HEADER HYDROLASE 10-MAR-15 5AM9
TITLE CRYSTAL STRUCTURE OF THE ANGIOTENSIN-1 CONVERTING ENZYME N-DOMAIN IN
TITLE 2 COMPLEX WITH AMYLOID-BETA 10-16
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANGIOTENSIN-CONVERTING ENZYME;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: N DOMAIN, UNP RESIDUES 30-658;
COMPND 5 SYNONYM: ACE, DIPEPTIDYL CARBOXYPEPTIDASE I, KININASE II, CD143,
COMPND 6 ANGIOTENSIN-CONVERTING ENZYME, SOLUBLE FORM;
COMPND 7 EC: 3.2.1.-, 3.4.15.1;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES;
COMPND 10 OTHER_DETAILS: MINIMALLY GLYCOSYLATED MUTANT
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: CHO K1
KEYWDS HYDROLASE, METALLOPROTEASE, AMYLOID- BETA
EXPDTA X-RAY DIFFRACTION
AUTHOR G.MASUYER,K.M.LARMUTH,R.G.DOUGLAS,E.D.STURROCK,K.R.ACHARYA
REVDAT 5 10-JAN-24 5AM9 1 HETSYN
REVDAT 4 29-JUL-20 5AM9 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE ATOM
REVDAT 3 06-APR-16 5AM9 1 JRNL
REVDAT 2 20-JAN-16 5AM9 1 JRNL
REVDAT 1 13-JAN-16 5AM9 0
JRNL AUTH K.M.LARMUTH,G.MASUYER,R.G.DOUGLAS,E.D.STURROCK,K.R.ACHARYA
JRNL TITL THE KINETIC AND STRUCTURAL CHARACTERISATION OF AMYLOID-BETA
JRNL TITL 2 METABOLISM BY HUMAN ANGIOTENSIN-1- CONVERTING ENZYME (ACE)
JRNL REF FEBS J. V. 283 1060 2016
JRNL REFN ISSN 1742-464X
JRNL PMID 26748546
JRNL DOI 10.1111/FEBS.13647
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0103
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 113.27
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 277219
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) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 14478
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 20272
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.57
REMARK 3 BIN R VALUE (WORKING SET) : 0.3660
REMARK 3 BIN FREE R VALUE SET COUNT : 1023
REMARK 3 BIN FREE R VALUE : 0.3830
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 19810
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 642
REMARK 3 SOLVENT ATOMS : 1649
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.35
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.13000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 1.08000
REMARK 3 B12 (A**2) : -0.14000
REMARK 3 B13 (A**2) : -0.03000
REMARK 3 B23 (A**2) : 0.05000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.125
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.120
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.108
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.626
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 21170 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 19291 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 28807 ; 1.454 ; 1.960
REMARK 3 BOND ANGLES OTHERS (DEGREES): 44389 ; 0.979 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2444 ; 5.961 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1073 ;35.368 ;23.784
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3242 ;13.097 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 134 ;18.082 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3022 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 23752 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 5224 ; 0.002 ; 0.020
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): 9761 ; 1.113 ; 2.457
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 9760 ; 1.112 ; 2.457
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12189 ; 1.837 ; 3.677
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 11409 ; 1.411 ; 2.720
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
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 1203
REMARK 3 ORIGIN FOR THE GROUP (A): -13.1301 46.4750 -29.0133
REMARK 3 T TENSOR
REMARK 3 T11: 0.0032 T22: 0.0057
REMARK 3 T33: 0.0197 T12: 0.0009
REMARK 3 T13: -0.0079 T23: -0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 0.0182 L22: 0.0069
REMARK 3 L33: 0.0307 L12: 0.0058
REMARK 3 L13: 0.0207 L23: 0.0126
REMARK 3 S TENSOR
REMARK 3 S11: 0.0028 S12: 0.0090 S13: -0.0055
REMARK 3 S21: 0.0009 S22: 0.0055 S23: -0.0037
REMARK 3 S31: 0.0030 S32: 0.0132 S33: -0.0082
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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. FOR AMYLOID-BETA FRAGMENT 10-16, ONLY DI-PEPTIDE
REMARK 3 PRODUCT OF THE ACE ENZYMATIC ACTIVITY WERE SEEN.
REMARK 4
REMARK 4 5AM9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-MAR-15.
REMARK 100 THE DEPOSITION ID IS D_1290063276.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-NOV-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 291734
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 31.470
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.76000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.400
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 3NXQ
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.06 M DIVALENT CATIONS, 0.1 M
REMARK 280 TRIS/BICINE PH 8.5, 30 % PEG550MME/PEG20000
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: C, K, L, M
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, H, I, J
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, N, O, P
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 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, E, F, G
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 PRO A 130
REMARK 465 GLN A 131
REMARK 465 LYS A 132
REMARK 465 THR A 133
REMARK 465 ALA A 134
REMARK 465 GLU A 609
REMARK 465 GLY A 610
REMARK 465 ILE A 611
REMARK 465 ASP A 612
REMARK 465 LEU A 613
REMARK 465 VAL A 614
REMARK 465 THR A 615
REMARK 465 ASP A 616
REMARK 465 GLU A 617
REMARK 465 ALA A 618
REMARK 465 GLU A 619
REMARK 465 ALA A 620
REMARK 465 SER A 621
REMARK 465 LYS A 622
REMARK 465 PHE A 623
REMARK 465 VAL A 624
REMARK 465 GLU A 625
REMARK 465 GLU A 626
REMARK 465 TYR A 627
REMARK 465 ASP A 628
REMARK 465 LEU A 629
REMARK 465 LYS B 132
REMARK 465 THR B 133
REMARK 465 ALA B 134
REMARK 465 GLU B 609
REMARK 465 GLY B 610
REMARK 465 ILE B 611
REMARK 465 ASP B 612
REMARK 465 LEU B 613
REMARK 465 VAL B 614
REMARK 465 THR B 615
REMARK 465 ASP B 616
REMARK 465 GLU B 617
REMARK 465 ALA B 618
REMARK 465 GLU B 619
REMARK 465 ALA B 620
REMARK 465 SER B 621
REMARK 465 LYS B 622
REMARK 465 PHE B 623
REMARK 465 VAL B 624
REMARK 465 GLU B 625
REMARK 465 GLU B 626
REMARK 465 TYR B 627
REMARK 465 ASP B 628
REMARK 465 LEU B 629
REMARK 465 PRO C 130
REMARK 465 GLN C 131
REMARK 465 LYS C 132
REMARK 465 THR C 133
REMARK 465 ALA C 134
REMARK 465 GLU C 617
REMARK 465 ALA C 618
REMARK 465 GLU C 619
REMARK 465 ALA C 620
REMARK 465 SER C 621
REMARK 465 LYS C 622
REMARK 465 PHE C 623
REMARK 465 VAL C 624
REMARK 465 GLU C 625
REMARK 465 GLU C 626
REMARK 465 TYR C 627
REMARK 465 ASP C 628
REMARK 465 LEU C 629
REMARK 465 PRO D 130
REMARK 465 GLN D 131
REMARK 465 LYS D 132
REMARK 465 LEU D 613
REMARK 465 VAL D 614
REMARK 465 THR D 615
REMARK 465 ASP D 616
REMARK 465 GLU D 617
REMARK 465 ALA D 618
REMARK 465 GLU D 619
REMARK 465 ALA D 620
REMARK 465 SER D 621
REMARK 465 LYS D 622
REMARK 465 PHE D 623
REMARK 465 VAL D 624
REMARK 465 GLU D 625
REMARK 465 GLU D 626
REMARK 465 TYR D 627
REMARK 465 ASP D 628
REMARK 465 LEU D 629
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 LEU A 129 CG CD1 CD2
REMARK 470 LYS A 341 CG CD CE NZ
REMARK 470 ARG A 413 CG CD NE CZ NH1 NH2
REMARK 470 PRO B 130 CG CD
REMARK 470 GLN B 131 CG CD OE1 NE2
REMARK 470 THR B 135 OG1 CG2
REMARK 470 LEU C 129 CG CD1 CD2
REMARK 470 THR C 135 OG1 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 C GLN A 915 N LYS A 916 1.33
REMARK 500 C GLU C 911 N VAL C 912 1.34
REMARK 500 C GLU B 911 N VAL B 912 1.34
REMARK 500 C GLN D 915 N LYS D 916 1.35
REMARK 500 ND2 ASN B 45 O5 NAG I 1 2.17
REMARK 500 OE1 GLU D 176 O HOH D 2144 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 326 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG A 541 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ASP B 354 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ARG B 541 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG C 541 NE - CZ - NH1 ANGL. DEV. = 3.6 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 ASN A 45 73.96 -172.30
REMARK 500 PHE A 271 72.04 -119.02
REMARK 500 ASP A 324 -146.96 -79.73
REMARK 500 ARG A 340 13.38 57.47
REMARK 500 LYS A 341 -45.91 -130.00
REMARK 500 ASN B 45 75.83 -169.02
REMARK 500 LYS B 341 -48.06 -133.19
REMARK 500 ASN C 45 78.27 -176.17
REMARK 500 ASN C 606 70.44 -119.77
REMARK 500 ASN D 45 79.47 -174.42
REMARK 500 ALA D 134 -86.10 -123.69
REMARK 500 LYS D 341 -46.08 -132.83
REMARK 500
REMARK 500 REMARK: NULL
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 ASP C 324 GLY C 325 -37.61
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 GLN A 915
REMARK 610 GLU B 911
REMARK 610 GLU C 911
REMARK 610 GLN D 915
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 NA A1003 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 262 OE2
REMARK 620 2 ASN A 263 OD1 99.4
REMARK 620 3 ASP A 354 OD2 97.3 85.6
REMARK 620 4 HOH A2208 O 77.6 91.8 173.8
REMARK 620 5 HOH A2211 O 82.7 175.8 90.5 92.2
REMARK 620 6 HOH A2213 O 166.9 79.2 95.6 89.4 99.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1001 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 361 NE2
REMARK 620 2 HIS A 365 NE2 105.1
REMARK 620 3 GLU A 389 OE1 93.6 102.2
REMARK 620 4 HOH A2273 O 117.5 125.8 106.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B1003 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 262 OE2
REMARK 620 2 ASN B 263 OD1 100.2
REMARK 620 3 ASP B 354 OD2 97.9 83.7
REMARK 620 4 HOH B2198 O 81.6 90.3 173.9
REMARK 620 5 HOH B2205 O 90.2 168.6 90.3 95.8
REMARK 620 6 HOH B2207 O 167.4 74.0 92.6 87.2 96.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1001 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 361 NE2
REMARK 620 2 HIS B 365 NE2 101.8
REMARK 620 3 GLU B 389 OE1 92.3 103.5
REMARK 620 4 HOH B2273 O 113.6 130.0 108.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C1003 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 262 OE2
REMARK 620 2 ASN C 263 OD1 102.3
REMARK 620 3 ASP C 354 OD2 99.5 84.8
REMARK 620 4 HOH C2244 O 83.3 92.7 176.5
REMARK 620 5 HOH C2250 O 92.5 165.1 91.0 90.8
REMARK 620 6 HOH C2252 O 169.3 76.7 91.0 86.1 89.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C1001 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 361 NE2
REMARK 620 2 HIS C 365 NE2 102.3
REMARK 620 3 GLU C 389 OE1 92.8 103.4
REMARK 620 4 HOH C2329 O 114.1 125.7 113.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA D1003 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 262 OE2
REMARK 620 2 ASN D 263 OD1 98.0
REMARK 620 3 ASP D 354 OD2 92.6 82.9
REMARK 620 4 HOH D2202 O 91.0 87.8 170.5
REMARK 620 5 HOH D2208 O 168.9 72.4 91.7 83.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D1001 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 361 NE2
REMARK 620 2 HIS D 365 NE2 104.4
REMARK 620 3 GLU D 389 OE1 91.8 102.5
REMARK 620 4 HOH D2277 O 115.8 127.9 107.7
REMARK 620 N 1 2 3
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4UFA RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE ANGIOTENSIN-1 CONVERTING ENZYME N-DOMAIN
REMARK 900 IN COMPLEX WITH AC-SD
REMARK 900 RELATED ID: 4UFB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE ANGIOTENSIN-1 CONVERTING ENZYME N-DOMAIN
REMARK 900 IN COMPLEX WITH LYS-PRO
REMARK 900 RELATED ID: 5AM8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE ANGIOTENSIN-1 CONVERTING ENZYME N-DOMAIN
REMARK 900 IN COMPLEX WITH AMYLOID-BETA 4-10
REMARK 900 RELATED ID: 5AMA RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE ANGIOTENSIN-1 CONVERTING ENZYME N-DOMAIN
REMARK 900 IN COMPLEX WITH AMYLOID-BETA 1-16
REMARK 900 RELATED ID: 5AMB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE ANGIOTENSIN-1 CONVERTING ENZYME N-DOMAIN
REMARK 900 IN COMPLEX WITH AMYLOID-BETA 35-42
REMARK 900 RELATED ID: 5AMC RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE ANGIOTENSIN-1 CONVERTING ENZYME N-DOMAIN
REMARK 900 IN COMPLEX WITH AMYLOID-BETA FLUOROGENIC FRAGMENT 4-10
DBREF 5AM9 A 1 629 UNP P12821 ACE_HUMAN 30 658
DBREF 5AM9 B 1 629 UNP P12821 ACE_HUMAN 30 658
DBREF 5AM9 C 1 629 UNP P12821 ACE_HUMAN 30 658
DBREF 5AM9 D 1 629 UNP P12821 ACE_HUMAN 30 658
SEQADV 5AM9 GLN A 9 UNP P12821 ASN 38 ENGINEERED MUTATION
SEQADV 5AM9 GLN A 25 UNP P12821 ASN 54 ENGINEERED MUTATION
SEQADV 5AM9 GLN A 82 UNP P12821 ASN 111 ENGINEERED MUTATION
SEQADV 5AM9 GLN A 117 UNP P12821 ASN 146 ENGINEERED MUTATION
SEQADV 5AM9 GLN A 131 UNP P12821 ASN 160 ENGINEERED MUTATION
SEQADV 5AM9 GLN A 289 UNP P12821 ASN 318 ENGINEERED MUTATION
SEQADV 5AM9 ARG A 545 UNP P12821 GLN 574 ENGINEERED MUTATION
SEQADV 5AM9 LEU A 576 UNP P12821 PRO 605 ENGINEERED MUTATION
SEQADV 5AM9 LEU A 629 UNP P12821 ARG 658 ENGINEERED MUTATION
SEQADV 5AM9 GLN B 9 UNP P12821 ASN 38 ENGINEERED MUTATION
SEQADV 5AM9 GLN B 25 UNP P12821 ASN 54 ENGINEERED MUTATION
SEQADV 5AM9 GLN B 82 UNP P12821 ASN 111 ENGINEERED MUTATION
SEQADV 5AM9 GLN B 117 UNP P12821 ASN 146 ENGINEERED MUTATION
SEQADV 5AM9 GLN B 289 UNP P12821 ASN 318 ENGINEERED MUTATION
SEQADV 5AM9 ARG B 545 UNP P12821 GLN 574 ENGINEERED MUTATION
SEQADV 5AM9 LEU B 576 UNP P12821 PRO 605 ENGINEERED MUTATION
SEQADV 5AM9 LEU B 629 UNP P12821 ARG 658 ENGINEERED MUTATION
SEQADV 5AM9 GLN C 9 UNP P12821 ASN 38 ENGINEERED MUTATION
SEQADV 5AM9 GLN C 25 UNP P12821 ASN 54 ENGINEERED MUTATION
SEQADV 5AM9 GLN C 82 UNP P12821 ASN 111 ENGINEERED MUTATION
SEQADV 5AM9 GLN C 117 UNP P12821 ASN 146 ENGINEERED MUTATION
SEQADV 5AM9 GLN C 131 UNP P12821 ASN 160 ENGINEERED MUTATION
SEQADV 5AM9 GLN C 289 UNP P12821 ASN 318 ENGINEERED MUTATION
SEQADV 5AM9 ARG C 545 UNP P12821 GLN 574 ENGINEERED MUTATION
SEQADV 5AM9 LEU C 576 UNP P12821 PRO 605 ENGINEERED MUTATION
SEQADV 5AM9 LEU C 629 UNP P12821 ARG 658 ENGINEERED MUTATION
SEQADV 5AM9 GLN D 9 UNP P12821 ASN 38 ENGINEERED MUTATION
SEQADV 5AM9 GLN D 25 UNP P12821 ASN 54 ENGINEERED MUTATION
SEQADV 5AM9 GLN D 82 UNP P12821 ASN 111 ENGINEERED MUTATION
SEQADV 5AM9 GLN D 117 UNP P12821 ASN 146 ENGINEERED MUTATION
SEQADV 5AM9 GLN D 131 UNP P12821 ASN 160 ENGINEERED MUTATION
SEQADV 5AM9 GLN D 289 UNP P12821 ASN 318 ENGINEERED MUTATION
SEQADV 5AM9 ARG D 545 UNP P12821 GLN 574 ENGINEERED MUTATION
SEQADV 5AM9 LEU D 576 UNP P12821 PRO 605 ENGINEERED MUTATION
SEQADV 5AM9 LEU D 629 UNP P12821 ARG 658 ENGINEERED MUTATION
SEQRES 1 A 629 LEU ASP PRO GLY LEU GLN PRO GLY GLN PHE SER ALA ASP
SEQRES 2 A 629 GLU ALA GLY ALA GLN LEU PHE ALA GLN SER TYR GLN SER
SEQRES 3 A 629 SER ALA GLU GLN VAL LEU PHE GLN SER VAL ALA ALA SER
SEQRES 4 A 629 TRP ALA HIS ASP THR ASN ILE THR ALA GLU ASN ALA ARG
SEQRES 5 A 629 ARG GLN GLU GLU ALA ALA LEU LEU SER GLN GLU PHE ALA
SEQRES 6 A 629 GLU ALA TRP GLY GLN LYS ALA LYS GLU LEU TYR GLU PRO
SEQRES 7 A 629 ILE TRP GLN GLN PHE THR ASP PRO GLN LEU ARG ARG ILE
SEQRES 8 A 629 ILE GLY ALA VAL ARG THR LEU GLY SER ALA ASN LEU PRO
SEQRES 9 A 629 LEU ALA LYS ARG GLN GLN TYR ASN ALA LEU LEU SER GLN
SEQRES 10 A 629 MET SER ARG ILE TYR SER THR ALA LYS VAL CYS LEU PRO
SEQRES 11 A 629 GLN LYS THR ALA THR CYS TRP SER LEU ASP PRO ASP LEU
SEQRES 12 A 629 THR ASN ILE LEU ALA SER SER ARG SER TYR ALA MET LEU
SEQRES 13 A 629 LEU PHE ALA TRP GLU GLY TRP HIS ASN ALA ALA GLY ILE
SEQRES 14 A 629 PRO LEU LYS PRO LEU TYR GLU ASP PHE THR ALA LEU SER
SEQRES 15 A 629 ASN GLU ALA TYR LYS GLN ASP GLY PHE THR ASP THR GLY
SEQRES 16 A 629 ALA TYR TRP ARG SER TRP TYR ASN SER PRO THR PHE GLU
SEQRES 17 A 629 ASP ASP LEU GLU HIS LEU TYR GLN GLN LEU GLU PRO LEU
SEQRES 18 A 629 TYR LEU ASN LEU HIS ALA PHE VAL ARG ARG ALA LEU HIS
SEQRES 19 A 629 ARG ARG TYR GLY ASP ARG TYR ILE ASN LEU ARG GLY PRO
SEQRES 20 A 629 ILE PRO ALA HIS LEU LEU GLY ASP MET TRP ALA GLN SER
SEQRES 21 A 629 TRP GLU ASN ILE TYR ASP MET VAL VAL PRO PHE PRO ASP
SEQRES 22 A 629 LYS PRO ASN LEU ASP VAL THR SER THR MET LEU GLN GLN
SEQRES 23 A 629 GLY TRP GLN ALA THR HIS MET PHE ARG VAL ALA GLU GLU
SEQRES 24 A 629 PHE PHE THR SER LEU GLU LEU SER PRO MET PRO PRO GLU
SEQRES 25 A 629 PHE TRP GLU GLY SER MET LEU GLU LYS PRO ALA ASP GLY
SEQRES 26 A 629 ARG GLU VAL VAL CYS HIS ALA SER ALA TRP ASP PHE TYR
SEQRES 27 A 629 ASN ARG LYS ASP PHE ARG ILE LYS GLN CYS THR ARG VAL
SEQRES 28 A 629 THR MET ASP GLN LEU SER THR VAL HIS HIS GLU MET GLY
SEQRES 29 A 629 HIS ILE GLN TYR TYR LEU GLN TYR LYS ASP LEU PRO VAL
SEQRES 30 A 629 SER LEU ARG ARG GLY ALA ASN PRO GLY PHE HIS GLU ALA
SEQRES 31 A 629 ILE GLY ASP VAL LEU ALA LEU SER VAL SER THR PRO GLU
SEQRES 32 A 629 HIS LEU HIS LYS ILE GLY LEU LEU ASP ARG VAL THR ASN
SEQRES 33 A 629 ASP THR GLU SER ASP ILE ASN TYR LEU LEU LYS MET ALA
SEQRES 34 A 629 LEU GLU LYS ILE ALA PHE LEU PRO PHE GLY TYR LEU VAL
SEQRES 35 A 629 ASP GLN TRP ARG TRP GLY VAL PHE SER GLY ARG THR PRO
SEQRES 36 A 629 PRO SER ARG TYR ASN PHE ASP TRP TRP TYR LEU ARG THR
SEQRES 37 A 629 LYS TYR GLN GLY ILE CYS PRO PRO VAL THR ARG ASN GLU
SEQRES 38 A 629 THR HIS PHE ASP ALA GLY ALA LYS PHE HIS VAL PRO ASN
SEQRES 39 A 629 VAL THR PRO TYR ILE ARG TYR PHE VAL SER PHE VAL LEU
SEQRES 40 A 629 GLN PHE GLN PHE HIS GLU ALA LEU CYS LYS GLU ALA GLY
SEQRES 41 A 629 TYR GLU GLY PRO LEU HIS GLN CYS ASP ILE TYR ARG SER
SEQRES 42 A 629 THR LYS ALA GLY ALA LYS LEU ARG LYS VAL LEU ARG ALA
SEQRES 43 A 629 GLY SER SER ARG PRO TRP GLN GLU VAL LEU LYS ASP MET
SEQRES 44 A 629 VAL GLY LEU ASP ALA LEU ASP ALA GLN PRO LEU LEU LYS
SEQRES 45 A 629 TYR PHE GLN LEU VAL THR GLN TRP LEU GLN GLU GLN ASN
SEQRES 46 A 629 GLN GLN ASN GLY GLU VAL LEU GLY TRP PRO GLU TYR GLN
SEQRES 47 A 629 TRP HIS PRO PRO LEU PRO ASP ASN TYR PRO GLU GLY ILE
SEQRES 48 A 629 ASP LEU VAL THR ASP GLU ALA GLU ALA SER LYS PHE VAL
SEQRES 49 A 629 GLU GLU TYR ASP LEU
SEQRES 1 B 629 LEU ASP PRO GLY LEU GLN PRO GLY GLN PHE SER ALA ASP
SEQRES 2 B 629 GLU ALA GLY ALA GLN LEU PHE ALA GLN SER TYR GLN SER
SEQRES 3 B 629 SER ALA GLU GLN VAL LEU PHE GLN SER VAL ALA ALA SER
SEQRES 4 B 629 TRP ALA HIS ASP THR ASN ILE THR ALA GLU ASN ALA ARG
SEQRES 5 B 629 ARG GLN GLU GLU ALA ALA LEU LEU SER GLN GLU PHE ALA
SEQRES 6 B 629 GLU ALA TRP GLY GLN LYS ALA LYS GLU LEU TYR GLU PRO
SEQRES 7 B 629 ILE TRP GLN GLN PHE THR ASP PRO GLN LEU ARG ARG ILE
SEQRES 8 B 629 ILE GLY ALA VAL ARG THR LEU GLY SER ALA ASN LEU PRO
SEQRES 9 B 629 LEU ALA LYS ARG GLN GLN TYR ASN ALA LEU LEU SER GLN
SEQRES 10 B 629 MET SER ARG ILE TYR SER THR ALA LYS VAL CYS LEU PRO
SEQRES 11 B 629 GLN LYS THR ALA THR CYS TRP SER LEU ASP PRO ASP LEU
SEQRES 12 B 629 THR ASN ILE LEU ALA SER SER ARG SER TYR ALA MET LEU
SEQRES 13 B 629 LEU PHE ALA TRP GLU GLY TRP HIS ASN ALA ALA GLY ILE
SEQRES 14 B 629 PRO LEU LYS PRO LEU TYR GLU ASP PHE THR ALA LEU SER
SEQRES 15 B 629 ASN GLU ALA TYR LYS GLN ASP GLY PHE THR ASP THR GLY
SEQRES 16 B 629 ALA TYR TRP ARG SER TRP TYR ASN SER PRO THR PHE GLU
SEQRES 17 B 629 ASP ASP LEU GLU HIS LEU TYR GLN GLN LEU GLU PRO LEU
SEQRES 18 B 629 TYR LEU ASN LEU HIS ALA PHE VAL ARG ARG ALA LEU HIS
SEQRES 19 B 629 ARG ARG TYR GLY ASP ARG TYR ILE ASN LEU ARG GLY PRO
SEQRES 20 B 629 ILE PRO ALA HIS LEU LEU GLY ASP MET TRP ALA GLN SER
SEQRES 21 B 629 TRP GLU ASN ILE TYR ASP MET VAL VAL PRO PHE PRO ASP
SEQRES 22 B 629 LYS PRO ASN LEU ASP VAL THR SER THR MET LEU GLN GLN
SEQRES 23 B 629 GLY TRP GLN ALA THR HIS MET PHE ARG VAL ALA GLU GLU
SEQRES 24 B 629 PHE PHE THR SER LEU GLU LEU SER PRO MET PRO PRO GLU
SEQRES 25 B 629 PHE TRP GLU GLY SER MET LEU GLU LYS PRO ALA ASP GLY
SEQRES 26 B 629 ARG GLU VAL VAL CYS HIS ALA SER ALA TRP ASP PHE TYR
SEQRES 27 B 629 ASN ARG LYS ASP PHE ARG ILE LYS GLN CYS THR ARG VAL
SEQRES 28 B 629 THR MET ASP GLN LEU SER THR VAL HIS HIS GLU MET GLY
SEQRES 29 B 629 HIS ILE GLN TYR TYR LEU GLN TYR LYS ASP LEU PRO VAL
SEQRES 30 B 629 SER LEU ARG ARG GLY ALA ASN PRO GLY PHE HIS GLU ALA
SEQRES 31 B 629 ILE GLY ASP VAL LEU ALA LEU SER VAL SER THR PRO GLU
SEQRES 32 B 629 HIS LEU HIS LYS ILE GLY LEU LEU ASP ARG VAL THR ASN
SEQRES 33 B 629 ASP THR GLU SER ASP ILE ASN TYR LEU LEU LYS MET ALA
SEQRES 34 B 629 LEU GLU LYS ILE ALA PHE LEU PRO PHE GLY TYR LEU VAL
SEQRES 35 B 629 ASP GLN TRP ARG TRP GLY VAL PHE SER GLY ARG THR PRO
SEQRES 36 B 629 PRO SER ARG TYR ASN PHE ASP TRP TRP TYR LEU ARG THR
SEQRES 37 B 629 LYS TYR GLN GLY ILE CYS PRO PRO VAL THR ARG ASN GLU
SEQRES 38 B 629 THR HIS PHE ASP ALA GLY ALA LYS PHE HIS VAL PRO ASN
SEQRES 39 B 629 VAL THR PRO TYR ILE ARG TYR PHE VAL SER PHE VAL LEU
SEQRES 40 B 629 GLN PHE GLN PHE HIS GLU ALA LEU CYS LYS GLU ALA GLY
SEQRES 41 B 629 TYR GLU GLY PRO LEU HIS GLN CYS ASP ILE TYR ARG SER
SEQRES 42 B 629 THR LYS ALA GLY ALA LYS LEU ARG LYS VAL LEU ARG ALA
SEQRES 43 B 629 GLY SER SER ARG PRO TRP GLN GLU VAL LEU LYS ASP MET
SEQRES 44 B 629 VAL GLY LEU ASP ALA LEU ASP ALA GLN PRO LEU LEU LYS
SEQRES 45 B 629 TYR PHE GLN LEU VAL THR GLN TRP LEU GLN GLU GLN ASN
SEQRES 46 B 629 GLN GLN ASN GLY GLU VAL LEU GLY TRP PRO GLU TYR GLN
SEQRES 47 B 629 TRP HIS PRO PRO LEU PRO ASP ASN TYR PRO GLU GLY ILE
SEQRES 48 B 629 ASP LEU VAL THR ASP GLU ALA GLU ALA SER LYS PHE VAL
SEQRES 49 B 629 GLU GLU TYR ASP LEU
SEQRES 1 C 629 LEU ASP PRO GLY LEU GLN PRO GLY GLN PHE SER ALA ASP
SEQRES 2 C 629 GLU ALA GLY ALA GLN LEU PHE ALA GLN SER TYR GLN SER
SEQRES 3 C 629 SER ALA GLU GLN VAL LEU PHE GLN SER VAL ALA ALA SER
SEQRES 4 C 629 TRP ALA HIS ASP THR ASN ILE THR ALA GLU ASN ALA ARG
SEQRES 5 C 629 ARG GLN GLU GLU ALA ALA LEU LEU SER GLN GLU PHE ALA
SEQRES 6 C 629 GLU ALA TRP GLY GLN LYS ALA LYS GLU LEU TYR GLU PRO
SEQRES 7 C 629 ILE TRP GLN GLN PHE THR ASP PRO GLN LEU ARG ARG ILE
SEQRES 8 C 629 ILE GLY ALA VAL ARG THR LEU GLY SER ALA ASN LEU PRO
SEQRES 9 C 629 LEU ALA LYS ARG GLN GLN TYR ASN ALA LEU LEU SER GLN
SEQRES 10 C 629 MET SER ARG ILE TYR SER THR ALA LYS VAL CYS LEU PRO
SEQRES 11 C 629 GLN LYS THR ALA THR CYS TRP SER LEU ASP PRO ASP LEU
SEQRES 12 C 629 THR ASN ILE LEU ALA SER SER ARG SER TYR ALA MET LEU
SEQRES 13 C 629 LEU PHE ALA TRP GLU GLY TRP HIS ASN ALA ALA GLY ILE
SEQRES 14 C 629 PRO LEU LYS PRO LEU TYR GLU ASP PHE THR ALA LEU SER
SEQRES 15 C 629 ASN GLU ALA TYR LYS GLN ASP GLY PHE THR ASP THR GLY
SEQRES 16 C 629 ALA TYR TRP ARG SER TRP TYR ASN SER PRO THR PHE GLU
SEQRES 17 C 629 ASP ASP LEU GLU HIS LEU TYR GLN GLN LEU GLU PRO LEU
SEQRES 18 C 629 TYR LEU ASN LEU HIS ALA PHE VAL ARG ARG ALA LEU HIS
SEQRES 19 C 629 ARG ARG TYR GLY ASP ARG TYR ILE ASN LEU ARG GLY PRO
SEQRES 20 C 629 ILE PRO ALA HIS LEU LEU GLY ASP MET TRP ALA GLN SER
SEQRES 21 C 629 TRP GLU ASN ILE TYR ASP MET VAL VAL PRO PHE PRO ASP
SEQRES 22 C 629 LYS PRO ASN LEU ASP VAL THR SER THR MET LEU GLN GLN
SEQRES 23 C 629 GLY TRP GLN ALA THR HIS MET PHE ARG VAL ALA GLU GLU
SEQRES 24 C 629 PHE PHE THR SER LEU GLU LEU SER PRO MET PRO PRO GLU
SEQRES 25 C 629 PHE TRP GLU GLY SER MET LEU GLU LYS PRO ALA ASP GLY
SEQRES 26 C 629 ARG GLU VAL VAL CYS HIS ALA SER ALA TRP ASP PHE TYR
SEQRES 27 C 629 ASN ARG LYS ASP PHE ARG ILE LYS GLN CYS THR ARG VAL
SEQRES 28 C 629 THR MET ASP GLN LEU SER THR VAL HIS HIS GLU MET GLY
SEQRES 29 C 629 HIS ILE GLN TYR TYR LEU GLN TYR LYS ASP LEU PRO VAL
SEQRES 30 C 629 SER LEU ARG ARG GLY ALA ASN PRO GLY PHE HIS GLU ALA
SEQRES 31 C 629 ILE GLY ASP VAL LEU ALA LEU SER VAL SER THR PRO GLU
SEQRES 32 C 629 HIS LEU HIS LYS ILE GLY LEU LEU ASP ARG VAL THR ASN
SEQRES 33 C 629 ASP THR GLU SER ASP ILE ASN TYR LEU LEU LYS MET ALA
SEQRES 34 C 629 LEU GLU LYS ILE ALA PHE LEU PRO PHE GLY TYR LEU VAL
SEQRES 35 C 629 ASP GLN TRP ARG TRP GLY VAL PHE SER GLY ARG THR PRO
SEQRES 36 C 629 PRO SER ARG TYR ASN PHE ASP TRP TRP TYR LEU ARG THR
SEQRES 37 C 629 LYS TYR GLN GLY ILE CYS PRO PRO VAL THR ARG ASN GLU
SEQRES 38 C 629 THR HIS PHE ASP ALA GLY ALA LYS PHE HIS VAL PRO ASN
SEQRES 39 C 629 VAL THR PRO TYR ILE ARG TYR PHE VAL SER PHE VAL LEU
SEQRES 40 C 629 GLN PHE GLN PHE HIS GLU ALA LEU CYS LYS GLU ALA GLY
SEQRES 41 C 629 TYR GLU GLY PRO LEU HIS GLN CYS ASP ILE TYR ARG SER
SEQRES 42 C 629 THR LYS ALA GLY ALA LYS LEU ARG LYS VAL LEU ARG ALA
SEQRES 43 C 629 GLY SER SER ARG PRO TRP GLN GLU VAL LEU LYS ASP MET
SEQRES 44 C 629 VAL GLY LEU ASP ALA LEU ASP ALA GLN PRO LEU LEU LYS
SEQRES 45 C 629 TYR PHE GLN LEU VAL THR GLN TRP LEU GLN GLU GLN ASN
SEQRES 46 C 629 GLN GLN ASN GLY GLU VAL LEU GLY TRP PRO GLU TYR GLN
SEQRES 47 C 629 TRP HIS PRO PRO LEU PRO ASP ASN TYR PRO GLU GLY ILE
SEQRES 48 C 629 ASP LEU VAL THR ASP GLU ALA GLU ALA SER LYS PHE VAL
SEQRES 49 C 629 GLU GLU TYR ASP LEU
SEQRES 1 D 629 LEU ASP PRO GLY LEU GLN PRO GLY GLN PHE SER ALA ASP
SEQRES 2 D 629 GLU ALA GLY ALA GLN LEU PHE ALA GLN SER TYR GLN SER
SEQRES 3 D 629 SER ALA GLU GLN VAL LEU PHE GLN SER VAL ALA ALA SER
SEQRES 4 D 629 TRP ALA HIS ASP THR ASN ILE THR ALA GLU ASN ALA ARG
SEQRES 5 D 629 ARG GLN GLU GLU ALA ALA LEU LEU SER GLN GLU PHE ALA
SEQRES 6 D 629 GLU ALA TRP GLY GLN LYS ALA LYS GLU LEU TYR GLU PRO
SEQRES 7 D 629 ILE TRP GLN GLN PHE THR ASP PRO GLN LEU ARG ARG ILE
SEQRES 8 D 629 ILE GLY ALA VAL ARG THR LEU GLY SER ALA ASN LEU PRO
SEQRES 9 D 629 LEU ALA LYS ARG GLN GLN TYR ASN ALA LEU LEU SER GLN
SEQRES 10 D 629 MET SER ARG ILE TYR SER THR ALA LYS VAL CYS LEU PRO
SEQRES 11 D 629 GLN LYS THR ALA THR CYS TRP SER LEU ASP PRO ASP LEU
SEQRES 12 D 629 THR ASN ILE LEU ALA SER SER ARG SER TYR ALA MET LEU
SEQRES 13 D 629 LEU PHE ALA TRP GLU GLY TRP HIS ASN ALA ALA GLY ILE
SEQRES 14 D 629 PRO LEU LYS PRO LEU TYR GLU ASP PHE THR ALA LEU SER
SEQRES 15 D 629 ASN GLU ALA TYR LYS GLN ASP GLY PHE THR ASP THR GLY
SEQRES 16 D 629 ALA TYR TRP ARG SER TRP TYR ASN SER PRO THR PHE GLU
SEQRES 17 D 629 ASP ASP LEU GLU HIS LEU TYR GLN GLN LEU GLU PRO LEU
SEQRES 18 D 629 TYR LEU ASN LEU HIS ALA PHE VAL ARG ARG ALA LEU HIS
SEQRES 19 D 629 ARG ARG TYR GLY ASP ARG TYR ILE ASN LEU ARG GLY PRO
SEQRES 20 D 629 ILE PRO ALA HIS LEU LEU GLY ASP MET TRP ALA GLN SER
SEQRES 21 D 629 TRP GLU ASN ILE TYR ASP MET VAL VAL PRO PHE PRO ASP
SEQRES 22 D 629 LYS PRO ASN LEU ASP VAL THR SER THR MET LEU GLN GLN
SEQRES 23 D 629 GLY TRP GLN ALA THR HIS MET PHE ARG VAL ALA GLU GLU
SEQRES 24 D 629 PHE PHE THR SER LEU GLU LEU SER PRO MET PRO PRO GLU
SEQRES 25 D 629 PHE TRP GLU GLY SER MET LEU GLU LYS PRO ALA ASP GLY
SEQRES 26 D 629 ARG GLU VAL VAL CYS HIS ALA SER ALA TRP ASP PHE TYR
SEQRES 27 D 629 ASN ARG LYS ASP PHE ARG ILE LYS GLN CYS THR ARG VAL
SEQRES 28 D 629 THR MET ASP GLN LEU SER THR VAL HIS HIS GLU MET GLY
SEQRES 29 D 629 HIS ILE GLN TYR TYR LEU GLN TYR LYS ASP LEU PRO VAL
SEQRES 30 D 629 SER LEU ARG ARG GLY ALA ASN PRO GLY PHE HIS GLU ALA
SEQRES 31 D 629 ILE GLY ASP VAL LEU ALA LEU SER VAL SER THR PRO GLU
SEQRES 32 D 629 HIS LEU HIS LYS ILE GLY LEU LEU ASP ARG VAL THR ASN
SEQRES 33 D 629 ASP THR GLU SER ASP ILE ASN TYR LEU LEU LYS MET ALA
SEQRES 34 D 629 LEU GLU LYS ILE ALA PHE LEU PRO PHE GLY TYR LEU VAL
SEQRES 35 D 629 ASP GLN TRP ARG TRP GLY VAL PHE SER GLY ARG THR PRO
SEQRES 36 D 629 PRO SER ARG TYR ASN PHE ASP TRP TRP TYR LEU ARG THR
SEQRES 37 D 629 LYS TYR GLN GLY ILE CYS PRO PRO VAL THR ARG ASN GLU
SEQRES 38 D 629 THR HIS PHE ASP ALA GLY ALA LYS PHE HIS VAL PRO ASN
SEQRES 39 D 629 VAL THR PRO TYR ILE ARG TYR PHE VAL SER PHE VAL LEU
SEQRES 40 D 629 GLN PHE GLN PHE HIS GLU ALA LEU CYS LYS GLU ALA GLY
SEQRES 41 D 629 TYR GLU GLY PRO LEU HIS GLN CYS ASP ILE TYR ARG SER
SEQRES 42 D 629 THR LYS ALA GLY ALA LYS LEU ARG LYS VAL LEU ARG ALA
SEQRES 43 D 629 GLY SER SER ARG PRO TRP GLN GLU VAL LEU LYS ASP MET
SEQRES 44 D 629 VAL GLY LEU ASP ALA LEU ASP ALA GLN PRO LEU LEU LYS
SEQRES 45 D 629 TYR PHE GLN LEU VAL THR GLN TRP LEU GLN GLU GLN ASN
SEQRES 46 D 629 GLN GLN ASN GLY GLU VAL LEU GLY TRP PRO GLU TYR GLN
SEQRES 47 D 629 TRP HIS PRO PRO LEU PRO ASP ASN TYR PRO GLU GLY ILE
SEQRES 48 D 629 ASP LEU VAL THR ASP GLU ALA GLU ALA SER LYS PHE VAL
SEQRES 49 D 629 GLU GLU TYR ASP LEU
MODRES 5AM9 ASN A 45 ASN GLYCOSYLATION SITE
MODRES 5AM9 ASN A 416 ASN GLYCOSYLATION SITE
MODRES 5AM9 ASN A 480 ASN GLYCOSYLATION SITE
MODRES 5AM9 ASN B 45 ASN GLYCOSYLATION SITE
MODRES 5AM9 ASN B 416 ASN GLYCOSYLATION SITE
MODRES 5AM9 ASN B 480 ASN GLYCOSYLATION SITE
MODRES 5AM9 ASN C 45 ASN GLYCOSYLATION SITE
MODRES 5AM9 ASN C 416 ASN GLYCOSYLATION SITE
MODRES 5AM9 ASN C 480 ASN GLYCOSYLATION SITE
MODRES 5AM9 ASN D 45 ASN GLYCOSYLATION SITE
MODRES 5AM9 ASN D 416 ASN GLYCOSYLATION SITE
MODRES 5AM9 ASN D 480 ASN GLYCOSYLATION SITE
HET NAG E 1 14
HET FUL E 2 10
HET NAG F 1 14
HET NAG F 2 14
HET NAG G 1 14
HET NAG G 2 14
HET MAN G 3 11
HET NAG H 1 14
HET FUC H 2 10
HET NAG I 1 14
HET NAG I 2 14
HET NAG J 1 14
HET NAG J 2 14
HET MAN J 3 11
HET NAG K 1 14
HET FUC K 2 10
HET NAG L 1 14
HET NAG L 2 14
HET NAG M 1 14
HET NAG M 2 14
HET BMA M 3 11
HET FUC M 4 10
HET NAG N 1 14
HET FUC N 2 10
HET NAG O 1 14
HET NAG O 2 14
HET NAG P 1 14
HET NAG P 2 14
HET BMA P 3 11
HET FUC P 4 10
HET GLN A 915 9
HET LYS A 916 10
HET ZN A1001 1
HET CL A1002 1
HET NA A1003 1
HET PEG A1200 7
HET PEG A1201 7
HET P6G A1202 19
HET PEG A1203 7
HET GLU B 911 9
HET VAL B 912 8
HET ZN B1001 1
HET CL B1002 1
HET CA B1003 1
HET PEG B1201 7
HET PEG B1202 7
HET P6G B1203 19
HET P6G B1204 19
HET PEG B1205 7
HET GLU C 911 9
HET VAL C 912 8
HET ZN C1001 1
HET CL C1002 1
HET CA C1003 1
HET PEG C1200 7
HET PEG C1201 7
HET PEG C1202 7
HET PEG C1203 7
HET GLN D 915 9
HET LYS D 916 10
HET ZN D1001 1
HET CL D1002 1
HET NA D1003 1
HET PEG D1200 7
HET P6G D1201 19
HET PEG D1202 7
HET PEG D1203 7
HET PEG D1204 7
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM FUL BETA-L-FUCOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM GLN GLUTAMINE
HETNAM LYS LYSINE
HETNAM ZN ZINC ION
HETNAM CL CHLORIDE ION
HETNAM NA SODIUM ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM P6G HEXAETHYLENE GLYCOL
HETNAM GLU GLUTAMIC ACID
HETNAM VAL VALINE
HETNAM CA CALCIUM ION
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN FUL BETA-L-FUCOSE; 6-DEOXY-BETA-L-GALACTOPYRANOSE; L-
HETSYN 2 FUL FUCOSE; FUCOSE; 6-DEOXY-BETA-L-GALACTOSE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L-
HETSYN 2 FUC FUCOSE; FUCOSE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN P6G POLYETHYLENE GLYCOL PEG400
FORMUL 5 NAG 20(C8 H15 N O6)
FORMUL 5 FUL C6 H12 O5
FORMUL 7 MAN 2(C6 H12 O6)
FORMUL 8 FUC 5(C6 H12 O5)
FORMUL 13 BMA 2(C6 H12 O6)
FORMUL 17 GLN 2(C5 H10 N2 O3)
FORMUL 18 LYS 2(C6 H15 N2 O2 1+)
FORMUL 19 ZN 4(ZN 2+)
FORMUL 20 CL 4(CL 1-)
FORMUL 21 NA 2(NA 1+)
FORMUL 22 PEG 14(C4 H10 O3)
FORMUL 24 P6G 4(C12 H26 O7)
FORMUL 26 GLU 2(C5 H9 N O4)
FORMUL 27 VAL 2(C5 H11 N O2)
FORMUL 30 CA 2(CA 2+)
FORMUL 55 HOH *1649(H2 O)
HELIX 1 1 ASP A 2 GLN A 6 5 5
HELIX 2 2 ASP A 13 THR A 44 1 32
HELIX 3 3 THR A 47 GLU A 77 1 31
HELIX 4 4 PRO A 78 PHE A 83 5 6
HELIX 5 5 ASP A 85 ARG A 96 1 12
HELIX 6 6 LEU A 98 LEU A 103 5 6
HELIX 7 7 PRO A 104 ALA A 125 1 22
HELIX 8 8 PRO A 141 SER A 150 1 10
HELIX 9 9 SER A 152 GLN A 188 1 37
HELIX 10 10 ASP A 193 TRP A 201 1 9
HELIX 11 11 THR A 206 GLY A 238 1 33
HELIX 12 12 TRP A 261 ASN A 263 5 3
HELIX 13 13 ILE A 264 VAL A 269 1 6
HELIX 14 14 VAL A 279 GLN A 286 1 8
HELIX 15 15 GLN A 289 LEU A 304 1 16
HELIX 16 16 PRO A 310 SER A 317 1 8
HELIX 17 17 THR A 352 TYR A 372 1 21
HELIX 18 18 PRO A 376 ARG A 380 5 5
HELIX 19 19 ASN A 384 THR A 401 1 18
HELIX 20 20 THR A 401 ILE A 408 1 8
HELIX 21 21 ASP A 417 ILE A 433 1 17
HELIX 22 22 ALA A 434 SER A 451 1 18
HELIX 23 23 PRO A 455 SER A 457 5 3
HELIX 24 24 ARG A 458 GLY A 472 1 15
HELIX 25 25 PHE A 484 LYS A 489 5 6
HELIX 26 26 TYR A 498 ALA A 519 1 22
HELIX 27 27 PRO A 524 CYS A 528 5 5
HELIX 28 28 SER A 533 GLY A 547 1 15
HELIX 29 29 PRO A 551 GLY A 561 1 11
HELIX 30 30 ALA A 567 ASN A 588 1 22
HELIX 31 31 ASP B 2 GLN B 6 5 5
HELIX 32 32 ASP B 13 THR B 44 1 32
HELIX 33 33 THR B 47 GLU B 77 1 31
HELIX 34 34 ILE B 79 PHE B 83 5 5
HELIX 35 35 ASP B 85 ARG B 96 1 12
HELIX 36 36 LEU B 98 LEU B 103 5 6
HELIX 37 37 PRO B 104 ALA B 125 1 22
HELIX 38 38 PRO B 141 SER B 150 1 10
HELIX 39 39 SER B 152 GLN B 188 1 37
HELIX 40 40 ASP B 193 TRP B 201 1 9
HELIX 41 41 THR B 206 GLY B 238 1 33
HELIX 42 42 TRP B 261 ASN B 263 5 3
HELIX 43 43 ILE B 264 VAL B 269 1 6
HELIX 44 44 VAL B 279 GLN B 286 1 8
HELIX 45 45 GLN B 289 LEU B 304 1 16
HELIX 46 46 PRO B 310 SER B 317 1 8
HELIX 47 47 THR B 352 LYS B 373 1 22
HELIX 48 48 PRO B 376 ARG B 380 5 5
HELIX 49 49 ASN B 384 SER B 400 1 17
HELIX 50 50 THR B 401 ILE B 408 1 8
HELIX 51 51 ASP B 417 ILE B 433 1 17
HELIX 52 52 ALA B 434 GLY B 452 1 19
HELIX 53 53 PRO B 455 SER B 457 5 3
HELIX 54 54 ARG B 458 GLY B 472 1 15
HELIX 55 55 PHE B 484 LYS B 489 5 6
HELIX 56 56 TYR B 498 ALA B 519 1 22
HELIX 57 57 PRO B 524 CYS B 528 5 5
HELIX 58 58 SER B 533 GLY B 547 1 15
HELIX 59 59 PRO B 551 GLY B 561 1 11
HELIX 60 60 ALA B 567 ASN B 588 1 22
HELIX 61 61 ASP C 2 GLN C 6 5 5
HELIX 62 62 ASP C 13 THR C 44 1 32
HELIX 63 63 THR C 47 GLU C 77 1 31
HELIX 64 64 ILE C 79 PHE C 83 5 5
HELIX 65 65 ASP C 85 ARG C 96 1 12
HELIX 66 66 LEU C 98 LEU C 103 5 6
HELIX 67 67 PRO C 104 ALA C 125 1 22
HELIX 68 68 PRO C 141 SER C 150 1 10
HELIX 69 69 SER C 152 GLN C 188 1 37
HELIX 70 70 ASP C 193 TRP C 201 1 9
HELIX 71 71 THR C 206 GLY C 238 1 33
HELIX 72 72 TRP C 261 ASN C 263 5 3
HELIX 73 73 ILE C 264 VAL C 269 1 6
HELIX 74 74 VAL C 279 GLN C 286 1 8
HELIX 75 75 GLN C 289 LEU C 304 1 16
HELIX 76 76 PRO C 310 SER C 317 1 8
HELIX 77 77 THR C 352 LYS C 373 1 22
HELIX 78 78 PRO C 376 ARG C 380 5 5
HELIX 79 79 ASN C 384 SER C 400 1 17
HELIX 80 80 THR C 401 ILE C 408 1 8
HELIX 81 81 ASP C 417 ILE C 433 1 17
HELIX 82 82 ALA C 434 GLY C 452 1 19
HELIX 83 83 PRO C 455 SER C 457 5 3
HELIX 84 84 ARG C 458 GLY C 472 1 15
HELIX 85 85 PHE C 484 LYS C 489 5 6
HELIX 86 86 TYR C 498 ALA C 519 1 22
HELIX 87 87 PRO C 524 CYS C 528 5 5
HELIX 88 88 SER C 533 GLY C 547 1 15
HELIX 89 89 PRO C 551 GLY C 561 1 11
HELIX 90 90 ALA C 567 GLY C 589 1 23
HELIX 91 91 ILE C 611 THR C 615 5 5
HELIX 92 92 ASP D 2 GLN D 6 5 5
HELIX 93 93 ASP D 13 THR D 44 1 32
HELIX 94 94 THR D 47 GLU D 77 1 31
HELIX 95 95 ILE D 79 PHE D 83 5 5
HELIX 96 96 ASP D 85 ARG D 96 1 12
HELIX 97 97 LEU D 98 LEU D 103 5 6
HELIX 98 98 PRO D 104 ALA D 125 1 22
HELIX 99 99 PRO D 141 SER D 150 1 10
HELIX 100 100 SER D 152 GLN D 188 1 37
HELIX 101 101 ASP D 193 TRP D 201 1 9
HELIX 102 102 THR D 206 GLY D 238 1 33
HELIX 103 103 TRP D 261 ASN D 263 5 3
HELIX 104 104 ILE D 264 VAL D 269 1 6
HELIX 105 105 VAL D 279 GLN D 286 1 8
HELIX 106 106 GLN D 289 LEU D 304 1 16
HELIX 107 107 PRO D 310 SER D 317 1 8
HELIX 108 108 THR D 352 LYS D 373 1 22
HELIX 109 109 PRO D 376 ARG D 380 5 5
HELIX 110 110 ASN D 384 SER D 400 1 17
HELIX 111 111 THR D 401 ILE D 408 1 8
HELIX 112 112 ASP D 417 ILE D 433 1 17
HELIX 113 113 ALA D 434 SER D 451 1 18
HELIX 114 114 PRO D 455 SER D 457 5 3
HELIX 115 115 ARG D 458 GLY D 472 1 15
HELIX 116 116 PHE D 484 LYS D 489 5 6
HELIX 117 117 TYR D 498 ALA D 519 1 22
HELIX 118 118 PRO D 524 CYS D 528 5 5
HELIX 119 119 SER D 533 GLY D 547 1 15
HELIX 120 120 PRO D 551 GLY D 561 1 11
HELIX 121 121 ALA D 567 ASN D 588 1 22
SHEET 1 AA 2 LYS A 126 CYS A 128 0
SHEET 2 AA 2 CYS A 136 SER A 138 -1 O TRP A 137 N VAL A 127
SHEET 1 AB 2 ILE A 248 PRO A 249 0
SHEET 2 AB 2 ILE A 473 CYS A 474 1 N CYS A 474 O ILE A 248
SHEET 1 AC 2 SER A 333 ASP A 336 0
SHEET 2 AC 2 PHE A 343 LYS A 346 -1 O ARG A 344 N TRP A 335
SHEET 1 BA 2 LYS B 126 VAL B 127 0
SHEET 2 BA 2 TRP B 137 SER B 138 -1 O TRP B 137 N VAL B 127
SHEET 1 BB 2 ILE B 248 PRO B 249 0
SHEET 2 BB 2 ILE B 473 CYS B 474 1 N CYS B 474 O ILE B 248
SHEET 1 BC 2 SER B 333 ASP B 336 0
SHEET 2 BC 2 PHE B 343 LYS B 346 -1 O ARG B 344 N TRP B 335
SHEET 1 CA 2 LYS C 126 CYS C 128 0
SHEET 2 CA 2 CYS C 136 SER C 138 -1 O TRP C 137 N VAL C 127
SHEET 1 CB 2 ILE C 248 PRO C 249 0
SHEET 2 CB 2 ILE C 473 CYS C 474 1 N CYS C 474 O ILE C 248
SHEET 1 CC 2 SER C 333 ASP C 336 0
SHEET 2 CC 2 PHE C 343 LYS C 346 -1 O ARG C 344 N TRP C 335
SHEET 1 DA 2 LYS D 126 VAL D 127 0
SHEET 2 DA 2 TRP D 137 SER D 138 -1 O TRP D 137 N VAL D 127
SHEET 1 DB 2 ILE D 248 PRO D 249 0
SHEET 2 DB 2 ILE D 473 CYS D 474 1 N CYS D 474 O ILE D 248
SHEET 1 DC 2 SER D 333 ASP D 336 0
SHEET 2 DC 2 PHE D 343 LYS D 346 -1 O ARG D 344 N TRP D 335
SSBOND 1 CYS A 128 CYS A 136 1555 1555 2.06
SSBOND 2 CYS A 330 CYS A 348 1555 1555 2.07
SSBOND 3 CYS A 516 CYS A 528 1555 1555 2.02
SSBOND 4 CYS B 128 CYS B 136 1555 1555 2.05
SSBOND 5 CYS B 330 CYS B 348 1555 1555 2.07
SSBOND 6 CYS B 516 CYS B 528 1555 1555 2.03
SSBOND 7 CYS C 128 CYS C 136 1555 1555 2.07
SSBOND 8 CYS C 330 CYS C 348 1555 1555 2.03
SSBOND 9 CYS C 516 CYS C 528 1555 1555 2.04
SSBOND 10 CYS D 128 CYS D 136 1555 1555 2.04
SSBOND 11 CYS D 330 CYS D 348 1555 1555 2.02
SSBOND 12 CYS D 516 CYS D 528 1555 1555 2.04
LINK ND2 ASN A 45 C1 NAG F 1 1555 1555 1.44
LINK ND2 ASN A 416 C1 NAG G 1 1555 1555 1.44
LINK ND2 ASN A 480 C1 NAG E 1 1555 1555 1.44
LINK ND2 ASN B 45 C1 NAG I 1 1555 1555 1.42
LINK ND2 ASN B 416 C1 NAG J 1 1555 1555 1.42
LINK ND2 ASN B 480 C1 NAG H 1 1555 1555 1.45
LINK ND2 ASN C 45 C1 NAG L 1 1555 1555 1.45
LINK ND2 ASN C 416 C1 NAG M 1 1555 1555 1.44
LINK ND2 ASN C 480 C1 NAG K 1 1555 1555 1.46
LINK ND2 ASN D 45 C1 NAG O 1 1555 1555 1.44
LINK ND2 ASN D 416 C1 NAG P 1 1555 1555 1.44
LINK ND2 ASN D 480 C1 NAG N 1 1555 1555 1.46
LINK O6 NAG E 1 C1 FUL E 2 1555 1555 1.44
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.46
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.44
LINK O4 NAG G 2 C1 MAN G 3 1555 1555 1.46
LINK O6 NAG H 1 C1 FUC H 2 1555 1555 1.45
LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.44
LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.44
LINK O4 NAG J 2 C1 MAN J 3 1555 1555 1.46
LINK O6 NAG K 1 C1 FUC K 2 1555 1555 1.45
LINK O4 NAG L 1 C1 NAG L 2 1555 1555 1.44
LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.43
LINK O6 NAG M 1 C1 FUC M 4 1555 1555 1.46
LINK O4 NAG M 2 C1 BMA M 3 1555 1555 1.44
LINK O6 NAG N 1 C1 FUC N 2 1555 1555 1.44
LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.45
LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.44
LINK O6 NAG P 1 C1 FUC P 4 1555 1555 1.44
LINK O4 NAG P 2 C1 BMA P 3 1555 1555 1.44
LINK OE2 GLU A 262 NA NA A1003 1555 1555 2.26
LINK OD1 ASN A 263 NA NA A1003 1555 1555 2.71
LINK OD2 ASP A 354 NA NA A1003 1555 1555 2.36
LINK NE2 HIS A 361 ZN ZN A1001 1555 1555 2.07
LINK NE2 HIS A 365 ZN ZN A1001 1555 1555 2.06
LINK OE1 GLU A 389 ZN ZN A1001 1555 1555 1.95
LINK ZN ZN A1001 O HOH A2273 1555 1555 2.02
LINK NA NA A1003 O HOH A2208 1555 1555 2.29
LINK NA NA A1003 O HOH A2211 1555 1555 2.35
LINK NA NA A1003 O HOH A2213 1555 1555 2.55
LINK OE2 GLU B 262 CA CA B1003 1555 1555 2.11
LINK OD1 ASN B 263 CA CA B1003 1555 1555 2.65
LINK OD2 ASP B 354 CA CA B1003 1555 1555 2.47
LINK NE2 HIS B 361 ZN ZN B1001 1555 1555 2.07
LINK NE2 HIS B 365 ZN ZN B1001 1555 1555 2.09
LINK OE1 GLU B 389 ZN ZN B1001 1555 1555 1.95
LINK ZN ZN B1001 O HOH B2273 1555 1555 2.07
LINK CA CA B1003 O HOH B2198 1555 1555 2.35
LINK CA CA B1003 O HOH B2205 1555 1555 2.46
LINK CA CA B1003 O HOH B2207 1555 1555 2.67
LINK OE2 GLU C 262 CA CA C1003 1555 1555 2.22
LINK OD1 ASN C 263 CA CA C1003 1555 1555 2.51
LINK OD2 ASP C 354 CA CA C1003 1555 1555 2.39
LINK NE2 HIS C 361 ZN ZN C1001 1555 1555 2.11
LINK NE2 HIS C 365 ZN ZN C1001 1555 1555 2.12
LINK OE1 GLU C 389 ZN ZN C1001 1555 1555 1.89
LINK ZN ZN C1001 O HOH C2329 1555 1555 2.06
LINK CA CA C1003 O HOH C2244 1555 1555 2.33
LINK CA CA C1003 O HOH C2250 1555 1555 2.31
LINK CA CA C1003 O HOH C2252 1555 1555 2.47
LINK OE2 GLU D 262 NA NA D1003 1555 1555 2.22
LINK OD1 ASN D 263 NA NA D1003 1555 1555 2.89
LINK OD2 ASP D 354 NA NA D1003 1555 1555 2.37
LINK NE2 HIS D 361 ZN ZN D1001 1555 1555 2.13
LINK NE2 HIS D 365 ZN ZN D1001 1555 1555 2.04
LINK OE1 GLU D 389 ZN ZN D1001 1555 1555 1.94
LINK ZN ZN D1001 O HOH D2277 1555 1555 2.00
LINK NA NA D1003 O HOH D2202 1555 1555 2.00
LINK NA NA D1003 O HOH D2208 1555 1555 2.45
CISPEP 1 ASP A 140 PRO A 141 0 10.79
CISPEP 2 TYR A 607 PRO A 608 0 -6.97
CISPEP 3 ASP B 140 PRO B 141 0 12.80
CISPEP 4 TYR B 607 PRO B 608 0 -0.78
CISPEP 5 ASP C 140 PRO C 141 0 17.85
CISPEP 6 TYR C 607 PRO C 608 0 1.74
CISPEP 7 ASP D 140 PRO D 141 0 14.30
CISPEP 8 TYR D 607 PRO D 608 0 1.41
CRYST1 73.348 101.800 113.950 85.04 85.55 81.88 P 1 4
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 0.013634 -0.001945 -0.000915 0.00000
SCALE2 0.000000 0.009923 -0.000761 0.00000
SCALE3 0.000000 0.000000 0.008828 0.00000
(ATOM LINES ARE NOT SHOWN.)
END