR GLY LEU ASN ALA ASP PHE LEU ARG GLN LEU LYS ARG
SEQRES 39 E 1073 LYS GLY PHE ALA ASP ALA ARG LEU ALA LYS LEU ALA GLY
SEQRES 40 E 1073 VAL ARG GLU ALA GLU ILE ARG LYS LEU ARG ASP GLN TYR
SEQRES 41 E 1073 ASP LEU HIS PRO VAL TYR LYS ARG VAL ASP THR CYS ALA
SEQRES 42 E 1073 ALA GLU PHE ALA THR ASP THR ALA TYR MET TYR SER THR
SEQRES 43 E 1073 TYR GLU GLU GLU CYS GLU ALA ASN PRO SER THR ASP ARG
SEQRES 44 E 1073 GLU LYS ILE MET VAL LEU GLY GLY GLY PRO ASN ARG ILE
SEQRES 45 E 1073 GLY GLN GLY ILE GLU PHE ASP TYR CYS CYS VAL HIS ALA
SEQRES 46 E 1073 SER LEU ALA LEU ARG GLU ASP GLY TYR GLU THR ILE MET
SEQRES 47 E 1073 VAL ASN CYS ASN PRO GLU THR VAL SER THR ASP TYR ASP
SEQRES 48 E 1073 THR SER ASP ARG LEU TYR PHE GLU PRO VAL THR LEU GLU
SEQRES 49 E 1073 ASP VAL LEU GLU ILE VAL ARG ILE GLU LYS PRO LYS GLY
SEQRES 50 E 1073 VAL ILE VAL GLN TYR GLY GLY GLN THR PRO LEU LYS LEU
SEQRES 51 E 1073 ALA ARG ALA LEU GLU ALA ALA GLY VAL PRO VAL ILE GLY
SEQRES 52 E 1073 THR SER PRO ASP ALA ILE ASP ARG ALA GLU ASP ARG GLU
SEQRES 53 E 1073 ARG PHE GLN HIS ALA VAL GLU ARG LEU LYS LEU LYS GLN
SEQRES 54 E 1073 PRO ALA ASN ALA THR VAL THR ALA ILE GLU MET ALA VAL
SEQRES 55 E 1073 GLU LYS ALA LYS GLU ILE GLY TYR PRO LEU VAL VAL ARG
SEQRES 56 E 1073 ALA SER TYR VAL LEU GLY GLY ARG ALA MET GLU ILE VAL
SEQRES 57 E 1073 TYR ASP GLU ALA ASP LEU ARG ARG TYR PHE GLN THR ALA
SEQRES 58 E 1073 VAL SER VAL SER ASN ASP ALA PRO VAL LEU LEU ASP HIS
SEQRES 59 E 1073 PHE LEU ASP ASP ALA VAL GLU VAL ASP VAL ASP ALA ILE
SEQRES 60 E 1073 CYS ASP GLY GLU MET VAL LEU ILE GLY GLY ILE MET GLU
SEQRES 61 E 1073 HIS ILE GLU GLN ALA GLY VAL HIS SER GLY ASP SER ALA
SEQRES 62 E 1073 CYS SER LEU PRO ALA TYR THR LEU SER GLN GLU ILE GLN
SEQRES 63 E 1073 ASP VAL MET ARG GLN GLN VAL GLN LYS LEU ALA PHE GLU
SEQRES 64 E 1073 LEU GLN VAL ARG GLY LEU MET ASN VAL GLN PHE ALA VAL
SEQRES 65 E 1073 LYS ASN ASN GLU VAL TYR LEU ILE GLU VAL ASN PRO ARG
SEQRES 66 E 1073 ALA ALA ARG THR VAL PRO PHE VAL SER LYS ALA THR GLY
SEQRES 67 E 1073 VAL PRO LEU ALA LYS VAL ALA ALA ARG VAL MET ALA GLY
SEQRES 68 E 1073 LYS SER LEU ALA GLU GLN GLY VAL THR LYS GLU VAL ILE
SEQRES 69 E 1073 PRO PRO TYR TYR SER VAL LYS GLU VAL VAL LEU PRO PHE
SEQRES 70 E 1073 ASN LYS PHE PRO GLY VAL ASP PRO LEU LEU GLY PRO GLU
SEQRES 71 E 1073 MET ARG SER THR GLY GLU VAL MET GLY VAL GLY ARG THR
SEQRES 72 E 1073 PHE ALA GLU ALA PHE ALA LYS ALA GLN LEU GLY SER ASN
SEQRES 73 E 1073 SER THR MET LYS LYS HIS GLY ARG ALA LEU LEU SER VAL
SEQRES 74 E 1073 ARG GLU GLY ASP LYS GLU ARG VAL VAL ASP LEU ALA ALA
SEQRES 75 E 1073 LYS LEU LEU LYS GLN GLY PHE GLU LEU ASP ALA THR HIS
SEQRES 76 E 1073 GLY THR ALA ILE VAL LEU GLY GLU ALA GLY ILE ASN PRO
SEQRES 77 E 1073 ARG LEU VAL ASN LYS VAL HIS GLU GLY ARG PRO HIS ILE
SEQRES 78 E 1073 GLN ASP ARG ILE LYS ASN GLY GLU TYR THR TYR ILE ILE
SEQRES 79 E 1073 ASN THR THR SER GLY ARG ARG ALA ILE GLU ASP SER ARG
SEQRES 80 E 1073 VAL ILE ARG ARG SER ALA LEU GLN TYR LYS VAL HIS TYR
SEQRES 81 E 1073 ASP THR THR LEU ASN GLY GLY PHE ALA THR ALA MET ALA
SEQRES 82 E 1073 LEU ASN ALA ASP ALA THR GLU LYS VAL ILE SER VAL GLN
SEQRES 83 E 1073 GLU MET HIS ALA GLN ILE LYS
SEQRES 1 F 379 ILE LYS SER ALA LEU LEU VAL LEU GLU ASP GLY THR GLN
SEQRES 2 F 379 PHE HIS GLY ARG ALA ILE GLY ALA THR GLY SER ALA VAL
SEQRES 3 F 379 GLY GLU VAL VAL PHE ASN THR SER MET THR GLY TYR GLN
SEQRES 4 F 379 GLU ILE LEU THR ASP PRO SER TYR SER ARG GLN ILE VAL
SEQRES 5 F 379 THR LEU THR TYR PRO HIS ILE GLY ASN VAL GLY THR ASN
SEQRES 6 F 379 ASP ALA ASP GLU GLU SER SER GLN VAL HIS ALA GLN GLY
SEQRES 7 F 379 LEU VAL ILE ARG ASP LEU PRO LEU ILE ALA SER ASN PHE
SEQRES 8 F 379 ARG ASN THR GLU ASP LEU SER SER TYR LEU LYS ARG HIS
SEQRES 9 F 379 ASN ILE VAL ALA ILE ALA ASP ILE ASP THR ARG LYS LEU
SEQRES 10 F 379 THR ARG LEU LEU ARG GLU LYS GLY ALA GLN ASN GLY CYS
SEQRES 11 F 379 ILE ILE ALA GLY ASP ASN PRO ASP ALA ALA LEU ALA LEU
SEQRES 12 F 379 GLU LYS ALA ARG ALA PHE PRO GLY LEU ASN GLY MET ASP
SEQRES 13 F 379 LEU ALA LYS GLU VAL THR THR ALA GLU ALA TYR SER TRP
SEQRES 14 F 379 THR GLN GLY SER TRP THR LEU THR GLY GLY LEU PRO GLN
SEQRES 15 F 379 ALA LYS LYS GLU ASP GLU LEU PRO PHE HIS VAL VAL ALA
SEQRES 16 F 379 TYR ASP PHE GLY ALA LYS ARG ASN ILE LEU ARG MET LEU
SEQRES 17 F 379 VAL ASP ARG GLY CYS ARG LEU THR ILE VAL PRO ALA GLN
SEQRES 18 F 379 THR SER ALA GLU ASP VAL LEU LYS MET ASN PRO ASP GLY
SEQRES 19 F 379 ILE PHE LEU SER ASN GLY PRO GLY ASP PRO ALA PRO CYS
SEQRES 20 F 379 ASP TYR ALA ILE THR ALA ILE GLN LYS PHE LEU GLU THR
SEQRES 21 F 379 ASP ILE PRO VAL PHE GLY ILE CYG LEU GLY HIS GLN LEU
SEQRES 22 F 379 LEU ALA LEU ALA SER GLY ALA LYS THR VAL LYS MET LYS
SEQRES 23 F 379 PHE GLY HIS HIS GLY GLY ASN HIS PRO VAL LYS ASP VAL
SEQRES 24 F 379 GLU LYS ASN VAL VAL MET ILE THR ALA GLN ASN HIS GLY
SEQRES 25 F 379 PHE ALA VAL ASP GLU ALA THR LEU PRO ALA ASN LEU ARG
SEQRES 26 F 379 VAL THR HIS LYS SER LEU PHE ASP GLY THR LEU GLN GLY
SEQRES 27 F 379 ILE HIS ARG THR ASP LYS PRO ALA PHE SER PHE GLN GLY
SEQRES 28 F 379 ASN PRO GLU ALA SER PRO GLY PRO HIS ASP ALA ALA PRO
SEQRES 29 F 379 LEU PHE ASP HIS PHE ILE GLU LEU ILE GLU GLN TYR ARG
SEQRES 30 F 379 LYS THR
SEQRES 1 G 1073 MET PRO LYS ARG THR ASP ILE LYS SER ILE LEU ILE LEU
SEQRES 2 G 1073 GLY ALA GLY PRO ILE VAL ILE GLY GLN ALA CYS GLU PHE
SEQRES 3 G 1073 ASP TYR SER GLY ALA GLN ALA CYS LYS ALA LEU ARG GLU
SEQRES 4 G 1073 GLU GLY TYR ARG VAL ILE ASN VAL ASN SER ASN PRO ALA
SEQRES 5 G 1073 THR ILE MET THR ASP PRO GLU MET ALA ASP ALA THR TYR
SEQRES 6 G 1073 ILE GLU PRO ILE HIS TRP GLU VAL VAL ARG LYS ILE ILE
SEQRES 7 G 1073 GLU LYS GLU ARG PRO ASP ALA VAL LEU PRO THR MET GLY
SEQRES 8 G 1073 GLY GLN THR ALA LEU ASN CYS ALA LEU GLU LEU GLU ARG
SEQRES 9 G 1073 GLN GLY VAL LEU GLU GLU PHE GLY VAL THR MET ILE GLY
SEQRES 10 G 1073 ALA THR ALA ASP ALA ILE ASP LYS ALA GLU ASP ARG ARG
SEQRES 11 G 1073 ARG PHE ASP VAL ALA MET LYS LYS ILE GLY LEU GLU THR
SEQRES 12 G 1073 ALA ARG SER GLY ILE ALA HIS THR MET GLU GLU ALA LEU
SEQRES 13 G 1073 ALA VAL ALA ALA ASP VAL GLY PHE PRO CYS ILE ILE ARG
SEQRES 14 G 1073 PRO SER PHE THR MET GLY GLY SER GLY GLY GLY ILE ALA
SEQRES 15 G 1073 TYR ASN ARG GLU GLU PHE GLU GLU ILE CYS ALA ARG GLY
SEQRES 16 G 1073 LEU ASP LEU SER PRO THR LYS GLU LEU LEU ILE ASP GLU
SEQRES 17 G 1073 SER LEU ILE GLY TRP LYS GLU TYR GLU MET GLU VAL VAL
SEQRES 18 G 1073 ARG ASP LYS ASN ASP ASN CYS ILE ILE VAL CYS SER ILE
SEQRES 19 G 1073 GLU ASN PHE ASP ALA MET GLY ILE HIS THR GLY ASP SER
SEQRES 20 G 1073 ILE THR VAL ALA PRO ALA GLN THR LEU THR ASP LYS GLU
SEQRES 21 G 1073 TYR GLN ILE MET ARG ASN ALA SER MET ALA VAL LEU ARG
SEQRES 22 G 1073 GLU ILE GLY VAL GLU THR GLY GLY SER ASN VAL GLN PHE
SEQRES 23 G 1073 ALA VAL ASN PRO LYS ASN GLY ARG LEU ILE VAL ILE GLU
SEQRES 24 G 1073 MET ASN PRO ARG VAL SER ARG SER SER ALA LEU ALA SER
SEQRES 25 G 1073 LYS ALA THR GLY PHE PRO ILE ALA LYS VAL ALA ALA LYS
SEQRES 26 G 1073 LEU ALA VAL GLY TYR THR LEU ASP GLU LEU MET ASN ASP
SEQRES 27 G 1073 ILE THR GLY GLY ARG THR PRO ALA SER PHE GLU PRO SER
SEQRES 28 G 1073 ILE ASP TYR VAL VAL THR LYS ILE PRO ARG PHE ASN PHE
SEQRES 29 G 1073 GLU LYS PHE ALA GLY ALA ASN ASP ARG LEU THR THR GLN
SEQRES 30 G 1073 MET LYS SER VAL GLY GLU VAL MET ALA ILE GLY ARG THR
SEQRES 31 G 1073 GLN GLN GLU SER LEU GLN LYS ALA LEU ARG GLY LEU GLU
SEQRES 32 G 1073 VAL GLY ALA THR GLY PHE ASP PRO LYS VAL SER LEU ASP
SEQRES 33 G 1073 ASP PRO GLU ALA LEU THR LYS ILE ARG ARG GLU LEU LYS
SEQRES 34 G 1073 ASP ALA GLY ALA ASP ARG ILE TRP TYR ILE ALA ASP ALA
SEQRES 35 G 1073 PHE ARG ALA GLY LEU SER VAL ASP GLY VAL PHE ASN LEU
SEQRES 36 G 1073 THR ASN ILE ASP ARG TRP PHE LEU VAL GLN ILE GLU GLU
SEQRES 37 G 1073 LEU VAL ARG LEU GLU GLU LYS VAL ALA GLU VAL GLY ILE
SEQRES 38 G 1073 THR GLY LEU ASN ALA ASP PHE LEU ARG GLN LEU LYS ARG
SEQRES 39 G 1073 LYS GLY PHE ALA ASP ALA ARG LEU ALA LYS LEU ALA GLY
SEQRES 40 G 1073 VAL ARG GLU ALA GLU ILE ARG LYS LEU ARG ASP GLN TYR
SEQRES 41 G 1073 ASP LEU HIS PRO VAL TYR LYS ARG VAL ASP THR CYS ALA
SEQRES 42 G 1073 ALA GLU PHE ALA THR ASP THR ALA TYR MET TYR SER THR
SEQRES 43 G 1073 TYR GLU GLU GLU CYS GLU ALA ASN PRO SER THR ASP ARG
SEQRES 44 G 1073 GLU LYS ILE MET VAL LEU GLY GLY GLY PRO ASN ARG ILE
SEQRES 45 G 1073 GLY GLN GLY ILE GLU PHE ASP TYR CYS CYS VAL HIS ALA
SEQRES 46 G 1073 SER LEU ALA LEU ARG GLU ASP GLY TYR GLU THR ILE MET
SEQRES 47 G 1073 VAL ASN CYS ASN PRO GLU THR VAL SER THR ASP TYR ASP
SEQRES 48 G 1073 THR SER ASP ARG LEU TYR PHE GLU PRO VAL THR LEU GLU
SEQRES 49 G 1073 ASP VAL LEU GLU ILE VAL ARG ILE GLU LYS PRO LYS GLY
SEQRES 50 G 1073 VAL ILE VAL GLN TYR GLY GLY GLN THR PRO LEU LYS LEU
SEQRES 51 G 1073 ALA ARG ALA LEU GLU ALA ALA GLY VAL PRO VAL ILE GLY
SEQRES 52 G 1073 THR SER PRO ASP ALA ILE ASP ARG ALA GLU ASP ARG GLU
SEQRES 53 G 1073 ARG PHE GLN HIS ALA VAL GLU ARG LEU LYS LEU LYS GLN
SEQRES 54 G 1073 PRO ALA ASN ALA THR VAL THR ALA ILE GLU MET ALA VAL
SEQRES 55 G 1073 GLU LYS ALA LYS GLU ILE GLY TYR PRO LEU VAL VAL ARG
SEQRES 56 G 1073 ALA SER TYR VAL LEU GLY GLY ARG ALA MET GLU ILE VAL
SEQRES 57 G 1073 TYR ASP GLU ALA ASP LEU ARG ARG TYR PHE GLN THR ALA
SEQRES 58 G 1073 VAL SER VAL SER ASN ASP ALA PRO VAL LEU LEU ASP HIS
SEQRES 59 G 1073 PHE LEU ASP ASP ALA VAL GLU VAL ASP VAL ASP ALA ILE
SEQRES 60 G 1073 CYS ASP GLY GLU MET VAL LEU ILE GLY GLY ILE MET GLU
SEQRES 61 G 1073 HIS ILE GLU GLN ALA GLY VAL HIS SER GLY ASP SER ALA
SEQRES 62 G 1073 CYS SER LEU PRO ALA TYR THR LEU SER GLN GLU ILE GLN
SEQRES 63 G 1073 ASP VAL MET ARG GLN GLN VAL GLN LYS LEU ALA PHE GLU
SEQRES 64 G 1073 LEU GLN VAL ARG GLY LEU MET ASN VAL GLN PHE ALA VAL
SEQRES 65 G 1073 LYS ASN ASN GLU VAL TYR LEU ILE GLU VAL ASN PRO ARG
SEQRES 66 G 1073 ALA ALA ARG THR VAL PRO PHE VAL SER LYS ALA THR GLY
SEQRES 67 G 1073 VAL PRO LEU ALA LYS VAL ALA ALA ARG VAL MET ALA GLY
SEQRES 68 G 1073 LYS SER LEU ALA GLU GLN GLY VAL THR LYS GLU VAL ILE
SEQRES 69 G 1073 PRO PRO TYR TYR SER VAL LYS GLU VAL VAL LEU PRO PHE
SEQRES 70 G 1073 ASN LYS PHE PRO GLY VAL ASP PRO LEU LEU GLY PRO GLU
SEQRES 71 G 1073 MET ARG SER THR GLY GLU VAL MET GLY VAL GLY ARG THR
SEQRES 72 G 1073 PHE ALA GLU ALA PHE ALA LYS ALA GLN LEU GLY SER ASN
SEQRES 73 G 1073 SER THR MET LYS LYS HIS GLY ARG ALA LEU LEU SER VAL
SEQRES 74 G 1073 ARG GLU GLY ASP LYS GLU ARG VAL VAL ASP LEU ALA ALA
SEQRES 75 G 1073 LYS LEU LEU LYS GLN GLY PHE GLU LEU ASP ALA THR HIS
SEQRES 76 G 1073 GLY THR ALA ILE VAL LEU GLY GLU ALA GLY ILE ASN PRO
SEQRES 77 G 1073 ARG LEU VAL ASN LYS VAL HIS GLU GLY ARG PRO HIS ILE
SEQRES 78 G 1073 GLN ASP ARG ILE LYS ASN GLY GLU TYR THR TYR ILE ILE
SEQRES 79 G 1073 ASN THR THR SER GLY ARG ARG ALA ILE GLU ASP SER ARG
SEQRES 80 G 1073 VAL ILE ARG ARG SER ALA LEU GLN TYR LYS VAL HIS TYR
SEQRES 81 G 1073 ASP THR THR LEU ASN GLY GLY PHE ALA THR ALA MET ALA
SEQRES 82 G 1073 LEU ASN ALA ASP ALA THR GLU LYS VAL ILE SER VAL GLN
SEQRES 83 G 1073 GLU MET HIS ALA GLN ILE LYS
SEQRES 1 H 379 ILE LYS SER ALA LEU LEU VAL LEU GLU ASP GLY THR GLN
SEQRES 2 H 379 PHE HIS GLY ARG ALA ILE GLY ALA THR GLY SER ALA VAL
SEQRES 3 H 379 GLY GLU VAL VAL PHE ASN THR SER MET THR GLY TYR GLN
SEQRES 4 H 379 GLU ILE LEU THR ASP PRO SER TYR SER ARG GLN ILE VAL
SEQRES 5 H 379 THR LEU THR TYR PRO HIS ILE GLY ASN VAL GLY THR ASN
SEQRES 6 H 379 ASP ALA ASP GLU GLU SER SER GLN VAL HIS ALA GLN GLY
SEQRES 7 H 379 LEU VAL ILE ARG ASP LEU PRO LEU ILE ALA SER ASN PHE
SEQRES 8 H 379 ARG ASN THR GLU ASP LEU SER SER TYR LEU LYS ARG HIS
SEQRES 9 H 379 ASN ILE VAL ALA ILE ALA ASP ILE ASP THR ARG LYS LEU
SEQRES 10 H 379 THR ARG LEU LEU ARG GLU LYS GLY ALA GLN ASN GLY CYS
SEQRES 11 H 379 ILE ILE ALA GLY ASP ASN PRO ASP ALA ALA LEU ALA LEU
SEQRES 12 H 379 GLU LYS ALA ARG ALA PHE PRO GLY LEU ASN GLY MET ASP
SEQRES 13 H 379 LEU ALA LYS GLU VAL THR THR ALA GLU ALA TYR SER TRP
SEQRES 14 H 379 THR GLN GLY SER TRP THR LEU THR GLY GLY LEU PRO GLN
SEQRES 15 H 379 ALA LYS LYS GLU ASP GLU LEU PRO PHE HIS VAL VAL ALA
SEQRES 16 H 379 TYR ASP PHE GLY ALA LYS ARG ASN ILE LEU ARG MET LEU
SEQRES 17 H 379 VAL ASP ARG GLY CYS ARG LEU THR ILE VAL PRO ALA GLN
SEQRES 18 H 379 THR SER ALA GLU ASP VAL LEU LYS MET ASN PRO ASP GLY
SEQRES 19 H 379 ILE PHE LEU SER ASN GLY PRO GLY ASP PRO ALA PRO CYS
SEQRES 20 H 379 ASP TYR ALA ILE THR ALA ILE GLN LYS PHE LEU GLU THR
SEQRES 21 H 379 ASP ILE PRO VAL PHE GLY ILE CYG LEU GLY HIS GLN LEU
SEQRES 22 H 379 LEU ALA LEU ALA SER GLY ALA LYS THR VAL LYS MET LYS
SEQRES 23 H 379 PHE GLY HIS HIS GLY GLY ASN HIS PRO VAL LYS ASP VAL
SEQRES 24 H 379 GLU LYS ASN VAL VAL MET ILE THR ALA GLN ASN HIS GLY
SEQRES 25 H 379 PHE ALA VAL ASP GLU ALA THR LEU PRO ALA ASN LEU ARG
SEQRES 26 H 379 VAL THR HIS LYS SER LEU PHE ASP GLY THR LEU GLN GLY
SEQRES 27 H 379 ILE HIS ARG THR ASP LYS PRO ALA PHE SER PHE GLN GLY
SEQRES 28 H 379 ASN PRO GLU ALA SER PRO GLY PRO HIS ASP ALA ALA PRO
SEQRES 29 H 379 LEU PHE ASP HIS PHE ILE GLU LEU ILE GLU GLN TYR ARG
SEQRES 30 H 379 LYS THR
MODRES 1A9X CYG B 1769 CYS
MODRES 1A9X CYG D 3769 CYS
MODRES 1A9X CYG F 5769 CYS
MODRES 1A9X CYG H 7769 CYS
HET CYG B1769 15
HET CYG D3769 15
HET CYG F5769 15
HET CYG H7769 15
HET MN G7901 1
HET MN G7902 1
HET K G7903 1
HET K G7904 1
HET PO4 G7906 5
HET MN G7911 1
HET K G7912 1
HET K G7913 1
HET CL G7930 1
HET CL G7931 1
HET CL G7932 1
HET CL H7933 1
HET CL G7934 1
HET CL G7935 1
HET CL G7936 1
HET K G7940 1
HET K H7941 1
HET K G7942 1
HET K G7943 1
HET PO4 A1980 5
HET PO4 A1981 5
HET PO4 A1982 5
HET MN C3901 1
HET MN C3902 1
HET K C3903 1
HET K C3904 1
HET PO4 C3906 5
HET MN C3911 1
HET K C3912 1
HET K C3913 1
HET CL C3930 1
HET CL C3931 1
HET CL C3932 1
HET CL D3933 1
HET CL C3934 1
HET CL C3935 1
HET CL C3936 1
HET K C3940 1
HET K D3941 1
HET K C3942 1
HET K C3943 1
HET PO4 C3980 5
HET PO4 C3981 5
HET PO4 C3982 5
HET MN E5901 1
HET MN E5902 1
HET K E5903 1
HET K E5904 1
HET PO4 E5906 5
HET MN E5911 1
HET K E5912 1
HET K E5913 1
HET CL E5930 1
HET CL E5931 1
HET CL E5932 1
HET CL F5933 1
HET CL E5934 1
HET CL E5935 1
HET CL E5936 1
HET K E5940 1
HET K F5941 1
HET K E5942 1
HET K E5943 1
HET PO4 E5980 5
HET PO4 E5981 5
HET PO4 G7980 5
HET PO4 G7981 5
HET PO4 G7982 5
HET MN A1901 1
HET MN A1902 1
HET K A1903 1
HET K A1904 1
HET PO4 A1906 5
HET MN A1911 1
HET K A1912 1
HET K A1913 1
HET CL A1930 1
HET CL A1931 1
HET CL A1932 1
HET CL B1933 1
HET CL A1934 1
HET CL A1935 1
HET CL A1936 1
HET K A1940 1
HET K B1941 1
HET K A1942 1
HET K A1943 1
HET ADP G7900 27
HET ADP G7910 27
HET ORN G7920 9
HET NET G7950 9
HET ADP C3900 27
HET ADP C3910 27
HET ORN C3920 9
HET NET C3950 9
HET ADP E5900 27
HET ADP E5910 27
HET ORN E5920 9
HET NET E5950 9
HET ADP A1900 27
HET ADP A1910 27
HET ORN A1920 9
HET NET A1950 9
HETNAM CYG 2-AMINO-4-(AMINO-3-OXO-PROPYLSULFANYLCARBONYL)-BUTYRIC
HETNAM 2 CYG ACID
HETNAM MN MANGANESE (II) ION
HETNAM K POTASSIUM ION
HETNAM PO4 PHOSPHATE ION
HETNAM CL CHLORIDE ION
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM ORN L-ORNITHINE
HETNAM NET TETRAETHYLAMMONIUM ION
FORMUL 2 CYG 4(C8 H14 N2 O5 S)
FORMUL 9 MN 12(MN 2+)
FORMUL 11 K 32(K 1+)
FORMUL 13 PO4 15(O4 P 3-)
FORMUL 17 CL 28(CL 1-)
FORMUL 96 ADP 8(C10 H15 N5 O10 P2)
FORMUL 98 ORN 4(C5 H12 N2 O2)
FORMUL 99 NET 4(C8 H20 N 1+)
FORMUL 11 HOH *4528(H2 O)
HELIX 1 1 CYS A 24 GLU A 40 5 17
HELIX 2 2 ILE A 54 THR A 56 5 3
HELIX 3 3 PRO A 58 MET A 60 5 3
HELIX 4 4 TRP A 71 GLU A 81 1 11
HELIX 5 5 GLY A 92 ARG A 104 1 13
HELIX 6 6 VAL A 107 PHE A 111 1 5
HELIX 7 7 ALA A 120 GLU A 127 1 8
HELIX 8 8 ARG A 129 LYS A 138 1 10
HELIX 9 9 MET A 152 VAL A 162 1 11
HELIX 10 10 ARG A 185 LEU A 198 1 14
HELIX 11 11 THR A 244 ASP A 246 5 3
HELIX 12 12 ASP A 258 ILE A 275 1 18
HELIX 13 13 ARG A 306 THR A 315 1 10
HELIX 14 14 ILE A 319 ALA A 327 1 9
HELIX 15 15 LEU A 332 GLU A 334 5 3
HELIX 16 16 PHE A 364 LYS A 366 5 3
HELIX 17 17 GLN A 391 GLY A 401 1 11
HELIX 18 18 ALA A 420 LYS A 429 1 10
HELIX 19 19 ARG A 435 ARG A 444 1 10
HELIX 20 20 VAL A 449 THR A 456 1 8
HELIX 21 21 ARG A 460 VAL A 479 1 20
HELIX 22 22 ILE A 481 GLY A 483 5 3
HELIX 23 23 ALA A 486 LYS A 495 1 10
HELIX 24 24 ASP A 499 LEU A 505 1 7
HELIX 25 25 GLU A 510 GLN A 519 1 10
HELIX 26 26 ILE A 576 GLU A 591 1 16
HELIX 27 27 LEU A 623 GLU A 633 1 11
HELIX 28 28 GLN A 645 ALA A 656 1 12
HELIX 29 29 PRO A 666 GLU A 673 1 8
HELIX 30 30 ARG A 675 LEU A 685 1 11
HELIX 31 31 ILE A 698 ILE A 708 1 11
HELIX 32 32 GLU A 731 THR A 740 1 10
HELIX 33 33 SER A 789 ASP A 791 5 3
HELIX 34 34 GLN A 803 GLU A 819 1 17
HELIX 35 35 VAL A 850 THR A 857 1 8
HELIX 36 36 LEU A 861 MET A 869 1 9
HELIX 37 37 LEU A 874 GLN A 877 1 4
HELIX 38 38 PRO A 896 LYS A 899 5 4
HELIX 39 39 PHE A 924 GLY A 934 1 11
HELIX 40 40 GLU A 951 LYS A 954 5 4
HELIX 41 41 VAL A 957 LYS A 966 1 10
HELIX 42 42 HIS A 975 ALA A 984 1 10
HELIX 43 43 ILE A 1001 ASN A 1007 1 7
HELIX 44 44 ARG A 1020 GLN A 1035 1 16
HELIX 45 45 LEU A 1044 ASN A 1055 1 12
HELIX 46 46 VAL A 1065 GLN A 1071 1 7
HELIX 47 47 TYR B 1539 LEU B 1543 1 5
HELIX 48 48 PRO B 1546 TYR B 1548 5 3
HELIX 49 49 ASP B 1567 ASP B 1569 5 3
HELIX 50 50 LEU B 1598 ARG B 1604 1 7
HELIX 51 51 THR B 1615 LYS B 1625 1 11
HELIX 52 52 ALA B 1640 ALA B 1649 1 10
HELIX 53 53 ALA B 1659 VAL B 1662 1 4
HELIX 54 54 GLU B 1687 GLU B 1689 5 3
HELIX 55 55 ARG B 1703 ARG B 1712 1 10
HELIX 56 56 ALA B 1725 MET B 1731 1 7
HELIX 57 57 ASP B 1749 GLU B 1760 1 12
HELIX 58 58 GLY B 1771 SER B 1779 1 9
HELIX 59 59 ALA B 1864 ARG B 1878 5 15
HELIX 60 60 CYS C 2024 GLU C 2039 5 16
HELIX 61 61 ILE C 2054 THR C 2056 5 3
HELIX 62 62 PRO C 2058 MET C 2060 5 3
HELIX 63 63 TRP C 2071 GLU C 2081 1 11
HELIX 64 64 GLY C 2092 ARG C 2104 1 13
HELIX 65 65 VAL C 2107 GLU C 2110 1 4
HELIX 66 66 ALA C 2120 GLU C 2127 1 8
HELIX 67 67 ARG C 2129 LYS C 2138 1 10
HELIX 68 68 MET C 2152 VAL C 2162 1 11
HELIX 69 69 ARG C 2185 LEU C 2198 1 14
HELIX 70 70 THR C 2244 ASP C 2246 5 3
HELIX 71 71 ASP C 2258 ILE C 2275 1 18
HELIX 72 72 ARG C 2306 THR C 2315 1 10
HELIX 73 73 ILE C 2319 ALA C 2327 1 9
HELIX 74 74 LEU C 2332 GLU C 2334 5 3
HELIX 75 75 PHE C 2364 LYS C 2366 5 3
HELIX 76 76 GLN C 2391 GLY C 2401 1 11
HELIX 77 77 ALA C 2420 LYS C 2429 1 10
HELIX 78 78 ARG C 2435 ARG C 2444 1 10
HELIX 79 79 VAL C 2449 THR C 2456 1 8
HELIX 80 80 ARG C 2460 VAL C 2479 1 20
HELIX 81 81 ILE C 2481 GLY C 2483 5 3
HELIX 82 82 ALA C 2486 ARG C 2494 1 9
HELIX 83 83 ASP C 2499 ALA C 2506 1 8
HELIX 84 84 GLU C 2510 TYR C 2520 1 11
HELIX 85 85 ILE C 2576 GLU C 2591 1 16
HELIX 86 86 TYR C 2610 THR C 2612 5 3
HELIX 87 87 LEU C 2623 GLU C 2633 1 11
HELIX 88 88 GLN C 2645 ALA C 2656 1 12
HELIX 89 89 PRO C 2666 GLU C 2673 1 8
HELIX 90 90 ARG C 2675 ARG C 2684 1 10
HELIX 91 91 ILE C 2698 ILE C 2708 1 11
HELIX 92 92 GLU C 2731 THR C 2740 1 10
HELIX 93 93 SER C 2789 ASP C 2791 5 3
HELIX 94 94 GLN C 2803 LEU C 2820 1 18
HELIX 95 95 VAL C 2850 THR C 2857 1 8
HELIX 96 96 LEU C 2861 MET C 2869 1 9
HELIX 97 97 LEU C 2874 GLN C 2877 1 4
HELIX 98 98 PHE C 2897 LYS C 2899 5 3
HELIX 99 99 PHE C 2924 GLY C 2934 1 11
HELIX 100 100 GLU C 2951 LYS C 2966 5 16
HELIX 101 101 HIS C 2975 ALA C 2984 1 10
HELIX 102 102 VAL C 2994 GLU C 2996 5 3
HELIX 103 103 ILE C 3001 ASN C 3007 1 7
HELIX 104 104 ARG C 3020 TYR C 3036 1 17
HELIX 105 105 LEU C 3044 ASN C 3055 1 12
HELIX 106 106 VAL C 3065 ALA C 3070 1 6
HELIX 107 107 TYR D 3539 LEU D 3543 1 5
HELIX 108 108 PRO D 3546 TYR D 3548 5 3
HELIX 109 109 ASP D 3567 ASP D 3569 5 3
HELIX 110 110 LEU D 3598 HIS D 3605 1 8
HELIX 111 111 THR D 3615 LYS D 3625 1 11
HELIX 112 112 ALA D 3640 ALA D 3649 1 10
HELIX 113 113 ALA D 3659 VAL D 3662 1 4
HELIX 114 114 GLU D 3687 GLU D 3689 5 3
HELIX 115 115 ARG D 3703 ASP D 3711 1 9
HELIX 116 116 ALA D 3725 MET D 3731 1 7
HELIX 117 117 ASP D 3749 GLU D 3760 1 12
HELIX 118 118 GLY D 3771 SER D 3779 1 9
HELIX 119 119 GLU D 3818 THR D 3820 5 3
HELIX 120 120 ALA D 3864 ARG D 3878 5 15
HELIX 121 121 CYS E 4024 GLU E 4039 5 16
HELIX 122 122 ILE E 4054 THR E 4056 5 3
HELIX 123 123 PRO E 4058 MET E 4060 5 3
HELIX 124 124 TRP E 4071 GLU E 4081 1 11
HELIX 125 125 GLY E 4092 ARG E 4104 1 13
HELIX 126 126 VAL E 4107 GLU E 4110 1 4
HELIX 127 127 ALA E 4120 GLU E 4127 1 8
HELIX 128 128 ARG E 4129 LYS E 4138 1 10
HELIX 129 129 MET E 4152 VAL E 4162 1 11
HELIX 130 130 ARG E 4185 LEU E 4198 1 14
HELIX 131 131 THR E 4244 ASP E 4246 5 3
HELIX 132 132 ASP E 4258 ILE E 4275 1 18
HELIX 133 133 ARG E 4306 THR E 4315 1 10
HELIX 134 134 ILE E 4319 VAL E 4328 1 10
HELIX 135 135 LEU E 4332 GLU E 4334 5 3
HELIX 136 136 ASP E 4338 THR E 4340 5 3
HELIX 137 137 PHE E 4364 LYS E 4366 5 3
HELIX 138 138 GLN E 4391 GLY E 4401 1 11
HELIX 139 139 ALA E 4420 LYS E 4429 1 10
HELIX 140 140 ARG E 4435 ARG E 4444 1 10
HELIX 141 141 VAL E 4449 THR E 4456 1 8
HELIX 142 142 ARG E 4460 VAL E 4479 1 20
HELIX 143 143 ILE E 4481 GLY E 4483 5 3
HELIX 144 144 ALA E 4486 LYS E 4495 1 10
HELIX 145 145 ASP E 4499 ALA E 4506 1 8
HELIX 146 146 GLU E 4510 GLN E 4519 1 10
HELIX 147 147 ILE E 4576 GLU E 4591 1 16
HELIX 148 148 VAL E 4606 THR E 4608 5 3
HELIX 149 149 TYR E 4610 THR E 4612 5 3
HELIX 150 150 LEU E 4623 GLU E 4633 1 11
HELIX 151 151 GLN E 4645 ALA E 4656 1 12
HELIX 152 152 PRO E 4666 GLU E 4673 1 8
HELIX 153 153 ARG E 4675 LEU E 4685 1 11
HELIX 154 154 ILE E 4698 ILE E 4708 1 11
HELIX 155 155 GLU E 4731 THR E 4740 1 10
HELIX 156 156 SER E 4789 ASP E 4791 5 3
HELIX 157 157 GLN E 4803 LEU E 4820 1 18
HELIX 158 158 VAL E 4850 THR E 4857 1 8
HELIX 159 159 LEU E 4861 MET E 4869 1 9
HELIX 160 160 LEU E 4874 GLN E 4877 1 4
HELIX 161 161 PRO E 4896 LYS E 4899 5 4
HELIX 162 162 PHE E 4924 GLY E 4934 1 11
HELIX 163 163 ARG E 4956 LYS E 4966 5 11
HELIX 164 164 HIS E 4975 GLU E 4983 1 9
HELIX 165 165 VAL E 4994 GLU E 4996 5 3
HELIX 166 166 ILE E 5001 LYS E 5006 1 6
HELIX 167 167 ARG E 5020 GLN E 5035 1 16
HELIX 168 168 LEU E 5044 ASN E 5055 1 12
HELIX 169 169 VAL E 5065 GLN E 5071 1 7
HELIX 170 170 TYR F 5539 LEU F 5543 1 5
HELIX 171 171 PRO F 5546 TYR F 5548 5 3
HELIX 172 172 ASP F 5567 ASP F 5569 5 3
HELIX 173 173 LEU F 5598 ARG F 5604 1 7
HELIX 174 174 THR F 5615 LYS F 5625 1 11
HELIX 175 175 ALA F 5640 ALA F 5649 1 10
HELIX 176 176 ALA F 5659 VAL F 5662 1 4
HELIX 177 177 GLU F 5687 GLU F 5689 5 3
HELIX 178 178 ARG F 5703 ARG F 5712 1 10
HELIX 179 179 ALA F 5725 MET F 5731 1 7
HELIX 180 180 ASP F 5749 GLU F 5760 1 12
HELIX 181 181 GLY F 5771 ALA F 5778 1 8
HELIX 182 182 GLU F 5818 THR F 5820 5 3
HELIX 183 183 ASP F 5862 ARG F 5878 5 17
HELIX 184 184 CYS G 6024 GLU G 6039 5 16
HELIX 185 185 ILE G 6054 THR G 6056 5 3
HELIX 186 186 PRO G 6058 MET G 6060 5 3
HELIX 187 187 TRP G 6071 GLU G 6081 1 11
HELIX 188 188 GLY G 6092 ARG G 6104 1 13
HELIX 189 189 VAL G 6107 GLU G 6110 1 4
HELIX 190 190 ALA G 6120 GLU G 6127 1 8
HELIX 191 191 ARG G 6129 LYS G 6138 1 10
HELIX 192 192 MET G 6152 VAL G 6162 1 11
HELIX 193 193 ARG G 6185 LEU G 6198 1 14
HELIX 194 194 THR G 6244 ASP G 6246 5 3
HELIX 195 195 ASP G 6258 ILE G 6275 1 18
HELIX 196 196 ARG G 6306 THR G 6315 1 10
HELIX 197 197 ILE G 6319 VAL G 6328 1 10
HELIX 198 198 LEU G 6332 GLU G 6334 5 3
HELIX 199 199 ASP G 6338 THR G 6340 5 3
HELIX 200 200 PHE G 6364 LYS G 6366 5 3
HELIX 201 201 GLN G 6391 GLY G 6401 1 11
HELIX 202 202 ALA G 6420 LYS G 6429 1 10
HELIX 203 203 ARG G 6435 ARG G 6444 1 10
HELIX 204 204 VAL G 6449 THR G 6456 1 8
HELIX 205 205 ARG G 6460 VAL G 6479 1 20
HELIX 206 206 ILE G 6481 GLY G 6483 5 3
HELIX 207 207 ALA G 6486 ARG G 6494 1 9
HELIX 208 208 ASP G 6499 LEU G 6505 1 7
HELIX 209 209 GLU G 6510 TYR G 6520 1 11
HELIX 210 210 ILE G 6576 GLU G 6591 1 16
HELIX 211 211 VAL G 6606 THR G 6608 5 3
HELIX 212 212 TYR G 6610 THR G 6612 5 3
HELIX 213 213 LEU G 6623 GLU G 6633 1 11
HELIX 214 214 GLN G 6645 ALA G 6657 1 13
HELIX 215 215 PRO G 6666 GLU G 6673 1 8
HELIX 216 216 ARG G 6675 LEU G 6685 1 11
HELIX 217 217 ILE G 6698 ILE G 6708 1 11
HELIX 218 218 GLU G 6731 THR G 6740 1 10
HELIX 219 219 SER G 6789 ASP G 6791 5 3
HELIX 220 220 GLN G 6803 LEU G 6820 1 18
HELIX 221 221 VAL G 6850 THR G 6857 1 8
HELIX 222 222 LEU G 6861 ALA G 6870 1 10
HELIX 223 223 LEU G 6874 GLN G 6877 1 4
HELIX 224 224 PRO G 6896 LYS G 6899 5 4
HELIX 225 225 PHE G 6924 GLY G 6934 1 11
HELIX 226 226 GLU G 6951 LYS G 6954 1 4
HELIX 227 227 ARG G 6956 LYS G 6966 5 11
HELIX 228 228 HIS G 6975 ALA G 6984 1 10
HELIX 229 229 VAL G 6994 GLU G 6996 5 3
HELIX 230 230 ILE G 7001 LYS G 7006 1 6
HELIX 231 231 ARG G 7020 GLN G 7035 1 16
HELIX 232 232 LEU G 7044 ASN G 7055 1 12
HELIX 233 233 VAL G 7065 ALA G 7070 1 6
HELIX 234 234 TYR H 7539 LEU H 7543 1 5
HELIX 235 235 PRO H 7546 TYR H 7548 5 3
HELIX 236 236 ASP H 7567 ASP H 7569 5 3
HELIX 237 237 LEU H 7598 HIS H 7605 1 8
HELIX 238 238 THR H 7615 LYS H 7625 1 11
HELIX 239 239 ALA H 7640 ALA H 7649 1 10
HELIX 240 240 ALA H 7659 VAL H 7662 1 4
HELIX 241 241 GLU H 7687 GLU H 7689 5 3
HELIX 242 242 ARG H 7703 ARG H 7712 1 10
HELIX 243 243 ALA H 7725 MET H 7731 1 7
HELIX 244 244 ASP H 7749 GLU H 7760 1 12
HELIX 245 245 GLY H 7771 ALA H 7778 1 8
HELIX 246 246 GLU H 7818 THR H 7820 5 3
HELIX 247 247 ALA H 7864 ARG H 7878 5 15
SHEET 1 A 5 THR A 114 ILE A 116 0
SHEET 2 A 5 ALA A 85 LEU A 87 1 N VAL A 86 O THR A 114
SHEET 3 A 5 SER A 9 LEU A 13 1 N LEU A 11 O ALA A 85
SHEET 4 A 5 ARG A 43 VAL A 47 1 N ARG A 43 O ILE A 10
SHEET 5 A 5 ALA A 63 TYR A 65 1 N ALA A 63 O ASN A 46
SHEET 1 B 4 SER A 146 ALA A 149 0
SHEET 2 B 4 LEU A 204 GLU A 208 -1 N ILE A 206 O GLY A 147
SHEET 3 B 4 CYS A 166 PRO A 170 -1 N ARG A 169 O LEU A 205
SHEET 4 B 4 GLY A 180 ALA A 182 -1 N ALA A 182 O CYS A 166
SHEET 1 C 4 CYS A 228 GLU A 235 0
SHEET 2 C 4 LYS A 214 ARG A 222 -1 N VAL A 221 O ILE A 229
SHEET 3 C 4 GLY A 280 VAL A 288 -1 N VAL A 288 O LYS A 214
SHEET 4 C 4 LEU A 295 ASN A 301 -1 N ASN A 301 O ASN A 283
SHEET 1 D 3 THR A 249 ALA A 251 0
SHEET 2 D 3 VAL A 355 ARG A 361 -1 N LYS A 358 O THR A 249
SHEET 3 D 3 GLY A 382 GLY A 388 -1 N GLY A 388 O VAL A 355
SHEET 1 E 6 VAL A 525 ARG A 528 0
SHEET 2 E 6 ALA A 541 THR A 546 -1 N THR A 546 O VAL A 525
SHEET 3 E 6 ARG A 615 PHE A 618 1 N LEU A 616 O ALA A 541
SHEET 4 E 6 GLU A 595 ASN A 600 1 N MET A 598 O ARG A 615
SHEET 5 E 6 LYS A 561 LEU A 565 1 N ILE A 562 O GLU A 595
SHEET 6 E 6 GLY A 637 ILE A 639 1 N GLY A 637 O MET A 563
SHEET 1 F 2 ASN A 692 VAL A 695 0
SHEET 2 F 2 VAL A 750 ASP A 753 -1 N LEU A 752 O ALA A 693
SHEET 1 G 2 LEU A 712 VAL A 714 0
SHEET 2 G 2 GLU A 726 VAL A 728 -1 N VAL A 728 O LEU A 712
SHEET 1 H 4 VAL A 773 GLU A 780 0
SHEET 2 H 4 VAL A 760 CYS A 768 -1 N ILE A 767 O LEU A 774
SHEET 3 H 4 GLY A 824 VAL A 832 -1 N VAL A 832 O VAL A 760
SHEET 4 H 4 VAL A 837 ASN A 843 -1 N ASN A 843 O ASN A 827
SHEET 1 I 3 CYS A 794 LEU A 796 0
SHEET 2 I 3 TYR A 888 LEU A 895 -1 N LYS A 891 O CYS A 794
SHEET 3 I 3 SER A 913 GLY A 921 -1 N GLY A 921 O TYR A 888
SHEET 1 J 4 GLU A 970 ALA A 973 0
SHEET 2 J 4 ARG A 944 SER A 948 1 N ALA A 945 O GLU A 970
SHEET 3 J 4 TYR A1012 ASN A1015 1 N TYR A1012 O LEU A 946
SHEET 4 J 4 HIS A1039 ASP A1041 1 N HIS A1039 O ILE A1013
SHEET 1 K 7 GLN B1514 ARG B1518 0
SHEET 2 K 7 SER B1504 LEU B1509 -1 N LEU B1507 O PHE B1515
SHEET 3 K 7 GLN B1628 ALA B1634 -1 N ILE B1633 O LEU B1506
SHEET 4 K 7 GLY B1524 ASN B1533 -1 N VAL B1530 O GLN B1628
SHEET 5 K 7 GLN B1551 LEU B1555 1 N ILE B1552 O GLU B1529
SHEET 6 K 7 GLY B1579 VAL B1581 1 N GLY B1579 O VAL B1553
SHEET 7 K 7 VAL B1608 ILE B1610 1 N VAL B1608 O LEU B1580
SHEET 1 L10 TYR B1668 TRP B1670 0
SHEET 2 L10 CYS B1714 PRO B1720 -1 N ILE B1718 O TYR B1668
SHEET 3 L10 PHE B1692 ASP B1698 1 N PHE B1692 O ARG B1715
SHEET 4 L10 GLY B1735 LEU B1738 1 N GLY B1735 O VAL B1695
SHEET 5 L10 PRO B1764 GLY B1767 1 N PRO B1764 O ILE B1736
SHEET 6 L10 ALA B1847 PHE B1850 1 N PHE B1848 O VAL B1765
SHEET 7 L10 GLY B1839 ARG B1842 -1 N ILE B1840 O SER B1849
SHEET 8 L10 LEU B1825 SER B1831 -1 N HIS B1829 O GLY B1839
SHEET 9 L10 HIS B1795 ASP B1799 -1 N LYS B1798 O LYS B1830
SHEET 10 L10 VAL B1804 THR B1808 -1 N THR B1808 O HIS B1795
SHEET 1 M 2 THR B1783 LYS B1785 0
SHEET 2 M 2 PHE B1814 VAL B1816 -1 N ALA B1815 O VAL B1784
SHEET 1 N 2 HIS B1790 GLY B1792 0
SHEET 2 N 2 GLN B1810 HIS B1812 -1 N HIS B1812 O HIS B1790
SHEET 1 O 5 THR C2114 ILE C2116 0
SHEET 2 O 5 ALA C2085 LEU C2087 1 N VAL C2086 O THR C2114
SHEET 3 O 5 SER C2009 LEU C2013 1 N LEU C2011 O ALA C2085
SHEET 4 O 5 ARG C2043 VAL C2047 1 N ARG C2043 O ILE C2010
SHEET 5 O 5 ALA C2063 TYR C2065 1 N ALA C2063 O ASN C2046
SHEET 1 P 4 SER C2146 ALA C2149 0
SHEET 2 P 4 LEU C2204 GLU C2208 -1 N ILE C2206 O GLY C2147
SHEET 3 P 4 CYS C2166 PRO C2170 -1 N ARG C2169 O LEU C2205
SHEET 4 P 4 GLY C2180 ALA C2182 -1 N ALA C2182 O CYS C2166
SHEET 1 Q 4 CYS C2228 GLU C2235 0
SHEET 2 Q 4 LYS C2214 ARG C2222 -1 N VAL C2221 O ILE C2229
SHEET 3 Q 4 GLY C2280 VAL C2288 -1 N VAL C2288 O LYS C2214
SHEET 4 Q 4 LEU C2295 ASN C2301 -1 N ASN C2301 O ASN C2283
SHEET 1 R 3 THR C2249 ALA C2251 0
SHEET 2 R 3 VAL C2355 ARG C2361 -1 N LYS C2358 O THR C2249
SHEET 3 R 3 GLY C2382 GLY C2388 -1 N GLY C2388 O VAL C2355
SHEET 1 S 6 VAL C2525 ARG C2528 0
SHEET 2 S 6 ALA C2541 THR C2546 -1 N THR C2546 O VAL C2525
SHEET 3 S 6 ARG C2615 PHE C2618 1 N LEU C2616 O ALA C2541
SHEET 4 S 6 GLU C2595 ASN C2600 1 N MET C2598 O ARG C2615
SHEET 5 S 6 LYS C2561 LEU C2565 1 N ILE C2562 O GLU C2595
SHEET 6 S 6 GLY C2637 ILE C2639 1 N GLY C2637 O MET C2563
SHEET 1 T 4 ASN C2692 VAL C2695 0
SHEET 2 T 4 VAL C2750 HIS C2754 -1 N LEU C2752 O ALA C2693
SHEET 3 T 4 LEU C2712 ARG C2715 -1 N ARG C2715 O LEU C2751
SHEET 4 T 4 GLU C2726 VAL C2728 -1 N VAL C2728 O LEU C2712
SHEET 1 U 4 VAL C2773 GLU C2780 0
SHEET 2 U 4 VAL C2760 CYS C2768 -1 N ILE C2767 O LEU C2774
SHEET 3 U 4 GLY C2824 LYS C2833 -1 N VAL C2832 O VAL C2760
SHEET 4 U 4 GLU C2836 ASN C2843 -1 N ASN C2843 O ASN C2827
SHEET 1 V 3 CYS C2794 LEU C2796 0
SHEET 2 V 3 TYR C2888 LEU C2895 -1 N LYS C2891 O CYS C2794
SHEET 3 V 3 SER C2913 GLY C2921 -1 N GLY C2921 O TYR C2888
SHEET 1 W 4 TYR C3012 ASN C3015 0
SHEET 2 W 4 ARG C2944 SER C2948 1 N LEU C2946 O TYR C3012
SHEET 3 W 4 GLU C2970 THR C2974 1 N GLU C2970 O ALA C2945
SHEET 4 W 4 ARG C2989 VAL C2991 1 N ARG C2989 O ALA C2973
SHEET 1 X 7 GLN D3514 ARG D3518 0
SHEET 2 X 7 SER D3504 LEU D3509 -1 N LEU D3507 O PHE D3515
SHEET 3 X 7 GLN D3628 ALA D3634 -1 N ILE D3633 O LEU D3506
SHEET 4 X 7 GLY D3524 ASN D3533 -1 N VAL D3530 O GLN D3628
SHEET 5 X 7 GLN D3551 LEU D3555 1 N ILE D3552 O GLU D3529
SHEET 6 X 7 GLY D3579 VAL D3581 1 N GLY D3579 O VAL D3553
SHEET 7 X 7 VAL D3608 ILE D3610 1 N VAL D3608 O LEU D3580
SHEET 1 Y10 TYR D3668 TRP D3670 0
SHEET 2 Y10 CYS D3714 PRO D3720 -1 N ILE D3718 O TYR D3668
SHEET 3 Y10 PHE D3692 ASP D3698 1 N PHE D3692 O ARG D3715
SHEET 4 Y10 GLY D3735 LEU D3738 1 N GLY D3735 O VAL D3695
SHEET 5 Y10 PRO D3764 GLY D3767 1 N PRO D3764 O ILE D3736
SHEET 6 Y10 ALA D3847 PHE D3850 1 N PHE D3848 O VAL D3765
SHEET 7 Y10 GLY D3839 ARG D3842 -1 N ILE D3840 O SER D3849
SHEET 8 Y10 LEU D3825 SER D3831 -1 N HIS D3829 O GLY D3839
SHEET 9 Y10 HIS D3795 ASP D3799 -1 N LYS D3798 O LYS D3830
SHEET 10 Y10 VAL D3804 THR D3808 -1 N THR D3808 O HIS D3795
SHEET 1 Z 2 THR D3783 LYS D3785 0
SHEET 2 Z 2 PHE D3814 VAL D3816 -1 N ALA D3815 O VAL D3784
SHEET 1 AA 2 HIS D3790 GLY D3792 0
SHEET 2 AA 2 GLN D3810 HIS D3812 -1 N HIS D3812 O HIS D3790
SHEET 1 AB 5 THR E4114 ILE E4116 0
SHEET 2 AB 5 ALA E4085 LEU E4087 1 N VAL E4086 O THR E4114
SHEET 3 AB 5 SER E4009 LEU E4013 1 N LEU E4011 O ALA E4085
SHEET 4 AB 5 ARG E4043 VAL E4047 1 N ARG E4043 O ILE E4010
SHEET 5 AB 5 ALA E4063 TYR E4065 1 N ALA E4063 O ASN E4046
SHEET 1 AC 4 SER E4146 ALA E4149 0
SHEET 2 AC 4 LEU E4204 GLU E4208 -1 N ILE E4206 O GLY E4147
SHEET 3 AC 4 CYS E4166 PRO E4170 -1 N ARG E4169 O LEU E4205
SHEET 4 AC 4 GLY E4180 ALA E4182 -1 N ALA E4182 O CYS E4166
SHEET 1 AD 4 CYS E4228 GLU E4235 0
SHEET 2 AD 4 LYS E4214 ARG E4222 -1 N VAL E4221 O ILE E4229
SHEET 3 AD 4 GLY E4280 ASN E4289 -1 N VAL E4288 O LYS E4214
SHEET 4 AD 4 ARG E4294 ASN E4301 -1 N ASN E4301 O ASN E4283
SHEET 1 AE 3 THR E4249 ALA E4251 0
SHEET 2 AE 3 VAL E4355 ARG E4361 -1 N LYS E4358 O THR E4249
SHEET 3 AE 3 GLY E4382 GLY E4388 -1 N GLY E4388 O VAL E4355
SHEET 1 AF 2 VAL E4525 ARG E4528 0
SHEET 2 AF 2 MET E4543 THR E4546 -1 N THR E4546 O VAL E4525
SHEET 1 AG 4 GLY E4637 ILE E4639 0
SHEET 2 AG 4 LYS E4561 LEU E4565 1 N MET E4563 O GLY E4637
SHEET 3 AG 4 GLU E4595 ASN E4600 1 N GLU E4595 O ILE E4562
SHEET 4 AG 4 ARG E4615 PHE E4618 1 N ARG E4615 O MET E4598
SHEET 1 AH 4 ASN E4692 VAL E4695 0
SHEET 2 AH 4 VAL E4750 HIS E4754 -1 N LEU E4752 O ALA E4693
SHEET 3 AH 4 LEU E4712 ARG E4715 -1 N ARG E4715 O LEU E4751
SHEET 4 AH 4 GLU E4726 VAL E4728 -1 N VAL E4728 O LEU E4712
SHEET 1 AI 4 VAL E4773 GLU E4780 0
SHEET 2 AI 4 VAL E4760 CYS E4768 -1 N ILE E4767 O LEU E4774
SHEET 3 AI 4 GLY E4824 LYS E4833 -1 N VAL E4832 O VAL E4760
SHEET 4 AI 4 GLU E4836 ASN E4843 -1 N ASN E4843 O ASN E4827
SHEET 1 AJ 3 CYS E4794 LEU E4796 0
SHEET 2 AJ 3 TYR E4888 LEU E4895 -1 N LYS E4891 O CYS E4794
SHEET 3 AJ 3 SER E4913 GLY E4921 -1 N GLY E4921 O TYR E4888
SHEET 1 AK 5 HIS E5039 ASP E5041 0
SHEET 2 AK 5 TYR E5012 ASN E5015 1 N ILE E5013 O HIS E5039
SHEET 3 AK 5 ARG E4944 SER E4948 1 N LEU E4946 O TYR E5012
SHEET 4 AK 5 GLU E4970 THR E4974 1 N GLU E4970 O ALA E4945
SHEET 5 AK 5 ARG E4989 VAL E4991 1 N ARG E4989 O ALA E4973
SHEET 1 AL 7 GLN F5514 ARG F5518 0
SHEET 2 AL 7 SER F5504 LEU F5509 -1 N LEU F5507 O PHE F5515
SHEET 3 AL 7 GLN F5628 ALA F5634 -1 N ILE F5633 O LEU F5506
SHEET 4 AL 7 GLY F5524 ASN F5533 -1 N VAL F5530 O GLN F5628
SHEET 5 AL 7 GLN F5551 LEU F5555 1 N ILE F5552 O GLU F5529
SHEET 6 AL 7 GLY F5579 VAL F5581 1 N GLY F5579 O VAL F5553
SHEET 7 AL 7 VAL F5608 ILE F5610 1 N VAL F5608 O LEU F5580
SHEET 1 AM10 TYR F5668 TRP F5670 0
SHEET 2 AM10 CYS F5714 PRO F5720 -1 N ILE F5718 O TYR F5668
SHEET 3 AM10 PHE F5692 ASP F5698 1 N PHE F5692 O ARG F5715
SHEET 4 AM10 GLY F5735 LEU F5738 1 N GLY F5735 O VAL F5695
SHEET 5 AM10 PRO F5764 GLY F5767 1 N PRO F5764 O ILE F5736
SHEET 6 AM10 ALA F5847 PHE F5850 1 N PHE F5848 O VAL F5765
SHEET 7 AM10 GLY F5839 ARG F5842 -1 N ILE F5840 O SER F5849
SHEET 8 AM10 LEU F5825 SER F5831 -1 N HIS F5829 O GLY F5839
SHEET 9 AM10 HIS F5795 ASP F5799 -1 N LYS F5798 O LYS F5830
SHEET 10 AM10 VAL F5804 THR F5808 -1 N THR F5808 O HIS F5795
SHEET 1 AN 2 THR F5783 LYS F5785 0
SHEET 2 AN 2 PHE F5814 VAL F5816 -1 N ALA F5815 O VAL F5784
SHEET 1 AO 2 HIS F5790 GLY F5792 0
SHEET 2 AO 2 GLN F5810 HIS F5812 -1 N HIS F5812 O HIS F5790
SHEET 1 AP 5 THR G6114 ILE G6116 0
SHEET 2 AP 5 ALA G6085 LEU G6087 1 N VAL G6086 O THR G6114
SHEET 3 AP 5 SER G6009 LEU G6013 1 N LEU G6011 O ALA G6085
SHEET 4 AP 5 ARG G6043 VAL G6047 1 N ARG G6043 O ILE G6010
SHEET 5 AP 5 ALA G6063 TYR G6065 1 N ALA G6063 O ASN G6046
SHEET 1 AQ 4 SER G6146 ALA G6149 0
SHEET 2 AQ 4 LEU G6204 GLU G6208 -1 N ILE G6206 O GLY G6147
SHEET 3 AQ 4 CYS G6166 PRO G6170 -1 N ARG G6169 O LEU G6205
SHEET 4 AQ 4 GLY G6180 ALA G6182 -1 N ALA G6182 O CYS G6166
SHEET 1 AR 4 CYS G6228 GLU G6235 0
SHEET 2 AR 4 LYS G6214 ARG G6222 -1 N VAL G6221 O ILE G6229
SHEET 3 AR 4 GLY G6280 ASN G6289 -1 N VAL G6288 O LYS G6214
SHEET 4 AR 4 ARG G6294 ASN G6301 -1 N ASN G6301 O ASN G6283
SHEET 1 AS 3 THR G6249 ALA G6251 0
SHEET 2 AS 3 VAL G6355 ARG G6361 -1 N LYS G6358 O THR G6249
SHEET 3 AS 3 GLY G6382 GLY G6388 -1 N GLY G6388 O VAL G6355
SHEET 1 AT 6 VAL G6525 ARG G6528 0
SHEET 2 AT 6 ALA G6541 THR G6546 -1 N THR G6546 O VAL G6525
SHEET 3 AT 6 ARG G6615 PHE G6618 1 N LEU G6616 O ALA G6541
SHEET 4 AT 6 GLU G6595 ASN G6600 1 N MET G6598 O ARG G6615
SHEET 5 AT 6 LYS G6561 LEU G6565 1 N ILE G6562 O GLU G6595
SHEET 6 AT 6 GLY G6637 ILE G6639 1 N GLY G6637 O MET G6563
SHEET 1 AU 4 ASN G6692 THR G6694 0
SHEET 2 AU 4 LEU G6751 HIS G6754 -1 N LEU G6752 O ALA G6693
SHEET 3 AU 4 LEU G6712 ARG G6715 -1 N ARG G6715 O LEU G6751
SHEET 4 AU 4 GLU G6726 VAL G6728 -1 N VAL G6728 O LEU G6712
SHEET 1 AV 4 VAL G6773 GLU G6780 0
SHEET 2 AV 4 VAL G6760 CYS G6768 -1 N ILE G6767 O LEU G6774
SHEET 3 AV 4 GLY G6824 VAL G6832 -1 N VAL G6832 O VAL G6760
SHEET 4 AV 4 VAL G6837 ASN G6843 -1 N ASN G6843 O ASN G6827
SHEET 1 AW 3 CYS G6794 LEU G6796 0
SHEET 2 AW 3 TYR G6888 LEU G6895 -1 N LYS G6891 O CYS G6794
SHEET 3 AW 3 SER G6913 GLY G6921 -1 N GLY G6921 O TYR G6888
SHEET 1 AX 5 HIS G7039 ASP G7041 0
SHEET 2 AX 5 TYR G7012 ASN G7015 1 N ILE G7013 O HIS G7039
SHEET 3 AX 5 ARG G6944 SER G6948 1 N LEU G6946 O TYR G7012
SHEET 4 AX 5 GLU G6970 THR G6974 1 N GLU G6970 O ALA G6945
SHEET 5 AX 5 ARG G6989 VAL G6991 1 N ARG G6989 O ALA G6973
SHEET 1 AY 7 GLN H7514 ARG H7518 0
SHEET 2 AY 7 SER H7504 LEU H7509 -1 N LEU H7507 O PHE H7515
SHEET 3 AY 7 GLN H7628 ALA H7634 -1 N ILE H7633 O LEU H7506
SHEET 4 AY 7 GLY H7524 ASN H7533 -1 N VAL H7530 O GLN H7628
SHEET 5 AY 7 GLN H7551 LEU H7555 1 N ILE H7552 O GLU H7529
SHEET 6 AY 7 GLY H7579 VAL H7581 1 N GLY H7579 O VAL H7553
SHEET 7 AY 7 VAL H7608 ILE H7610 1 N VAL H7608 O LEU H7580
SHEET 1 AZ10 TYR H7668 TRP H7670 0
SHEET 2 AZ10 CYS H7714 VAL H7719 -1 N ILE H7718 O TYR H7668
SHEET 3 AZ10 PHE H7692 TYR H7697 1 N PHE H7692 O ARG H7715
SHEET 4 AZ10 GLY H7735 LEU H7738 1 N GLY H7735 O VAL H7695
SHEET 5 AZ10 VAL H7765 GLY H7767 1 N PHE H7766 O ILE H7736
SHEET 6 AZ10 ALA H7847 PHE H7850 1 N PHE H7848 O VAL H7765
SHEET 7 AZ10 GLY H7839 ARG H7842 -1 N ILE H7840 O SER H7849
SHEET 8 AZ10 LEU H7825 SER H7831 -1 N HIS H7829 O GLY H7839
SHEET 9 AZ10 HIS H7795 ASP H7799 -1 N LYS H7798 O LYS H7830
SHEET 10 AZ10 VAL H7804 THR H7808 -1 N THR H7808 O HIS H7795
SHEET 1 BA 2 THR H7783 LYS H7785 0
SHEET 2 BA 2 PHE H7814 VAL H7816 -1 N ALA H7815 O VAL H7784
SHEET 1 BB 2 HIS H7790 GLY H7792 0
SHEET 2 BB 2 GLN H7810 HIS H7812 -1 N HIS H7812 O HIS H7790
LINK N CYG B1769 C ILE B1768 1555 1555 1.32
LINK C CYG B1769 N LEU B1770 1555 1555 1.35
LINK N CYG D3769 C ILE D3768 1555 1555 1.35
LINK C CYG D3769 N LEU D3770 1555 1555 1.33
LINK N CYG F5769 C ILE F5768 1555 1555 1.33
LINK C CYG F5769 N LEU F5770 1555 1555 1.33
LINK N CYG H7769 C ILE H7768 1555 1555 1.34
LINK C CYG H7769 N LEU H7770 1555 1555 1.33
LINK O1A ADP A1900 MN MN A1902 1555 1555 2.04
LINK MN MN A1901 O HOH A2674 1555 1555 2.25
LINK MN MN A1901 OE1 GLU A 299 1555 1555 2.43
LINK MN MN A1901 OE2 GLU A 299 1555 1555 2.45
LINK MN MN A1901 O3B ADP A1900 1555 1555 2.23
LINK MN MN A1901 OD1 ASN A 301 1555 1555 2.07
LINK MN MN A1901 O1 PO4 A1906 1555 1555 2.05
LINK MN MN A1902 OE2 GLU A 299 1555 1555 2.24
LINK MN MN A1902 O1B ADP A1900 1555 1555 2.19
LINK MN MN A1902 OE1 GLN A 285 1555 1555 2.10
LINK MN MN A1902 O2 PO4 A1906 1555 1555 2.14
LINK K K A1903 OE1 GLU A 215 1555 1555 2.70
LINK K K A1903 O ALA A 239 1555 1555 2.87
LINK K K A1903 O ILE A 242 1555 1555 2.61
LINK K K A1903 OD1 ASN A 236 1555 1555 2.70
LINK K K A1903 O ASP A 238 1555 1555 2.93
LINK K K A1903 OG SER A 247 1555 1555 2.80
LINK K K A1904 OE2 GLU A 127 1555 1555 3.02
LINK K K A1904 O HOH A2081 1555 1555 3.17
LINK K K A1904 O HOH A2085 1555 1555 3.30
LINK K K A1904 O HOH A2674 1555 1555 2.88
LINK K K A1904 O ALA A 126 1555 1555 3.31
LINK K K A1904 O MET A 300 1555 1555 2.61
LINK K K A1904 OE1 GLU A 299 1555 1555 2.83
LINK K K A1904 OD1 ASN A 301 1555 1555 3.59
LINK MN MN A1911 OE1 GLN A 829 1555 1555 2.44
LINK MN MN A1911 OE2 GLU A 841 1555 1555 2.02
LINK MN MN A1911 O3B ADP A1910 1555 1555 2.24
LINK MN MN A1911 O2A ADP A1910 1555 1555 2.09
LINK K K A1912 OE2 GLU A 841 1555 1555 2.82
LINK K K A1912 O3B ADP A1910 1555 1555 3.29
LINK K K A1912 O HOH A2561 1555 1555 3.55
LINK K K A1912 O2B ADP A1910 1555 1555 2.81
LINK K K A1912 O HOH A2791 1555 1555 3.39
LINK K K A1912 OE1 GLU A 841 1555 1555 2.76
LINK K K A1912 OD1 ASN A 843 1555 1555 2.70
LINK K K A1912 O HOH A2789 1555 1555 3.67
LINK K K A1913 O GLU A 783 1555 1555 2.90
LINK K K A1913 O GLN A 784 1555 1555 2.89
LINK K K A1913 O VAL A 787 1555 1555 2.67
LINK K K A1913 OG SER A 792 1555 1555 2.79
LINK K K A1913 OE1 GLU A 761 1555 1555 2.61
LINK K K A1913 ND1 HIS A 781 1555 1555 2.80
LINK K K A1940 O ASP A 84 1555 1555 2.74
LINK K K A1940 O GLY A 112 1555 1555 2.73
LINK K K A1940 N THR A 114 1555 1555 3.65
LINK K K A1940 OG1 THR A 114 1555 1555 2.84
LINK K K A1940 O HOH A2426 1555 1555 3.07
LINK K K A1940 O HOH A2615 1555 1555 3.54
LINK K K A1940 O HOH A2628 1555 1555 2.89
LINK K K A1942 OD1 ASN A 283 1555 1555 3.17
LINK K K A1942 OE1 GLN A 285 1555 1555 2.97
LINK K K A1942 O2 PO4 A1906 1555 1555 3.04
LINK K K A1942 O HOH A2124 1555 1555 2.94
LINK K K A1942 OE1 GLU A 217 1555 1555 2.76
LINK K K A1942 OG1 THR A 244 1555 1555 3.21
LINK K K A1942 O HOH A2125 1555 1555 3.29
LINK K K A1942 ND2 ASN A 283 1555 1555 3.60
LINK K K A1942 OG SER A 307 1555 1555 3.65
LINK K K A1943 O HOH A2479 1555 1555 3.26
LINK K K A1943 OG1 THR A 143 1555 1555 3.15
LINK K K A1943 O ALA A 144 1555 1555 3.14
LINK K K A1943 O HOH A2478 1555 1555 2.65
LINK K K A1943 O THR A 143 1555 1555 3.00
LINK K K A1943 O HOH A2477 1555 1555 3.36
LINK K K B1941 O ASP B1612 1555 1555 2.63
LINK K K B1941 O HOH A2417 1555 1555 3.41
LINK K K B1941 O HIS B1516 1555 1555 2.66
LINK K K B1941 O HOH A2288 1555 1555 3.35
LINK K K B1941 O HOH B1977 1555 1555 3.58
LINK K K B1941 O HOH B1984 1555 1555 2.60
LINK K K B1941 O HOH B2143 1555 1555 3.21
LINK O1A ADP C3900 MN MN C3902 1555 1555 2.02
LINK MN MN C3901 O HOH C4447 1555 1555 2.17
LINK MN MN C3901 OD1 ASN C2301 1555 1555 2.22
LINK MN MN C3901 O1 PO4 C3906 1555 1555 2.17
LINK MN MN C3901 OE2 GLU C2299 1555 1555 2.47
LINK MN MN C3901 OE1 GLU C2299 1555 1555 2.17
LINK MN MN C3901 O3B ADP C3900 1555 1555 2.07
LINK MN MN C3902 OE2 GLU C2299 1555 1555 2.30
LINK MN MN C3902 OE1 GLN C2285 1555 1555 2.22
LINK MN MN C3902 O2 PO4 C3906 1555 1555 2.12
LINK MN MN C3902 O1B ADP C3900 1555 1555 2.41
LINK MN MN C3902 O HOH C4661 1555 1555 2.24
LINK K K C3903 O ASP C2238 1555 1555 2.91
LINK K K C3903 O ALA C2239 1555 1555 2.97
LINK K K C3903 OE1 GLU C2215 1555 1555 2.56
LINK K K C3903 OD1 ASN C2236 1555 1555 2.59
LINK K K C3903 OG SER C2247 1555 1555 2.72
LINK K K C3903 O ILE C2242 1555 1555 2.60
LINK K K C3904 O ALA C2126 1555 1555 3.35
LINK K K C3904 OE2 GLU C2127 1555 1555 2.99
LINK K K C3904 OE1 GLU C2299 1555 1555 2.63
LINK K K C3904 O MET C2300 1555 1555 2.68
LINK K K C3904 O HOH C4079 1555 1555 2.95
LINK K K C3904 O HOH C4632 1555 1555 2.69
LINK K K C3904 O HOH C4083 1555 1555 3.62
LINK K K C3904 O HOH C4447 1555 1555 3.14
LINK K K C3904 OD1 ASN C2301 1555 1555 3.21
LINK K K C3904 MN MN C3901 1555 1555 3.69
LINK MN MN C3911 OE2 GLU C2841 1555 1555 1.92
LINK MN MN C3911 O3B ADP C3910 1555 1555 2.06
LINK MN MN C3911 OE1 GLN C2829 1555 1555 2.39
LINK MN MN C3911 NE2 GLN C2829 1555 1555 2.76
LINK MN MN C3911 O HOH C4825 1555 1555 2.41
LINK MN MN C3911 O2A ADP C3910 1555 1555 2.21
LINK K K C3912 OE1 GLU C2841 1555 1555 2.65
LINK K K C3912 OE2 GLU C2841 1555 1555 3.29
LINK K K C3912 OD1 ASN C2843 1555 1555 3.26
LINK K K C3912 O3B ADP C3910 1555 1555 3.26
LINK K K C3912 O2B ADP C3910 1555 1555 2.67
LINK K K C3913 O VAL C2787 1555 1555 2.65
LINK K K C3913 ND1 HIS C2781 1555 1555 2.99
LINK K K C3913 OE1 GLU C2761 1555 1555 2.64
LINK K K C3913 O GLU C2783 1555 1555 2.79
LINK K K C3913 O GLN C2784 1555 1555 2.89
LINK K K C3913 OG SER C2792 1555 1555 2.79
LINK K K C3940 OG1 THR C2114 1555 1555 2.82
LINK K K C3940 O HOH C4424 1555 1555 3.35
LINK K K C3940 O ASP C2084 1555 1555 2.60
LINK K K C3940 O GLY C2112 1555 1555 2.96
LINK K K C3940 N THR C2114 1555 1555 3.55
LINK K K C3942 ND2 ASN C2283 1555 1555 3.21
LINK K K C3942 O HOH C4123 1555 1555 3.49
LINK K K C3942 O2 PO4 C3906 1555 1555 2.93
LINK K K C3942 OE1 GLN C2285 1555 1555 2.65
LINK K K C3942 O HOH C4122 1555 1555 2.93
LINK K K C3942 OG1 THR C2244 1555 1555 3.55
LINK K K C3942 OD1 ASN C2283 1555 1555 3.30
LINK K K C3942 OE1 GLU C2217 1555 1555 3.43
LINK K K C3943 O THR C2143 1555 1555 2.92
LINK K K C3943 O HOH C4473 1555 1555 2.70
LINK K K C3943 O HOH C4648 1555 1555 2.72
LINK K K C3943 OG1 THR C2143 1555 1555 3.17
LINK K K C3943 O HOH C4640 1555 1555 3.48
LINK K K C3943 O HOH C4475 1555 1555 3.52
LINK K K C3943 O ALA C2144 1555 1555 3.36
LINK K K C3943 O HOH C4474 1555 1555 2.70
LINK K K D3941 O HIS D3516 1555 1555 2.76
LINK K K D3941 O HOH C4414 1555 1555 3.12
LINK K K D3941 O HOH D3986 1555 1555 2.66
LINK K K D3941 O ASP D3612 1555 1555 2.70
LINK K K D3941 O HOH C4283 1555 1555 3.61
LINK MN MN E5901 OE1 GLU E4299 1555 1555 2.36
LINK MN MN E5901 OE2 GLU E4299 1555 1555 2.42
LINK MN MN E5901 O HOH E6698 1555 1555 2.15
LINK MN MN E5901 O3B ADP E5900 1555 1555 2.22
LINK MN MN E5901 O1 PO4 E5906 1555 1555 1.90
LINK MN MN E5901 OD1 ASN E4301 1555 1555 2.07
LINK MN MN E5902 O1A ADP E5900 1555 1555 2.08
LINK MN MN E5902 O2 PO4 E5906 1555 1555 2.13
LINK MN MN E5902 OE2 GLU E4299 1555 1555 2.16
LINK MN MN E5902 OE1 GLN E4285 1555 1555 2.16
LINK MN MN E5902 O1B ADP E5900 1555 1555 2.09
LINK MN MN E5902 O HOH E6707 1555 1555 2.17
LINK K K E5903 O ASP E4238 1555 1555 2.72
LINK K K E5903 O ALA E4239 1555 1555 2.82
LINK K K E5903 OG SER E4247 1555 1555 2.76
LINK K K E5903 OE1 GLU E4215 1555 1555 2.38
LINK K K E5903 OD1 ASN E4236 1555 1555 2.88
LINK K K E5903 O ILE E4242 1555 1555 2.57
LINK K K E5904 OE2 GLU E4127 1555 1555 2.81
LINK K K E5904 OE1 GLU E4299 1555 1555 2.76
LINK K K E5904 O HOH E6087 1555 1555 3.24
LINK K K E5904 O ALA E4126 1555 1555 3.34
LINK K K E5904 O HOH E6083 1555 1555 2.61
LINK K K E5904 OD1 ASN E4301 1555 1555 3.51
LINK K K E5904 O HOH E6698 1555 1555 3.04
LINK K K E5904 O MET E4300 1555 1555 2.59
LINK MN MN E5911 OE1 GLN E4829 1555 1555 2.35
LINK MN MN E5911 O3B ADP E5910 1555 1555 2.22
LINK MN MN E5911 OE2 GLU E4841 1555 1555 1.92
LINK MN MN E5911 O2A ADP E5910 1555 1555 2.07
LINK K K E5912 OE1 GLU E4841 1555 1555 2.75
LINK K K E5912 OE2 GLU E4841 1555 1555 2.92
LINK K K E5912 O2B ADP E5910 1555 1555 2.70
LINK K K E5912 O3B ADP E5910 1555 1555 3.26
LINK K K E5912 OD1 ASN E4843 1555 1555 3.19
LINK K K E5913 ND1 HIS E4781 1555 1555 2.84
LINK K K E5913 O GLU E4783 1555 1555 2.80
LINK K K E5913 OG SER E4792 1555 1555 2.74
LINK K K E5913 OE1 GLU E4761 1555 1555 2.63
LINK K K E5913 O GLN E4784 1555 1555 2.86
LINK K K E5913 O VAL E4787 1555 1555 2.50
LINK K K E5940 N THR E4114 1555 1555 3.60
LINK K K E5940 OG1 THR E4114 1555 1555 2.55
LINK K K E5940 O HOH E6628 1555 1555 3.26
LINK K K E5940 O HOH E6431 1555 1555 2.88
LINK K K E5940 O GLY E4112 1555 1555 2.79
LINK K K E5940 O ASP E4084 1555 1555 2.92
LINK K K E5942 OD1 ASN E4283 1555 1555 3.17
LINK K K E5942 ND2 ASN E4283 1555 1555 3.64
LINK K K E5942 O HOH E6128 1555 1555 3.10
LINK K K E5942 OG1 THR E4244 1555 1555 3.49
LINK K K E5942 OE1 GLN E4285 1555 1555 2.53
LINK K K E5942 MN MN E5902 1555 1555 3.70
LINK K K E5942 O2 PO4 E5906 1555 1555 2.97
LINK K K E5942 OE1 GLU E4217 1555 1555 2.80
LINK K K E5943 OG1 THR E4143 1555 1555 2.80
LINK K K E5943 O HOH E6485 1555 1555 3.06
LINK K K E5943 O HOH E6483 1555 1555 2.81
LINK K K E5943 O ALA E4144 1555 1555 3.05
LINK K K E5943 O THR E4143 1555 1555 3.25
LINK K K E5943 O HOH E6484 1555 1555 2.51
LINK K K F5941 O HOH E6291 1555 1555 3.60
LINK K K F5941 O ASP F5612 1555 1555 2.85
LINK K K F5941 O HOH E6419 1555 1555 2.88
LINK K K F5941 O HIS F5516 1555 1555 2.74
LINK K K F5941 O HOH F2588 1555 1555 2.68
LINK MN MN G7901 O3B ADP G7900 1555 1555 2.44
LINK MN MN G7901 O1 PO4 G7906 1555 1555 1.80
LINK MN MN G7901 OD1 ASN G6301 1555 1555 2.21
LINK MN MN G7901 OE2 GLU G6299 1555 1555 2.39
LINK MN MN G7901 OE1 GLU G6299 1555 1555 2.29
LINK MN MN G7901 O HOH G 851 1555 1555 2.49
LINK MN MN G7902 O1B ADP G7900 1555 1555 2.22
LINK MN MN G7902 O HOH G 874 1555 1555 2.18
LINK MN MN G7902 O1A ADP G7900 1555 1555 2.08
LINK MN MN G7902 O2 PO4 G7906 1555 1555 2.18
LINK MN MN G7902 OE2 GLU G6299 1555 1555 2.22
LINK MN MN G7902 OE1 GLN G6285 1555 1555 2.02
LINK K K G7903 O ALA G6239 1555 1555 2.77
LINK K K G7903 OD1 ASN G6236 1555 1555 2.81
LINK K K G7903 OG SER G6247 1555 1555 2.77
LINK K K G7903 OE1 GLU G6215 1555 1555 2.46
LINK K K G7903 O ASP G6238 1555 1555 2.84
LINK K K G7903 O ILE G6242 1555 1555 2.57
LINK K K G7904 O HOH G 96 1555 1555 2.97
LINK K K G7904 OE2 GLU G6127 1555 1555 2.86
LINK K K G7904 O MET G6300 1555 1555 2.82
LINK K K G7904 OE1 GLU G6299 1555 1555 2.72
LINK K K G7904 OD1 ASN G6301 1555 1555 3.59
LINK K K G7904 O HOH G 851 1555 1555 2.74
LINK K K G7904 O ALA G6126 1555 1555 3.37
LINK K K G7904 O HOH G 100 1555 1555 3.24
LINK MN MN G7911 O3B ADP G7910 1555 1555 2.17
LINK MN MN G7911 O2A ADP G7910 1555 1555 2.18
LINK MN MN G7911 OE2 GLU G6841 1555 1555 1.93
LINK MN MN G7911 OE1 GLN G6829 1555 1555 2.23
LINK K K G7912 OE2 GLU G6841 1555 1555 3.04
LINK K K G7912 O3B ADP G7910 1555 1555 3.22
LINK K K G7912 OE1 GLU G6841 1555 1555 2.91
LINK K K G7912 O2B ADP G7910 1555 1555 2.76
LINK K K G7912 OD1 ASN G6843 1555 1555 3.23
LINK K K G7913 OG SER G6792 1555 1555 2.73
LINK K K G7913 O GLN G6784 1555 1555 2.84
LINK K K G7913 O VAL G6787 1555 1555 2.66
LINK K K G7913 O GLU G6783 1555 1555 2.73
LINK K K G7913 OE1 GLU G6761 1555 1555 2.36
LINK K K G7913 ND1 HIS G6781 1555 1555 2.96
LINK K K G7940 OG1 THR G6114 1555 1555 3.00
LINK K K G7940 O GLY G6112 1555 1555 2.63
LINK K K G7940 O HOH G 835 1555 1555 2.91
LINK K K G7940 O ASP G6084 1555 1555 2.79
LINK K K G7940 O HOH G 626 1555 1555 3.37
LINK K K G7942 O HOH G 143 1555 1555 2.54
LINK K K G7942 OG1 THR G6244 1555 1555 3.37
LINK K K G7942 O HOH G 144 1555 1555 3.34
LINK K K G7942 OD1 ASN G6283 1555 1555 3.53
LINK K K G7942 OE1 GLN G6285 1555 1555 2.92
LINK K K G7942 O2 PO4 G7906 1555 1555 2.89
LINK K K G7942 O HOH G 874 1555 1555 3.71
LINK K K G7942 OG SER G6307 1555 1555 3.60
LINK K K G7942 ND2 ASN G6283 1555 1555 3.48
LINK K K G7942 OE1 GLU G6217 1555 1555 3.09
LINK K K G7943 O HOH G 677 1555 1555 2.95
LINK K K G7943 O HOH G 678 1555 1555 2.66
LINK K K G7943 O HOH G 679 1555 1555 3.34
LINK K K G7943 O ALA G6144 1555 1555 3.42
LINK K K G7943 O THR G6143 1555 1555 2.88
LINK K K G7943 OG1 THR G6143 1555 1555 2.96
LINK K K H7941 O ASP H7612 1555 1555 2.66
LINK K K H7941 O HIS H7516 1555 1555 2.96
LINK K K H7941 O HOH G 549 1555 1555 3.47
LINK K K H7941 O HOH H 468 1555 1555 2.76
CISPEP 1 PHE A 164 PRO A 165 0 -0.01
CISPEP 2 ALA A 251 PRO A 252 0 0.45
CISPEP 3 TYR A 710 PRO A 711 0 -0.23
CISPEP 4 LEU A 796 PRO A 797 0 1.80
CISPEP 5 ARG A 998 PRO A 999 0 -2.50
CISPEP 6 SER B 1857 PRO B 1858 0 4.44
CISPEP 7 PHE C 2164 PRO C 2165 0 -0.11
CISPEP 8 ALA C 2251 PRO C 2252 0 2.76
CISPEP 9 TYR C 2710 PRO C 2711 0 0.05
CISPEP 10 LEU C 2796 PRO C 2797 0 1.77
CISPEP 11 ARG C 2998 PRO C 2999 0 -2.15
CISPEP 12 SER D 3857 PRO D 3858 0 4.92
CISPEP 13 PHE E 4164 PRO E 4165 0 0.34
CISPEP 14 ALA E 4251 PRO E 4252 0 -3.02
CISPEP 15 TYR E 4710 PRO E 4711 0 2.12
CISPEP 16 LEU E 4796 PRO E 4797 0 0.83
CISPEP 17 ARG E 4998 PRO E 4999 0 -1.49
CISPEP 18 SER F 5857 PRO F 5858 0 3.73
CISPEP 19 PHE G 6164 PRO G 6165 0 -0.68
CISPEP 20 ALA G 6251 PRO G 6252 0 0.71
CISPEP 21 TYR G 6710 PRO G 6711 0 -0.16
CISPEP 22 LEU G 6796 PRO G 6797 0 3.21
CISPEP 23 ARG G 6998 PRO G 6999 0 1.32
CISPEP 24 SER H 7857 PRO H 7858 0 3.01
SITE 1 AD1 11 ARG A 129 ARG A 169 GLY A 176 GLU A 208
SITE 2 AD1 11 LEU A 210 GLU A 215 GLY A 241 ILE A 242
SITE 3 AD1 11 HIS A 243 GLN A 285 GLU A 299
SITE 1 AD2 8 ARG A 715 HIS A 754 LEU A 756 GLU A 761
SITE 2 AD2 8 GLY A 786 VAL A 787 HIS A 788 GLU A 841
SITE 1 OR1 5 ASP A 791 GLU A 783 GLU A 892 TYR A1040
SITE 2 OR1 5 THR A1042
SITE 1 CY1 6 SER B1547 GLY B1741 GLY B1743 GLN B1773
SITE 2 CY1 6 GLY B1813 PHE B1814
SITE 1 AD3 11 ARG C2129 ARG C2169 GLY C2176 GLU C2208
SITE 2 AD3 11 LEU C2210 GLU C2215 GLY C2241 ILE C2242
SITE 3 AD3 11 HIS C2243 GLN C2285 GLU C2299
SITE 1 AD4 8 ARG C2715 HIS C2754 LEU C2756 GLU C2761
SITE 2 AD4 8 GLY C2786 VAL C2787 HIS C2788 GLU C2841
SITE 1 OR2 5 ASP C2791 GLU C2783 GLU C2892 TYR C3040
SITE 2 OR2 5 THR C3042
SITE 1 CY2 6 SER D3547 GLY D3741 GLY D3743 GLN D3773
SITE 2 CY2 6 GLY D3813 PHE D3814
SITE 1 AD5 11 ARG E4129 ARG E4169 GLY E4176 GLU E4208
SITE 2 AD5 11 LEU E4210 GLU E4215 GLY E4241 ILE E4242
SITE 3 AD5 11 HIS E4243 GLN E4285 GLU E4299
SITE 1 AD6 8 ARG E4715 HIS E4754 LEU E4756 GLU E4761
SITE 2 AD6 8 GLY E4786 VAL E4787 HIS E4788 GLU E4841
SITE 1 OR3 5 ASP E4791 GLU E4783 GLU E4892 TYR E5040
SITE 2 OR3 5 THR E5042
SITE 1 CY3 6 SER F5547 GLY F5741 GLY F5743 GLN F5773
SITE 2 CY3 6 GLY F5813 PHE F5814
SITE 1 AD7 11 ARG G6129 ARG G6169 GLY G6176 GLU G6208
SITE 2 AD7 11 LEU G6210 GLU G6215 GLY G6241 ILE G6242
SITE 3 AD7 11 HIS G6243 GLN G6285 GLU G6299
SITE 1 AD8 8 ARG G6715 HIS G6754 LEU G6756 GLU G6761
SITE 2 AD8 8 GLY G6786 VAL G6787 HIS G6788 GLU G6841
SITE 1 OR4 5 ASP G6791 GLU G6783 GLU G6892 TYR G7040
SITE 2 OR4 5 THR G7042
SITE 1 CY4 6 SER H7547 GLY H7741 GLY H7743 GLN H7773
SITE 2 CY4 6 GLY H7813 PHE H7814
SITE 1 AC1 6 HOH G 851 MET G6174 GLU G6299 ASN G6301
SITE 2 AC1 6 ADP G7900 PO4 G7906
SITE 1 AC2 5 HOH G 874 GLN G6285 GLU G6299 ADP G7900
SITE 2 AC2 5 PO4 G7906
SITE 1 AC3 6 GLU G6215 ASN G6236 ASP G6238 ALA G6239
SITE 2 AC3 6 ILE G6242 SER G6247
SITE 1 AC4 7 HOH G 96 HOH G 851 ALA G6126 GLU G6127
SITE 2 AC4 7 GLU G6299 MET G6300 ASN G6301
SITE 1 AC5 14 HOH G 32 HOH G 874 MET G6174 GLY G6175
SITE 2 AC5 14 HIS G6243 GLN G6285 GLU G6299 ASN G6301
SITE 3 AC5 14 ARG G6303 ARG G6306 ADP G7900 MN G7901
SITE 4 AC5 14 MN G7902 K G7942
SITE 1 AC6 3 GLN G6829 GLU G6841 ADP G7910
SITE 1 AC7 3 GLU G6841 ASN G6843 ADP G7910
SITE 1 AC8 6 GLU G6761 HIS G6781 GLU G6783 GLN G6784
SITE 2 AC8 6 VAL G6787 SER G6792
SITE 1 AC9 4 HOH G 64 GLN G6093 THR G6173 MET G6174
SITE 1 BC1 3 ASN G6289 ASN G6292 ARG G6294
SITE 1 BC2 6 HOH G 261 ALA G6370 ASN G6371 PHE G6900
SITE 2 BC2 6 PRO G6901 GLY G6902
SITE 1 BC3 2 PHE H7515 ASP H7614
SITE 1 BC4 3 ARG G6845 ALA G6847 ARG G6848
SITE 1 BC5 2 HOH G 645 TRP G6071
SITE 1 BC6 2 LYS G6475 ASN G6485
SITE 1 BC7 4 HOH G 835 ASP G6084 GLY G6112 THR G6114
SITE 1 BC8 3 HOH H 468 HIS H7516 ASP H7612
SITE 1 BC9 7 HOH G 143 GLU G6217 THR G6244 ASN G6283
SITE 2 BC9 7 GLN G6285 SER G6307 PO4 G7906
SITE 1 CC1 4 HOH G 677 HOH G 678 THR G6143 ALA G6144
SITE 1 CC2 2 ALA A 798 LEU A 801
SITE 1 CC3 3 GLU A 560 ASP A 592 GLY A 593
SITE 1 CC4 6 GLU C2299 ASN C2301 ADP C3900 K C3904
SITE 2 CC4 6 PO4 C3906 HOH C4447
SITE 1 CC5 5 GLN C2285 GLU C2299 ADP C3900 PO4 C3906
SITE 2 CC5 5 HOH C4661
SITE 1 CC6 6 GLU C2215 ASN C2236 ASP C2238 ALA C2239
SITE 2 CC6 6 ILE C2242 SER C2247
SITE 1 CC7 8 ALA C2126 GLU C2127 GLU C2299 MET C2300
SITE 2 CC7 8 ASN C2301 MN C3901 HOH C4079 HOH C4632
SITE 1 CC8 14 MET C2174 GLY C2175 HIS C2243 GLN C2285
SITE 2 CC8 14 GLU C2299 ASN C2301 ARG C2303 ARG C2306
SITE 3 CC8 14 ADP C3900 MN C3901 MN C3902 K C3942
SITE 4 CC8 14 HOH C4015 HOH C4122
SITE 1 CC9 4 GLN C2829 GLU C2841 ADP C3910 HOH C4825
SITE 1 DC1 3 GLU C2841 ASN C2843 ADP C3910
SITE 1 DC2 6 GLU C2761 HIS C2781 GLU C2783 GLN C2784
SITE 2 DC2 6 VAL C2787 SER C2792
SITE 1 DC3 3 THR C2173 MET C2174 HOH C4012
SITE 1 DC4 3 ASN C2289 ASN C2292 ARG C2294
SITE 1 DC5 5 ALA C2370 ASN C2371 PHE C2900 PRO C2901
SITE 2 DC5 5 GLY C2902
SITE 1 DC6 4 HOH C4414 PHE D3515 ASP D3614 HOH D3973
SITE 1 DC7 4 PHE C2578 ARG C2845 ALA C2847 ARG C2848
SITE 1 DC8 2 HIS C2070 TRP C2071
SITE 1 DC9 2 LYS C2475 ASN C2485
SITE 1 EC1 3 ASP C2084 GLY C2112 THR C2114
SITE 1 EC2 3 HIS D3516 ASP D3612 HOH D3986
SITE 1 EC3 6 GLU C2217 THR C2244 ASN C2283 GLN C2285
SITE 2 EC3 6 PO4 C3906 HOH C4122
SITE 1 EC4 5 THR C2143 ALA C2144 HOH C4473 HOH C4474
SITE 2 EC4 5 HOH C4648
SITE 1 EC5 2 ASP C2518 GLN C2519
SITE 1 EC6 2 ASP C2592 GLY C2593
SITE 1 EC7 3 LEU C2801 HOH C4827 HOH C4828
SITE 1 EC8 6 GLU E4299 ASN E4301 ADP E5900 MN E5902
SITE 2 EC8 6 PO4 E5906 HOH E6698
SITE 1 EC9 7 GLN E4285 GLU E4299 ADP E5900 MN E5901
SITE 2 EC9 7 PO4 E5906 K E5942 HOH E6707
SITE 1 FC1 6 GLU E4215 ASN E4236 ASP E4238 ALA E4239
SITE 2 FC1 6 ILE E4242 SER E4247
SITE 1 FC2 7 ALA E4126 GLU E4127 GLU E4299 MET E4300
SITE 2 FC2 7 ASN E4301 HOH E6083 HOH E6698
SITE 1 FC3 14 MET E4174 GLY E4175 HIS E4243 GLN E4285
SITE 2 FC3 14 GLU E4299 ASN E4301 ARG E4303 ARG E4306
SITE 3 FC3 14 ADP E5900 MN E5901 MN E5902 K E5942
SITE 4 FC3 14 HOH E6018 HOH E6128
SITE 1 FC4 3 GLN E4829 GLU E4841 ADP E5910
SITE 1 FC5 3 GLU E4841 ASN E4843 ADP E5910
SITE 1 FC6 6 GLU E4761 HIS E4781 GLU E4783 GLN E4784
SITE 2 FC6 6 VAL E4787 SER E4792
SITE 1 FC7 5 GLN E4093 THR E4173 MET E4174 HOH E6013
SITE 2 FC7 5 HOH E6051
SITE 1 FC8 3 ASN E4289 ASN E4292 ARG E4294
SITE 1 FC9 4 ALA E4370 ASN E4371 PRO E4901 GLY E4902
SITE 1 GC1 3 PHE F5515 ILE F5613 ASP F5614
SITE 1 GC2 4 PHE E4578 ALA E4847 ARG E4848 HOH E6824
SITE 1 GC3 1 TRP E4071
SITE 1 GC4 3 LYS E4475 ASN E4485 HOH E6286
SITE 1 GC5 4 ASP E4084 GLY E4112 THR E4114 HOH E6431
SITE 1 GC6 4 HOH E6419 HOH F2588 HIS F5516 ASP F5612
SITE 1 GC7 7 GLU E4217 THR E4244 ASN E4283 GLN E4285
SITE 2 GC7 7 MN E5902 PO4 E5906 HOH E6128
SITE 1 GC8 5 THR E4143 ALA E4144 HOH E6483 HOH E6484
SITE 2 GC8 5 HOH E6485
SITE 1 GC9 3 TYR E4799 THR E4800 LEU E4801
SITE 1 HC1 1 GLU E4560
SITE 1 HC2 2 LYS G6475 GLN G6491
SITE 1 HC3 4 ALA G6798 TYR G6799 THR G6800 LEU G6801
SITE 1 HC4 2 ASP G6592 GLY G6593
SITE 1 HC5 5 GLU A 299 ASN A 301 ADP A1900 PO4 A1906
SITE 2 HC5 5 HOH A2674
SITE 1 HC6 4 GLN A 285 GLU A 299 ADP A1900 PO4 A1906
SITE 1 HC7 6 GLU A 215 ASN A 236 ASP A 238 ALA A 239
SITE 2 HC7 6 ILE A 242 SER A 247
SITE 1 HC8 6 ALA A 126 GLU A 127 GLU A 299 MET A 300
SITE 2 HC8 6 ASN A 301 HOH A2674
SITE 1 HC9 13 MET A 174 GLY A 175 HIS A 243 GLN A 285
SITE 2 HC9 13 GLU A 299 ASN A 301 ARG A 303 ARG A 306
SITE 3 HC9 13 ADP A1900 MN A1901 MN A1902 K A1942
SITE 4 HC9 13 HOH A2124
SITE 1 IC1 3 GLN A 829 GLU A 841 ADP A1910
SITE 1 IC2 3 GLU A 841 ASN A 843 ADP A1910
SITE 1 IC3 6 GLU A 761 HIS A 781 GLU A 783 GLN A 784
SITE 2 IC3 6 VAL A 787 SER A 792
SITE 1 IC4 5 GLN A 93 THR A 173 MET A 174 HOH A2013
SITE 2 IC4 5 HOH A2049
SITE 1 IC5 3 ASN A 289 ASN A 292 ARG A 294
SITE 1 IC6 5 ALA A 370 ASN A 371 PHE A 900 PRO A 901
SITE 2 IC6 5 GLY A 902
SITE 1 IC7 2 ASP B1614 HOH B1972
SITE 1 IC8 4 PHE A 578 ARG A 845 ALA A 847 ARG A 848
SITE 1 IC9 1 TRP A 71
SITE 1 JC1 5 LYS A 475 ASN A 485 PHE A 488 HOH A2284
SITE 2 JC1 5 HOH A2747
SITE 1 JC2 5 ASP A 84 GLY A 112 THR A 114 HOH A2426
SITE 2 JC2 5 HOH A2628
SITE 1 JC3 3 HIS B1516 ASP B1612 HOH B1984
SITE 1 JC4 7 GLU A 217 THR A 244 ASN A 283 GLN A 285
SITE 2 JC4 7 SER A 307 PO4 A1906 HOH A2124
SITE 1 JC5 3 THR A 143 ALA A 144 HOH A2478
SITE 1 JC6 23 HOH G 141 HOH G 874 ARG G6129 ILE G6167
SITE 2 JC6 23 ARG G6169 THR G6173 MET G6174 GLY G6175
SITE 3 JC6 23 GLY G6176 GLU G6208 LEU G6210 GLU G6215
SITE 4 JC6 23 MET G6240 GLY G6241 ILE G6242 HIS G6243
SITE 5 JC6 23 THR G6244 GLN G6285 GLU G6299 THR G6376
SITE 6 JC6 23 MN G7901 MN G7902 PO4 G7906
SITE 1 JC7 17 HOH G 763 PRO G6690 ARG G6715 MET G6725
SITE 2 JC7 17 HIS G6754 PHE G6755 LEU G6756 GLU G6761
SITE 3 JC7 17 ALA G6785 GLY G6786 VAL G6787 HIS G6788
SITE 4 JC7 17 SER G6789 GLN G6829 GLU G6841 MN G7911
SITE 5 JC7 17 K G7912
SITE 1 JC8 11 HOH G 85 HOH G 418 HOH G 903 GLU G6783
SITE 2 JC8 11 ASP G6791 GLU G6892 VAL G6893 LEU G6907
SITE 3 JC8 11 TYR G7040 ASP G7041 THR G7042
SITE 1 JC9 4 GLN G6022 GLN G6093 THR G6094 ASN G6097
SITE 1 KC1 28 ARG C2129 ILE C2167 ARG C2169 THR C2173
SITE 2 KC1 28 MET C2174 GLY C2175 GLY C2176 GLU C2208
SITE 3 KC1 28 SER C2209 LEU C2210 ILE C2211 GLU C2215
SITE 4 KC1 28 MET C2240 GLY C2241 ILE C2242 HIS C2243
SITE 5 KC1 28 THR C2244 GLN C2285 ILE C2298 GLU C2299
SITE 6 KC1 28 THR C2376 MN C3901 MN C3902 PO4 C3906
SITE 7 KC1 28 HOH C4120 HOH C4447 HOH C4633 HOH C4661
SITE 1 KC2 16 PRO C2690 ARG C2715 MET C2725 HIS C2754
SITE 2 KC2 16 PHE C2755 LEU C2756 GLU C2761 ALA C2785
SITE 3 KC2 16 GLY C2786 VAL C2787 HIS C2788 SER C2789
SITE 4 KC2 16 GLN C2829 GLU C2841 MN C3911 K C3912
SITE 1 KC3 12 GLU C2783 ASP C2791 ALA C2793 GLU C2892
SITE 2 KC3 12 VAL C2893 LEU C2907 TYR C3040 ASP C3041
SITE 3 KC3 12 THR C3042 HOH C4066 HOH C4068 HOH C4365
SITE 1 KC4 4 THR C2094 ASN C2097 ASN C2936 HOH C4001
SITE 1 KC5 24 ARG E4129 ILE E4167 ARG E4169 MET E4174
SITE 2 KC5 24 GLY E4175 GLY E4176 GLU E4208 LEU E4210
SITE 3 KC5 24 ILE E4211 GLU E4215 MET E4240 GLY E4241
SITE 4 KC5 24 ILE E4242 HIS E4243 THR E4244 GLN E4285
SITE 5 KC5 24 ILE E4298 GLU E4299 THR E4376 MN E5901
SITE 6 KC5 24 MN E5902 PO4 E5906 HOH E6126 HOH E6707
SITE 1 KC6 19 PRO E4690 VAL E4713 ARG E4715 MET E4725
SITE 2 KC6 19 HIS E4754 PHE E4755 LEU E4756 GLU E4761
SITE 3 KC6 19 ALA E4785 GLY E4786 VAL E4787 HIS E4788
SITE 4 KC6 19 SER E4789 GLN E4829 GLU E4841 PRO E4909
SITE 5 KC6 19 MN E5911 K E5912 HOH E6798
SITE 1 KC7 11 GLU E4783 ASP E4791 GLU E4892 VAL E4893
SITE 2 KC7 11 LEU E4907 TYR E5040 ASP E5041 THR E5042
SITE 3 KC7 11 HOH E6070 HOH E6072 HOH E6370
SITE 1 KC8 4 GLN E4022 THR E4094 ASN E4097 HOH E6004
SITE 1 KC9 21 ARG A 129 ILE A 167 ARG A 169 MET A 174
SITE 2 KC9 21 GLY A 175 GLY A 176 GLU A 208 LEU A 210
SITE 3 KC9 21 GLU A 215 MET A 240 GLY A 241 ILE A 242
SITE 4 KC9 21 HIS A 243 THR A 244 GLN A 285 GLU A 299
SITE 5 KC9 21 THR A 376 MN A1901 MN A1902 PO4 A1906
SITE 6 KC9 21 HOH A2672
SITE 1 LC1 20 PRO A 690 ARG A 715 MET A 725 HIS A 754
SITE 2 LC1 20 PHE A 755 LEU A 756 GLU A 761 ALA A 785
SITE 3 LC1 20 GLY A 786 VAL A 787 HIS A 788 SER A 789
SITE 4 LC1 20 GLN A 829 GLU A 841 MN A1911 K A1912
SITE 5 LC1 20 HOH A2561 HOH A2810 HOH A2845 HOH A2846
SITE 1 LC2 10 GLU A 783 ASP A 791 ALA A 793 GLU A 892
SITE 2 LC2 10 LEU A 907 TYR A1040 ASP A1041 THR A1042
SITE 3 LC2 10 HOH A2070 HOH A2370
SITE 1 LC3 2 GLN A 22 THR A 94
CRYST1 152.100 164.400 332.300 90.00 90.00 90.00 P 21 21 21 16
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 0.006575 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006083 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003009 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
