HEADER SIGNALING PROTEIN 08-OCT-08 3ETO
TITLE 2 ANGSTROM XRAY STRUCTURE OF THE NOTCH1 NEGATIVE REGULATORY REGION
TITLE 2 (NRR)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUROGENIC LOCUS NOTCH HOMOLOG PROTEIN 1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: NOTCH1 NEGATIVE REGULATORY REGION, RESIDUES 1447-1734;
COMPND 5 SYNONYM: NOTCH 1, HN1, TRANSLOCATION-ASSOCIATED NOTCH PROTEIN TAN-1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_TAXID: 9606;
SOURCE 4 GENE: NOTCH1, TAN1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 ROSETTA PLYSS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: HIS6-NOTCH1 NRR-LOOPOUT;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: NOVAGEN PET15B
KEYWDS ALPHA-BETA SANDWICH, HD DOMAIN, LNR REPEAT, CALCIUM-BINDING, SEA
KEYWDS 2 DOMAIN, AUTOINHIBITION, ACTIVATOR, T-ALL, LEUKEMIA, ONCOGENE, ANK
KEYWDS 3 REPEAT, DEVELOPMENTAL PROTEIN, DIFFERENTIATION, EGF-LIKE DOMAIN,
KEYWDS 4 GLYCOPROTEIN, MEMBRANE, METAL-BINDING, NOTCH SIGNALING PATHWAY,
KEYWDS 5 NUCLEUS, PHOSPHOPROTEIN, RECEPTOR, TRANSCRIPTION, TRANSCRIPTION
KEYWDS 6 REGULATION, TRANSMEMBRANE, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR W.R.GORDON,S.C.BLACKLOW
REVDAT 4 06-SEP-23 3ETO 1 REMARK SEQADV
REVDAT 3 13-JUL-11 3ETO 1 VERSN
REVDAT 2 19-MAY-09 3ETO 1 JRNL
REVDAT 1 23-DEC-08 3ETO 0
JRNL AUTH W.R.GORDON,M.ROY,D.VARDAR-ULU,M.GARFINKEL,M.R.MANSOUR,
JRNL AUTH 2 J.C.ASTER,S.C.BLACKLOW
JRNL TITL STRUCTURE OF THE NOTCH1-NEGATIVE REGULATORY REGION:
JRNL TITL 2 IMPLICATIONS FOR NORMAL ACTIVATION AND PATHOGENIC SIGNALING
JRNL TITL 3 IN T-ALL.
JRNL REF BLOOD V. 113 4381 2009
JRNL REFN ISSN 0006-4971
JRNL PMID 19075186
JRNL DOI 10.1182/BLOOD-2008-08-174748
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.4.0066
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.7
REMARK 3 NUMBER OF REFLECTIONS : 52098
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.213
REMARK 3 R VALUE (WORKING SET) : 0.211
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2761
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2340
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 57.56
REMARK 3 BIN R VALUE (WORKING SET) : 0.2490
REMARK 3 BIN FREE R VALUE SET COUNT : 118
REMARK 3 BIN FREE R VALUE : 0.2500
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3563
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 50
REMARK 3 SOLVENT ATOMS : 271
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 33.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.64
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.82000
REMARK 3 B22 (A**2) : 0.40000
REMARK 3 B33 (A**2) : 1.10000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.49000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.143
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.143
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.096
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.336
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.944
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.917
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3700 ; 0.015 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4974 ; 1.471 ; 1.930
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 460 ; 6.057 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 194 ;35.783 ;25.258
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 553 ;14.600 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;20.280 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 516 ; 0.103 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2898 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2300 ; 0.983 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3654 ; 1.803 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1400 ; 2.576 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1320 ; 3.932 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1569 A 1720 4
REMARK 3 1 B 1569 B 1720 4
REMARK 3 2 A 1470 A 1568 5
REMARK 3 2 B 1470 B 1568 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 1219 ; 0.22 ; 0.50
REMARK 3 LOOSE POSITIONAL 1 A (A): 373 ; 0.37 ; 5.00
REMARK 3 MEDIUM THERMAL 1 B (A**2): 1219 ; 1.86 ; 2.00
REMARK 3 LOOSE THERMAL 1 B (A**2): 373 ; 2.07 ; 10.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3ETO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-OCT-08.
REMARK 100 THE DEPOSITION ID IS D_1000049753.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-JUN-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54862
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.6
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 60.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.20200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2OO4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM ACETATE PH 4.0, 1.0-1.5M
REMARK 280 NACL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 84.96350
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.87950
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 84.96350
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 45.87950
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
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: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 GLY A 1446
REMARK 465 GLU A 1447
REMARK 465 GLU A 1448
REMARK 465 GLU A 1728
REMARK 465 PRO A 1729
REMARK 465 PRO A 1730
REMARK 465 PRO A 1731
REMARK 465 PRO A 1732
REMARK 465 ALA A 1733
REMARK 465 GLN A 1734
REMARK 465 GLY B 1446
REMARK 465 GLU B 1447
REMARK 465 GLU B 1448
REMARK 465 GLU B 1728
REMARK 465 PRO B 1729
REMARK 465 PRO B 1730
REMARK 465 PRO B 1731
REMARK 465 PRO B 1732
REMARK 465 ALA B 1733
REMARK 465 GLN B 1734
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A1451 CG CD OE1 OE2
REMARK 470 LYS A1462 CG CD CE NZ
REMARK 470 GLN A1614 CG CD OE1 NE2
REMARK 470 GLU B1451 CG CD OE1 OE2
REMARK 470 LEU B1452 CG CD1 CD2
REMARK 470 GLU B1454 CG CD OE1 OE2
REMARK 470 VAL B1727 CG1 CG2
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 B 1622 N MET B 1670 1.71
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 A1569 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG A1569 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 GLY A1622 CA - C - N ANGL. DEV. = 24.9 DEGREES
REMARK 500 GLY A1622 O - C - N ANGL. DEV. = -29.7 DEGREES
REMARK 500 GLY B1622 CA - C - N ANGL. DEV. = 23.7 DEGREES
REMARK 500 GLY B1622 O - C - N ANGL. DEV. = -37.5 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 GLU A1451 43.95 -87.26
REMARK 500 ASP A1486 74.36 55.19
REMARK 500 ASN A1530 118.19 -34.57
REMARK 500 ASP A1610 -169.20 -79.54
REMARK 500 GLN A1692 58.54 -90.44
REMARK 500 PRO A1716 34.35 -80.61
REMARK 500 GLU B1451 -81.83 -54.66
REMARK 500 GLU B1454 -2.66 -59.17
REMARK 500 ASP B1486 76.81 53.62
REMARK 500 PHE B1517 27.09 49.51
REMARK 500 ASN B1530 115.66 -30.58
REMARK 500 LEU B1560 -1.77 79.02
REMARK 500 PRO B1716 32.80 -79.92
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 GLY A1622 25.47
REMARK 500 GLY B1622 37.22
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A2003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B2003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1735
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1736
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1737
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1735
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1736
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1737
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THIS CONSTRUCT CONTAINS AN N-TERMINAL HIS6 TAG,
REMARK 999 FOLLOWED BY A TEV PROTEASE CLEAVAGE SITE.
REMARK 999 TEV CLEAVAGE RESULTS IN A NON-NATIVE GLY AT THE
REMARK 999 N-TERMINUS. THE CONSTRUCT ENCODES GLU1447 TO GLN1734
REMARK 999 AND HAS BEEN ENGINEERED TO REMOVE THE UNSTRUCTURED
REMARK 999 LOOP CONTAINING THE FURIN CLEAVAGE SITE.
REMARK 999 RESIDUES 1623-1669 WERE REMOVED.
DBREF 3ETO A 1447 1734 UNP P46531 NOTC1_HUMAN 1447 1734
DBREF 3ETO B 1447 1734 UNP P46531 NOTC1_HUMAN 1447 1734
SEQADV 3ETO GLY A 1446 UNP P46531 EXPRESSION TAG
SEQADV 3ETO A UNP P46531 ARG 1623 DELETION
SEQADV 3ETO A UNP P46531 GLU 1624 DELETION
SEQADV 3ETO A UNP P46531 GLU 1625 DELETION
SEQADV 3ETO A UNP P46531 GLU 1626 DELETION
SEQADV 3ETO A UNP P46531 LEU 1627 DELETION
SEQADV 3ETO A UNP P46531 ARG 1628 DELETION
SEQADV 3ETO A UNP P46531 LYS 1629 DELETION
SEQADV 3ETO A UNP P46531 HIS 1630 DELETION
SEQADV 3ETO A UNP P46531 PRO 1631 DELETION
SEQADV 3ETO A UNP P46531 ILE 1632 DELETION
SEQADV 3ETO A UNP P46531 LYS 1633 DELETION
SEQADV 3ETO A UNP P46531 ARG 1634 DELETION
SEQADV 3ETO A UNP P46531 ALA 1635 DELETION
SEQADV 3ETO A UNP P46531 ALA 1636 DELETION
SEQADV 3ETO A UNP P46531 GLU 1637 DELETION
SEQADV 3ETO A UNP P46531 GLY 1638 DELETION
SEQADV 3ETO A UNP P46531 TRP 1639 DELETION
SEQADV 3ETO A UNP P46531 ALA 1640 DELETION
SEQADV 3ETO A UNP P46531 ALA 1641 DELETION
SEQADV 3ETO A UNP P46531 PRO 1642 DELETION
SEQADV 3ETO A UNP P46531 ASP 1643 DELETION
SEQADV 3ETO A UNP P46531 ALA 1644 DELETION
SEQADV 3ETO A UNP P46531 LEU 1645 DELETION
SEQADV 3ETO A UNP P46531 LEU 1646 DELETION
SEQADV 3ETO A UNP P46531 GLY 1647 DELETION
SEQADV 3ETO A UNP P46531 GLN 1648 DELETION
SEQADV 3ETO A UNP P46531 VAL 1649 DELETION
SEQADV 3ETO A UNP P46531 LYS 1650 DELETION
SEQADV 3ETO A UNP P46531 ALA 1651 DELETION
SEQADV 3ETO A UNP P46531 SER 1652 DELETION
SEQADV 3ETO A UNP P46531 LEU 1653 DELETION
SEQADV 3ETO A UNP P46531 LEU 1654 DELETION
SEQADV 3ETO A UNP P46531 PRO 1655 DELETION
SEQADV 3ETO A UNP P46531 GLY 1656 DELETION
SEQADV 3ETO A UNP P46531 GLY 1657 DELETION
SEQADV 3ETO A UNP P46531 SER 1658 DELETION
SEQADV 3ETO A UNP P46531 GLU 1659 DELETION
SEQADV 3ETO A UNP P46531 GLY 1660 DELETION
SEQADV 3ETO A UNP P46531 GLY 1661 DELETION
SEQADV 3ETO A UNP P46531 ARG 1662 DELETION
SEQADV 3ETO A UNP P46531 ARG 1663 DELETION
SEQADV 3ETO A UNP P46531 ARG 1664 DELETION
SEQADV 3ETO A UNP P46531 ARG 1665 DELETION
SEQADV 3ETO A UNP P46531 GLU 1666 DELETION
SEQADV 3ETO A UNP P46531 LEU 1667 DELETION
SEQADV 3ETO A UNP P46531 ASP 1668 DELETION
SEQADV 3ETO A UNP P46531 PRO 1669 DELETION
SEQADV 3ETO GLY B 1446 UNP P46531 EXPRESSION TAG
SEQADV 3ETO B UNP P46531 ARG 1623 DELETION
SEQADV 3ETO B UNP P46531 GLU 1624 DELETION
SEQADV 3ETO B UNP P46531 GLU 1625 DELETION
SEQADV 3ETO B UNP P46531 GLU 1626 DELETION
SEQADV 3ETO B UNP P46531 LEU 1627 DELETION
SEQADV 3ETO B UNP P46531 ARG 1628 DELETION
SEQADV 3ETO B UNP P46531 LYS 1629 DELETION
SEQADV 3ETO B UNP P46531 HIS 1630 DELETION
SEQADV 3ETO B UNP P46531 PRO 1631 DELETION
SEQADV 3ETO B UNP P46531 ILE 1632 DELETION
SEQADV 3ETO B UNP P46531 LYS 1633 DELETION
SEQADV 3ETO B UNP P46531 ARG 1634 DELETION
SEQADV 3ETO B UNP P46531 ALA 1635 DELETION
SEQADV 3ETO B UNP P46531 ALA 1636 DELETION
SEQADV 3ETO B UNP P46531 GLU 1637 DELETION
SEQADV 3ETO B UNP P46531 GLY 1638 DELETION
SEQADV 3ETO B UNP P46531 TRP 1639 DELETION
SEQADV 3ETO B UNP P46531 ALA 1640 DELETION
SEQADV 3ETO B UNP P46531 ALA 1641 DELETION
SEQADV 3ETO B UNP P46531 PRO 1642 DELETION
SEQADV 3ETO B UNP P46531 ASP 1643 DELETION
SEQADV 3ETO B UNP P46531 ALA 1644 DELETION
SEQADV 3ETO B UNP P46531 LEU 1645 DELETION
SEQADV 3ETO B UNP P46531 LEU 1646 DELETION
SEQADV 3ETO B UNP P46531 GLY 1647 DELETION
SEQADV 3ETO B UNP P46531 GLN 1648 DELETION
SEQADV 3ETO B UNP P46531 VAL 1649 DELETION
SEQADV 3ETO B UNP P46531 LYS 1650 DELETION
SEQADV 3ETO B UNP P46531 ALA 1651 DELETION
SEQADV 3ETO B UNP P46531 SER 1652 DELETION
SEQADV 3ETO B UNP P46531 LEU 1653 DELETION
SEQADV 3ETO B UNP P46531 LEU 1654 DELETION
SEQADV 3ETO B UNP P46531 PRO 1655 DELETION
SEQADV 3ETO B UNP P46531 GLY 1656 DELETION
SEQADV 3ETO B UNP P46531 GLY 1657 DELETION
SEQADV 3ETO B UNP P46531 SER 1658 DELETION
SEQADV 3ETO B UNP P46531 GLU 1659 DELETION
SEQADV 3ETO B UNP P46531 GLY 1660 DELETION
SEQADV 3ETO B UNP P46531 GLY 1661 DELETION
SEQADV 3ETO B UNP P46531 ARG 1662 DELETION
SEQADV 3ETO B UNP P46531 ARG 1663 DELETION
SEQADV 3ETO B UNP P46531 ARG 1664 DELETION
SEQADV 3ETO B UNP P46531 ARG 1665 DELETION
SEQADV 3ETO B UNP P46531 GLU 1666 DELETION
SEQADV 3ETO B UNP P46531 LEU 1667 DELETION
SEQADV 3ETO B UNP P46531 ASP 1668 DELETION
SEQADV 3ETO B UNP P46531 PRO 1669 DELETION
SEQRES 1 A 242 GLY GLU GLU ALA CYS GLU LEU PRO GLU CYS GLN GLU ASP
SEQRES 2 A 242 ALA GLY ASN LYS VAL CYS SER LEU GLN CYS ASN ASN HIS
SEQRES 3 A 242 ALA CYS GLY TRP ASP GLY GLY ASP CYS SER LEU ASN PHE
SEQRES 4 A 242 ASN ASP PRO TRP LYS ASN CYS THR GLN SER LEU GLN CYS
SEQRES 5 A 242 TRP LYS TYR PHE SER ASP GLY HIS CYS ASP SER GLN CYS
SEQRES 6 A 242 ASN SER ALA GLY CYS LEU PHE ASP GLY PHE ASP CYS GLN
SEQRES 7 A 242 ARG ALA GLU GLY GLN CYS ASN PRO LEU TYR ASP GLN TYR
SEQRES 8 A 242 CYS LYS ASP HIS PHE SER ASP GLY HIS CYS ASP GLN GLY
SEQRES 9 A 242 CYS ASN SER ALA GLU CYS GLU TRP ASP GLY LEU ASP CYS
SEQRES 10 A 242 ALA GLU HIS VAL PRO GLU ARG LEU ALA ALA GLY THR LEU
SEQRES 11 A 242 VAL VAL VAL VAL LEU MET PRO PRO GLU GLN LEU ARG ASN
SEQRES 12 A 242 SER SER PHE HIS PHE LEU ARG GLU LEU SER ARG VAL LEU
SEQRES 13 A 242 HIS THR ASN VAL VAL PHE LYS ARG ASP ALA HIS GLY GLN
SEQRES 14 A 242 GLN MET ILE PHE PRO TYR TYR GLY MET ASP VAL ARG GLY
SEQRES 15 A 242 SER ILE VAL TYR LEU GLU ILE ASP ASN ARG GLN CYS VAL
SEQRES 16 A 242 GLN ALA SER SER GLN CYS PHE GLN SER ALA THR ASP VAL
SEQRES 17 A 242 ALA ALA PHE LEU GLY ALA LEU ALA SER LEU GLY SER LEU
SEQRES 18 A 242 ASN ILE PRO TYR LYS ILE GLU ALA VAL GLN SER GLU THR
SEQRES 19 A 242 VAL GLU PRO PRO PRO PRO ALA GLN
SEQRES 1 B 242 GLY GLU GLU ALA CYS GLU LEU PRO GLU CYS GLN GLU ASP
SEQRES 2 B 242 ALA GLY ASN LYS VAL CYS SER LEU GLN CYS ASN ASN HIS
SEQRES 3 B 242 ALA CYS GLY TRP ASP GLY GLY ASP CYS SER LEU ASN PHE
SEQRES 4 B 242 ASN ASP PRO TRP LYS ASN CYS THR GLN SER LEU GLN CYS
SEQRES 5 B 242 TRP LYS TYR PHE SER ASP GLY HIS CYS ASP SER GLN CYS
SEQRES 6 B 242 ASN SER ALA GLY CYS LEU PHE ASP GLY PHE ASP CYS GLN
SEQRES 7 B 242 ARG ALA GLU GLY GLN CYS ASN PRO LEU TYR ASP GLN TYR
SEQRES 8 B 242 CYS LYS ASP HIS PHE SER ASP GLY HIS CYS ASP GLN GLY
SEQRES 9 B 242 CYS ASN SER ALA GLU CYS GLU TRP ASP GLY LEU ASP CYS
SEQRES 10 B 242 ALA GLU HIS VAL PRO GLU ARG LEU ALA ALA GLY THR LEU
SEQRES 11 B 242 VAL VAL VAL VAL LEU MET PRO PRO GLU GLN LEU ARG ASN
SEQRES 12 B 242 SER SER PHE HIS PHE LEU ARG GLU LEU SER ARG VAL LEU
SEQRES 13 B 242 HIS THR ASN VAL VAL PHE LYS ARG ASP ALA HIS GLY GLN
SEQRES 14 B 242 GLN MET ILE PHE PRO TYR TYR GLY MET ASP VAL ARG GLY
SEQRES 15 B 242 SER ILE VAL TYR LEU GLU ILE ASP ASN ARG GLN CYS VAL
SEQRES 16 B 242 GLN ALA SER SER GLN CYS PHE GLN SER ALA THR ASP VAL
SEQRES 17 B 242 ALA ALA PHE LEU GLY ALA LEU ALA SER LEU GLY SER LEU
SEQRES 18 B 242 ASN ILE PRO TYR LYS ILE GLU ALA VAL GLN SER GLU THR
SEQRES 19 B 242 VAL GLU PRO PRO PRO PRO ALA GLN
HET CA A2001 1
HET CA A2002 1
HET CA A2003 1
HET CL A 2 1
HET GOL A 1 6
HET GOL A1735 6
HET GOL A1736 6
HET GOL A1737 6
HET CA B2001 1
HET CA B2002 1
HET CA B2003 1
HET CL B 1 1
HET GOL B1735 6
HET GOL B1736 6
HET GOL B1737 6
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 CA 6(CA 2+)
FORMUL 6 CL 2(CL 1-)
FORMUL 7 GOL 7(C3 H8 O3)
FORMUL 18 HOH *271(H2 O)
HELIX 1 1 LEU A 1452 ALA A 1459 1 8
HELIX 2 2 SER A 1465 ASN A 1469 5 5
HELIX 3 3 ASN A 1470 ALA A 1472 5 3
HELIX 4 4 CYS A 1473 GLY A 1478 1 6
HELIX 5 5 THR A 1492 TYR A 1500 5 9
HELIX 6 6 ASP A 1507 ASN A 1511 5 5
HELIX 7 7 SER A 1512 ASP A 1521 5 10
HELIX 8 8 TYR A 1533 PHE A 1541 1 9
HELIX 9 9 ASP A 1547 ASN A 1551 5 5
HELIX 10 10 SER A 1552 ASP A 1561 5 10
HELIX 11 11 PRO A 1582 SER A 1589 1 8
HELIX 12 12 SER A 1589 HIS A 1602 1 14
HELIX 13 13 GLN A 1685 SER A 1690 1 6
HELIX 14 14 SER A 1696 LEU A 1710 1 15
HELIX 15 15 LEU B 1452 ALA B 1459 1 8
HELIX 16 16 SER B 1465 ASN B 1469 5 5
HELIX 17 17 ASN B 1470 ALA B 1472 5 3
HELIX 18 18 CYS B 1473 GLY B 1478 1 6
HELIX 19 19 THR B 1492 TYR B 1500 5 9
HELIX 20 20 ASP B 1507 ASN B 1511 5 5
HELIX 21 21 SER B 1512 ASP B 1521 5 10
HELIX 22 22 TYR B 1533 HIS B 1540 1 8
HELIX 23 23 ASP B 1547 ASN B 1551 5 5
HELIX 24 24 CYS B 1555 ASP B 1561 5 7
HELIX 25 25 PRO B 1582 ASN B 1588 1 7
HELIX 26 26 SER B 1589 HIS B 1602 1 14
HELIX 27 27 GLN B 1685 SER B 1690 1 6
HELIX 28 28 SER B 1696 LEU B 1710 1 15
SHEET 1 A 3 ASN A1604 PHE A1607 0
SHEET 2 A 3 ARG A1673 ASP A1682 -1 O ASP A1682 N ASN A1604
SHEET 3 A 3 ILE A1617 TYR A1621 -1 N TYR A1620 O GLY A1674
SHEET 1 B 4 ASN A1604 PHE A1607 0
SHEET 2 B 4 ARG A1673 ASP A1682 -1 O ASP A1682 N ASN A1604
SHEET 3 B 4 THR A1574 VAL A1579 -1 N VAL A1579 O SER A1675
SHEET 4 B 4 ILE A1719 GLU A1725 -1 O GLN A1723 N VAL A1576
SHEET 1 C 3 ASN B1604 PHE B1607 0
SHEET 2 C 3 ARG B1673 ASP B1682 -1 O ASP B1682 N ASN B1604
SHEET 3 C 3 ILE B1617 TYR B1621 -1 N TYR B1620 O GLY B1674
SHEET 1 D 4 ASN B1604 PHE B1607 0
SHEET 2 D 4 ARG B1673 ASP B1682 -1 O ASP B1682 N ASN B1604
SHEET 3 D 4 THR B1574 VAL B1579 -1 N LEU B1575 O LEU B1679
SHEET 4 D 4 ILE B1719 GLU B1725 -1 O GLU B1720 N VAL B1578
SSBOND 1 CYS A 1450 CYS A 1473 1555 1555 2.04
SSBOND 2 CYS A 1455 CYS A 1468 1555 1555 2.03
SSBOND 3 CYS A 1464 CYS A 1480 1555 1555 2.04
SSBOND 4 CYS A 1491 CYS A 1515 1555 1555 2.05
SSBOND 5 CYS A 1497 CYS A 1510 1555 1555 2.02
SSBOND 6 CYS A 1506 CYS A 1522 1555 1555 2.08
SSBOND 7 CYS A 1529 CYS A 1555 1555 1555 2.05
SSBOND 8 CYS A 1537 CYS A 1550 1555 1555 2.05
SSBOND 9 CYS A 1546 CYS A 1562 1555 1555 2.09
SSBOND 10 CYS A 1686 CYS A 1693 1555 1555 2.05
SSBOND 11 CYS B 1450 CYS B 1473 1555 1555 2.04
SSBOND 12 CYS B 1455 CYS B 1468 1555 1555 2.06
SSBOND 13 CYS B 1464 CYS B 1480 1555 1555 2.05
SSBOND 14 CYS B 1491 CYS B 1515 1555 1555 2.07
SSBOND 15 CYS B 1497 CYS B 1510 1555 1555 2.03
SSBOND 16 CYS B 1506 CYS B 1522 1555 1555 2.06
SSBOND 17 CYS B 1529 CYS B 1555 1555 1555 2.04
SSBOND 18 CYS B 1537 CYS B 1550 1555 1555 2.06
SSBOND 19 CYS B 1546 CYS B 1562 1555 1555 2.11
SSBOND 20 CYS B 1686 CYS B 1693 1555 1555 2.03
CISPEP 1 ALA A 1449 CYS A 1450 0 4.69
CISPEP 2 TYR A 1621 GLY A 1622 0 22.37
CISPEP 3 ALA B 1449 CYS B 1450 0 7.08
CISPEP 4 TYR B 1621 GLY B 1622 0 26.63
SITE 1 AC1 5 ASP A1458 ASN A1461 VAL A1463 ASP A1476
SITE 2 AC1 5 ASP A1479
SITE 1 AC2 6 TYR A1500 ASP A1503 HIS A1505 ASP A1507
SITE 2 AC2 6 ASP A1518 ASP A1521
SITE 1 AC3 6 HIS A1540 ASP A1543 HIS A1545 ASP A1547
SITE 2 AC3 6 ASP A1558 ASP A1561
SITE 1 AC4 4 HIS A1471 TRP A1475 ASP A1486 TRP A1488
SITE 1 AC5 5 ASP B1458 ASN B1461 VAL B1463 ASP B1476
SITE 2 AC5 5 ASP B1479
SITE 1 AC6 6 TYR B1500 ASP B1503 HIS B1505 ASP B1507
SITE 2 AC6 6 ASP B1518 ASP B1521
SITE 1 AC7 3 SER A1542 GLY A1559 ASP A1561
SITE 1 AC8 6 HIS B1540 ASP B1543 HIS B1545 ASP B1547
SITE 2 AC8 6 ASP B1558 ASP B1561
SITE 1 AC9 3 ARG A1609 MET A1616 GOL A1737
SITE 1 BC1 2 ILE A1715 PRO A1716
SITE 1 BC2 3 HOH A 212 VAL A1727 GOL A1735
SITE 1 BC3 5 HIS B1471 TRP B1475 ASP B1486 PRO B1487
SITE 2 BC3 5 TRP B1488
SITE 1 BC4 5 HOH B 123 SER B1542 GLY B1559 LEU B1560
SITE 2 BC4 5 ASP B1561
SITE 1 BC5 2 ILE B1715 PRO B1716
SITE 1 BC6 3 HOH B 202 MET B1616 VAL B1727
CRYST1 169.927 91.759 59.844 90.00 109.38 90.00 C 1 2 1 8
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 0.005885 0.000000 0.002070 0.00000
SCALE2 0.000000 0.010898 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017714 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
