HEADER HYDROLASE 12-JUL-13 4BXK
TITLE CRYSTAL STRUCTURE OF THE ANGIOTENSIN-1 CONVERTING ENZYME N-DOMAIN IN
TITLE 2 COMPLEX WITH A DOMAIN-SPECIFIC INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANGIOTENSIN-CONVERTING ENZYME;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: N DOMAIN, RESIDUES 30-657;
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
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, PROTEASE INHIBITOR
EXPDTA X-RAY DIFFRACTION
AUTHOR R.G.DOUGLAS,R.K.SHARMA,G.MASUYER,L.LUBBE,I.ZAMORA,K.R.ACHARYA,
AUTHOR 2 K.CHIBALE,E.D.STURROCK
REVDAT 6 20-DEC-23 4BXK 1 HETSYN
REVDAT 5 29-JUL-20 4BXK 1 COMPND REMARK HETNAM LINK
REVDAT 5 2 1 SITE ATOM
REVDAT 4 13-NOV-13 4BXK 1 REMARK LINK ATOM ANISOU
REVDAT 3 06-NOV-13 4BXK 1 JRNL
REVDAT 2 25-SEP-13 4BXK 1 JRNL LINK
REVDAT 1 18-SEP-13 4BXK 0
JRNL AUTH R.G.DOUGLAS,R.K.SHARMA,G.MASUYER,L.LUBBE,I.ZAMORA,
JRNL AUTH 2 K.R.ACHARYA,K.CHIBALE,E.D.STURROCK
JRNL TITL FRAGMENT-BASED DESIGN FOR THE DEVELOPMENT OF N-DOMAIN
JRNL TITL 2 SELECTIVE ANGIOTENSIN-1 CONVERTING ENZYME INHIBITORS
JRNL REF CLIN.SCI. V. 126 305 2014
JRNL REFN ISSN 0143-5221
JRNL PMID 24015848
JRNL DOI 10.1042/CS20130403
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.69
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.4
REMARK 3 NUMBER OF REFLECTIONS : 69351
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) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3660
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4914
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.48
REMARK 3 BIN R VALUE (WORKING SET) : 0.2770
REMARK 3 BIN FREE R VALUE SET COUNT : 257
REMARK 3 BIN FREE R VALUE : 0.3150
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9885
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 329
REMARK 3 SOLVENT ATOMS : 409
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.29000
REMARK 3 B22 (A**2) : 0.12000
REMARK 3 B33 (A**2) : 0.65000
REMARK 3 B12 (A**2) : 1.99000
REMARK 3 B13 (A**2) : 0.63000
REMARK 3 B23 (A**2) : 0.08000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.272
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.199
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.146
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.844
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.932
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10576 ; 0.008 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 9612 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14406 ; 1.183 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): 22017 ; 0.807 ; 3.003
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1220 ; 5.589 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 532 ;35.227 ;23.797
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1596 ;14.102 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 65 ;14.779 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1510 ; 0.067 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11905 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2626 ; 0.001 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 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 30 A 610
REMARK 3 ORIGIN FOR THE GROUP (A): 1.6645 -15.5400 -18.6678
REMARK 3 T TENSOR
REMARK 3 T11: 0.0112 T22: 0.0974
REMARK 3 T33: 0.0348 T12: -0.0046
REMARK 3 T13: -0.0051 T23: -0.0178
REMARK 3 L TENSOR
REMARK 3 L11: 0.3541 L22: 0.4082
REMARK 3 L33: 0.0320 L12: -0.1086
REMARK 3 L13: -0.0999 L23: 0.0415
REMARK 3 S TENSOR
REMARK 3 S11: 0.0410 S12: -0.0067 S13: -0.0163
REMARK 3 S21: -0.0534 S22: -0.0332 S23: -0.0029
REMARK 3 S31: -0.0115 S32: -0.0042 S33: -0.0078
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 30 B 610
REMARK 3 ORIGIN FOR THE GROUP (A): -2.0424 14.6842 18.7376
REMARK 3 T TENSOR
REMARK 3 T11: 0.0270 T22: 0.0506
REMARK 3 T33: 0.0314 T12: -0.0226
REMARK 3 T13: -0.0092 T23: -0.0203
REMARK 3 L TENSOR
REMARK 3 L11: 0.0653 L22: 0.5265
REMARK 3 L33: 0.8745 L12: -0.1821
REMARK 3 L13: -0.1475 L23: 0.3786
REMARK 3 S TENSOR
REMARK 3 S11: 0.0105 S12: 0.0041 S13: -0.0027
REMARK 3 S21: -0.0005 S22: -0.0109 S23: -0.0074
REMARK 3 S31: 0.0057 S32: -0.0611 S33: 0.0004
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. RESIDUES 130-132 ARE DISORDERED
REMARK 4
REMARK 4 4BXK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-JUL-13.
REMARK 100 THE DEPOSITION ID IS D_1290057666.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-DEC-12
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 : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.920
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 73018
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 29.670
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.4
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.85000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
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
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, C, D, E
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, 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 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 PRO B 130
REMARK 465 GLN B 131
REMARK 465 LYS B 132
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 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 A 56 CD OE1 OE2
REMARK 470 LEU A 129 CG CD1 CD2
REMARK 470 LYS A 341 CD CE NZ
REMARK 470 LYS A 542 CE NZ
REMARK 470 GLU B 56 CD OE1 OE2
REMARK 470 LYS B 341 CD CE NZ
REMARK 470 ARG B 413 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 542 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 DISTANCE
REMARK 500 ND2 ASN B 480 C2 NAG B 1612 1.53
REMARK 500 OG SER B 260 OE1 GLU B 262 1.86
REMARK 500 OG1 THR B 282 O HOH B 2082 2.18
REMARK 500 O CYS A 330 O HOH A 2150 2.19
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 80.04 -172.15
REMARK 500 ASN A 203 64.45 30.04
REMARK 500 ASN A 203 68.03 25.70
REMARK 500 ASP A 324 -173.56 -67.07
REMARK 500 ALA B 12 49.65 -88.52
REMARK 500 ASN B 45 79.68 -175.26
REMARK 500 ALA B 134 -86.69 -73.52
REMARK 500 GLN B 575 -53.86 -28.64
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 P6G A 704
REMARK 610 PG4 B 704
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 ZN A1620 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 361 NE2
REMARK 620 2 HIS A 365 NE2 105.3
REMARK 620 3 GLU A 389 OE1 91.7 99.7
REMARK 620 4 1IU A1001 OAH 115.7 131.5 103.5
REMARK 620 5 1IU A1001 OAI 99.4 83.2 167.3 66.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1619 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 361 NE2
REMARK 620 2 HIS B 365 NE2 100.1
REMARK 620 3 GLU B 389 OE1 91.6 107.1
REMARK 620 4 1IU B1001 OAH 109.1 137.8 102.0
REMARK 620 5 1IU B1001 OAI 98.0 80.9 166.3 65.7
REMARK 620 N 1 2 3 4
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 N-DOMAIN WITH MUTATIONS N9Q, N25Q, N82Q, N117Q, N131Q,
REMARK 999 N289Q, Q545R, P576L, R629L (SIMILAR CONSTRUCT TO PDB 3NXQ)
DBREF 4BXK A 1 628 UNP P12821 ACE_HUMAN 30 657
DBREF 4BXK B 1 628 UNP P12821 ACE_HUMAN 30 657
SEQADV 4BXK LEU A 629 UNP P12821 EXPRESSION TAG
SEQADV 4BXK GLN A 9 UNP P12821 ASN 38 ENGINEERED MUTATION
SEQADV 4BXK GLN A 25 UNP P12821 ASN 54 ENGINEERED MUTATION
SEQADV 4BXK GLN A 82 UNP P12821 ASN 111 ENGINEERED MUTATION
SEQADV 4BXK GLN A 117 UNP P12821 ASN 146 ENGINEERED MUTATION
SEQADV 4BXK GLN A 131 UNP P12821 ASN 160 ENGINEERED MUTATION
SEQADV 4BXK GLN A 289 UNP P12821 ASN 318 ENGINEERED MUTATION
SEQADV 4BXK ARG A 545 UNP P12821 GLN 574 ENGINEERED MUTATION
SEQADV 4BXK LEU A 576 UNP P12821 PRO 605 ENGINEERED MUTATION
SEQADV 4BXK LEU B 629 UNP P12821 EXPRESSION TAG
SEQADV 4BXK GLN B 9 UNP P12821 ASN 38 ENGINEERED MUTATION
SEQADV 4BXK GLN B 25 UNP P12821 ASN 54 ENGINEERED MUTATION
SEQADV 4BXK GLN B 82 UNP P12821 ASN 111 ENGINEERED MUTATION
SEQADV 4BXK GLN B 117 UNP P12821 ASN 146 ENGINEERED MUTATION
SEQADV 4BXK GLN B 131 UNP P12821 ASN 160 ENGINEERED MUTATION
SEQADV 4BXK GLN B 289 UNP P12821 ASN 318 ENGINEERED MUTATION
SEQADV 4BXK ARG B 545 UNP P12821 GLN 574 ENGINEERED MUTATION
SEQADV 4BXK LEU B 576 UNP P12821 PRO 605 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
MODRES 4BXK ASN A 45 ASN GLYCOSYLATION SITE
MODRES 4BXK ASN A 416 ASN GLYCOSYLATION SITE
MODRES 4BXK ASN A 480 ASN GLYCOSYLATION SITE
MODRES 4BXK ASN B 45 ASN GLYCOSYLATION SITE
MODRES 4BXK ASN B 416 ASN GLYCOSYLATION SITE
MODRES 4BXK ASN B 480 ASN GLYCOSYLATION SITE
HET NAG C 1 14
HET FUC C 2 10
HET NAG D 1 14
HET NAG D 2 14
HET NAG E 1 14
HET NAG E 2 14
HET BMA E 3 11
HET FUC E 4 10
HET NAG F 1 14
HET NAG F 2 14
HET NAG G 1 14
HET NAG G 2 14
HET BMA G 3 11
HET PEG A 701 7
HET PEG A 702 7
HET PEG A 703 7
HET P6G A 704 13
HET 1IU A1001 33
HET ZN A1620 1
HET CL A1621 1
HET PEG B 701 7
HET PG4 B 704 10
HET P6G B 709 19
HET PEG B 711 7
HET 1IU B1001 33
HET NAG B1612 14
HET ZN B1619 1
HET CL B1620 1
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM P6G HEXAETHYLENE GLYCOL
HETNAM 1IU [3-[[(2S)-1-AZANYL-1-OXIDANYLIDENE-PROPAN-2-YL]AMINO]-
HETNAM 2 1IU 2-METHYL-3-OXIDANYLIDENE-PROPYL]-[(1R)-1-[[(2R)-2-
HETNAM 3 1IU AZANYL-3-(1H-1,2,3,4-TETRAZOL-5-YL)PROPANOYL]AMINO]-2-
HETNAM 4 1IU PHENYL-ETHYL]PHOSPHINIC ACID
HETNAM ZN ZINC ION
HETNAM CL CHLORIDE ION
HETNAM PG4 TETRAETHYLENE GLYCOL
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 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 3 NAG 10(C8 H15 N O6)
FORMUL 3 FUC 2(C6 H12 O5)
FORMUL 5 BMA 2(C6 H12 O6)
FORMUL 8 PEG 5(C4 H10 O3)
FORMUL 11 P6G 2(C12 H26 O7)
FORMUL 12 1IU 2(C19 H29 N8 O5 P)
FORMUL 13 ZN 2(ZN 2+)
FORMUL 14 CL 2(CL 1-)
FORMUL 16 PG4 C8 H18 O5
FORMUL 23 HOH *409(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 ILE A 79 PHE A 83 5 5
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 SER A 200 1 8
HELIX 11 11 TRP A 201 ASN A 203 5 3
HELIX 12 12 THR A 206 GLY A 238 1 33
HELIX 13 13 TRP A 261 ASN A 263 5 3
HELIX 14 14 ILE A 264 VAL A 269 1 6
HELIX 15 15 VAL A 279 GLY A 287 1 9
HELIX 16 16 GLN A 289 LEU A 304 1 16
HELIX 17 17 PRO A 310 SER A 317 1 8
HELIX 18 18 THR A 352 TYR A 372 1 21
HELIX 19 19 PRO A 376 ARG A 380 5 5
HELIX 20 20 ASN A 384 SER A 400 1 17
HELIX 21 21 THR A 401 ILE A 408 1 8
HELIX 22 22 ASP A 417 ILE A 433 1 17
HELIX 23 23 ALA A 434 SER A 451 1 18
HELIX 24 24 PRO A 455 SER A 457 5 3
HELIX 25 25 ARG A 458 GLY A 472 1 15
HELIX 26 26 PHE A 484 LYS A 489 5 6
HELIX 27 27 TYR A 498 ALA A 519 1 22
HELIX 28 28 PRO A 524 CYS A 528 5 5
HELIX 29 29 SER A 533 GLY A 547 1 15
HELIX 30 30 PRO A 551 GLY A 561 1 11
HELIX 31 31 ALA A 567 ASN A 588 1 22
HELIX 32 32 ASP B 2 GLN B 6 5 5
HELIX 33 33 ASP B 13 THR B 44 1 32
HELIX 34 34 THR B 47 GLU B 77 1 31
HELIX 35 35 ILE B 79 PHE B 83 5 5
HELIX 36 36 ASP B 85 THR B 97 1 13
HELIX 37 37 LEU B 98 LEU B 103 5 6
HELIX 38 38 PRO B 104 ALA B 125 1 22
HELIX 39 39 PRO B 141 SER B 150 1 10
HELIX 40 40 SER B 152 GLN B 188 1 37
HELIX 41 41 ASP B 193 TRP B 201 1 9
HELIX 42 42 THR B 206 GLY B 238 1 33
HELIX 43 43 TRP B 261 ASN B 263 5 3
HELIX 44 44 ILE B 264 VAL B 269 1 6
HELIX 45 45 VAL B 279 GLY B 287 1 9
HELIX 46 46 GLN B 289 LEU B 304 1 16
HELIX 47 47 PRO B 310 SER B 317 1 8
HELIX 48 48 THR B 352 LYS B 373 1 22
HELIX 49 49 PRO B 376 ARG B 380 5 5
HELIX 50 50 ASN B 384 ILE B 408 1 25
HELIX 51 51 ASP B 417 ILE B 433 1 17
HELIX 52 52 PHE B 435 SER B 451 1 17
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 ALA B 546 1 14
HELIX 59 59 PRO B 551 GLY B 561 1 11
HELIX 60 60 ALA B 567 GLY B 589 1 23
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 CYS B 128 0
SHEET 2 BA 2 CYS B 136 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
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 2.03
SSBOND 4 CYS B 128 CYS B 136 1555 1555 2.06
SSBOND 5 CYS B 330 CYS B 348 1555 1555 2.11
SSBOND 6 CYS B 516 CYS B 528 1555 1555 2.04
LINK ND2 ASN A 45 C1 NAG D 1 1555 1555 1.44
LINK ND2 ASN A 416 C1 NAG E 1 1555 1555 1.45
LINK ND2 ASN A 480 C1 NAG C 1 1555 1555 1.45
LINK ND2 ASN B 45 C1 NAG F 1 1555 1555 1.45
LINK ND2 ASN B 416 C1 NAG G 1 1555 1555 1.45
LINK ND2 ASN B 480 C1 NAG B1612 1555 1555 1.44
LINK O6 NAG C 1 C1 FUC C 2 1555 1555 1.44
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44
LINK O6 NAG E 1 C1 FUC E 4 1555 1555 1.44
LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.45
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.44
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.45
LINK O4 NAG G 2 C1 BMA G 3 1555 1555 1.45
LINK NE2 HIS A 361 ZN ZN A1620 1555 1555 2.14
LINK NE2 HIS A 365 ZN ZN A1620 1555 1555 2.08
LINK OE1 GLU A 389 ZN ZN A1620 1555 1555 2.03
LINK OAH 1IU A1001 ZN ZN A1620 1555 1555 1.99
LINK OAI 1IU A1001 ZN ZN A1620 1555 1555 2.51
LINK NE2 HIS B 361 ZN ZN B1619 1555 1555 2.12
LINK NE2 HIS B 365 ZN ZN B1619 1555 1555 2.11
LINK OE1 GLU B 389 ZN ZN B1619 1555 1555 2.08
LINK OAH 1IU B1001 ZN ZN B1619 1555 1555 2.11
LINK OAI 1IU B1001 ZN ZN B1619 1555 1555 2.43
CISPEP 1 ASP A 140 PRO A 141 0 8.48
CISPEP 2 TYR A 607 PRO A 608 0 -4.71
CISPEP 3 ASP B 140 PRO B 141 0 12.58
CISPEP 4 TYR B 607 PRO B 608 0 2.54
CRYST1 73.142 77.255 82.866 88.43 64.28 75.29 P 1 2
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 0.013672 -0.003589 -0.006958 0.00000
SCALE2 0.000000 0.013383 0.001277 0.00000
SCALE3 0.000000 0.000000 0.013456 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
