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HEADER HYDROLASE 20-AUG-03 1Q83
TITLE CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-TZ2PA6
TITLE 2 SYN COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ACHE;
COMPND 5 EC: 3.1.1.7;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 GENE: ACHE;
SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: HEK 293;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: LAMBDA CLONING VECTOR;
SOURCE 9 OTHER_DETAILS: LAMBDA-ZAP, LAMBDA-FIX CDNA
KEYWDS HYDROLASE, SERINE ESTERASE, ACETYLCHOLINESTERASE,
KEYWDS 2 BIFUNCTIONAL INHIBITOR
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.BOURNE,Z.RADIC,H.C.KOLB,K.B.SHARPLESS,P.TAYLOR,P.MARCHOT
REVDAT 1 10-FEB-04 1Q83 0
JRNL AUTH Y.BOURNE,Z.RADIC,H.C.KOLB,K.B.SHARPLESS,P.TAYLOR,
JRNL AUTH 2 P.MARCHOT
JRNL TITL FREEZE-FRAME INHIBITORS CAPTURE
JRNL TITL 2 ACETYLCHOLINESTERASE IN A UNIQUE GATING
JRNL TITL 3 CONFORMATION
JRNL REF PROC.NAT.ACAD.SCI.USA V. 101 1449 2004
JRNL REFN ASTM PNASA6 US ISSN 0027-8424
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 58332
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) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1202
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 2.65
REMARK 3 BIN RESOLUTION RANGE LOW : 2.72
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4204
REMARK 3 BIN R VALUE (WORKING SET) : 0.2740
REMARK 3 BIN FREE R VALUE SET COUNT : 89
REMARK 3 BIN FREE R VALUE : 0.3530
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 8768
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 61.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.49
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.34000
REMARK 3 B22 (A**2) : 2.97000
REMARK 3 B33 (A**2) : -6.31000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.299
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.229
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.168
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.258
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.935
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8775 ; 0.015 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 7858 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11997 ; 1.530 ; 1.972
REMARK 3 BOND ANGLES OTHERS (DEGREES): 18148 ; 1.070 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1063 ; 6.461 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1279 ; 0.085 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9830 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1899 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1833 ; 0.202 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 8990 ; 0.233 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 5094 ; 0.087 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 253 ; 0.182 ; 0.200
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): 15 ; 0.187 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 53 ; 0.345 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 9 ; 0.232 ; 0.200
REMARK 3 SYMMETRY H-BOND 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): 5328 ; 0.633 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8584 ; 1.241 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3447 ; 1.881 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3413 ; 3.331 ; 4.500
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 : 7
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 16 A 56 3
REMARK 3 1 B 16 B 56 3
REMARK 3 2 A 60 A 74 3
REMARK 3 2 B 60 B 74 3
REMARK 3 3 A 80 A 256 3
REMARK 3 3 B 80 B 256 3
REMARK 3 4 A 265 A 336 3
REMARK 3 4 B 265 B 336 3
REMARK 3 5 A 343 A 382 3
REMARK 3 5 B 343 B 382 3
REMARK 3 6 A 392 A 490 3
REMARK 3 6 B 392 B 490 3
REMARK 3 7 A 508 A 539 3
REMARK 3 7 B 508 B 539 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 2779 ; 0.04 ; 0.05
REMARK 3 LOOSE POSITIONAL 1 A (A): 4409 ; 0.39 ; 5.00
REMARK 3 TIGHT THERMAL 1 A (A**2): 2779 ; 1.31 ; 5.00
REMARK 3 LOOSE THERMAL 1 A (A**2): 4409 ; 1.95 ; 20.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 541
REMARK 3 ORIGIN FOR THE GROUP (A): 27.6795 12.4018 16.8917
REMARK 3 T TENSOR
REMARK 3 T11: 0.0541 T22: 0.0126
REMARK 3 T33: 0.0957 T12: 0.0132
REMARK 3 T13: 0.0117 T23: 0.0324
REMARK 3 L TENSOR
REMARK 3 L11: 0.8033 L22: 0.7245
REMARK 3 L33: 1.6962 L12: 0.0364
REMARK 3 L13: -0.0204 L23: -0.2488
REMARK 3 S TENSOR
REMARK 3 S11: -0.0490 S12: -0.0450 S13: -0.0540
REMARK 3 S21: -0.0267 S22: 0.0101 S23: 0.0419
REMARK 3 S31: 0.1664 S32: -0.1231 S33: 0.0388
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 4 B 540
REMARK 3 ORIGIN FOR THE GROUP (A): 7.8248 4.4608 -40.2036
REMARK 3 T TENSOR
REMARK 3 T11: 0.0645 T22: 0.0737
REMARK 3 T33: 0.1188 T12: -0.0304
REMARK 3 T13: -0.0192 T23: -0.0693
REMARK 3 L TENSOR
REMARK 3 L11: 0.6977 L22: 1.0247
REMARK 3 L33: 2.1183 L12: -0.1624
REMARK 3 L13: 0.1377 L23: 0.3909
REMARK 3 S TENSOR
REMARK 3 S11: 0.1096 S12: 0.0951 S13: -0.0617
REMARK 3 S21: 0.1079 S22: -0.0984 S23: 0.1037
REMARK 3 S31: 0.1463 S32: 0.0019 S33: -0.0111
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 : 1.40
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
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 1Q83 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-AUG-2003.
REMARK 100 THE RCSB ID CODE IS RCSB020034.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUL-2002
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.75
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.933
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 : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59650
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.650
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06500
REMARK 200 FOR THE DATA SET : 8.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: 1J06
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25-32% PEG 600, 20 MM HEPES, PH
REMARK 280 6.75, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-Z
REMARK 290 4555 1/2+X,1/2-Y,-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 39.87150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 113.28850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.97700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 113.28850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.87150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.97700
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 MET A -30
REMARK 465 ARG A -29
REMARK 465 PRO A -28
REMARK 465 PRO A -27
REMARK 465 TRP A -26
REMARK 465 TYR A -25
REMARK 465 PRO A -24
REMARK 465 LEU A -23
REMARK 465 HIS A -22
REMARK 465 THR A -21
REMARK 465 PRO A -20
REMARK 465 SER A -19
REMARK 465 LEU A -18
REMARK 465 ALA A -17
REMARK 465 PHE A -16
REMARK 465 PRO A -15
REMARK 465 LEU A -14
REMARK 465 LEU A -13
REMARK 465 PHE A -12
REMARK 465 LEU A -11
REMARK 465 LEU A -10
REMARK 465 LEU A -9
REMARK 465 SER A -8
REMARK 465 LEU A -7
REMARK 465 LEU A -6
REMARK 465 GLY A -5
REMARK 465 GLY A -4
REMARK 465 GLY A -3
REMARK 465 ALA A -2
REMARK 465 ARG A -1
REMARK 465 ALA A 0
REMARK 465 PRO A 259
REMARK 465 GLY A 260
REMARK 465 GLY A 261
REMARK 465 ALA A 262
REMARK 465 GLY A 263
REMARK 465 ALA A 542
REMARK 465 THR A 543
REMARK 465 ASP A 544
REMARK 465 THR A 545
REMARK 465 LEU A 546
REMARK 465 ASP A 547
REMARK 465 GLU A 548
REMARK 465 ALA A 549
REMARK 465 MET B -30
REMARK 465 ARG B -29
REMARK 465 PRO B -28
REMARK 465 PRO B -27
REMARK 465 TRP B -26
REMARK 465 TYR B -25
REMARK 465 PRO B -24
REMARK 465 LEU B -23
REMARK 465 HIS B -22
REMARK 465 THR B -21
REMARK 465 PRO B -20
REMARK 465 SER B -19
REMARK 465 LEU B -18
REMARK 465 ALA B -17
REMARK 465 PHE B -16
REMARK 465 PRO B -15
REMARK 465 LEU B -14
REMARK 465 LEU B -13
REMARK 465 PHE B -12
REMARK 465 LEU B -11
REMARK 465 LEU B -10
REMARK 465 LEU B -9
REMARK 465 SER B -8
REMARK 465 LEU B -7
REMARK 465 LEU B -6
REMARK 465 GLY B -5
REMARK 465 GLY B -4
REMARK 465 GLY B -3
REMARK 465 ALA B -2
REMARK 465 ARG B -1
REMARK 465 ALA B 0
REMARK 465 GLU B 1
REMARK 465 GLY B 2
REMARK 465 ARG B 3
REMARK 465 PRO B 259
REMARK 465 GLY B 260
REMARK 465 GLY B 261
REMARK 465 ALA B 262
REMARK 465 GLY B 263
REMARK 465 GLY B 264
REMARK 465 SER B 541
REMARK 465 ALA B 542
REMARK 465 THR B 543
REMARK 465 ASP B 544
REMARK 465 THR B 545
REMARK 465 LEU B 546
REMARK 465 ASP B 547
REMARK 465 GLU B 548
REMARK 465 ALA B 549
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 SER A 495 OG
REMARK 470 LYS A 496 CG CD CE NZ
REMARK 470 ARG B 493 CG CD NE CZ NH1 NH2
REMARK 470 SER B 495 OG
REMARK 470 LYS B 496 CG CD CE NZ
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
REMARK 500 O HOH 641 O HOH 666 1.95
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),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 MET A 195 SD MET A 195 CE 0.185
REMARK 500 MET A 211 CG MET A 211 SD -0.101
REMARK 500 PRO A 258 CB PRO A 258 CG 0.199
REMARK 500 PRO A 258 CG PRO A 258 CD 0.132
REMARK 500 MET A 443 SD MET A 443 CE -0.110
REMARK 500 MET B 195 SD MET B 195 CE 0.156
REMARK 500 MET B 211 CG MET B 211 SD -0.102
REMARK 500 PRO B 258 CB PRO B 258 CG 0.132
REMARK 500 MET B 443 SD MET B 443 CE -0.140
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A 161 CA - CB - CG ANGL. DEV. =-12.5 DEGREES
REMARK 500 TYR A 341 CB - CA - C ANGL. DEV. = 9.5 DEGREES
REMARK 500 GLY A 342 N - CA - C ANGL. DEV. = 9.9 DEGREES
REMARK 500 GLY A 422 N - CA - C ANGL. DEV. = 9.4 DEGREES
REMARK 500 VAL B 145 N - CA - C ANGL. DEV. = -9.9 DEGREES
REMARK 500 GLY B 342 N - CA - C ANGL. DEV. = 13.0 DEGREES
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 M RES CSSEQI PSI PHI
REMARK 500 SER B 497 -131.45 27.51
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LYS B 496 SER B 497 149.96
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH 765 DISTANCE = 5.45 ANGSTROMS
REMARK 525 HOH 792 DISTANCE = 13.57 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1J06 RELATED DB: PDB
REMARK 900 RELATED ID: 1J07 RELATED DB: PDB
REMARK 900 RELATED ID: 1N5M RELATED DB: PDB
REMARK 900 RELATED ID: 1N5R RELATED DB: PDB
DBREF 1Q83 A -30 549 SWS P21836 ACES_MOUSE 1 580
DBREF 1Q83 B -30 549 SWS P21836 ACES_MOUSE 1 580
SEQRES 1 A 580 MET ARG PRO PRO TRP TYR PRO LEU HIS THR PRO SER LEU
SEQRES 2 A 580 ALA PHE PRO LEU LEU PHE LEU LEU LEU SER LEU LEU GLY
SEQRES 3 A 580 GLY GLY ALA ARG ALA GLU GLY ARG GLU ASP PRO GLN LEU
SEQRES 4 A 580 LEU VAL ARG VAL ARG GLY GLY GLN LEU ARG GLY ILE ARG
SEQRES 5 A 580 LEU LYS ALA PRO GLY GLY PRO VAL SER ALA PHE LEU GLY
SEQRES 6 A 580 ILE PRO PHE ALA GLU PRO PRO VAL GLY SER ARG ARG PHE
SEQRES 7 A 580 MET PRO PRO GLU PRO LYS ARG PRO TRP SER GLY VAL LEU
SEQRES 8 A 580 ASP ALA THR THR PHE GLN ASN VAL CYS TYR GLN TYR VAL
SEQRES 9 A 580 ASP THR LEU TYR PRO GLY PHE GLU GLY THR GLU MET TRP
SEQRES 10 A 580 ASN PRO ASN ARG GLU LEU SER GLU ASP CYS LEU TYR LEU
SEQRES 11 A 580 ASN VAL TRP THR PRO TYR PRO ARG PRO ALA SER PRO THR
SEQRES 12 A 580 PRO VAL LEU ILE TRP ILE TYR GLY GLY GLY PHE TYR SER
SEQRES 13 A 580 GLY ALA ALA SER LEU ASP VAL TYR ASP GLY ARG PHE LEU
SEQRES 14 A 580 ALA GLN VAL GLU GLY ALA VAL LEU VAL SER MET ASN TYR
SEQRES 15 A 580 ARG VAL GLY THR PHE GLY PHE LEU ALA LEU PRO GLY SER
SEQRES 16 A 580 ARG GLU ALA PRO GLY ASN VAL GLY LEU LEU ASP GLN ARG
SEQRES 17 A 580 LEU ALA LEU GLN TRP VAL GLN GLU ASN ILE ALA ALA PHE
SEQRES 18 A 580 GLY GLY ASP PRO MET SER VAL THR LEU PHE GLY GLU SER
SEQRES 19 A 580 ALA GLY ALA ALA SER VAL GLY MET HIS ILE LEU SER LEU
SEQRES 20 A 580 PRO SER ARG SER LEU PHE HIS ARG ALA VAL LEU GLN SER
SEQRES 21 A 580 GLY THR PRO ASN GLY PRO TRP ALA THR VAL SER ALA GLY
SEQRES 22 A 580 GLU ALA ARG ARG ARG ALA THR LEU LEU ALA ARG LEU VAL
SEQRES 23 A 580 GLY CYS PRO PRO GLY GLY ALA GLY GLY ASN ASP THR GLU
SEQRES 24 A 580 LEU ILE ALA CYS LEU ARG THR ARG PRO ALA GLN ASP LEU
SEQRES 25 A 580 VAL ASP HIS GLU TRP HIS VAL LEU PRO GLN GLU SER ILE
SEQRES 26 A 580 PHE ARG PHE SER PHE VAL PRO VAL VAL ASP GLY ASP PHE
SEQRES 27 A 580 LEU SER ASP THR PRO GLU ALA LEU ILE ASN THR GLY ASP
SEQRES 28 A 580 PHE GLN ASP LEU GLN VAL LEU VAL GLY VAL VAL LYS ASP
SEQRES 29 A 580 GLU GLY SER TYR PHE LEU VAL TYR GLY VAL PRO GLY PHE
SEQRES 30 A 580 SER LYS ASP ASN GLU SER LEU ILE SER ARG ALA GLN PHE
SEQRES 31 A 580 LEU ALA GLY VAL ARG ILE GLY VAL PRO GLN ALA SER ASP
SEQRES 32 A 580 LEU ALA ALA GLU ALA VAL VAL LEU HIS TYR THR ASP TRP
SEQRES 33 A 580 LEU HIS PRO GLU ASP PRO THR HIS LEU ARG ASP ALA MET
SEQRES 34 A 580 SER ALA VAL VAL GLY ASP HIS ASN VAL VAL CYS PRO VAL
SEQRES 35 A 580 ALA GLN LEU ALA GLY ARG LEU ALA ALA GLN GLY ALA ARG
SEQRES 36 A 580 VAL TYR ALA TYR ILE PHE GLU HIS ARG ALA SER THR LEU
SEQRES 37 A 580 THR TRP PRO LEU TRP MET GLY VAL PRO HIS GLY TYR GLU
SEQRES 38 A 580 ILE GLU PHE ILE PHE GLY LEU PRO LEU ASP PRO SER LEU
SEQRES 39 A 580 ASN TYR THR THR GLU GLU ARG ILE PHE ALA GLN ARG LEU
SEQRES 40 A 580 MET LYS TYR TRP THR ASN PHE ALA ARG THR GLY ASP PRO
SEQRES 41 A 580 ASN ASP PRO ARG ASP SER LYS SER PRO GLN TRP PRO PRO
SEQRES 42 A 580 TYR THR THR ALA ALA GLN GLN TYR VAL SER LEU ASN LEU
SEQRES 43 A 580 LYS PRO LEU GLU VAL ARG ARG GLY LEU ARG ALA GLN THR
SEQRES 44 A 580 CYS ALA PHE TRP ASN ARG PHE LEU PRO LYS LEU LEU SER
SEQRES 45 A 580 ALA THR ASP THR LEU ASP GLU ALA
SEQRES 1 B 580 MET ARG PRO PRO TRP TYR PRO LEU HIS THR PRO SER LEU
SEQRES 2 B 580 ALA PHE PRO LEU LEU PHE LEU LEU LEU SER LEU LEU GLY
SEQRES 3 B 580 GLY GLY ALA ARG ALA GLU GLY ARG GLU ASP PRO GLN LEU
SEQRES 4 B 580 LEU VAL ARG VAL ARG GLY GLY GLN LEU ARG GLY ILE ARG
SEQRES 5 B 580 LEU LYS ALA PRO GLY GLY PRO VAL SER ALA PHE LEU GLY
SEQRES 6 B 580 ILE PRO PHE ALA GLU PRO PRO VAL GLY SER ARG ARG PHE
SEQRES 7 B 580 MET PRO PRO GLU PRO LYS ARG PRO TRP SER GLY VAL LEU
SEQRES 8 B 580 ASP ALA THR THR PHE GLN ASN VAL CYS TYR GLN TYR VAL
SEQRES 9 B 580 ASP THR LEU TYR PRO GLY PHE GLU GLY THR GLU MET TRP
SEQRES 10 B 580 ASN PRO ASN ARG GLU LEU SER GLU ASP CYS LEU TYR LEU
SEQRES 11 B 580 ASN VAL TRP THR PRO TYR PRO ARG PRO ALA SER PRO THR
SEQRES 12 B 580 PRO VAL LEU ILE TRP ILE TYR GLY GLY GLY PHE TYR SER
SEQRES 13 B 580 GLY ALA ALA SER LEU ASP VAL TYR ASP GLY ARG PHE LEU
SEQRES 14 B 580 ALA GLN VAL GLU GLY ALA VAL LEU VAL SER MET ASN TYR
SEQRES 15 B 580 ARG VAL GLY THR PHE GLY PHE LEU ALA LEU PRO GLY SER
SEQRES 16 B 580 ARG GLU ALA PRO GLY ASN VAL GLY LEU LEU ASP GLN ARG
SEQRES 17 B 580 LEU ALA LEU GLN TRP VAL GLN GLU ASN ILE ALA ALA PHE
SEQRES 18 B 580 GLY GLY ASP PRO MET SER VAL THR LEU PHE GLY GLU SER
SEQRES 19 B 580 ALA GLY ALA ALA SER VAL GLY MET HIS ILE LEU SER LEU
SEQRES 20 B 580 PRO SER ARG SER LEU PHE HIS ARG ALA VAL LEU GLN SER
SEQRES 21 B 580 GLY THR PRO ASN GLY PRO TRP ALA THR VAL SER ALA GLY
SEQRES 22 B 580 GLU ALA ARG ARG ARG ALA THR LEU LEU ALA ARG LEU VAL
SEQRES 23 B 580 GLY CYS PRO PRO GLY GLY ALA GLY GLY ASN ASP THR GLU
SEQRES 24 B 580 LEU ILE ALA CYS LEU ARG THR ARG PRO ALA GLN ASP LEU
SEQRES 25 B 580 VAL ASP HIS GLU TRP HIS VAL LEU PRO GLN GLU SER ILE
SEQRES 26 B 580 PHE ARG PHE SER PHE VAL PRO VAL VAL ASP GLY ASP PHE
SEQRES 27 B 580 LEU SER ASP THR PRO GLU ALA LEU ILE ASN THR GLY ASP
SEQRES 28 B 580 PHE GLN ASP LEU GLN VAL LEU VAL GLY VAL VAL LYS ASP
SEQRES 29 B 580 GLU GLY SER TYR PHE LEU VAL TYR GLY VAL PRO GLY PHE
SEQRES 30 B 580 SER LYS ASP ASN GLU SER LEU ILE SER ARG ALA GLN PHE
SEQRES 31 B 580 LEU ALA GLY VAL ARG ILE GLY VAL PRO GLN ALA SER ASP
SEQRES 32 B 580 LEU ALA ALA GLU ALA VAL VAL LEU HIS TYR THR ASP TRP
SEQRES 33 B 580 LEU HIS PRO GLU ASP PRO THR HIS LEU ARG ASP ALA MET
SEQRES 34 B 580 SER ALA VAL VAL GLY ASP HIS ASN VAL VAL CYS PRO VAL
SEQRES 35 B 580 ALA GLN LEU ALA GLY ARG LEU ALA ALA GLN GLY ALA ARG
SEQRES 36 B 580 VAL TYR ALA TYR ILE PHE GLU HIS ARG ALA SER THR LEU
SEQRES 37 B 580 THR TRP PRO LEU TRP MET GLY VAL PRO HIS GLY TYR GLU
SEQRES 38 B 580 ILE GLU PHE ILE PHE GLY LEU PRO LEU ASP PRO SER LEU
SEQRES 39 B 580 ASN TYR THR THR GLU GLU ARG ILE PHE ALA GLN ARG LEU
SEQRES 40 B 580 MET LYS TYR TRP THR ASN PHE ALA ARG THR GLY ASP PRO
SEQRES 41 B 580 ASN ASP PRO ARG ASP SER LYS SER PRO GLN TRP PRO PRO
SEQRES 42 B 580 TYR THR THR ALA ALA GLN GLN TYR VAL SER LEU ASN LEU
SEQRES 43 B 580 LYS PRO LEU GLU VAL ARG ARG GLY LEU ARG ALA GLN THR
SEQRES 44 B 580 CYS ALA PHE TRP ASN ARG PHE LEU PRO LYS LEU LEU SER
SEQRES 45 B 580 ALA THR ASP THR LEU ASP GLU ALA
MODRES 1Q83 ASN A 350 ASN GLYCOSYLATION SITE
MODRES 1Q83 ASN A 464 ASN GLYCOSYLATION SITE
MODRES 1Q83 ASN B 350 ASN GLYCOSYLATION SITE
HET NAG C1501 14
HET FUL C1502 10
HET NAG B1601 14
HET NAG A1701 14
HET P6G 1901 19
HET TZ5 1951 50
HET TZ5 1952 50
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM FUL BETA-L-FUCOSE
HETNAM P6G HEXAETHYLENE GLYCOL
HETNAM TZ5 3,8-DIAMINO-6-PHENYL-5-[6-[1-[2-[(1,2,3,4-TETRAHYDRO-
HETNAM 2 TZ5 9-ACRIDINYL)AMINO]ETHYL]-1H-1,2,3-TRIAZOL-5-YL]HEXYL]-
HETNAM 3 TZ5 PHENANTHRIDINIUM
HETSYN NAG NAG
HETSYN FUL 6-DEOXY-BETA-L-GALACTOSE
HETSYN P6G POLYETHYLENE GLYCOL PEG400
FORMUL 3 NAG 3(C8 H15 N1 O6)
FORMUL 3 FUL C6 H12 O5
FORMUL 6 P6G C12 H26 O7
FORMUL 7 TZ5 2(C42 H45 N8 1+)
FORMUL 9 HOH *273(H2 O1)
HELIX 1 1 ASP A 5 GLN A 7 5 3
HELIX 2 2 VAL A 42 ARG A 46 5 5
HELIX 3 3 PHE A 80 MET A 85 1 6
HELIX 4 4 LEU A 130 ASP A 134 5 5
HELIX 5 5 GLY A 135 GLY A 143 1 9
HELIX 6 6 VAL A 153 LEU A 159 1 7
HELIX 7 7 ASN A 170 ILE A 187 1 18
HELIX 8 8 ALA A 188 PHE A 190 5 3
HELIX 9 9 SER A 203 LEU A 214 1 12
HELIX 10 10 SER A 215 SER A 220 1 6
HELIX 11 11 ALA A 241 VAL A 255 1 15
HELIX 12 12 ASN A 265 THR A 275 1 11
HELIX 13 13 PRO A 277 GLU A 285 1 9
HELIX 14 14 TRP A 286 LEU A 289 5 4
HELIX 15 15 THR A 311 GLY A 319 1 9
HELIX 16 16 TYR A 337 VAL A 343 1 7
HELIX 17 17 SER A 355 VAL A 367 1 13
HELIX 18 18 SER A 371 THR A 383 1 13
HELIX 19 19 ASP A 390 VAL A 407 1 18
HELIX 20 20 VAL A 407 GLN A 421 1 15
HELIX 21 21 PRO A 440 GLY A 444 5 5
HELIX 22 22 GLU A 450 PHE A 455 1 6
HELIX 23 23 GLY A 456 ASN A 464 5 9
HELIX 24 24 THR A 466 GLY A 487 1 22
HELIX 25 25 ARG A 525 PHE A 535 1 11
HELIX 26 26 LEU A 536 LEU A 539 5 4
HELIX 27 27 ASP B 5 GLN B 7 5 3
HELIX 28 28 VAL B 42 ARG B 46 5 5
HELIX 29 29 PHE B 80 MET B 85 1 6
HELIX 30 30 LEU B 130 ASP B 134 5 5
HELIX 31 31 GLY B 135 GLY B 143 1 9
HELIX 32 32 VAL B 153 LEU B 159 1 7
HELIX 33 33 ASN B 170 ILE B 187 1 18
HELIX 34 34 ALA B 188 PHE B 190 5 3
HELIX 35 35 SER B 203 LEU B 214 1 12
HELIX 36 36 SER B 215 SER B 220 1 6
HELIX 37 37 ALA B 241 VAL B 255 1 15
HELIX 38 38 ASN B 265 ARG B 274 1 10
HELIX 39 39 PRO B 277 GLU B 285 1 9
HELIX 40 40 TRP B 286 LEU B 289 5 4
HELIX 41 41 THR B 311 GLY B 319 1 9
HELIX 42 42 GLY B 335 TYR B 337 5 3
HELIX 43 43 PHE B 338 VAL B 343 1 6
HELIX 44 44 SER B 355 VAL B 367 1 13
HELIX 45 45 SER B 371 THR B 383 1 13
HELIX 46 46 ASP B 390 VAL B 407 1 18
HELIX 47 47 VAL B 407 GLN B 421 1 15
HELIX 48 48 PRO B 440 GLY B 444 5 5
HELIX 49 49 GLU B 450 PHE B 455 1 6
HELIX 50 50 GLY B 456 ASN B 464 5 9
HELIX 51 51 THR B 466 GLY B 487 1 22
HELIX 52 52 ARG B 525 ARG B 534 1 10
HELIX 53 53 PHE B 535 LEU B 539 5 5
SHEET 1 A 3 LEU A 9 VAL A 12 0
SHEET 2 A 3 GLY A 15 ARG A 18 -1 O LEU A 17 N VAL A 10
SHEET 3 A 3 VAL A 59 ASP A 61 1 O LEU A 60 N GLN A 16
SHEET 1 B11 ILE A 20 ALA A 24 0
SHEET 2 B11 GLY A 27 PRO A 36 -1 O VAL A 29 N LEU A 22
SHEET 3 B11 TYR A 98 PRO A 104 -1 O VAL A 101 N PHE A 32
SHEET 4 B11 VAL A 145 MET A 149 -1 O SER A 148 N ASN A 100
SHEET 5 B11 THR A 112 ILE A 118 1 N LEU A 115 O VAL A 147
SHEET 6 B11 GLY A 192 GLU A 202 1 O ASP A 193 N THR A 112
SHEET 7 B11 ARG A 224 GLN A 228 1 O ARG A 224 N LEU A 199
SHEET 8 B11 GLN A 325 VAL A 331 1 O LEU A 327 N LEU A 227
SHEET 9 B11 ARG A 424 PHE A 430 1 O PHE A 430 N VAL A 330
SHEET 10 B11 GLN A 509 LEU A 513 1 O LEU A 513 N ILE A 429
SHEET 11 B11 GLU A 519 ARG A 522 -1 O ARG A 521 N TYR A 510
SHEET 1 C 2 VAL A 68 CYS A 69 0
SHEET 2 C 2 LEU A 92 SER A 93 1 O SER A 93 N VAL A 68
SHEET 1 D 2 VAL A 239 SER A 240 0
SHEET 2 D 2 VAL A 302 VAL A 303 1 O VAL A 303 N VAL A 239
SHEET 1 E 3 LEU B 9 VAL B 12 0
SHEET 2 E 3 GLY B 15 ARG B 18 -1 O GLY B 15 N VAL B 12
SHEET 3 E 3 VAL B 59 ASP B 61 1 O LEU B 60 N GLN B 16
SHEET 1 F11 ILE B 20 ALA B 24 0
SHEET 2 F11 GLY B 27 PRO B 36 -1 O VAL B 29 N LEU B 22
SHEET 3 F11 TYR B 98 PRO B 104 -1 O VAL B 101 N PHE B 32
SHEET 4 F11 VAL B 145 MET B 149 -1 O SER B 148 N ASN B 100
SHEET 5 F11 THR B 112 ILE B 118 1 N LEU B 115 O VAL B 147
SHEET 6 F11 GLY B 192 GLU B 202 1 O ASP B 193 N THR B 112
SHEET 7 F11 ARG B 224 GLN B 228 1 O ARG B 224 N LEU B 199
SHEET 8 F11 GLN B 325 VAL B 331 1 O LEU B 327 N LEU B 227
SHEET 9 F11 ARG B 424 PHE B 430 1 O TYR B 426 N VAL B 328
SHEET 10 F11 GLN B 509 LEU B 513 1 O LEU B 513 N ILE B 429
SHEET 11 F11 GLU B 519 ARG B 522 -1 O ARG B 521 N TYR B 510
SHEET 1 G 2 VAL B 68 CYS B 69 0
SHEET 2 G 2 LEU B 92 SER B 93 1 O SER B 93 N VAL B 68
SHEET 1 H 2 VAL B 239 SER B 240 0
SHEET 2 H 2 VAL B 302 VAL B 303 1 O VAL B 303 N VAL B 239
SSBOND 1 CYS A 69 CYS A 96
SSBOND 2 CYS A 257 CYS A 272
SSBOND 3 CYS A 409 CYS A 529
SSBOND 4 CYS B 69 CYS B 96
SSBOND 5 CYS B 257 CYS B 272
SSBOND 6 CYS B 409 CYS B 529
LINK ND2 ASN A 350 C1 NAG C1501
LINK ND2 ASN A 464 C1 NAG A1701
LINK ND2 ASN B 350 C1 NAG B1601
LINK O6 NAG C1501 C1 FUL C1502
CISPEP 1 TYR A 105 PRO A 106 0 -4.45
CISPEP 2 CYS A 257 PRO A 258 0 15.25
CISPEP 3 TYR B 105 PRO B 106 0 2.95
CISPEP 4 CYS B 257 PRO B 258 0 3.23
CISPEP 5 SER B 497 PRO B 498 0 -13.07
CRYST1 79.743 111.954 226.577 90.00 90.00 90.00 P 21 21 21 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 0.012540 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008932 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004414 0.00000
TER 4183 SER A 541
TER 8326 LEU B 540
MASTER 485 0 7 53 36 0 0 6 8768 2 186 90
END |