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2VJ3.pdb
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1455 lines (1455 loc) · 115 KB
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HEADER TRANSCRIPTION 06-DEC-07 2VJ3
TITLE HUMAN NOTCH-1 EGFS 11-13
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUROGENIC LOCUS NOTCH HOMOLOG PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: EGFS 11-13, RESIDUES 411-526;
COMPND 5 SYNONYM: NOTCH 1, HN1, TRANSLOCATION-ASSOCIATED NOTCH PROTEIN TAN-1,
COMPND 6 NOTCH-1;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: NM554;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PQE30
KEYWDS TRANSCRIPTION, METAL-BINDING, TRANSMEMBRANE, DEVELOPMENTAL PROTEIN,
KEYWDS 2 NOTCH SIGNALING PATHWAY, DIFFERENTIATION, PHOSPHORYLATION, EGF-LIKE
KEYWDS 3 DOMAIN, TRANSCRIPTION REGULATION, RECEPTOR, ACTIVATOR, ANK REPEAT,
KEYWDS 4 SIGNALLING, POLYMORPHISM, GLYCOPROTEIN, EXTRACELLULAR, EGF, NOTCH,
KEYWDS 5 JAGGED, NUCLEUS, CALCIUM, MEMBRANE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.JOHNSON,J.CORDLE,J.Z.TAY,P.ROVERSI,S.M.LEA
REVDAT 4 05-JUL-17 2VJ3 1 REMARK
REVDAT 3 25-AUG-10 2VJ3 1 JRNL REMARK FORMUL
REVDAT 2 24-FEB-09 2VJ3 1 VERSN
REVDAT 1 29-JUL-08 2VJ3 0
JRNL AUTH J.CORDLE,S.JOHNSON,J.Z.TAY,P.ROVERSI,M.B.WILKIN,
JRNL AUTH 2 B.H.DE MADRID,H.SHIMIZU,S.JENSEN,P.WHITEMAN,B.JIN,
JRNL AUTH 3 C.REDFIELD,M.BARON,S.M.LEA,P.A.HANDFORD
JRNL TITL A CONSERVED FACE OF THE JAGGED/SERRATE DSL DOMAIN IS
JRNL TITL 2 INVOLVED IN NOTCH TRANS-ACTIVATION AND CIS-INHIBITION.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 15 849 2008
JRNL REFN ISSN 1545-9993
JRNL PMID 18660822
JRNL DOI 10.1038/NSMB.1457
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT 5.6.1
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 95.40
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 4080
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.239
REMARK 3 R VALUE (WORKING SET) : 0.239
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 190
REMARK 3
REMARK 3 USING ALL DATA, NO SIGMA CUTOFF.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.2390
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.2390
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.00
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 190
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 897
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 8
REMARK 3 SOLVENT ATOMS : 23
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : 52.500
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : 0.005 ; 2.000 ; 922
REMARK 3 BOND ANGLES (DEGREES) : 0.680 ; 2.000 ; 1250
REMARK 3 TORSION ANGLES (DEGREES) : 13.600; 0.000 ; 180
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : 0.001 ; 2.000 ; 35
REMARK 3 GENERAL PLANES (A) : 0.020 ; 5.000 ; 132
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : 1.066 ; 20.000; 922
REMARK 3 NON-BONDED CONTACTS (A) : 0.086 ; 5.000 ; 4
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : 0
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : BABINET SCALING
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 124.0
REMARK 3
REMARK 3 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : TNT PROTGEO
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : TNT BCORREL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BUSTER-TNT-GELLY 2.1.1 E. BLANC, P.
REMARK 3 ROVERSI, C. VONRHEIN, C. FLENSBURG, S. M. LEA AND G.BRICOGNE
REMARK 4
REMARK 4 2VJ3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-DEC-07.
REMARK 100 THE DEPOSITION ID IS D_1290034695.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-MAR-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : BRUKER AXS MICROSTAR
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.542
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 4321
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.570
REMARK 200 RESOLUTION RANGE LOW (A) : 24.250
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.3
REMARK 200 DATA REDUNDANCY : 8.200
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.57
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.71
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.15000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1EDM
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% (W/V) PEG-5000-MME, 100MM SODIUM
REMARK 280 ACETATE, PH5.7
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 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+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 93.90000
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 187.80000
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 187.80000
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 93.90000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 CA CA A1534 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 SER A 409
REMARK 465 ALA A 410
REMARK 465 HIS A 531
REMARK 465 ILE A 532
REMARK 465 LEU A 533
REMARK 465 ASP A 534
REMARK 465 ALA A 535
REMARK 465 GLN A 536
REMARK 465 LYS A 537
REMARK 465 MET A 538
REMARK 465 VAL A 539
REMARK 465 TRP A 540
REMARK 465 ASN A 541
REMARK 465 HIS A 542
REMARK 465 ARG A 543
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 GLY A 481 O HOH A 2015 2.14
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 SER A 435 -148.07 -148.70
REMARK 500 LYS A 508 -157.46 -127.29
REMARK 500
REMARK 500 REMARK: NULL
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 CA A1531 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL A 453 O
REMARK 620 2 GLU A 455 OE1 67.9
REMARK 620 3 ASP A 469 OD1 80.9 74.7
REMARK 620 4 HOH A2007 O 81.9 85.2 157.3
REMARK 620 5 HOH A2009 O 146.8 143.3 95.6 106.9
REMARK 620 6 ASP A 452 OD1 93.9 143.7 135.4 60.6 65.5
REMARK 620 7 GLN A 470 O 137.2 70.6 97.9 84.8 76.0 114.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1532 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 415 OE1
REMARK 620 2 HOH A2002 O 84.7
REMARK 620 3 VAL A 413 O 68.3 72.2
REMARK 620 4 ASN A 431 OD1 95.6 166.3 95.1
REMARK 620 5 ASP A 412 OD1 135.6 53.3 83.9 121.7
REMARK 620 6 THR A 432 O 143.4 112.1 146.7 75.5 74.8
REMARK 620 7 SER A 435 O 74.9 103.7 143.2 89.5 123.9 69.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1533 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 493 OE1
REMARK 620 2 LYS A 508 O 90.5
REMARK 620 3 HOH A2015 O 84.0 107.5
REMARK 620 4 ASN A 490 OD1 157.2 99.9 73.5
REMARK 620 5 ASP A 507 OD1 68.9 85.7 150.2 131.8
REMARK 620 6 ASP A 507 OD2 112.7 85.3 159.2 88.5 43.9
REMARK 620 7 THR A 491 O 73.9 159.6 84.3 99.3 76.6 88.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1534 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 511 OE2
REMARK 620 2 HIS A 523 NE2 101.2
REMARK 620 3 HIS A 523 NE2 99.3 133.3
REMARK 620 4 GLU A 511 OE2 124.1 97.3 104.9
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1531
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1532
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1533
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1534
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 1535
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 1536
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1537
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1538
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1TOZ RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF THE HUMAN NOTCH-1 LIGAND BINDING REGION
REMARK 900 RELATED ID: 2F8Y RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN NOTCH1 ANKYRIN REPEATS TO
REMARK 900 1.55ARESOLUTION.
REMARK 900 RELATED ID: 1YYH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN NOTCH 1 ANKYRIN DOMAIN
REMARK 900 RELATED ID: 1PB5 RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF A PROTOTYPE LNR MODULE FROM HUMAN NOTCH1
REMARK 900 RELATED ID: 2F8X RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACTIVATED NOTCH, CSL AND MAML ON HES-1PROMOTER
REMARK 900 DNA SEQUENCE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 M477I IS A PUBLISHED CONFLICT. THE DETAILS OF WHICH CAN BE
REMARK 999 FOUND IN HAMBLETON ET AL (2004) STRUCTURE. 12:2173-83
DBREF 2VJ3 A 409 410 PDB 2VJ3 2VJ3 409 410
DBREF 2VJ3 A 411 526 UNP P46531 NOTC1_HUMAN 411 526
DBREF 2VJ3 A 527 543 PDB 2VJ3 2VJ3 527 543
SEQADV 2VJ3 ILE A 477 UNP P46531 MET 477 CONFLICT
SEQRES 1 A 135 SER ALA GLN ASP VAL ASP GLU CYS SER LEU GLY ALA ASN
SEQRES 2 A 135 PRO CYS GLU HIS ALA GLY LYS CYS ILE ASN THR LEU GLY
SEQRES 3 A 135 SER PHE GLU CYS GLN CYS LEU GLN GLY TYR THR GLY PRO
SEQRES 4 A 135 ARG CYS GLU ILE ASP VAL ASN GLU CYS VAL SER ASN PRO
SEQRES 5 A 135 CYS GLN ASN ASP ALA THR CYS LEU ASP GLN ILE GLY GLU
SEQRES 6 A 135 PHE GLN CYS ILE CYS MET PRO GLY TYR GLU GLY VAL HIS
SEQRES 7 A 135 CYS GLU VAL ASN THR ASP GLU CYS ALA SER SER PRO CYS
SEQRES 8 A 135 LEU HIS ASN GLY ARG CYS LEU ASP LYS ILE ASN GLU PHE
SEQRES 9 A 135 GLN CYS GLU CYS PRO THR GLY PHE THR GLY HIS LEU CYS
SEQRES 10 A 135 GLN VAL ASP LEU HIS HIS ILE LEU ASP ALA GLN LYS MET
SEQRES 11 A 135 VAL TRP ASN HIS ARG
HET CA A1531 1
HET CA A1532 1
HET CA A1533 1
HET CA A1534 1
HET NA A1535 1
HET NA A1536 1
HET CL A1537 1
HET CL A1538 1
HETNAM CA CALCIUM ION
HETNAM NA SODIUM ION
HETNAM CL CHLORIDE ION
FORMUL 2 CA 4(CA 2+)
FORMUL 6 NA 2(NA 1+)
FORMUL 8 CL 2(CL 1-)
FORMUL 10 HOH *23(H2 O)
SHEET 1 AA 2 LYS A 428 ASN A 431 0
SHEET 2 AA 2 PHE A 436 GLN A 439 -1 O GLU A 437 N ILE A 430
SHEET 1 AB 2 TYR A 444 THR A 445 0
SHEET 2 AB 2 ILE A 451 ASP A 452 -1 O ILE A 451 N THR A 445
SHEET 1 AC 2 THR A 466 ASP A 469 0
SHEET 2 AC 2 PHE A 474 ILE A 477 -1 O GLN A 475 N LEU A 468
SHEET 1 AD 2 TYR A 482 GLU A 483 0
SHEET 2 AD 2 VAL A 489 ASN A 490 -1 O VAL A 489 N GLU A 483
SHEET 1 AE 2 ARG A 504 ASP A 507 0
SHEET 2 AE 2 PHE A 512 GLU A 515 -1 O GLN A 513 N LEU A 506
SHEET 1 AF 2 PHE A 520 THR A 521 0
SHEET 2 AF 2 VAL A 527 ASP A 528 -1 O VAL A 527 N THR A 521
SSBOND 1 CYS A 416 CYS A 429 1555 1555 2.03
SSBOND 2 CYS A 423 CYS A 438 1555 1555 2.03
SSBOND 3 CYS A 440 CYS A 449 1555 1555 2.03
SSBOND 4 CYS A 456 CYS A 467 1555 1555 2.02
SSBOND 5 CYS A 461 CYS A 476 1555 1555 2.03
SSBOND 6 CYS A 478 CYS A 487 1555 1555 2.03
SSBOND 7 CYS A 494 CYS A 505 1555 1555 2.03
SSBOND 8 CYS A 499 CYS A 514 1555 1555 2.03
SSBOND 9 CYS A 516 CYS A 525 1555 1555 2.03
LINK CA CA A1531 O VAL A 453 1555 1555 2.33
LINK CA CA A1531 OE1 GLU A 455 1555 1555 2.64
LINK CA CA A1531 OD1 ASP A 469 1555 1555 2.68
LINK CA CA A1531 O HOH A2007 1555 1555 2.40
LINK CA CA A1531 O HOH A2009 1555 1555 2.43
LINK CA CA A1531 OD1 ASP A 452 1555 1555 2.95
LINK CA CA A1531 O GLN A 470 1555 1555 2.40
LINK CA CA A1532 OE1 GLU A 415 1555 1555 2.56
LINK CA CA A1532 O HOH A2002 1555 1555 2.53
LINK CA CA A1532 O VAL A 413 1555 1555 2.59
LINK CA CA A1532 OD1 ASN A 431 1555 1555 2.44
LINK CA CA A1532 OD1 ASP A 412 1555 1555 2.82
LINK CA CA A1532 O THR A 432 1555 1555 2.60
LINK CA CA A1532 O SER A 435 1555 1555 2.40
LINK CA CA A1533 OE1 GLU A 493 1555 1555 2.59
LINK CA CA A1533 O LYS A 508 1555 1555 2.18
LINK CA CA A1533 O HOH A2015 1555 1555 2.51
LINK CA CA A1533 OD1 ASN A 490 1555 1555 2.55
LINK CA CA A1533 OD1 ASP A 507 1555 1555 2.79
LINK CA CA A1533 OD2 ASP A 507 1555 1555 3.05
LINK CA CA A1533 O THR A 491 1555 1555 2.23
LINK CA CA A1534 OE2 GLU A 511 1555 5554 2.37
LINK CA CA A1534 NE2 HIS A 523 1555 1555 2.53
LINK CA CA A1534 NE2 HIS A 523 1555 5554 2.44
LINK CA CA A1534 OE2 GLU A 511 1555 1555 2.34
CISPEP 1 THR A 518 GLY A 519 0 -2.42
CISPEP 2 THR A 521 GLY A 522 0 -3.77
SITE 1 AC1 7 ASP A 452 VAL A 453 GLU A 455 ASP A 469
SITE 2 AC1 7 GLN A 470 HOH A2007 HOH A2009
SITE 1 AC2 7 ASP A 412 VAL A 413 GLU A 415 ASN A 431
SITE 2 AC2 7 THR A 432 SER A 435 HOH A2002
SITE 1 AC3 6 ASN A 490 THR A 491 GLU A 493 ASP A 507
SITE 2 AC3 6 LYS A 508 HOH A2015
SITE 1 AC4 2 GLU A 511 HIS A 523
SITE 1 AC5 4 LEU A 524 CYS A 525 GLN A 526 CL A1537
SITE 1 AC6 2 GLU A 483 ASP A 528
SITE 1 AC7 3 GLU A 493 ASN A 510 NA A1535
SITE 1 AC8 3 GLN A 475 CYS A 476 VAL A 485
CRYST1 28.000 28.000 281.700 90.00 90.00 120.00 P 31 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 0.035733 0.020630 0.000000 0.00000
SCALE2 0.000000 0.041260 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003549 0.00000
ATOM 1 N GLN A 411 -13.690 13.713 28.298 1.00 52.12 N
ATOM 2 CA GLN A 411 -13.548 12.274 27.936 1.00 51.85 C
ATOM 3 C GLN A 411 -13.850 12.049 26.464 1.00 54.80 C
ATOM 4 O GLN A 411 -14.811 12.605 25.924 1.00 54.84 O
ATOM 5 CB GLN A 411 -14.454 11.400 28.807 1.00 52.58 C
ATOM 6 CG GLN A 411 -14.252 9.888 28.652 1.00 60.65 C
ATOM 7 CD GLN A 411 -12.840 9.426 28.993 1.00 71.36 C
ATOM 8 OE1 GLN A 411 -12.199 9.948 29.908 1.00 64.27 O
ATOM 9 NE2 GLN A 411 -12.354 8.432 28.256 1.00 64.83 N
ATOM 10 N ASP A 412 -13.021 11.231 25.820 1.00 49.63 N
ATOM 11 CA ASP A 412 -13.160 10.932 24.398 1.00 48.47 C
ATOM 12 C ASP A 412 -13.309 9.433 24.147 1.00 49.52 C
ATOM 13 O ASP A 412 -12.623 8.617 24.768 1.00 49.39 O
ATOM 14 CB ASP A 412 -11.958 11.482 23.622 1.00 50.34 C
ATOM 15 CG ASP A 412 -12.064 11.243 22.124 1.00 61.43 C
ATOM 16 OD1 ASP A 412 -13.110 11.581 21.529 1.00 61.25 O
ATOM 17 OD2 ASP A 412 -11.093 10.717 21.537 1.00 66.56 O
ATOM 18 N VAL A 413 -14.214 9.084 23.236 1.00 43.21 N
ATOM 19 CA VAL A 413 -14.407 7.697 22.814 1.00 40.97 C
ATOM 20 C VAL A 413 -13.799 7.474 21.424 1.00 40.51 C
ATOM 21 O VAL A 413 -14.055 8.240 20.494 1.00 40.03 O
ATOM 22 CB VAL A 413 -15.912 7.271 22.875 1.00 45.43 C
ATOM 23 CG1 VAL A 413 -16.801 8.201 22.043 1.00 45.43 C
ATOM 24 CG2 VAL A 413 -16.096 5.811 22.458 1.00 44.99 C
ATOM 25 N ASP A 414 -12.975 6.436 21.304 1.00 34.20 N
ATOM 26 CA ASP A 414 -12.337 6.087 20.038 1.00 32.61 C
ATOM 27 C ASP A 414 -13.311 5.311 19.149 1.00 34.36 C
ATOM 28 O ASP A 414 -13.485 4.101 19.313 1.00 33.46 O
ATOM 29 CB ASP A 414 -11.059 5.274 20.293 1.00 33.87 C
ATOM 30 CG ASP A 414 -10.238 5.034 19.028 1.00 39.33 C
ATOM 31 OD1 ASP A 414 -10.675 5.419 17.922 1.00 37.80 O
ATOM 32 OD2 ASP A 414 -9.140 4.451 19.146 1.00 42.36 O
ATOM 33 N GLU A 415 -13.935 6.020 18.208 1.00 28.92 N
ATOM 34 CA GLU A 415 -14.910 5.428 17.286 1.00 28.44 C
ATOM 35 C GLU A 415 -14.294 4.401 16.345 1.00 33.53 C
ATOM 36 O GLU A 415 -14.990 3.514 15.853 1.00 32.89 O
ATOM 37 CB GLU A 415 -15.624 6.514 16.483 1.00 30.08 C
ATOM 38 CG GLU A 415 -16.709 7.273 17.234 1.00 37.01 C
ATOM 39 CD GLU A 415 -16.184 8.483 17.988 1.00 47.65 C
ATOM 40 OE1 GLU A 415 -14.996 8.837 17.824 1.00 37.81 O
ATOM 41 OE2 GLU A 415 -16.971 9.092 18.743 1.00 37.13 O
ATOM 42 N CYS A 416 -12.992 4.531 16.101 1.00 30.16 N
ATOM 43 CA CYS A 416 -12.263 3.629 15.221 1.00 30.21 C
ATOM 44 C CYS A 416 -11.996 2.274 15.874 1.00 37.41 C
ATOM 45 O CYS A 416 -11.975 1.245 15.196 1.00 37.69 O
ATOM 46 CB CYS A 416 -10.944 4.267 14.776 1.00 30.34 C
ATOM 47 SG CYS A 416 -11.115 5.926 14.077 1.00 34.37 S
ATOM 48 N SER A 417 -11.797 2.286 17.174 1.00 36.40 N
ATOM 49 CA SER A 417 -11.520 1.069 17.939 1.00 37.43 C
ATOM 50 C SER A 417 -12.772 0.231 18.202 1.00 41.63 C
ATOM 51 O SER A 417 -12.671 -0.940 18.572 1.00 41.83 O
ATOM 52 CB SER A 417 -10.822 1.408 19.259 1.00 42.28 C
ATOM 53 OG SER A 417 -9.475 1.784 19.040 1.00 54.74 O
ATOM 54 N LEU A 418 -13.944 0.835 18.003 1.00 38.26 N
ATOM 55 CA LEU A 418 -15.231 0.148 18.158 1.00 37.36 C
ATOM 56 C LEU A 418 -15.382 -1.038 17.198 1.00 40.48 C
ATOM 57 O LEU A 418 -14.560 -1.226 16.303 1.00 40.36 O
ATOM 58 CB LEU A 418 -16.389 1.139 17.978 1.00 37.39 C
ATOM 59 CG LEU A 418 -17.083 1.744 19.208 1.00 43.02 C
ATOM 60 CD1 LEU A 418 -16.115 2.385 20.197 1.00 43.03 C
ATOM 61 CD2 LEU A 418 -18.136 2.752 18.769 1.00 45.46 C
ATOM 62 N GLY A 419 -16.434 -1.829 17.405 1.00 36.31 N
ATOM 63 CA GLY A 419 -16.684 -3.047 16.639 1.00 35.37 C
ATOM 64 C GLY A 419 -16.454 -2.930 15.151 1.00 38.45 C
ATOM 65 O GLY A 419 -15.618 -3.639 14.588 1.00 38.46 O
ATOM 66 N ALA A 420 -17.192 -2.025 14.514 1.00 34.50 N
ATOM 67 CA ALA A 420 -17.100 -1.822 13.071 1.00 33.43 C
ATOM 68 C ALA A 420 -16.302 -0.573 12.709 1.00 36.08 C
ATOM 69 O ALA A 420 -16.219 0.375 13.494 1.00 35.98 O
ATOM 70 CB ALA A 420 -18.494 -1.755 12.459 1.00 33.85 C
ATOM 71 N ASN A 421 -15.713 -0.590 11.515 1.00 30.35 N
ATOM 72 CA ASN A 421 -15.056 0.579 10.945 1.00 29.86 C
ATOM 73 C ASN A 421 -16.113 1.505 10.340 1.00 33.45 C
ATOM 74 O ASN A 421 -16.823 1.108 9.411 1.00 33.38 O
ATOM 75 CB ASN A 421 -14.030 0.144 9.889 1.00 31.91 C
ATOM 76 CG ASN A 421 -13.214 1.305 9.329 1.00 56.41 C
ATOM 77 OD1 ASN A 421 -13.123 2.375 9.931 1.00 50.13 O
ATOM 78 ND2 ASN A 421 -12.606 1.086 8.168 1.00 48.67 N
ATOM 79 N PRO A 422 -16.238 2.735 10.879 1.00 28.69 N
ATOM 80 CA PRO A 422 -17.224 3.697 10.376 1.00 28.54 C
ATOM 81 C PRO A 422 -16.898 4.233 8.980 1.00 30.87 C
ATOM 82 O PRO A 422 -17.761 4.832 8.335 1.00 30.87 O
ATOM 83 CB PRO A 422 -17.171 4.825 11.410 1.00 30.40 C
ATOM 84 CG PRO A 422 -15.820 4.734 12.003 1.00 34.79 C
ATOM 85 CD PRO A 422 -15.466 3.283 12.011 1.00 30.41 C
ATOM 86 N CYS A 423 -15.665 4.019 8.528 1.00 28.32 N
ATOM 87 CA CYS A 423 -15.244 4.412 7.186 1.00 27.05 C
ATOM 88 C CYS A 423 -15.531 3.291 6.195 1.00 31.51 C
ATOM 89 O CYS A 423 -15.011 2.180 6.327 1.00 31.06 O
ATOM 90 CB CYS A 423 -13.756 4.764 7.166 1.00 25.71 C
ATOM 91 SG CYS A 423 -13.243 5.935 8.435 1.00 28.46 S
ATOM 92 N GLU A 424 -16.367 3.591 5.222 1.00 29.52 N
ATOM 93 CA GLU A 424 -16.749 2.617 4.205 1.00 29.21 C
ATOM 94 C GLU A 424 -15.655 2.443 3.153 1.00 32.86 C
ATOM 95 O GLU A 424 -14.759 3.283 3.034 1.00 33.33 O
ATOM 96 CB GLU A 424 -18.073 3.018 3.548 1.00 31.11 C
ATOM 97 CG GLU A 424 -19.283 2.917 4.471 1.00 42.90 C
ATOM 98 CD GLU A 424 -20.548 3.499 3.862 1.00 64.61 C
ATOM 99 OE1 GLU A 424 -20.786 3.295 2.651 1.00 77.74 O
ATOM 100 OE2 GLU A 424 -21.313 4.159 4.599 1.00 51.63 O
ATOM 101 N HIS A 425 -15.739 1.342 2.405 1.00 31.11 N
ATOM 102 CA HIS A 425 -14.806 1.016 1.316 1.00 30.55 C
ATOM 103 C HIS A 425 -13.337 0.962 1.751 1.00 33.02 C
ATOM 104 O HIS A 425 -12.459 1.511 1.079 1.00 32.91 O
ATOM 105 CB HIS A 425 -15.002 1.958 0.119 1.00 30.33 C
ATOM 106 CG HIS A 425 -16.373 1.894 -0.479 1.00 34.38 C
ATOM 107 ND1 HIS A 425 -17.311 2.888 -0.298 1.00 36.88 N
ATOM 108 CD2 HIS A 425 -16.967 0.952 -1.249 1.00 36.10 C
ATOM 109 CE1 HIS A 425 -18.421 2.563 -0.935 1.00 36.49 C
ATOM 110 NE2 HIS A 425 -18.239 1.392 -1.519 1.00 36.81 N
ATOM 111 N ALA A 426 -13.091 0.294 2.880 1.00 29.27 N
ATOM 112 CA ALA A 426 -11.745 0.091 3.440 1.00 28.61 C
ATOM 113 C ALA A 426 -10.949 1.381 3.678 1.00 31.28 C
ATOM 114 O ALA A 426 -9.719 1.396 3.572 1.00 31.00 O
ATOM 115 CB ALA A 426 -10.944 -0.905 2.587 1.00 28.99 C
ATOM 116 N GLY A 427 -11.660 2.458 4.004 1.00 26.85 N
ATOM 117 CA GLY A 427 -11.033 3.731 4.348 1.00 25.83 C
ATOM 118 C GLY A 427 -10.417 3.678 5.731 1.00 28.99 C
ATOM 119 O GLY A 427 -10.913 2.970 6.593 1.00 29.38 O
ATOM 120 N LYS A 428 -9.332 4.421 5.925 1.00 25.50 N
ATOM 121 CA LYS A 428 -8.629 4.440 7.187 1.00 24.59 C
ATOM 122 C LYS A 428 -9.340 5.352 8.184 1.00 30.62 C
ATOM 123 O LYS A 428 -9.609 6.518 7.888 1.00 29.72 O
ATOM 124 CB LYS A 428 -7.174 4.880 6.999 1.00 26.15 C
ATOM 125 CG LYS A 428 -6.310 4.741 8.246 1.00 33.42 C
ATOM 126 CD LYS A 428 -4.939 5.363 8.044 1.00 38.95 C
ATOM 127 CE LYS A 428 -4.129 5.345 9.330 1.00 47.63 C
ATOM 128 NZ LYS A 428 -2.787 5.966 9.149 1.00 55.08 N
ATOM 129 N CYS A 429 -9.642 4.809 9.361 1.00 27.58 N
ATOM 130 CA CYS A 429 -10.258 5.587 10.430 1.00 27.19 C
ATOM 131 C CYS A 429 -9.194 6.247 11.294 1.00 29.60 C
ATOM 132 O CYS A 429 -8.297 5.579 11.814 1.00 30.16 O
ATOM 133 CB CYS A 429 -11.175 4.715 11.292 1.00 28.89 C
ATOM 134 SG CYS A 429 -12.252 5.647 12.417 1.00 31.52 S
ATOM 135 N ILE A 430 -9.303 7.564 11.432 1.00 25.12 N
ATOM 136 CA ILE A 430 -8.412 8.335 12.288 1.00 23.59 C
ATOM 137 C ILE A 430 -9.230 8.993 13.397 1.00 27.97 C
ATOM 138 O ILE A 430 -10.143 9.777 13.129 1.00 28.22 O
ATOM 139 CB ILE A 430 -7.616 9.393 11.484 1.00 27.88 C
ATOM 140 CG1 ILE A 430 -6.705 8.710 10.455 1.00 28.26 C
ATOM 141 CG2 ILE A 430 -6.801 10.277 12.422 1.00 28.97 C
ATOM 142 CD1 ILE A 430 -6.209 9.624 9.347 1.00 33.44 C
ATOM 143 N ASN A 431 -8.899 8.654 14.639 1.00 24.51 N
ATOM 144 CA ASN A 431 -9.611 9.163 15.805 1.00 23.78 C
ATOM 145 C ASN A 431 -9.225 10.599 16.137 1.00 28.12 C
ATOM 146 O ASN A 431 -8.044 10.954 16.120 1.00 28.35 O
ATOM 147 CB ASN A 431 -9.361 8.251 17.002 1.00 23.46 C
ATOM 148 CG ASN A 431 -10.151 8.667 18.225 1.00 35.40 C
ATOM 149 OD1 ASN A 431 -11.314 9.066 18.132 1.00 25.45 O
ATOM 150 ND2 ASN A 431 -9.519 8.569 19.389 1.00 27.95 N
ATOM 151 N THR A 432 -10.230 11.420 16.434 1.00 23.87 N
ATOM 152 CA THR A 432 -10.012 12.778 16.934 1.00 24.40 C
ATOM 153 C THR A 432 -10.682 12.949 18.294 1.00 29.98 C
ATOM 154 O THR A 432 -11.450 12.087 18.729 1.00 29.90 O
ATOM 155 CB THR A 432 -10.521 13.867 15.954 1.00 28.60 C
ATOM 156 OG1 THR A 432 -11.944 13.785 15.821 1.00 28.56 O
ATOM 157 CG2 THR A 432 -9.876 13.714 14.580 1.00 26.55 C
ATOM 158 N LEU A 433 -10.379 14.052 18.973 1.00 28.41 N
ATOM 159 CA LEU A 433 -10.996 14.358 20.262 1.00 28.38 C
ATOM 160 C LEU A 433 -12.381 14.966 20.058 1.00 32.42 C
ATOM 161 O LEU A 433 -12.510 16.104 19.598 1.00 32.19 O
ATOM 162 CB LEU A 433 -10.111 15.297 21.092 1.00 28.94 C
ATOM 163 CG LEU A 433 -8.742 14.801 21.578 1.00 33.71 C
ATOM 164 CD1 LEU A 433 -7.947 15.957 22.166 1.00 33.35 C
ATOM 165 CD2 LEU A 433 -8.868 13.665 22.591 1.00 36.13 C
ATOM 166 N GLY A 434 -13.410 14.192 20.393 1.00 29.17 N
ATOM 167 CA GLY A 434 -14.795 14.629 20.241 1.00 28.26 C
ATOM 168 C GLY A 434 -15.522 13.955 19.091 1.00 31.79 C
ATOM 169 O GLY A 434 -16.741 13.780 19.139 1.00 32.00 O
ATOM 170 N SER A 435 -14.773 13.579 18.055 1.00 26.74 N
ATOM 171 CA SER A 435 -15.343 12.945 16.875 1.00 26.05 C
ATOM 172 C SER A 435 -14.349 11.965 16.241 1.00 28.10 C
ATOM 173 O SER A 435 -13.553 11.339 16.944 1.00 26.41 O
ATOM 174 CB SER A 435 -15.779 14.014 15.876 1.00 28.96 C
ATOM 175 OG SER A 435 -16.554 13.451 14.834 1.00 38.21 O
ATOM 176 N PHE A 436 -14.414 11.829 14.926 1.00 22.93 N
ATOM 177 CA PHE A 436 -13.472 11.013 14.159 1.00 21.64 C
ATOM 178 C PHE A 436 -13.435 11.484 12.705 1.00 24.37 C
ATOM 179 O PHE A 436 -14.314 12.227 12.262 1.00 23.30 O
ATOM 180 CB PHE A 436 -13.833 9.520 14.241 1.00 23.46 C
ATOM 181 CG PHE A 436 -15.089 9.147 13.494 1.00 25.03 C
ATOM 182 CD1 PHE A 436 -15.023 8.688 12.180 1.00 26.60 C
ATOM 183 CD2 PHE A 436 -16.335 9.244 14.105 1.00 26.06 C
ATOM 184 CE1 PHE A 436 -16.177 8.345 11.485 1.00 27.29 C
ATOM 185 CE2 PHE A 436 -17.495 8.899 13.419 1.00 28.32 C
ATOM 186 CZ PHE A 436 -17.416 8.449 12.106 1.00 26.52 C
ATOM 187 N GLU A 437 -12.417 11.047 11.968 1.00 20.17 N
ATOM 188 CA GLU A 437 -12.296 11.368 10.546 1.00 21.09 C
ATOM 189 C GLU A 437 -11.887 10.149 9.721 1.00 26.22 C
ATOM 190 O GLU A 437 -11.249 9.226 10.232 1.00 24.86 O
ATOM 191 CB GLU A 437 -11.322 12.534 10.325 1.00 21.54 C
ATOM 192 CG GLU A 437 -9.926 12.324 10.904 1.00 27.90 C
ATOM 193 CD GLU A 437 -9.071 13.577 10.875 1.00 38.64 C
ATOM 194 OE1 GLU A 437 -9.627 14.697 10.875 1.00 31.77 O
ATOM 195 OE2 GLU A 437 -7.832 13.441 10.864 1.00 35.27 O
ATOM 196 N CYS A 438 -12.267 10.155 8.446 1.00 23.98 N
ATOM 197 CA CYS A 438 -11.948 9.062 7.534 1.00 24.60 C
ATOM 198 C CYS A 438 -10.968 9.492 6.451 1.00 28.08 C
ATOM 199 O CYS A 438 -11.185 10.493 5.779 1.00 28.38 O
ATOM 200 CB CYS A 438 -13.220 8.513 6.888 1.00 25.88 C
ATOM 201 SG CYS A 438 -14.296 7.615 8.013 1.00 30.48 S
ATOM 202 N GLN A 439 -9.887 8.729 6.318 1.00 23.96 N
ATOM 203 CA GLN A 439 -8.941 8.904 5.244 1.00 22.64 C
ATOM 204 C GLN A 439 -9.330 7.940 4.125 1.00 28.84 C
ATOM 205 O GLN A 439 -9.060 6.737 4.197 1.00 28.71 O
ATOM 206 CB GLN A 439 -7.512 8.649 5.726 1.00 24.52 C
ATOM 207 CG GLN A 439 -6.433 9.156 4.783 1.00 28.04 C
ATOM 208 CD GLN A 439 -5.038 8.981 5.346 1.00 41.22 C
ATOM 209 OE1 GLN A 439 -4.344 9.959 5.622 1.00 36.47 O
ATOM 210 NE2 GLN A 439 -4.621 7.732 5.529 1.00 30.52 N
ATOM 211 N CYS A 440 -9.981 8.481 3.099 1.00 26.06 N
ATOM 212 CA CYS A 440 -10.552 7.676 2.025 1.00 25.65 C
ATOM 213 C CYS A 440 -9.514 7.221 1.008 1.00 29.90 C
ATOM 214 O CYS A 440 -8.523 7.912 0.762 1.00 30.02 O
ATOM 215 CB CYS A 440 -11.667 8.447 1.314 1.00 27.35 C
ATOM 216 SG CYS A 440 -13.046 8.945 2.368 1.00 32.96 S
ATOM 217 N LEU A 441 -9.758 6.053 0.421 1.00 26.31 N
ATOM 218 CA LEU A 441 -8.929 5.538 -0.662 1.00 25.77 C
ATOM 219 C LEU A 441 -9.262 6.263 -1.963 1.00 28.47 C
ATOM 220 O LEU A 441 -10.310 6.904 -2.072 1.00 28.60 O
ATOM 221 CB LEU A 441 -9.126 4.026 -0.823 1.00 25.80 C
ATOM 222 CG LEU A 441 -8.722 3.108 0.338 1.00 29.86 C
ATOM 223 CD1 LEU A 441 -9.246 1.701 0.104 1.00 30.57 C
ATOM 224 CD2 LEU A 441 -7.212 3.089 0.547 1.00 32.53 C
ATOM 225 N GLN A 442 -8.365 6.161 -2.942 1.00 25.45 N
ATOM 226 CA GLN A 442 -8.524 6.845 -4.225 1.00 25.30 C
ATOM 227 C GLN A 442 -9.792 6.389 -4.948 1.00 28.75 C
ATOM 228 O GLN A 442 -9.945 5.208 -5.271 1.00 28.67 O
ATOM 229 CB GLN A 442 -7.285 6.629 -5.104 1.00 25.64 C
ATOM 230 CG GLN A 442 -7.152 7.600 -6.262 1.00 41.16 C
ATOM 231 CD GLN A 442 -6.489 8.921 -5.904 1.00 56.79 C
ATOM 232 OE1 GLN A 442 -6.793 9.522 -4.871 1.00 53.89 O
ATOM 233 NE2 GLN A 442 -5.582 9.385 -6.740 1.00 43.17 N
ATOM 234 N GLY A 443 -10.698 7.335 -5.178 1.00 23.56 N
ATOM 235 CA GLY A 443 -11.957 7.060 -5.865 1.00 23.25 C
ATOM 236 C GLY A 443 -13.180 7.105 -4.970 1.00 27.22 C
ATOM 237 O GLY A 443 -14.300 6.874 -5.429 1.00 26.70 O
ATOM 238 N TYR A 444 -12.964 7.400 -3.690 1.00 23.85 N
ATOM 239 CA TYR A 444 -14.052 7.505 -2.722 1.00 23.11 C
ATOM 240 C TYR A 444 -13.996 8.833 -1.971 1.00 28.13 C
ATOM 241 O TYR A 444 -12.916 9.312 -1.622 1.00 27.17 O
ATOM 242 CB TYR A 444 -14.019 6.330 -1.738 1.00 21.73 C
ATOM 243 CG TYR A 444 -14.096 4.968 -2.397 1.00 22.84 C
ATOM 244 CD1 TYR A 444 -15.300 4.487 -2.913 1.00 24.41 C
ATOM 245 CD2 TYR A 444 -12.965 4.159 -2.502 1.00 22.80 C
ATOM 246 CE1 TYR A 444 -15.375 3.237 -3.521 1.00 23.36 C
ATOM 247 CE2 TYR A 444 -13.030 2.906 -3.106 1.00 22.15 C
ATOM 248 CZ TYR A 444 -14.238 2.452 -3.612 1.00 27.52 C
ATOM 249 OH TYR A 444 -14.310 1.215 -4.211 1.00 27.49 O
ATOM 250 N THR A 445 -15.165 9.425 -1.737 1.00 26.32 N
ATOM 251 CA THR A 445 -15.260 10.695 -1.012 1.00 26.26 C
ATOM 252 C THR A 445 -16.420 10.717 -0.008 1.00 31.02 C
ATOM 253 O THR A 445 -17.237 9.794 0.032 1.00 30.67 O
ATOM 254 CB THR A 445 -15.329 11.913 -1.978 1.00 36.95 C
ATOM 255 OG1 THR A 445 -15.176 13.127 -1.232 1.00 38.45 O
ATOM 256 CG2 THR A 445 -16.650 11.950 -2.741 1.00 35.17 C
ATOM 257 N GLY A 446 -16.477 11.774 0.798 1.00 28.32 N
ATOM 258 CA GLY A 446 -17.464 11.889 1.868 1.00 27.58 C
ATOM 259 C GLY A 446 -16.825 11.691 3.233 1.00 31.56 C
ATOM 260 O GLY A 446 -15.740 11.111 3.328 1.00 31.15 O
ATOM 261 N PRO A 447 -17.493 12.167 4.303 1.00 28.99 N
ATOM 262 CA PRO A 447 -16.969 12.067 5.670 1.00 28.45 C
ATOM 263 C PRO A 447 -16.766 10.628 6.134 1.00 31.78 C
ATOM 264 O PRO A 447 -15.988 10.396 7.061 1.00 30.66 O
ATOM 265 CB PRO A 447 -18.047 12.763 6.495 1.00 29.30 C
ATOM 266 CG PRO A 447 -19.279 12.709 5.681 1.00 33.63 C
ATOM 267 CD PRO A 447 -18.803 12.843 4.274 1.00 29.96 C
ATOM 268 N ARG A 448 -17.461 9.682 5.521 1.00 27.41 N
ATOM 269 CA ARG A 448 -17.338 8.260 5.848 1.00 27.44 C
ATOM 270 C ARG A 448 -16.993 7.414 4.615 1.00 32.04 C
ATOM 271 O ARG A 448 -17.160 6.190 4.629 1.00 31.24 O
ATOM 272 CB ARG A 448 -18.624 7.747 6.489 1.00 28.30 C
ATOM 273 CG ARG A 448 -18.852 8.253 7.909 1.00 35.30 C
ATOM 274 CD ARG A 448 -20.235 7.878 8.435 1.00 40.41 C
ATOM 275 NE ARG A 448 -20.353 6.452 8.739 1.00 44.78 N
ATOM 276 CZ ARG A 448 -20.983 5.562 7.974 1.00 59.47 C
ATOM 277 NH1 ARG A 448 -21.027 4.289 8.345 1.00 46.59 N
ATOM 278 NH2 ARG A 448 -21.566 5.935 6.842 1.00 48.23 N
ATOM 279 N CYS A 449 -16.511 8.081 3.563 1.00 28.72 N
ATOM 280 CA CYS A 449 -16.112 7.450 2.291 1.00 27.94 C
ATOM 281 C CYS A 449 -17.245 6.679 1.603 1.00 32.49 C
ATOM 282 O CYS A 449 -17.006 5.650 0.964 1.00 32.12 O
ATOM 283 CB CYS A 449 -14.885 6.542 2.478 1.00 28.12 C
ATOM 284 SG CYS A 449 -13.511 7.261 3.402 1.00 30.01 S
ATOM 285 N GLU A 450 -18.470 7.186 1.726 1.00 29.42 N
ATOM 286 CA GLU A 450 -19.655 6.477 1.228 1.00 29.85 C
ATOM 287 C GLU A 450 -20.035 6.798 -0.225 1.00 32.57 C
ATOM 288 O GLU A 450 -20.965 6.187 -0.778 1.00 32.88 O
ATOM 289 CB GLU A 450 -20.859 6.669 2.170 1.00 29.95 C
ATOM 290 CG GLU A 450 -21.337 8.107 2.356 1.00 40.17 C
ATOM 291 CD GLU A 450 -20.616 8.832 3.477 1.00 53.74 C
ATOM 292 OE1 GLU A 450 -19.421 9.156 3.314 1.00 36.61 O
ATOM 293 OE2 GLU A 450 -21.254 9.091 4.520 1.00 50.02 O
ATOM 294 N ILE A 451 -19.326 7.747 -0.835 1.00 28.49 N
ATOM 295 CA ILE A 451 -19.565 8.109 -2.232 1.00 28.29 C
ATOM 296 C ILE A 451 -18.521 7.487 -3.154 1.00 31.02 C
ATOM 297 O ILE A 451 -17.324 7.747 -3.016 1.00 30.41 O
ATOM 298 CB ILE A 451 -19.573 9.646 -2.452 1.00 31.70 C
ATOM 299 CG1 ILE A 451 -20.674 10.316 -1.624 1.00 31.91 C
ATOM 300 CG2 ILE A 451 -19.729 9.983 -3.943 1.00 32.27 C
ATOM 301 CD1 ILE A 451 -20.694 11.828 -1.742 1.00 37.25 C
ATOM 302 N ASP A 452 -18.988 6.664 -4.089 1.00 27.08 N
ATOM 303 CA ASP A 452 -18.151 6.182 -5.178 1.00 25.51 C
ATOM 304 C ASP A 452 -18.153 7.245 -6.257 1.00 29.51 C
ATOM 305 O ASP A 452 -19.121 7.367 -7.015 1.00 29.08 O
ATOM 306 CB ASP A 452 -18.668 4.839 -5.706 1.00 27.19 C
ATOM 307 CG ASP A 452 -17.768 4.234 -6.762 1.00 35.72 C
ATOM 308 OD1 ASP A 452 -16.590 4.636 -6.876 1.00 37.49 O
ATOM 309 OD2 ASP A 452 -18.246 3.342 -7.494 1.00 42.04 O
ATOM 310 N VAL A 453 -17.070 8.019 -6.315 1.00 24.96 N
ATOM 311 CA VAL A 453 -16.939 9.144 -7.245 1.00 25.78 C
ATOM 312 C VAL A 453 -17.219 8.705 -8.681 1.00 31.04 C
ATOM 313 O VAL A 453 -16.609 7.757 -9.177 1.00 30.10 O
ATOM 314 CB VAL A 453 -15.531 9.797 -7.166 1.00 29.50 C
ATOM 315 CG1 VAL A 453 -15.451 11.032 -8.058 1.00 29.50 C
ATOM 316 CG2 VAL A 453 -15.180 10.162 -5.748 1.00 29.63 C
ATOM 317 N ASN A 454 -18.160 9.386 -9.331 1.00 29.32 N
ATOM 318 CA ASN A 454 -18.474 9.116 -10.728 1.00 28.80 C
ATOM 319 C ASN A 454 -17.541 9.911 -11.637 1.00 33.05 C
ATOM 320 O ASN A 454 -17.727 11.113 -11.836 1.00 32.80 O
ATOM 321 CB ASN A 454 -19.942 9.443 -11.029 1.00 30.16 C
ATOM 322 CG ASN A 454 -20.430 8.839 -12.341 1.00 51.16 C
ATOM 323 OD1 ASN A 454 -19.641 8.387 -13.172 1.00 43.33 O
ATOM 324 ND2 ASN A 454 -21.746 8.831 -12.529 1.00 43.18 N
ATOM 325 N GLU A 455 -16.533 9.229 -12.175 1.00 29.73 N
ATOM 326 CA GLU A 455 -15.562 9.856 -13.072 1.00 29.12 C
ATOM 327 C GLU A 455 -16.127 10.050 -14.481 1.00 33.19 C
ATOM 328 O GLU A 455 -15.460 10.605 -15.358 1.00 33.16 O
ATOM 329 CB GLU A 455 -14.258 9.050 -13.116 1.00 30.08 C
ATOM 330 CG GLU A 455 -13.371 9.198 -11.879 1.00 37.11 C
ATOM 331 CD GLU A 455 -13.740 8.246 -10.750 1.00 41.51 C
ATOM 332 OE1 GLU A 455 -14.534 7.308 -10.981 1.00 29.59 O
ATOM 333 OE2 GLU A 455 -13.225 8.431 -9.627 1.00 28.20 O
ATOM 334 N CYS A 456 -17.363 9.595 -14.681 1.00 30.22 N
ATOM 335 CA CYS A 456 -18.063 9.721 -15.957 1.00 30.26 C
ATOM 336 C CYS A 456 -19.178 10.768 -15.914 1.00 34.44 C
ATOM 337 O CYS A 456 -19.890 10.963 -16.895 1.00 34.08 O
ATOM 338 CB CYS A 456 -18.639 8.366 -16.366 1.00 29.99 C
ATOM 339 SG CYS A 456 -17.394 7.133 -16.758 1.00 32.62 S
ATOM 340 N VAL A 457 -19.315 11.441 -14.772 1.00 31.33 N
ATOM 341 CA VAL A 457 -20.406 12.397 -14.543 1.00 31.77 C
ATOM 342 C VAL A 457 -20.330 13.633 -15.454 1.00 35.33 C
ATOM 343 O VAL A 457 -21.358 14.224 -15.791 1.00 35.29 O
ATOM 344 CB VAL A 457 -20.507 12.799 -13.037 1.00 35.83 C
ATOM 345 CG1 VAL A 457 -19.429 13.812 -12.648 1.00 35.62 C
ATOM 346 CG2 VAL A 457 -21.899 13.327 -12.706 1.00 35.20 C
ATOM 347 N SER A 458 -19.116 14.001 -15.858 1.00 32.59 N
ATOM 348 CA SER A 458 -18.893 15.155 -16.721 1.00 31.63 C
ATOM 349 C SER A 458 -18.817 14.759 -18.190 1.00 34.46 C
ATOM 350 O SER A 458 -18.467 15.582 -19.042 1.00 34.40 O
ATOM 351 CB SER A 458 -17.619 15.894 -16.305 1.00 35.48 C
ATOM 352 OG SER A 458 -16.483 15.053 -16.424 1.00 47.43 O
ATOM 353 N ASN A 459 -19.157 13.502 -18.479 1.00 29.61 N
ATOM 354 CA ASN A 459 -19.091 12.927 -19.830 1.00 28.47 C
ATOM 355 C ASN A 459 -17.744 13.164 -20.527 1.00 30.26 C
ATOM 356 O ASN A 459 -17.668 13.938 -21.485 1.00 30.64 O
ATOM 357 CB ASN A 459 -20.261 13.418 -20.700 1.00 26.92 C
ATOM 358 CG ASN A 459 -21.620 13.064 -20.114 1.00 39.21 C
ATOM 359 OD1 ASN A 459 -22.510 13.923 -19.989 1.00 35.01 O
ATOM 360 ND2 ASN A 459 -21.816 11.797 -19.754 1.00 25.02 N
ATOM 361 N PRO A 460 -16.676 12.497 -20.045 1.00 27.13 N
ATOM 362 CA PRO A 460 -15.340 12.758 -20.582 1.00 26.06 C
ATOM 363 C PRO A 460 -15.072 12.062 -21.917 1.00 28.75 C
ATOM 364 O PRO A 460 -14.193 12.492 -22.667 1.00 28.33 O
ATOM 365 CB PRO A 460 -14.412 12.218 -19.491 1.00 27.14 C
ATOM 366 CG PRO A 460 -15.198 11.166 -18.800 1.00 32.09 C
ATOM 367 CD PRO A 460 -16.659 11.467 -18.988 1.00 28.12 C
ATOM 368 N CYS A 461 -15.827 11.004 -22.204 1.00 24.30 N
ATOM 369 CA CYS A 461 -15.672 10.248 -23.442 1.00 24.00 C
ATOM 370 C CYS A 461 -16.448 10.904 -24.579 1.00 28.59 C
ATOM 371 O CYS A 461 -17.653 11.144 -24.470 1.00 27.99 O
ATOM 372 CB CYS A 461 -16.118 8.799 -23.248 1.00 23.48 C
ATOM 373 SG CYS A 461 -15.293 7.949 -21.888 1.00 25.30 S
ATOM 374 N GLN A 462 -15.740 11.187 -25.667 1.00 24.83 N
ATOM 375 CA GLN A 462 -16.290 11.932 -26.794 1.00 24.03 C
ATOM 376 C GLN A 462 -16.681 11.022 -27.948 1.00 30.01 C
ATOM 377 O GLN A 462 -16.227 9.879 -28.029 1.00 29.67 O
ATOM 378 CB GLN A 462 -15.281 12.980 -27.265 1.00 25.88 C
ATOM 379 CG GLN A 462 -14.923 14.034 -26.229 1.00 37.34 C
ATOM 380 CD GLN A 462 -13.967 15.091 -26.756 1.00 53.35 C
ATOM 381 OE1 GLN A 462 -13.520 15.031 -27.894 1.00 45.70 O
ATOM 382 NE2 GLN A 462 -13.650 16.069 -25.914 1.00 49.14 N
ATOM 383 N ASN A 463 -17.525 11.548 -28.827 1.00 27.86 N
ATOM 384 CA ASN A 463 -17.941 10.868 -30.062 1.00 27.78 C
ATOM 385 C ASN A 463 -18.656 9.536 -29.830 1.00 32.06 C
ATOM 386 O ASN A 463 -18.233 8.492 -30.336 1.00 31.91 O
ATOM 387 CB ASN A 463 -16.755 10.708 -31.029 1.00 25.81 C
ATOM 388 CG ASN A 463 -16.059 12.025 -31.325 1.00 38.00 C
ATOM 389 OD1 ASN A 463 -16.693 12.998 -31.731 1.00 30.53 O
ATOM 390 ND2 ASN A 463 -14.747 12.060 -31.125 1.00 26.52 N
ATOM 391 N ASP A 464 -19.740 9.593 -29.056 1.00 30.32 N
ATOM 392 CA ASP A 464 -20.584 8.430 -28.735 1.00 30.40 C
ATOM 393 C ASP A 464 -19.845 7.260 -28.078 1.00 35.26 C
ATOM 394 O ASP A 464 -20.312 6.119 -28.119 1.00 34.81 O
ATOM 395 CB ASP A 464 -21.366 7.955 -29.973 1.00 32.20 C
ATOM 396 CG ASP A 464 -22.438 8.941 -30.408 1.00 42.35 C
ATOM 397 OD1 ASP A 464 -23.153 9.501 -29.535 1.00 42.87 O
ATOM 398 OD2 ASP A 464 -22.594 9.146 -31.630 1.00 48.05 O
ATOM 399 N ALA A 465 -18.704 7.551 -27.460 1.00 31.67 N
ATOM 400 CA ALA A 465 -17.936 6.541 -26.743 1.00 30.75 C
ATOM 401 C ALA A 465 -18.599 6.201 -25.410 1.00 34.64 C
ATOM 402 O ALA A 465 -19.323 7.022 -24.839 1.00 34.24 O
ATOM 403 CB ALA A 465 -16.512 7.014 -26.524 1.00 31.69 C
ATOM 404 N THR A 466 -18.349 4.987 -24.925 1.00 31.01 N
ATOM 405 CA THR A 466 -18.913 4.520 -23.661 1.00 30.06 C
ATOM 406 C THR A 466 -17.937 4.778 -22.514 1.00 33.08 C
ATOM 407 O THR A 466 -16.744 4.483 -22.624 1.00 32.36 O
ATOM 408 CB THR A 466 -19.270 3.017 -23.720 1.00 35.87 C
ATOM 409 OG1 THR A 466 -19.856 2.709 -24.992 1.00 34.41 O
ATOM 410 CG2 THR A 466 -20.252 2.649 -22.613 1.00 34.75 C
ATOM 411 N CYS A 467 -18.453 5.333 -21.420 1.00 29.61 N
ATOM 412 CA CYS A 467 -17.639 5.642 -20.249 1.00 28.81 C
ATOM 413 C CYS A 467 -17.815 4.597 -19.153 1.00 32.50 C
ATOM 414 O CYS A 467 -18.940 4.239 -18.795 1.00 31.42 O
ATOM 415 CB CYS A 467 -17.978 7.034 -19.709 1.00 29.81 C
ATOM 416 SG CYS A 467 -16.739 7.707 -18.579 1.00 33.26 S
ATOM 417 N LEU A 468 -16.693 4.117 -18.624 1.00 28.82 N
ATOM 418 CA LEU A 468 -16.697 3.113 -17.566 1.00 27.82 C
ATOM 419 C LEU A 468 -16.371 3.748 -16.226 1.00 31.01 C
ATOM 420 O LEU A 468 -15.256 4.226 -16.010 1.00 31.47 O
ATOM 421 CB LEU A 468 -15.705 1.986 -17.882 1.00 28.23 C
ATOM 422 CG LEU A 468 -15.896 1.164 -19.163 1.00 32.86 C
ATOM 423 CD1 LEU A 468 -14.628 0.393 -19.491 1.00 32.48 C
ATOM 424 CD2 LEU A 468 -17.092 0.220 -19.060 1.00 35.14 C
ATOM 425 N ASP A 469 -17.359 3.759 -15.342 1.00 27.58 N
ATOM 426 CA ASP A 469 -17.197 4.310 -14.000 1.00 25.81 C
ATOM 427 C ASP A 469 -16.435 3.317 -13.124 1.00 29.38 C
ATOM 428 O ASP A 469 -17.004 2.348 -12.615 1.00 29.70 O
ATOM 429 CB ASP A 469 -18.564 4.650 -13.392 1.00 28.10 C
ATOM 430 CG ASP A 469 -18.460 5.493 -12.127 1.00 36.37 C
ATOM 431 OD1 ASP A 469 -17.368 6.025 -11.829 1.00 35.50 O
ATOM 432 OD2 ASP A 469 -19.485 5.629 -11.425 1.00 40.49 O
ATOM 433 N GLN A 470 -15.139 3.572 -12.963 1.00 25.68 N
ATOM 434 CA GLN A 470 -14.240 2.677 -12.238 1.00 24.07 C
ATOM 435 C GLN A 470 -13.773 3.293 -10.919 1.00 28.16 C
ATOM 436 O GLN A 470 -14.097 4.443 -10.617 1.00 26.85 O
ATOM 437 CB GLN A 470 -13.041 2.315 -13.119 1.00 24.81 C
ATOM 438 CG GLN A 470 -13.411 1.541 -14.379 1.00 28.47 C
ATOM 439 CD GLN A 470 -12.322 1.555 -15.435 1.00 36.78 C
ATOM 440 OE1 GLN A 470 -11.190 1.968 -15.183 1.00 30.73 O
ATOM 441 NE2 GLN A 470 -12.662 1.095 -16.622 1.00 23.50 N
ATOM 442 N ILE A 471 -13.022 2.520 -10.135 1.00 23.72 N
ATOM 443 CA ILE A 471 -12.513 2.981 -8.843 1.00 23.30 C
ATOM 444 C ILE A 471 -11.315 3.914 -9.035 1.00 26.51 C
ATOM 445 O ILE A 471 -10.203 3.469 -9.331 1.00 25.81 O
ATOM 446 CB ILE A 471 -12.142 1.797 -7.909 1.00 26.54 C
ATOM 447 CG1 ILE A 471 -13.328 0.836 -7.759 1.00 26.50 C
ATOM 448 CG2 ILE A 471 -11.688 2.311 -6.540 1.00 26.02 C
ATOM 449 CD1 ILE A 471 -12.941 -0.578 -7.354 1.00 31.07 C
ATOM 450 N GLY A 472 -11.564 5.212 -8.878 1.00 23.50 N
ATOM 451 CA GLY A 472 -10.519 6.230 -8.978 1.00 23.86 C
ATOM 452 C GLY A 472 -10.133 6.630 -10.389 1.00 26.94 C
ATOM 453 O GLY A 472 -9.179 7.387 -10.580 1.00 26.80 O
ATOM 454 N GLU A 473 -10.875 6.126 -11.375 1.00 23.98 N
ATOM 455 CA GLU A 473 -10.582 6.385 -12.787 1.00 24.04 C
ATOM 456 C GLU A 473 -11.788 6.179 -13.704 1.00 25.90 C
ATOM 457 O GLU A 473 -12.822 5.656 -13.284 1.00 24.62 O
ATOM 458 CB GLU A 473 -9.409 5.517 -13.268 1.00 24.56 C
ATOM 459 CG GLU A 473 -9.616 4.013 -13.107 1.00 37.42 C
ATOM 460 CD GLU A 473 -8.523 3.182 -13.760 1.00 62.18 C
ATOM 461 OE1 GLU A 473 -7.720 3.738 -14.541 1.00 52.31 O
ATOM 462 OE2 GLU A 473 -8.473 1.962 -13.493 1.00 59.54 O
ATOM 463 N PHE A 474 -11.637 6.607 -14.955 1.00 21.97 N
ATOM 464 CA PHE A 474 -12.593 6.305 -16.009 1.00 21.04 C
ATOM 465 C PHE A 474 -11.849 5.753 -17.209 1.00 24.64 C
ATOM 466 O PHE A 474 -10.662 6.030 -17.395 1.00 23.32 O
ATOM 467 CB PHE A 474 -13.409 7.549 -16.392 1.00 21.44 C
ATOM 468 CG PHE A 474 -12.626 8.588 -17.147 1.00 23.34 C
ATOM 469 CD1 PHE A 474 -11.921 9.582 -16.485 1.00 26.50 C
ATOM 470 CD2 PHE A 474 -12.603 8.578 -18.540 1.00 24.89 C
ATOM 471 CE1 PHE A 474 -11.197 10.544 -17.178 1.00 26.43 C
ATOM 472 CE2 PHE A 474 -11.882 9.533 -19.250 1.00 27.18 C
ATOM 473 CZ PHE A 474 -11.179 10.519 -18.567 1.00 25.24 C
ATOM 474 N GLN A 475 -12.546 4.967 -18.023 1.00 21.52 N
ATOM 475 CA GLN A 475 -11.992 4.477 -19.281 1.00 20.69 C
ATOM 476 C GLN A 475 -13.008 4.601 -20.405 1.00 25.30 C
ATOM 477 O GLN A 475 -14.193 4.317 -20.220 1.00 25.97 O
ATOM 478 CB GLN A 475 -11.503 3.033 -19.150 1.00 22.55 C
ATOM 479 CG GLN A 475 -10.109 2.906 -18.545 1.00 34.46 C
ATOM 480 CD GLN A 475 -9.671 1.466 -18.346 1.00 48.37 C
ATOM 481 OE1 GLN A 475 -10.492 0.575 -18.132 1.00 41.02 O
ATOM 482 NE2 GLN A 475 -8.365 1.235 -18.406 1.00 42.59 N
ATOM 483 N CYS A 476 -12.531 5.032 -21.568 1.00 22.66 N
ATOM 484 CA CYS A 476 -13.386 5.224 -22.730 1.00 23.32 C
ATOM 485 C CYS A 476 -13.233 4.079 -23.727 1.00 27.28 C
ATOM 486 O CYS A 476 -12.119 3.738 -24.131 1.00 26.11 O
ATOM 487 CB CYS A 476 -13.077 6.561 -23.409 1.00 23.62 C
ATOM 488 SG CYS A 476 -13.324 8.023 -22.370 1.00 27.11 S
ATOM 489 N ILE A 477 -14.361 3.481 -24.100 1.00 23.37 N
ATOM 490 CA ILE A 477 -14.398 2.495 -25.174 1.00 23.26 C
ATOM 491 C ILE A 477 -14.846 3.231 -26.431 1.00 26.93 C
ATOM 492 O ILE A 477 -16.011 3.622 -26.553 1.00 27.27 O
ATOM 493 CB ILE A 477 -15.358 1.313 -24.870 1.00 27.77 C
ATOM 494 CG1 ILE A 477 -15.238 0.866 -23.407 1.00 28.08 C
ATOM 495 CG2 ILE A 477 -15.084 0.145 -25.823 1.00 25.77 C
ATOM 496 CD1 ILE A 477 -16.463 0.138 -22.874 1.00 34.04 C
ATOM 497 N CYS A 478 -13.908 3.429 -27.346 1.00 23.99 N
ATOM 498 CA CYS A 478 -14.147 4.250 -28.521 1.00 25.43 C
ATOM 499 C CYS A 478 -15.034 3.573 -29.559 1.00 31.96 C
ATOM 500 O CYS A 478 -14.953 2.361 -29.770 1.00 32.67 O
ATOM 501 CB CYS A 478 -12.823 4.666 -29.170 1.00 24.62 C
ATOM 502 SG CYS A 478 -11.698 5.620 -28.131 1.00 27.22 S
ATOM 503 N MET A 479 -15.883 4.377 -30.193 1.00 29.92 N
ATOM 504 CA MET A 479 -16.666 3.949 -31.343 1.00 31.05 C
ATOM 505 C MET A 479 -15.718 3.876 -32.543 1.00 35.50 C
ATOM 506 O MET A 479 -14.893 4.775 -32.723 1.00 36.11 O
ATOM 507 CB MET A 479 -17.793 4.954 -31.606 1.00 34.06 C
ATOM 508 CG MET A 479 -18.982 4.395 -32.375 1.00 38.92 C
ATOM 509 SD MET A 479 -19.927 3.174 -31.437 1.00 43.01 S
ATOM 510 CE MET A 479 -21.080 4.227 -30.565 1.00 41.15 C
ATOM 511 N PRO A 480 -15.816 2.798 -33.353 1.00 32.03 N
ATOM 512 CA PRO A 480 -14.909 2.562 -34.484 1.00 31.02 C
ATOM 513 C PRO A 480 -14.575 3.821 -35.287 1.00 33.31 C
ATOM 514 O PRO A 480 -15.475 4.576 -35.668 1.00 33.05 O
ATOM 515 CB PRO A 480 -15.688 1.571 -35.347 1.00 32.59 C
ATOM 516 CG PRO A 480 -16.472 0.783 -34.368 1.00 37.36 C
ATOM 517 CD PRO A 480 -16.812 1.715 -33.230 1.00 33.40 C
ATOM 518 N GLY A 481 -13.283 4.038 -35.523 1.00 27.75 N
ATOM 519 CA GLY A 481 -12.806 5.209 -36.254 1.00 27.17 C
ATOM 520 C GLY A 481 -12.235 6.296 -35.363 1.00 29.67 C
ATOM 521 O GLY A 481 -11.647 7.264 -35.853 1.00 28.79 O
ATOM 522 N TYR A 482 -12.410 6.135 -34.053 1.00 25.17 N
ATOM 523 CA TYR A 482 -11.932 7.109 -33.075 1.00 25.19 C
ATOM 524 C TYR A 482 -10.914 6.501 -32.114 1.00 29.61 C