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1jnd.pdb
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1jnd.pdb
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HEADER HORMONE/GROWTH FACTOR 23-JUL-01 1JND
TITLE CRYSTAL STRUCTURE OF IMAGINAL DISC GROWTH FACTOR-2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IMAGINAL DISC GROWTH FACTOR-2;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 3 ORGANISM_COMMON: FRUIT FLY;
SOURCE 4 ORGANISM_TAXID: 7227
KEYWDS IDGF, IMAGINAL DISC, GROWTH FACTOR, CHITINASE, INSULIN RECEPTOR,
KEYWDS 2 HEPARIN, HORMONE-GROWTH FACTOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR P.F.VARELA,A.S.LLERA,R.A.MARIUZZA,J.TORMO
REVDAT 4 13-JUL-11 1JND 1 VERSN
REVDAT 3 24-FEB-09 1JND 1 VERSN
REVDAT 2 01-APR-03 1JND 1 JRNL
REVDAT 1 01-MAY-02 1JND 0
JRNL AUTH P.F.VARELA,A.S.LLERA,R.A.MARIUZZA,J.TORMO
JRNL TITL CRYSTAL STRUCTURE OF IMAGINAL DISC GROWTH FACTOR-2. A MEMBER
JRNL TITL 2 OF A NEW FAMILY OF GROWTH-PROMOTING GLYCOPROTEINS FROM
JRNL TITL 3 DROSOPHILA MELANOGASTER.
JRNL REF J.BIOL.CHEM. V. 277 13229 2002
JRNL REFN ISSN 0021-9258
JRNL PMID 11821393
JRNL DOI 10.1074/JBC.M110502200
REMARK 2
REMARK 2 RESOLUTION. 1.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 100.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.176
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.202
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 2298
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 127327
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : NULL
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE (F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3166
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 50
REMARK 3 SOLVENT ATOMS : 700
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : NULL
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : NULL
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : NULL
REMARK 3 NUMBER OF RESTRAINTS : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 ANGLE DISTANCES (A) : 1.600
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : NULL
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : NULL
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : NULL
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : NULL
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : NULL
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : NULL
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JND COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUL-01.
REMARK 100 THE RCSB ID CODE IS RCSB013968.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-NOV-99
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X12B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9464
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 129904
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.300
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.3
REMARK 200 DATA REDUNDANCY : 1.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.02300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.33
REMARK 200 COMPLETENESS FOR SHELL (%) : 53.5
REMARK 200 DATA REDUNDANCY IN SHELL : 1.76
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.25700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.880
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1CTN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, SODIUM ACETATE, PH 5.0,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 59.99133
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 29.99567
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 29.99567
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 59.99133
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A1701 LIES ON A SPECIAL POSITION.
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 ALA A 1
REMARK 465 HIS A 142
REMARK 465 GLY A 143
REMARK 465 ASP A 144
REMARK 465 LEU A 145
REMARK 465 GLY A 146
REMARK 465 LEU A 147
REMARK 465 ALA A 148
REMARK 465 TRP A 149
REMARK 465 LYS A 150
REMARK 465 SER A 151
REMARK 465 ILE A 152
REMARK 465 LYS A 153
REMARK 465 LYS A 154
REMARK 465 LEU A 155
REMARK 465 PHE A 156
REMARK 465 THR A 157
REMARK 465 GLY A 158
REMARK 465 ASP A 159
REMARK 465 PHE A 160
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 A 1523 O HOH A 1649 0.96
REMARK 500 O HOH A 1456 O HOH A 1607 1.49
REMARK 500 O HOH A 1309 O HOH A 1596 1.78
REMARK 500 CE LYS A 140 O HOH A 1480 1.88
REMARK 500 O HOH A 1276 O HOH A 1593 1.90
REMARK 500 O HOH A 1245 O HOH A 1268 1.92
REMARK 500 CE LYS A 140 O HOH A 1278 1.99
REMARK 500 O HOH A 1444 O HOH A 1528 2.00
REMARK 500 O HOH A 1132 O HOH A 1429 2.02
REMARK 500 O HOH A 1413 O HOH A 1542 2.02
REMARK 500 O HOH A 1553 O HOH A 1699 2.07
REMARK 500 O2 MAN A 3103 O HOH A 1642 2.09
REMARK 500 O HOH A 1410 O HOH A 1530 2.10
REMARK 500 O HOH A 1176 O HOH A 1593 2.11
REMARK 500 O HOH A 1443 O HOH A 1694 2.12
REMARK 500 O4 NAG A 3101 O5 BMA A 3102 2.13
REMARK 500 OE1 GLU A 55 O HOH A 1325 2.14
REMARK 500 O3 BMA A 3102 C2 MAN A 3103 2.14
REMARK 500 OD2 ASP A 374 O HOH A 1560 2.15
REMARK 500 O HOH A 1171 O HOH A 1270 2.15
REMARK 500 OD1 ASP A 92 O HOH A 1619 2.15
REMARK 500 O HOH A 1442 O HOH A 1691 2.16
REMARK 500 O HOH A 1301 O HOH A 1350 2.16
REMARK 500 O HOH A 1444 O HOH A 1585 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 A 1412 O HOH A 1567 6765 2.13
REMARK 500 O HOH A 1371 O HOH A 1388 5665 2.15
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 LEU A 420 C LEU A 420 OXT 0.386
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 ARG A 15 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 GLU A 27 OE1 - CD - OE2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 ARG A 44 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 TYR A 97 CB - CG - CD1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 GLU A 117 CB - CG - CD ANGL. DEV. = -16.5 DEGREES
REMARK 500 ASP A 128 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ARG A 139 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 ARG A 229 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG A 249 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES
REMARK 500 PHE A 308 CB - CG - CD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ARG A 349 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG A 384 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ASP A 408 CB - CG - OD1 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ARG A 414 NE - CZ - NH1 ANGL. DEV. = -4.4 DEGREES
REMARK 500 TYR A 418 CB - CG - CD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 TYR A 418 CB - CG - CD1 ANGL. DEV. = -4.9 DEGREES
REMARK 500 ARG A 419 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
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 ILE A 59 -61.80 -105.57
REMARK 500 ASN A 198 17.25 57.49
REMARK 500 ALA A 238 53.79 -152.70
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 A1358 DISTANCE = 5.05 ANGSTROMS
REMARK 525 HOH A1508 DISTANCE = 5.07 ANGSTROMS
REMARK 525 HOH A1515 DISTANCE = 6.05 ANGSTROMS
REMARK 525 HOH A1522 DISTANCE = 5.06 ANGSTROMS
REMARK 525 HOH A1526 DISTANCE = 5.13 ANGSTROMS
REMARK 525 HOH A1542 DISTANCE = 5.37 ANGSTROMS
REMARK 525 HOH A1548 DISTANCE = 5.73 ANGSTROMS
REMARK 525 HOH A1587 DISTANCE = 5.43 ANGSTROMS
REMARK 525 HOH A1590 DISTANCE = 5.76 ANGSTROMS
REMARK 525 HOH A1610 DISTANCE = 6.77 ANGSTROMS
REMARK 525 HOH A1613 DISTANCE = 6.52 ANGSTROMS
REMARK 525 HOH A1640 DISTANCE = 5.12 ANGSTROMS
REMARK 525 HOH A1645 DISTANCE = 5.30 ANGSTROMS
REMARK 525 HOH A1648 DISTANCE = 6.80 ANGSTROMS
REMARK 525 HOH A1650 DISTANCE = 6.55 ANGSTROMS
REMARK 525 HOH A1654 DISTANCE = 5.73 ANGSTROMS
REMARK 525 HOH A1668 DISTANCE = 5.45 ANGSTROMS
REMARK 525 HOH A1670 DISTANCE = 5.28 ANGSTROMS
REMARK 525 HOH A1675 DISTANCE = 6.89 ANGSTROMS
REMARK 525 HOH A1677 DISTANCE = 6.45 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3100
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 3102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 3103
DBREF 1JND A 1 420 GB 4092089 AAC99418 21 440
SEQADV 1JND PHE A 257 GB 4092089 VAL 277 CONFLICT
SEQRES 1 A 420 ALA SER ASN LEU VAL CYS TYR TYR ASP SER SER SER TYR
SEQRES 2 A 420 THR ARG GLU GLY LEU GLY LYS LEU LEU ASN PRO ASP LEU
SEQRES 3 A 420 GLU ILE ALA LEU GLN PHE CYS SER HIS LEU VAL TYR GLY
SEQRES 4 A 420 TYR ALA GLY LEU ARG GLY GLU ASN LEU GLN ALA TYR SER
SEQRES 5 A 420 MET ASN GLU ASN LEU ASP ILE TYR LYS HIS GLN PHE SER
SEQRES 6 A 420 GLU VAL THR SER LEU LYS ARG LYS TYR PRO HIS LEU LYS
SEQRES 7 A 420 VAL LEU LEU SER VAL GLY GLY ASP HIS ASP ILE ASP PRO
SEQRES 8 A 420 ASP HIS PRO ASN LYS TYR ILE ASP LEU LEU GLU GLY GLU
SEQRES 9 A 420 LYS VAL ARG GLN ILE GLY PHE ILE ARG SER ALA TYR GLU
SEQRES 10 A 420 LEU VAL LYS THR TYR GLY PHE ASP GLY LEU ASP LEU ALA
SEQRES 11 A 420 TYR GLN PHE PRO LYS ASN LYS PRO ARG LYS VAL HIS GLY
SEQRES 12 A 420 ASP LEU GLY LEU ALA TRP LYS SER ILE LYS LYS LEU PHE
SEQRES 13 A 420 THR GLY ASP PHE ILE VAL ASP PRO HIS ALA ALA LEU HIS
SEQRES 14 A 420 LYS GLU GLN PHE THR ALA LEU VAL ARG ASP VAL LYS ASP
SEQRES 15 A 420 SER LEU ARG ALA ASP GLY PHE LEU LEU SER LEU THR VAL
SEQRES 16 A 420 LEU PRO ASN VAL ASN SER THR TRP TYR PHE ASP ILE PRO
SEQRES 17 A 420 ALA LEU ASN GLY LEU VAL ASP PHE VAL ASN LEU ALA THR
SEQRES 18 A 420 PHE ASP PHE LEU THR PRO ALA ARG ASN PRO GLU GLU ALA
SEQRES 19 A 420 ASP TYR SER ALA PRO ILE TYR HIS PRO ASP GLY SER LYS
SEQRES 20 A 420 ASP ARG LEU ALA HIS LEU ASN ALA ASP PHE GLN VAL GLU
SEQRES 21 A 420 TYR TRP LEU SER GLN GLY PHE PRO SER ASN LYS ILE ASN
SEQRES 22 A 420 LEU GLY VAL ALA THR TYR GLY ASN ALA TRP LYS LEU THR
SEQRES 23 A 420 LYS ASP SER GLY LEU GLU GLY VAL PRO VAL VAL PRO GLU
SEQRES 24 A 420 THR SER GLY PRO ALA PRO GLU GLY PHE GLN SER GLN LYS
SEQRES 25 A 420 PRO GLY LEU LEU SER TYR ALA GLU ILE CYS GLY LYS LEU
SEQRES 26 A 420 SER ASN PRO GLN ASN GLN PHE LEU LYS GLY ASN GLU SER
SEQRES 27 A 420 PRO LEU ARG ARG VAL SER ASP PRO THR LYS ARG PHE GLY
SEQRES 28 A 420 GLY ILE ALA TYR ARG PRO VAL ASP GLY GLN ILE THR GLU
SEQRES 29 A 420 GLY ILE TRP VAL SER TYR ASP ASP PRO ASP SER ALA SER
SEQRES 30 A 420 ASN LYS ALA ALA TYR ALA ARG VAL LYS ASN LEU GLY GLY
SEQRES 31 A 420 VAL ALA LEU PHE ASP LEU SER TYR ASP ASP PHE ARG GLY
SEQRES 32 A 420 GLN CYS SER GLY ASP LYS TYR PRO ILE LEU ARG ALA ILE
SEQRES 33 A 420 LYS TYR ARG LEU
MODRES 1JND ASN A 200 ASN GLYCOSYLATION SITE
HET NAG A3100 14
HET NAG A3101 14
HET BMA A3102 11
HET MAN A3103 11
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM BMA BETA-D-MANNOSE
HETNAM MAN ALPHA-D-MANNOSE
FORMUL 2 NAG 2(C8 H15 N O6)
FORMUL 2 BMA C6 H12 O6
FORMUL 3 MAN C6 H12 O6
FORMUL 4 HOH *700(H2 O)
HELIX 1 1 SER A 11 ARG A 15 5 5
HELIX 2 2 LEU A 22 LEU A 30 1 9
HELIX 3 3 GLN A 31 CYS A 33 5 3
HELIX 4 4 ASN A 54 ILE A 59 1 6
HELIX 5 5 HIS A 62 SER A 69 1 8
HELIX 6 6 LEU A 70 LYS A 73 5 4
HELIX 7 7 ASN A 95 GLU A 102 1 8
HELIX 8 8 GLU A 104 TYR A 122 1 19
HELIX 9 9 HIS A 165 ARG A 185 1 21
HELIX 10 10 ASN A 200 PHE A 205 1 6
HELIX 11 11 ASP A 206 GLY A 212 1 7
HELIX 12 12 ASN A 254 GLN A 265 1 12
HELIX 13 13 PRO A 268 ASN A 270 5 3
HELIX 14 14 THR A 286 GLY A 290 5 5
HELIX 15 15 TYR A 318 LEU A 325 1 8
HELIX 16 16 LYS A 334 SER A 338 5 5
HELIX 17 17 ASP A 372 LYS A 386 1 15
HELIX 18 18 ASP A 395 ASP A 399 5 5
HELIX 19 19 TYR A 410 LEU A 420 1 11
SHEET 1 A10 ALA A 50 SER A 52 0
SHEET 2 A10 HIS A 35 LEU A 43 -1 N GLY A 42 O TYR A 51
SHEET 3 A10 ASN A 3 ASP A 9 1 O LEU A 4 N HIS A 35
SHEET 4 A10 GLY A 390 PHE A 394 1 O VAL A 391 N VAL A 5
SHEET 5 A10 ILE A 272 ALA A 277 1 O ILE A 272 N GLY A 390
SHEET 6 A10 PHE A 216 LEU A 219 1 O VAL A 217 N ASN A 273
SHEET 7 A10 LEU A 190 VAL A 195 1 O LEU A 191 N PHE A 216
SHEET 8 A10 GLY A 126 ALA A 130 1 O LEU A 127 N SER A 192
SHEET 9 A10 LYS A 78 GLY A 84 1 O VAL A 79 N GLY A 126
SHEET 10 A10 HIS A 35 LEU A 43 1 O LEU A 36 N LEU A 80
SHEET 1 B 5 LEU A 315 SER A 317 0
SHEET 2 B 5 TYR A 279 LYS A 284 -1 N GLY A 280 O LEU A 316
SHEET 3 B 5 ILE A 366 TYR A 370 -1 O TRP A 367 N TRP A 283
SHEET 4 B 5 GLY A 352 ARG A 356 -1 O GLY A 352 N TYR A 370
SHEET 5 B 5 ARG A 341 VAL A 343 -1 N ARG A 341 O TYR A 355
SSBOND 1 CYS A 6 CYS A 33 1555 1555 2.05
SSBOND 2 CYS A 322 CYS A 405 1555 1555 2.03
LINK ND2 ASN A 200 C1 NAG A3100 1555 1555 1.44
LINK O4 NAG A3100 C1 NAG A3101 1555 1555 1.49
LINK O4 NAG A3101 C1 BMA A3102 1555 1555 1.43
LINK O3 BMA A3102 C1 MAN A3103 1555 1555 1.62
CISPEP 1 GLY A 39 TYR A 40 0 -0.84
CISPEP 2 PRO A 295 VAL A 296 0 0.76
CISPEP 3 PHE A 394 ASP A 395 0 -11.80
SITE 1 AC1 13 ASN A 136 ASN A 200 THR A 202 HIS A 252
SITE 2 AC1 13 PHE A 257 GLN A 258 HOH A1065 HOH A1066
SITE 3 AC1 13 HOH A1108 HOH A1267 HOH A1289 HOH A1376
SITE 4 AC1 13 NAG A3101
SITE 1 AC2 9 PHE A 257 HOH A1267 HOH A1274 HOH A1277
SITE 2 AC2 9 HOH A1368 HOH A1493 HOH A1632 NAG A3100
SITE 3 AC2 9 BMA A3102
SITE 1 AC3 6 ALA A 251 HOH A1226 HOH A1490 HOH A1697
SITE 2 AC3 6 NAG A3101 MAN A3103
SITE 1 AC4 3 HOH A1532 HOH A1642 BMA A3102
CRYST1 106.345 106.345 89.987 90.00 90.00 120.00 P 32 2 1 6
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 0.009403 0.005429 0.000000 0.00000
SCALE2 0.000000 0.010858 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011113 0.00000
ATOM 1 N SER A 2 72.119 33.529 -4.081 1.00 21.71 N
ATOM 2 CA SER A 2 71.994 34.876 -3.569 1.00 15.42 C
ATOM 3 C SER A 2 73.199 35.250 -2.735 1.00 17.75 C
ATOM 4 O SER A 2 73.890 34.377 -2.208 1.00 21.08 O
ATOM 5 CB SER A 2 70.741 34.923 -2.692 1.00 21.69 C
ATOM 6 OG SER A 2 69.575 35.205 -3.470 1.00 30.38 O
ATOM 7 N ASN A 3 73.468 36.539 -2.575 1.00 13.46 N
ATOM 8 CA ASN A 3 74.551 36.878 -1.668 1.00 13.50 C
ATOM 9 C ASN A 3 74.033 37.055 -0.218 1.00 10.31 C
ATOM 10 O ASN A 3 72.884 37.359 -0.016 1.00 10.46 O
ATOM 11 CB ASN A 3 75.178 38.136 -2.175 1.00 17.23 C
ATOM 12 CG ASN A 3 75.972 37.826 -3.471 1.00 18.95 C
ATOM 13 OD1 ASN A 3 76.682 36.819 -3.635 1.00 23.78 O
ATOM 14 ND2 ASN A 3 75.799 38.770 -4.354 1.00 20.45 N
ATOM 15 N LEU A 4 74.996 36.821 0.666 1.00 9.76 N
ATOM 16 CA LEU A 4 74.701 37.088 2.093 1.00 9.23 C
ATOM 17 C LEU A 4 75.941 37.819 2.626 1.00 8.61 C
ATOM 18 O LEU A 4 76.983 37.233 2.833 1.00 10.04 O
ATOM 19 CB LEU A 4 74.400 35.817 2.859 1.00 10.46 C
ATOM 20 CG LEU A 4 73.384 35.965 4.018 1.00 12.92 C
ATOM 21 CD1 LEU A 4 73.154 34.609 4.685 1.00 12.28 C
ATOM 22 CD2 LEU A 4 73.782 37.033 5.022 1.00 12.34 C
ATOM 23 N VAL A 5 75.793 39.125 2.730 1.00 8.94 N
ATOM 24 CA VAL A 5 76.892 40.041 3.039 1.00 7.72 C
ATOM 25 C VAL A 5 76.906 40.276 4.562 1.00 8.84 C
ATOM 26 O VAL A 5 76.013 40.945 5.080 1.00 10.34 O
ATOM 27 CB VAL A 5 76.699 41.329 2.257 1.00 7.50 C
ATOM 28 CG1 VAL A 5 77.820 42.306 2.562 1.00 9.65 C
ATOM 29 CG2 VAL A 5 76.639 41.075 0.736 1.00 10.25 C
ATOM 30 N CYS A 6 77.918 39.704 5.175 1.00 8.69 N
ATOM 31 CA CYS A 6 77.944 39.728 6.661 1.00 8.09 C
ATOM 32 C CYS A 6 78.786 40.877 7.129 1.00 6.40 C
ATOM 33 O CYS A 6 80.020 40.838 6.929 1.00 8.46 O
ATOM 34 CB CYS A 6 78.556 38.423 7.117 1.00 11.05 C
ATOM 35 SG CYS A 6 77.373 37.065 6.747 1.00 11.23 S
ATOM 36 N TYR A 7 78.204 41.873 7.731 1.00 8.25 N
ATOM 37 CA TYR A 7 78.961 42.956 8.379 1.00 9.75 C
ATOM 38 C TYR A 7 79.575 42.425 9.690 1.00 7.95 C
ATOM 39 O TYR A 7 78.996 41.632 10.407 1.00 9.14 O
ATOM 40 CB TYR A 7 78.085 44.200 8.620 1.00 8.97 C
ATOM 41 CG TYR A 7 78.139 45.034 7.325 1.00 7.95 C
ATOM 42 CD1 TYR A 7 77.515 44.554 6.180 1.00 8.69 C
ATOM 43 CD2 TYR A 7 78.836 46.245 7.279 1.00 8.72 C
ATOM 44 CE1 TYR A 7 77.577 45.323 5.017 1.00 9.11 C
ATOM 45 CE2 TYR A 7 78.903 46.991 6.103 1.00 8.49 C
ATOM 46 CZ TYR A 7 78.256 46.493 5.016 1.00 9.15 C
ATOM 47 OH TYR A 7 78.354 47.224 3.828 1.00 9.14 O
ATOM 48 N TYR A 8 80.774 42.939 9.928 1.00 9.48 N
ATOM 49 CA TYR A 8 81.549 42.594 11.137 1.00 9.12 C
ATOM 50 C TYR A 8 82.008 43.903 11.764 1.00 10.64 C
ATOM 51 O TYR A 8 82.889 44.561 11.220 1.00 9.90 O
ATOM 52 CB TYR A 8 82.717 41.687 10.765 1.00 8.72 C
ATOM 53 CG TYR A 8 83.803 41.569 11.851 1.00 9.17 C
ATOM 54 CD1 TYR A 8 83.494 40.910 13.048 1.00 10.17 C
ATOM 55 CD2 TYR A 8 85.065 42.097 11.664 1.00 9.71 C
ATOM 56 CE1 TYR A 8 84.486 40.820 14.032 1.00 10.15 C
ATOM 57 CE2 TYR A 8 86.065 42.000 12.627 1.00 9.20 C
ATOM 58 CZ TYR A 8 85.728 41.339 13.803 1.00 9.78 C
ATOM 59 OH TYR A 8 86.743 41.263 14.739 1.00 10.11 O
ATOM 60 N ASP A 9 81.394 44.265 12.895 1.00 9.91 N
ATOM 61 CA ASP A 9 81.804 45.483 13.598 1.00 10.86 C
ATOM 62 C ASP A 9 83.006 45.093 14.459 1.00 11.05 C
ATOM 63 O ASP A 9 82.826 44.365 15.452 1.00 10.62 O
ATOM 64 CB ASP A 9 80.669 46.035 14.436 1.00 11.19 C
ATOM 65 CG ASP A 9 81.080 47.267 15.262 1.00 12.27 C
ATOM 66 OD1 ASP A 9 82.249 47.615 15.286 1.00 12.91 O
ATOM 67 OD2 ASP A 9 80.129 47.810 15.860 1.00 16.18 O
ATOM 68 N SER A 10 84.204 45.513 14.068 1.00 10.30 N
ATOM 69 CA SER A 10 85.452 45.092 14.722 1.00 9.48 C
ATOM 70 C SER A 10 85.573 45.590 16.185 1.00 9.20 C
ATOM 71 O SER A 10 86.403 45.005 16.888 1.00 10.39 O
ATOM 72 CB SER A 10 86.593 45.577 13.825 1.00 12.80 C
ATOM 73 OG SER A 10 86.634 46.990 13.845 1.00 12.63 O
ATOM 74 N SER A 11 84.762 46.553 16.558 1.00 11.04 N
ATOM 75 CA SER A 11 84.805 46.919 18.006 1.00 10.53 C
ATOM 76 C SER A 11 84.401 45.721 18.837 1.00 9.91 C
ATOM 77 O SER A 11 84.725 45.621 20.058 1.00 10.97 O
ATOM 78 CB SER A 11 83.919 48.121 18.237 1.00 10.46 C
ATOM 79 OG SER A 11 82.535 47.849 18.017 1.00 11.60 O
ATOM 80 N SER A 12 83.698 44.737 18.263 1.00 8.60 N
ATOM 81 CA SER A 12 83.268 43.560 19.015 1.00 8.11 C
ATOM 82 C SER A 12 84.423 42.730 19.493 1.00 9.04 C
ATOM 83 O SER A 12 84.278 41.939 20.470 1.00 9.54 O
ATOM 84 CB SER A 12 82.305 42.657 18.176 1.00 9.30 C
ATOM 85 OG SER A 12 83.004 42.125 17.043 1.00 9.62 O
ATOM 86 N TYR A 13 85.607 42.857 18.918 1.00 8.84 N
ATOM 87 CA TYR A 13 86.754 42.078 19.330 1.00 8.46 C
ATOM 88 C TYR A 13 87.184 42.370 20.794 1.00 8.77 C
ATOM 89 O TYR A 13 87.745 41.457 21.413 1.00 9.94 O
ATOM 90 CB TYR A 13 87.912 42.383 18.339 1.00 10.98 C
ATOM 91 CG TYR A 13 89.052 41.381 18.479 1.00 11.13 C
ATOM 92 CD1 TYR A 13 88.987 40.211 17.748 1.00 12.43 C
ATOM 93 CD2 TYR A 13 90.152 41.629 19.298 1.00 13.02 C
ATOM 94 CE1 TYR A 13 89.970 39.248 17.807 1.00 14.19 C
ATOM 95 CE2 TYR A 13 91.153 40.665 19.364 1.00 13.53 C
ATOM 96 CZ TYR A 13 91.054 39.512 18.622 1.00 15.24 C
ATOM 97 OH TYR A 13 92.043 38.509 18.674 1.00 18.34 O
ATOM 98 N THR A 14 86.882 43.592 21.223 1.00 9.46 N
ATOM 99 CA THR A 14 87.375 43.979 22.558 1.00 8.71 C
ATOM 100 C THR A 14 86.248 44.200 23.533 1.00 11.92 C
ATOM 101 O THR A 14 86.508 44.758 24.619 1.00 11.56 O
ATOM 102 CB THR A 14 88.218 45.268 22.425 1.00 11.14 C
ATOM 103 OG1 THR A 14 87.423 46.247 21.823 1.00 12.44 O
ATOM 104 CG2 THR A 14 89.464 44.990 21.582 1.00 14.09 C
ATOM 105 N ARG A 15 85.016 43.823 23.228 1.00 10.78 N
ATOM 106 CA ARG A 15 83.942 44.004 24.204 1.00 9.04 C
ATOM 107 C ARG A 15 84.236 43.183 25.471 1.00 8.87 C
ATOM 108 O ARG A 15 84.825 42.120 25.465 1.00 9.34 O
ATOM 109 CB ARG A 15 82.595 43.625 23.569 1.00 7.69 C
ATOM 110 CG ARG A 15 82.205 44.734 22.570 1.00 9.80 C
ATOM 111 CD ARG A 15 80.947 44.346 21.772 1.00 10.19 C
ATOM 112 NE ARG A 15 80.838 45.327 20.678 1.00 9.79 N
ATOM 113 CZ ARG A 15 80.045 45.207 19.591 1.00 9.53 C
ATOM 114 NH1 ARG A 15 79.244 44.174 19.452 1.00 8.93 N
ATOM 115 NH2 ARG A 15 80.101 46.187 18.679 1.00 10.21 N
ATOM 116 N GLU A 16 83.730 43.801 26.571 1.00 9.15 N
ATOM 117 CA GLU A 16 83.915 43.140 27.853 1.00 8.13 C
ATOM 118 C GLU A 16 82.743 42.184 28.149 1.00 8.93 C
ATOM 119 O GLU A 16 81.627 42.744 28.255 1.00 10.08 O
ATOM 120 CB GLU A 16 83.994 44.217 28.962 1.00 8.66 C
ATOM 121 CG GLU A 16 85.334 44.942 28.986 1.00 8.97 C
ATOM 122 CD GLU A 16 86.433 44.070 29.490 1.00 14.51 C
ATOM 123 OE1 GLU A 16 86.224 43.011 30.119 1.00 10.91 O
ATOM 124 OE2 GLU A 16 87.617 44.473 29.232 1.00 20.54 O
ATOM 125 N GLY A 17 83.035 40.895 28.222 1.00 8.33 N
ATOM 126 CA GLY A 17 81.967 39.926 28.544 1.00 8.63 C
ATOM 127 C GLY A 17 81.602 39.108 27.296 1.00 10.78 C
ATOM 128 O GLY A 17 82.370 39.025 26.333 1.00 10.06 O
ATOM 129 N LEU A 18 80.419 38.510 27.374 1.00 9.26 N
ATOM 130 CA LEU A 18 79.994 37.532 26.363 1.00 9.96 C
ATOM 131 C LEU A 18 79.656 38.197 25.051 1.00 9.21 C
ATOM 132 O LEU A 18 79.495 37.434 24.050 1.00 10.98 O
ATOM 133 CB LEU A 18 78.805 36.693 26.889 1.00 10.65 C
ATOM 134 CG LEU A 18 79.188 35.780 28.051 1.00 12.76 C
ATOM 135 CD1 LEU A 18 77.920 35.069 28.533 1.00 13.89 C
ATOM 136 CD2 LEU A 18 80.311 34.812 27.704 1.00 15.72 C
ATOM 137 N GLY A 19 79.623 39.506 24.945 1.00 8.45 N
ATOM 138 CA GLY A 19 79.468 40.162 23.636 1.00 9.47 C
ATOM 139 C GLY A 19 80.804 40.180 22.899 1.00 10.83 C
ATOM 140 O GLY A 19 80.785 40.602 21.733 1.00 10.10 O
ATOM 141 N LYS A 20 81.913 39.744 23.486 1.00 9.82 N
ATOM 142 CA LYS A 20 83.197 39.690 22.781 1.00 8.34 C
ATOM 143 C LYS A 20 83.197 38.646 21.688 1.00 9.86 C
ATOM 144 O LYS A 20 82.885 37.480 21.921 1.00 9.47 O
ATOM 145 CB LYS A 20 84.313 39.400 23.807 1.00 9.39 C
ATOM 146 CG LYS A 20 85.725 39.585 23.254 1.00 9.87 C
ATOM 147 CD LYS A 20 86.752 38.890 24.122 1.00 12.10 C
ATOM 148 CE LYS A 20 86.753 39.354 25.570 1.00 13.15 C
ATOM 149 NZ LYS A 20 87.117 40.772 25.768 1.00 13.09 N
ATOM 150 N LEU A 21 83.552 39.134 20.477 1.00 9.08 N
ATOM 151 CA LEU A 21 83.592 38.256 19.290 1.00 9.82 C
ATOM 152 C LEU A 21 85.061 38.020 18.886 1.00 9.52 C
ATOM 153 O LEU A 21 85.635 38.906 18.257 1.00 9.88 O
ATOM 154 CB LEU A 21 82.786 38.937 18.176 1.00 8.58 C
ATOM 155 CG LEU A 21 82.743 38.153 16.825 1.00 9.58 C
ATOM 156 CD1 LEU A 21 82.379 36.699 17.043 1.00 10.82 C
ATOM 157 CD2 LEU A 21 81.758 38.886 15.910 1.00 9.54 C
ATOM 158 N LEU A 22 85.598 36.877 19.266 1.00 9.40 N
ATOM 159 CA LEU A 22 87.001 36.615 18.896 1.00 10.29 C
ATOM 160 C LEU A 22 86.989 35.844 17.595 1.00 10.56 C
ATOM 161 O LEU A 22 85.966 35.438 17.039 1.00 11.54 O
ATOM 162 CB LEU A 22 87.721 35.830 19.995 1.00 12.41 C
ATOM 163 CG LEU A 22 87.891 36.666 21.299 1.00 13.15 C
ATOM 164 CD1 LEU A 22 88.554 35.818 22.402 1.00 14.60 C
ATOM 165 CD2 LEU A 22 88.703 37.907 21.031 1.00 13.35 C
ATOM 166 N ASN A 23 88.197 35.626 17.050 1.00 10.91 N
ATOM 167 CA ASN A 23 88.230 35.178 15.641 1.00 11.02 C
ATOM 168 C ASN A 23 87.731 33.783 15.450 1.00 12.22 C
ATOM 169 O ASN A 23 87.094 33.506 14.390 1.00 12.02 O
ATOM 170 CB ASN A 23 89.658 35.405 15.078 1.00 10.52 C
ATOM 171 CG ASN A 23 89.932 36.883 14.926 1.00 13.50 C
ATOM 172 OD1 ASN A 23 89.061 37.747 14.837 1.00 12.65 O
ATOM 173 ND2 ASN A 23 91.232 37.222 14.875 1.00 13.60 N
ATOM 174 N PRO A 24 87.873 32.831 16.360 1.00 11.24 N
ATOM 175 CA PRO A 24 87.278 31.523 16.175 1.00 9.65 C
ATOM 176 C PRO A 24 85.752 31.602 16.051 1.00 12.91 C
ATOM 177 O PRO A 24 85.193 30.863 15.230 1.00 13.19 O
ATOM 178 CB PRO A 24 87.696 30.714 17.414 1.00 15.21 C
ATOM 179 CG PRO A 24 88.973 31.407 17.809 1.00 17.52 C
ATOM 180 CD PRO A 24 88.701 32.896 17.618 1.00 14.43 C
ATOM 181 N ASP A 25 85.121 32.461 16.860 1.00 12.55 N
ATOM 182 CA ASP A 25 83.671 32.593 16.733 1.00 15.14 C
ATOM 183 C ASP A 25 83.304 33.284 15.435 1.00 12.50 C
ATOM 184 O ASP A 25 82.255 33.019 14.839 1.00 14.07 O
ATOM 185 CB ASP A 25 83.126 33.331 17.983 1.00 12.64 C
ATOM 186 CG ASP A 25 82.920 32.332 19.117 1.00 16.88 C
ATOM 187 OD1 ASP A 25 82.828 31.111 18.866 1.00 16.51 O
ATOM 188 OD2 ASP A 25 82.832 32.860 20.259 1.00 19.38 O
ATOM 189 N LEU A 26 84.117 34.243 14.973 1.00 11.38 N
ATOM 190 CA LEU A 26 83.854 34.910 13.690 1.00 11.08 C
ATOM 191 C LEU A 26 83.889 33.891 12.553 1.00 11.99 C
ATOM 192 O LEU A 26 83.050 33.884 11.653 1.00 12.18 O
ATOM 193 CB LEU A 26 84.909 36.009 13.470 1.00 10.46 C
ATOM 194 CG LEU A 26 84.885 36.669 12.088 1.00 11.74 C
ATOM 195 CD1 LEU A 26 83.534 37.296 11.780 1.00 13.42 C
ATOM 196 CD2 LEU A 26 85.964 37.758 12.029 1.00 13.41 C
ATOM 197 N GLU A 27 84.874 32.978 12.610 1.00 11.70 N
ATOM 198 CA GLU A 27 85.025 31.993 11.534 1.00 12.48 C
ATOM 199 C GLU A 27 83.836 31.092 11.377 1.00 11.60 C
ATOM 200 O GLU A 27 83.521 30.660 10.242 1.00 12.90 O
ATOM 201 CB GLU A 27 86.268 31.130 11.830 1.00 13.86 C
ATOM 202 CG GLU A 27 86.938 30.655 10.549 1.00 28.90 C
ATOM 203 CD GLU A 27 88.227 29.884 10.897 1.00 27.54 C
ATOM 204 OE1 GLU A 27 89.039 30.512 11.587 1.00 30.23 O
ATOM 205 OE2 GLU A 27 88.237 28.728 10.446 1.00 36.13 O
ATOM 206 N ILE A 28 83.124 30.784 12.447 1.00 12.48 N
ATOM 207 CA ILE A 28 81.941 29.910 12.380 1.00 11.59 C
ATOM 208 C ILE A 28 80.919 30.524 11.440 1.00 13.04 C
ATOM 209 O ILE A 28 80.162 29.785 10.780 1.00 15.19 O
ATOM 210 CB ILE A 28 81.390 29.673 13.812 1.00 13.98 C
ATOM 211 CG1 ILE A 28 82.381 28.877 14.653 1.00 17.58 C
ATOM 212 CG2 ILE A 28 80.025 29.027 13.729 1.00 16.59 C
ATOM 213 CD1 ILE A 28 82.009 28.644 16.093 1.00 22.74 C
ATOM 214 N ALA A 29 80.851 31.846 11.350 1.00 10.82 N
ATOM 215 CA ALA A 29 79.852 32.448 10.464 1.00 10.86 C
ATOM 216 C ALA A 29 80.110 32.228 8.984 1.00 10.33 C
ATOM 217 O ALA A 29 79.177 32.299 8.151 1.00 11.32 O
ATOM 218 CB ALA A 29 79.822 33.968 10.674 1.00 11.62 C
ATOM 219 N LEU A 30 81.365 31.993 8.650 1.00 11.95 N
ATOM 220 CA LEU A 30 81.718 32.155 7.238 1.00 14.49 C
ATOM 221 C LEU A 30 81.139 31.064 6.352 1.00 18.38 C
ATOM 222 O LEU A 30 81.028 31.404 5.151 1.00 22.58 O
ATOM 223 CB LEU A 30 83.251 32.217 7.103 1.00 15.67 C
ATOM 224 CG LEU A 30 83.798 33.432 7.858 1.00 20.86 C
ATOM 225 CD1 LEU A 30 85.311 33.492 7.725 1.00 23.86 C
ATOM 226 CD2 LEU A 30 83.087 34.691 7.364 1.00 26.06 C
ATOM 227 N GLN A 31 80.777 29.940 6.910 1.00 14.89 N
ATOM 228 CA GLN A 31 80.127 28.925 6.074 1.00 26.76 C
ATOM 229 C GLN A 31 78.798 29.457 5.547 1.00 21.31 C
ATOM 230 O GLN A 31 78.295 28.890 4.581 1.00 22.59 O
ATOM 231 CB GLN A 31 79.871 27.645 6.866 1.00 25.16 C
ATOM 232 CG GLN A 31 78.901 27.767 8.012 1.00 23.57 C
ATOM 233 CD GLN A 31 79.056 26.683 9.064 1.00 39.20 C
ATOM 234 OE1 GLN A 31 78.869 25.525 8.672 1.00 36.51 O
ATOM 235 NE2 GLN A 31 79.351 26.949 10.338 1.00 26.64 N
ATOM 236 N PHE A 32 78.227 30.495 6.118 1.00 12.34 N
ATOM 237 CA PHE A 32 76.955 31.047 5.667 1.00 12.20 C
ATOM 238 C PHE A 32 77.114 32.332 4.865 1.00 14.08 C
ATOM 239 O PHE A 32 76.148 32.756 4.236 1.00 16.23 O
ATOM 240 CB PHE A 32 76.035 31.352 6.875 1.00 12.61 C
ATOM 241 CG PHE A 32 75.951 30.107 7.768 1.00 13.14 C
ATOM 242 CD1 PHE A 32 75.358 28.960 7.262 1.00 20.26 C
ATOM 243 CD2 PHE A 32 76.468 30.132 9.039 1.00 17.10 C
ATOM 244 CE1 PHE A 32 75.306 27.811 8.053 1.00 26.13 C
ATOM 245 CE2 PHE A 32 76.423 28.968 9.831 1.00 24.13 C
ATOM 246 CZ PHE A 32 75.833 27.818 9.338 1.00 22.96 C
ATOM 247 N CYS A 33 78.247 33.002 4.875 1.00 13.23 N
ATOM 248 CA CYS A 33 78.379 34.336 4.314 1.00 11.25 C
ATOM 249 C CYS A 33 79.078 34.312 2.956 1.00 11.63 C
ATOM 250 O CYS A 33 80.131 33.673 2.857 1.00 16.56 O
ATOM 251 CB CYS A 33 79.241 35.213 5.237 1.00 13.06 C
ATOM 252 SG CYS A 33 78.577 35.413 6.903 1.00 13.41 S
ATOM 253 N SER A 34 78.575 35.013 1.964 1.00 11.89 N
ATOM 254 CA SER A 34 79.319 35.128 0.722 1.00 12.52 C
ATOM 255 C SER A 34 80.351 36.238 0.779 1.00 14.59 C
ATOM 256 O SER A 34 81.379 36.212 0.065 1.00 14.99 O
ATOM 257 CB SER A 34 78.342 35.382 -0.416 1.00 13.86 C
ATOM 258 OG SER A 34 77.645 36.606 -0.249 1.00 13.60 O
ATOM 259 N HIS A 35 80.075 37.236 1.629 1.00 10.76 N
ATOM 260 CA HIS A 35 80.944 38.378 1.770 1.00 10.97 C
ATOM 261 C HIS A 35 81.061 38.678 3.285 1.00 10.92 C
ATOM 262 O HIS A 35 80.122 38.394 4.014 1.00 10.25 O
ATOM 263 CB HIS A 35 80.399 39.616 1.071 1.00 10.77 C
ATOM 264 CG HIS A 35 80.164 39.512 -0.414 1.00 9.30 C
ATOM 265 ND1 HIS A 35 79.259 38.634 -0.950 1.00 15.06 N
ATOM 266 CD2 HIS A 35 80.748 40.227 -1.400 1.00 11.78 C
ATOM 267 CE1 HIS A 35 79.282 38.791 -2.284 1.00 13.80 C
ATOM 268 NE2 HIS A 35 80.162 39.746 -2.560 1.00 13.46 N
ATOM 269 N LEU A 36 82.202 39.244 3.636 1.00 10.72 N
ATOM 270 CA LEU A 36 82.437 39.703 5.007 1.00 8.75 C
ATOM 271 C LEU A 36 82.860 41.154 4.878 1.00 9.88 C
ATOM 272 O LEU A 36 83.765 41.482 4.072 1.00 11.25 O
ATOM 273 CB LEU A 36 83.501 38.846 5.619 1.00 10.95 C
ATOM 274 CG LEU A 36 83.812 39.065 7.094 1.00 12.84 C
ATOM 275 CD1 LEU A 36 82.570 38.806 7.931 1.00 14.16 C
ATOM 276 CD2 LEU A 36 84.950 38.128 7.474 1.00 14.55 C
ATOM 277 N VAL A 37 82.249 42.039 5.634 1.00 8.03 N
ATOM 278 CA VAL A 37 82.557 43.446 5.519 1.00 8.14 C
ATOM 279 C VAL A 37 83.120 43.928 6.856 1.00 8.30 C
ATOM 280 O VAL A 37 82.376 43.860 7.847 1.00 9.28 O
ATOM 281 CB VAL A 37 81.385 44.297 5.041 1.00 9.02 C
ATOM 282 CG1 VAL A 37 81.848 45.747 4.801 1.00 9.81 C
ATOM 283 CG2 VAL A 37 80.763 43.684 3.787 1.00 9.68 C
ATOM 284 N TYR A 38 84.364 44.348 6.851 1.00 7.81 N
ATOM 285 CA TYR A 38 85.025 44.790 8.076 1.00 10.01 C
ATOM 286 C TYR A 38 84.651 46.230 8.366 1.00 9.01 C
ATOM 287 O TYR A 38 84.928 47.137 7.573 1.00 9.53 O
ATOM 288 CB TYR A 38 86.529 44.745 7.867 1.00 9.16 C
ATOM 289 CG TYR A 38 87.399 44.843 9.122 1.00 8.80 C
ATOM 290 CD1 TYR A 38 88.055 43.695 9.546 1.00 10.04 C
ATOM 291 CD2 TYR A 38 87.542 46.024 9.817 1.00 9.16 C
ATOM 292 CE1 TYR A 38 88.859 43.779 10.679 1.00 10.61 C
ATOM 293 CE2 TYR A 38 88.363 46.104 10.964 1.00 10.42 C
ATOM 294 CZ TYR A 38 88.970 44.961 11.325 1.00 9.19 C
ATOM 295 OH TYR A 38 89.791 44.993 12.478 1.00 14.58 O
ATOM 296 N GLY A 39 83.981 46.422 9.516 1.00 8.95 N
ATOM 297 CA GLY A 39 83.579 47.779 9.898 1.00 10.69 C
ATOM 298 C GLY A 39 84.414 48.258 11.101 1.00 9.72 C
ATOM 299 O GLY A 39 84.651 47.433 11.989 1.00 10.63 O
ATOM 300 N TYR A 40 84.828 49.499 11.114 1.00 9.84 N
ATOM 301 CA TYR A 40 84.642 50.541 10.144 1.00 10.58 C
ATOM 302 C TYR A 40 85.887 51.427 10.129 1.00 13.46 C
ATOM 303 O TYR A 40 86.446 51.699 11.214 1.00 13.32 O
ATOM 304 CB TYR A 40 83.426 51.405 10.465 1.00 11.19 C
ATOM 305 CG TYR A 40 82.164 50.600 10.419 1.00 10.27 C
ATOM 306 CD1 TYR A 40 81.449 50.468 9.225 1.00 9.72 C
ATOM 307 CD2 TYR A 40 81.634 49.926 11.523 1.00 12.13 C
ATOM 308 CE1 TYR A 40 80.288 49.719 9.152 1.00 9.74 C
ATOM 309 CE2 TYR A 40 80.490 49.181 11.452 1.00 11.64 C
ATOM 310 CZ TYR A 40 79.794 49.072 10.244 1.00 10.95 C
ATOM 311 OH TYR A 40 78.633 48.333 10.175 1.00 12.25 O
ATOM 312 N ALA A 41 86.249 51.906 8.959 1.00 10.64 N
ATOM 313 CA ALA A 41 87.236 52.984 8.876 1.00 10.79 C
ATOM 314 C ALA A 41 86.486 54.298 8.993 1.00 11.75 C
ATOM 315 O ALA A 41 85.275 54.387 8.810 1.00 11.71 O
ATOM 316 CB ALA A 41 87.980 52.919 7.542 1.00 11.83 C
ATOM 317 N GLY A 42 87.215 55.394 9.315 1.00 11.54 N
ATOM 318 CA GLY A 42 86.589 56.681 9.321 1.00 13.06 C
ATOM 319 C GLY A 42 87.365 57.713 8.504 1.00 12.39 C
ATOM 320 O GLY A 42 88.289 57.313 7.807 1.00 13.48 O
ATOM 321 N LEU A 43 86.950 58.969 8.662 1.00 11.10 N
ATOM 322 CA LEU A 43 87.635 60.062 8.017 1.00 13.54 C
ATOM 323 C LEU A 43 88.408 60.912 9.040 1.00 14.30 C
ATOM 324 O LEU A 43 87.827 61.288 10.050 1.00 15.47 O
ATOM 325 CB LEU A 43 86.657 61.028 7.322 1.00 14.61 C
ATOM 326 CG LEU A 43 85.768 60.404 6.236 1.00 11.65 C
ATOM 327 CD1 LEU A 43 84.943 61.517 5.614 1.00 13.40 C
ATOM 328 CD2 LEU A 43 86.637 59.685 5.241 1.00 14.17 C
ATOM 329 N ARG A 44 89.663 61.202 8.749 1.00 14.20 N
ATOM 330 CA ARG A 44 90.408 62.051 9.711 1.00 15.45 C
ATOM 331 C ARG A 44 89.809 63.439 9.753 1.00 19.62 C
ATOM 332 O ARG A 44 89.531 64.056 8.710 1.00 20.21 O
ATOM 333 CB ARG A 44 91.865 62.171 9.293 1.00 16.94 C
ATOM 334 CG ARG A 44 92.606 60.858 9.153 1.00 19.86 C
ATOM 335 CD ARG A 44 94.106 61.133 9.034 1.00 23.95 C
ATOM 336 NE ARG A 44 94.916 59.926 9.011 1.00 22.63 N
ATOM 337 CZ ARG A 44 95.264 59.199 10.069 1.00 20.76 C
ATOM 338 NH1 ARG A 44 94.905 59.492 11.298 1.00 29.16 N
ATOM 339 NH2 ARG A 44 96.017 58.119 9.862 1.00 31.60 N
ATOM 340 N GLY A 45 89.642 63.972 10.977 1.00 19.03 N
ATOM 341 CA GLY A 45 89.181 65.350 11.059 1.00 23.14 C
ATOM 342 C GLY A 45 90.091 66.377 10.408 1.00 18.56 C
ATOM 343 O GLY A 45 89.627 67.395 9.902 1.00 30.12 O
ATOM 344 N GLU A 46 91.397 66.170 10.384 1.00 24.23 N
ATOM 345 CA GLU A 46 92.284 67.192 9.834 1.00 35.61 C
ATOM 346 C GLU A 46 92.377 67.235 8.323 1.00 37.56 C
ATOM 347 O GLU A 46 92.655 68.316 7.772 1.00 35.23 O
ATOM 348 CB GLU A 46 93.703 66.931 10.384 1.00 58.23 C
ATOM 349 CG GLU A 46 94.244 65.579 9.934 1.00 73.59 C
ATOM 350 CD GLU A 46 94.283 64.541 11.043 1.00 87.52 C
ATOM 351 OE1 GLU A 46 93.441 64.575 11.972 1.00 60.89 O
ATOM 352 OE2 GLU A 46 95.189 63.675 10.972 1.00110.24 O
ATOM 353 N ASN A 47 92.215 66.114 7.617 1.00 18.72 N
ATOM 354 CA ASN A 47 92.454 66.122 6.185 1.00 22.14 C
ATOM 355 C ASN A 47 91.447 65.215 5.428 1.00 16.99 C
ATOM 356 O ASN A 47 91.655 65.140 4.227 1.00 19.21 O
ATOM 357 CB ASN A 47 93.863 65.664 5.765 1.00 20.57 C
ATOM 358 CG ASN A 47 94.264 64.358 6.430 1.00 26.26 C
ATOM 359 OD1 ASN A 47 93.443 63.464 6.663 1.00 18.85 O
ATOM 360 ND2 ASN A 47 95.538 64.206 6.788 1.00 31.59 N
ATOM 361 N LEU A 48 90.509 64.628 6.142 1.00 16.29 N
ATOM 362 CA LEU A 48 89.446 63.782 5.529 1.00 14.65 C
ATOM 363 C LEU A 48 89.979 62.543 4.881 1.00 16.13 C
ATOM 364 O LEU A 48 89.333 61.862 4.060 1.00 18.88 O
ATOM 365 CB LEU A 48 88.643 64.610 4.527 1.00 15.36 C
ATOM 366 CG LEU A 48 88.081 65.937 5.060 1.00 17.50 C
ATOM 367 CD1 LEU A 48 87.264 66.647 4.007 1.00 21.93 C
ATOM 368 CD2 LEU A 48 87.252 65.685 6.320 1.00 17.90 C
ATOM 369 N GLN A 49 91.194 62.093 5.164 1.00 15.72 N
ATOM 370 CA GLN A 49 91.676 60.807 4.712 1.00 15.35 C
ATOM 371 C GLN A 49 90.989 59.658 5.448 1.00 14.86 C
ATOM 372 O GLN A 49 90.564 59.767 6.595 1.00 14.27 O
ATOM 373 CB GLN A 49 93.205 60.672 4.940 1.00 20.04 C
ATOM 374 CG GLN A 49 93.959 61.533 3.944 1.00 20.60 C
ATOM 375 CD GLN A 49 95.458 61.432 4.045 1.00 32.98 C
ATOM 376 OE1 GLN A 49 95.967 60.412 4.483 1.00 38.70 O
ATOM 377 NE2 GLN A 49 96.109 62.526 3.649 1.00 32.46 N
ATOM 378 N ALA A 50 90.858 58.535 4.743 1.00 13.50 N
ATOM 379 CA ALA A 50 90.369 57.319 5.381 1.00 13.35 C
ATOM 380 C ALA A 50 91.432 56.777 6.326 1.00 14.70 C
ATOM 381 O ALA A 50 92.617 56.778 5.947 1.00 15.92 O
ATOM 382 CB ALA A 50 90.014 56.258 4.324 1.00 14.67 C
ATOM 383 N TYR A 51 90.971 56.267 7.466 1.00 13.68 N
ATOM 384 CA TYR A 51 91.941 55.769 8.448 1.00 13.99 C
ATOM 385 C TYR A 51 91.271 54.762 9.345 1.00 16.10 C
ATOM 386 O TYR A 51 90.049 54.695 9.522 1.00 14.09 O
ATOM 387 CB TYR A 51 92.523 56.949 9.285 1.00 15.30 C
ATOM 388 CG TYR A 51 91.634 57.455 10.382 1.00 16.48 C
ATOM 389 CD1 TYR A 51 90.411 58.067 10.172 1.00 16.66 C
ATOM 390 CD2 TYR A 51 92.028 57.326 11.728 1.00 17.83 C
ATOM 391 CE1 TYR A 51 89.588 58.529 11.176 1.00 17.27 C
ATOM 392 CE2 TYR A 51 91.215 57.785 12.738 1.00 23.14 C
ATOM 393 CZ TYR A 51 90.015 58.390 12.478 1.00 22.12 C
ATOM 394 OH TYR A 51 89.218 58.826 13.502 1.00 22.73 O
ATOM 395 N SER A 52 92.096 53.946 9.995 1.00 14.41 N
ATOM 396 CA SER A 52 91.635 53.013 10.998 1.00 16.51 C
ATOM 397 C SER A 52 91.289 53.711 12.307 1.00 16.28 C
ATOM 398 O SER A 52 92.143 54.503 12.750 1.00 18.87 O
ATOM 399 CB SER A 52 92.762 51.991 11.243 1.00 15.94 C
ATOM 400 OG SER A 52 92.444 51.301 12.429 1.00 16.31 O
ATOM 401 N MET A 53 90.115 53.441 12.860 1.00 16.25 N
ATOM 402 CA MET A 53 89.768 54.137 14.116 1.00 16.21 C
ATOM 403 C MET A 53 90.291 53.379 15.321 1.00 17.82 C
ATOM 404 O MET A 53 90.057 53.763 16.484 1.00 21.15 O
ATOM 405 CB MET A 53 88.240 54.331 14.150 1.00 18.74 C
ATOM 406 CG MET A 53 87.823 55.269 13.031 1.00 19.65 C
ATOM 407 SD MET A 53 86.103 55.819 13.090 1.00 21.87 S
ATOM 408 CE MET A 53 85.328 54.311 12.484 1.00 24.68 C
ATOM 409 N ASN A 54 90.986 52.266 15.095 1.00 14.83 N
ATOM 410 CA ASN A 54 91.694 51.553 16.155 1.00 14.50 C
ATOM 411 C ASN A 54 92.938 50.900 15.545 1.00 10.81 C
ATOM 412 O ASN A 54 92.958 49.694 15.376 1.00 13.57 O
ATOM 413 CB ASN A 54 90.855 50.460 16.813 1.00 16.79 C
ATOM 414 CG ASN A 54 91.510 49.850 18.029 1.00 17.99 C
ATOM 415 OD1 ASN A 54 92.703 50.007 18.323 1.00 18.02 O
ATOM 416 ND2 ASN A 54 90.759 49.084 18.839 1.00 23.53 N
ATOM 417 N GLU A 55 93.913 51.792 15.313 1.00 12.12 N
ATOM 418 CA GLU A 55 95.111 51.286 14.626 1.00 12.55 C
ATOM 419 C GLU A 55 95.813 50.182 15.399 1.00 11.42 C
ATOM 420 O GLU A 55 96.365 49.229 14.872 1.00 11.12 O
ATOM 421 CB GLU A 55 96.064 52.456 14.381 1.00 15.82 C
ATOM 422 CG GLU A 55 95.541 53.481 13.389 1.00 24.96 C
ATOM 423 CD GLU A 55 96.670 54.401 12.924 1.00 39.40 C
ATOM 424 OE1 GLU A 55 97.636 54.540 13.720 1.00 21.33 O
ATOM 425 OE2 GLU A 55 96.523 54.923 11.792 1.00 42.15 O
ATOM 426 N ASN A 56 95.803 50.365 16.745 1.00 12.80 N
ATOM 427 CA ASN A 56 96.507 49.354 17.535 1.00 11.39 C
ATOM 428 C ASN A 56 96.019 47.955 17.264 1.00 12.18 C
ATOM 429 O ASN A 56 96.778 46.987 17.109 1.00 14.25 O
ATOM 430 CB ASN A 56 96.378 49.670 19.053 1.00 11.77 C
ATOM 431 CG ASN A 56 97.333 48.762 19.823 1.00 16.43 C
ATOM 432 OD1 ASN A 56 98.534 48.685 19.545 1.00 16.66 O
ATOM 433 ND2 ASN A 56 96.843 48.090 20.838 1.00 18.30 N
ATOM 434 N LEU A 57 94.707 47.771 17.148 1.00 12.02 N
ATOM 435 CA LEU A 57 94.124 46.488 16.827 1.00 10.84 C
ATOM 436 C LEU A 57 94.182 46.146 15.323 1.00 9.31 C
ATOM 437 O LEU A 57 94.662 45.081 14.974 1.00 10.94 O
ATOM 438 CB LEU A 57 92.669 46.457 17.336 1.00 13.24 C
ATOM 439 CG LEU A 57 91.912 45.191 16.973 1.00 15.03 C
ATOM 440 CD1 LEU A 57 92.489 43.944 17.621 1.00 17.28 C
ATOM 441 CD2 LEU A 57 90.442 45.346 17.393 1.00 18.93 C
ATOM 442 N ASP A 58 93.660 47.068 14.501 1.00 10.70 N
ATOM 443 CA ASP A 58 93.456 46.771 13.066 1.00 10.65 C
ATOM 444 C ASP A 58 94.801 46.568 12.341 1.00 10.43 C
ATOM 445 O ASP A 58 94.869 45.712 11.475 1.00 9.94 O
ATOM 446 CB ASP A 58 92.700 47.894 12.388 1.00 11.92 C
ATOM 447 CG ASP A 58 91.242 48.207 12.842 1.00 10.96 C
ATOM 448 OD1 ASP A 58 90.709 47.283 13.465 1.00 13.68 O
ATOM 449 OD2 ASP A 58 90.830 49.317 12.532 1.00 13.84 O
ATOM 450 N ILE A 59 95.779 47.370 12.753 1.00 10.28 N
ATOM 451 CA ILE A 59 97.094 47.390 12.066 1.00 10.44 C
ATOM 452 C ILE A 59 98.160 46.672 12.908 1.00 9.81 C
ATOM 453 O ILE A 59 98.752 45.694 12.499 1.00 10.22 O
ATOM 454 CB ILE A 59 97.459 48.832 11.736 1.00 9.84 C
ATOM 455 CG1 ILE A 59 96.483 49.436 10.703 1.00 12.59 C
ATOM 456 CG2 ILE A 59 98.893 48.951 11.195 1.00 10.36 C
ATOM 457 CD1 ILE A 59 96.690 50.920 10.443 1.00 13.07 C
ATOM 458 N TYR A 60 98.392 47.238 14.118 1.00 11.61 N
ATOM 459 CA TYR A 60 99.590 46.749 14.858 1.00 10.38 C
ATOM 460 C TYR A 60 99.345 45.391 15.442 1.00 11.69 C
ATOM 461 O TYR A 60 100.296 44.650 15.751 1.00 13.69 O
ATOM 462 CB TYR A 60 100.044 47.829 15.914 1.00 11.55 C
ATOM 463 CG TYR A 60 100.432 49.030 15.093 1.00 10.15 C
ATOM 464 CD1 TYR A 60 99.581 50.094 14.884 1.00 12.11 C
ATOM 465 CD2 TYR A 60 101.694 49.020 14.465 1.00 10.09 C
ATOM 466 CE1 TYR A 60 99.963 51.180 14.099 1.00 13.92 C
ATOM 467 CE2 TYR A 60 102.055 50.085 13.687 1.00 11.41 C
ATOM 468 CZ TYR A 60 101.223 51.154 13.497 1.00 12.71 C
ATOM 469 OH TYR A 60 101.604 52.221 12.688 1.00 13.92 O
ATOM 470 N LYS A 61 98.098 44.885 15.592 1.00 10.76 N
ATOM 471 CA LYS A 61 97.871 43.501 15.940 1.00 12.54 C
ATOM 472 C LYS A 61 97.151 42.729 14.821 1.00 9.64 C
ATOM 473 O LYS A 61 96.590 41.675 15.008 1.00 11.24 O
ATOM 474 CB LYS A 61 97.089 43.382 17.285 1.00 17.65 C