HEADER HYDROLASE 13-DEC-04 1Y8J
TITLE CRYSTAL STRUCTURE OF HUMAN NEP COMPLEXED WITH AN IMIDAZO[4,5-
TITLE 2 C]PYRIDINE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEPRILYSIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: EXTRACELLULAR DOMAIN (RESIDUES 54-179);
COMPND 5 SYNONYM: NEUTRAL ENDOPEPTIDASE, NEP, ENKEPHALINASE, COMMON ACUTE
COMPND 6 LYMPHOCYTIC LEUKEMIA ANTIGEN, CALLA, NEUTRAL ENDOPEPTIDASE 24.11,
COMPND 7 CD10;
COMPND 8 EC: 3.4.24.11;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: MME, EPN;
SOURCE 6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 4932
KEYWDS LT1_6, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.SAHLI,B.FRANK,W.B.SCHWEIZER,F.DIEDERICH,D.BLUM-KAELIN,J.D.AEBI,
AUTHOR 2 H.J.BOHM,C.OEFNER,G.E.DALE
REVDAT 5 23-AUG-23 1Y8J 1 HETSYN
REVDAT 4 29-JUL-20 1Y8J 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE
REVDAT 3 13-JUL-11 1Y8J 1 VERSN
REVDAT 2 24-FEB-09 1Y8J 1 VERSN
REVDAT 1 07-JUN-05 1Y8J 0
JRNL AUTH S.SAHLI,B.FRANK,W.B.SCHWEIZER,F.DIEDERICH,D.BLUM-KAELIN,
JRNL AUTH 2 J.D.AEBI,H.J.BOHM,C.OEFNER,G.E.DALE
JRNL TITL SECOND-GENERATION INHIBITORS FOR THE METALLOPROTEASE
JRNL TITL 2 NEPRILYSIN BASED ON BICYCLIC HETEROAROMATIC SCAFFOLDS:
JRNL TITL 3 SYNTHESIS, BIOLOGICAL ACTIVITY, AND X-RAY CRYSTAL STRUCTURE
JRNL TITL 4 ANALYSIS
JRNL REF HELV.CHIM.ACTA V. 88 731 2005
JRNL REFN ISSN 0018-019X
JRNL DOI 10.1002/HLCA.200590051
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
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) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 3 NUMBER OF REFLECTIONS : 32573
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) : 0.230
REMARK 3 R VALUE (WORKING SET) : 0.226
REMARK 3 FREE R VALUE : 0.296
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1732
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.37
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4074
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2710
REMARK 3 BIN FREE R VALUE SET COUNT : 206
REMARK 3 BIN FREE R VALUE : 0.3400
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5595
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 66
REMARK 3 SOLVENT ATOMS : 212
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.67
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.32000
REMARK 3 B22 (A**2) : 0.32000
REMARK 3 B33 (A**2) : -0.48000
REMARK 3 B12 (A**2) : 0.16000
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): 0.423
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.293
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.310
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.474
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.917
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.866
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5788 ; 0.007 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 5066 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7834 ; 0.889 ; 1.954
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11826 ; 0.552 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 695 ; 9.083 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1037 ;24.031 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 840 ; 0.047 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6441 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1164 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1712 ; 0.299 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 5669 ; 0.278 ; 0.300
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 3 ; 0.749 ; 0.500
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 327 ; 0.208 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): 18 ; 0.182 ; 0.500
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 1 ; 0.161 ; 0.500
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 39 ; 0.664 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): 36 ; 0.437 ; 0.300
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 5 ; 0.472 ; 0.500
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): 3464 ; 1.899 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5574 ; 2.933 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2324 ; 1.925 ; 2.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2260 ; 2.951 ; 3.000
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 1Y8J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JAN-05.
REMARK 100 THE DEPOSITION ID IS D_1000031250.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-AUG-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : ENRAF-NONIUS FR591
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : OSMIC MIRROR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34323
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
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 (%) : 95.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.39
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.9
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 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1DMT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500005 -0.866017 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866033 -0.499995 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 74.97733
REMARK 290 SMTRY1 3 -0.499995 0.866017 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866033 -0.500005 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 37.48867
REMARK 290 SMTRY1 4 -0.500005 0.866012 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866033 0.500005 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 37.48867
REMARK 290 SMTRY1 6 -0.499995 -0.866023 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866033 0.499995 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 74.97733
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O GLN A 518 CD2 LEU A 522 1.42
REMARK 500 NZ LYS A 209 CD1 TYR A 299 1.61
REMARK 500 NH1 ARG A 256 O PRO A 262 1.73
REMARK 500 O GLN A 257 O HOH A 937 1.85
REMARK 500 CE LYS A 209 CE1 TYR A 299 1.93
REMARK 500 O LYS A 353 CD1 ILE A 357 1.94
REMARK 500 OH TYR A 661 OE1 GLU A 671 2.03
REMARK 500 CE MET A 579 O HOH A 909 2.10
REMARK 500 NH2 ARG A 140 OE1 GLU A 503 2.11
REMARK 500 NZ LYS A 209 CE1 TYR A 299 2.13
REMARK 500 O ASP A 530 NH2 ARG A 549 2.14
REMARK 500 OG SER A 612 O HOH A 1036 2.15
REMARK 500 OH TYR A 496 O HOH A 1003 2.16
REMARK 500 O TYR A 177 N SER A 180 2.17
REMARK 500 OD2 ASP A 604 O HOH A 1037 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE1 GLN A 175 O ARG A 260 5555 1.52
REMARK 500 OE1 GLN A 175 C ARG A 260 5555 1.58
REMARK 500 OE1 GLN A 175 N LEU A 261 5555 1.84
REMARK 500 OE1 GLN A 175 CA LEU A 261 5555 1.88
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 ALA A 179 -91.00 -34.67
REMARK 500 LEU A 199 -63.51 67.11
REMARK 500 ARG A 260 79.82 32.66
REMARK 500 PHE A 311 56.66 -145.82
REMARK 500 ASN A 316 -55.74 71.79
REMARK 500 LYS A 318 -95.30 -151.33
REMARK 500 PRO A 319 -141.59 -99.03
REMARK 500 ASN A 339 -5.53 -44.47
REMARK 500 ALA A 347 46.68 -143.63
REMARK 500 THR A 359 -6.61 -55.35
REMARK 500 MET A 376 -51.78 -17.39
REMARK 500 LEU A 382 -166.80 -102.09
REMARK 500 MET A 418 55.91 -143.06
REMARK 500 ASN A 550 58.86 39.39
REMARK 500 ALA A 556 -49.58 -29.50
REMARK 500 ASN A 737 1.73 89.51
REMARK 500 VAL A 748 -71.94 -118.70
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 TRP A 181 THR A 182 139.40
REMARK 500 PRO A 319 PHE A 320 -146.22
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 800 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 583 NE2
REMARK 620 2 HIS A 587 NE2 86.5
REMARK 620 3 GLU A 646 OE1 91.1 112.3
REMARK 620 4 STS A 900 S10 120.5 126.0 112.7
REMARK 620 N 1 2 3
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1R1J RELATED DB: PDB
REMARK 900 RELATED ID: 1R1I RELATED DB: PDB
REMARK 900 RELATED ID: 1R1H RELATED DB: PDB
REMARK 900 RELATED ID: 1DMT RELATED DB: PDB
DBREF 1Y8J A 54 749 UNP P08473 NEP_HUMAN 54 749
SEQRES 1 A 696 GLY ILE CYS LYS SER SER ASP CYS ILE LYS SER ALA ALA
SEQRES 2 A 696 ARG LEU ILE GLN ASN MET ASP ALA THR THR GLU PRO CYS
SEQRES 3 A 696 THR ASP PHE PHE LYS TYR ALA CYS GLY GLY TRP LEU LYS
SEQRES 4 A 696 ARG ASN VAL ILE PRO GLU THR SER SER ARG TYR GLY ASN
SEQRES 5 A 696 PHE ASP ILE LEU ARG ASP GLU LEU GLU VAL VAL LEU LYS
SEQRES 6 A 696 ASP VAL LEU GLN GLU PRO LYS THR GLU ASP ILE VAL ALA
SEQRES 7 A 696 VAL GLN LYS ALA LYS ALA LEU TYR ARG SER CYS ILE ASN
SEQRES 8 A 696 GLU SER ALA ILE ASP SER ARG GLY GLY GLU PRO LEU LEU
SEQRES 9 A 696 LYS LEU LEU PRO ASP ILE TYR GLY TRP PRO VAL ALA THR
SEQRES 10 A 696 GLU ASN TRP GLU GLN LYS TYR GLY ALA SER TRP THR ALA
SEQRES 11 A 696 GLU LYS ALA ILE ALA GLN LEU ASN SER LYS TYR GLY LYS
SEQRES 12 A 696 LYS VAL LEU ILE ASN LEU PHE VAL GLY THR ASP ASP LYS
SEQRES 13 A 696 ASN SER VAL ASN HIS VAL ILE HIS ILE ASP GLN PRO ARG
SEQRES 14 A 696 LEU GLY LEU PRO SER ARG ASP TYR TYR GLU CYS THR GLY
SEQRES 15 A 696 ILE TYR LYS GLU ALA CYS THR ALA TYR VAL ASP PHE MET
SEQRES 16 A 696 ILE SER VAL ALA ARG LEU ILE ARG GLN GLU GLU ARG LEU
SEQRES 17 A 696 PRO ILE ASP GLU ASN GLN LEU ALA LEU GLU MET ASN LYS
SEQRES 18 A 696 VAL MET GLU LEU GLU LYS GLU ILE ALA ASN ALA THR ALA
SEQRES 19 A 696 LYS PRO GLU ASP ARG ASN ASP PRO MET LEU LEU TYR ASN
SEQRES 20 A 696 LYS MET THR LEU ALA GLN ILE GLN ASN ASN PHE SER LEU
SEQRES 21 A 696 GLU ILE ASN GLY LYS PRO PHE SER TRP LEU ASN PHE THR
SEQRES 22 A 696 ASN GLU ILE MET SER THR VAL ASN ILE SER ILE THR ASN
SEQRES 23 A 696 GLU GLU ASP VAL VAL VAL TYR ALA PRO GLU TYR LEU THR
SEQRES 24 A 696 LYS LEU LYS PRO ILE LEU THR LYS TYR SER ALA ARG ASP
SEQRES 25 A 696 LEU GLN ASN LEU MET SER TRP ARG PHE ILE MET ASP LEU
SEQRES 26 A 696 VAL SER SER LEU SER ARG THR TYR LYS GLU SER ARG ASN
SEQRES 27 A 696 ALA PHE ARG LYS ALA LEU TYR GLY THR THR SER GLU THR
SEQRES 28 A 696 ALA THR TRP ARG ARG CYS ALA ASN TYR VAL ASN GLY ASN
SEQRES 29 A 696 MET GLU ASN ALA VAL GLY ARG LEU TYR VAL GLU ALA ALA
SEQRES 30 A 696 PHE ALA GLY GLU SER LYS HIS VAL VAL GLU ASP LEU ILE
SEQRES 31 A 696 ALA GLN ILE ARG GLU VAL PHE ILE GLN THR LEU ASP ASP
SEQRES 32 A 696 LEU THR TRP MET ASP ALA GLU THR LYS LYS ARG ALA GLU
SEQRES 33 A 696 GLU LYS ALA LEU ALA ILE LYS GLU ARG ILE GLY TYR PRO
SEQRES 34 A 696 ASP ASP ILE VAL SER ASN ASP ASN LYS LEU ASN ASN GLU
SEQRES 35 A 696 TYR LEU GLU LEU ASN TYR LYS GLU ASP GLU TYR PHE GLU
SEQRES 36 A 696 ASN ILE ILE GLN ASN LEU LYS PHE SER GLN SER LYS GLN
SEQRES 37 A 696 LEU LYS LYS LEU ARG GLU LYS VAL ASP LYS ASP GLU TRP
SEQRES 38 A 696 ILE SER GLY ALA ALA VAL VAL ASN ALA PHE TYR SER SER
SEQRES 39 A 696 GLY ARG ASN GLN ILE VAL PHE PRO ALA GLY ILE LEU GLN
SEQRES 40 A 696 PRO PRO PHE PHE SER ALA GLN GLN SER ASN SER LEU ASN
SEQRES 41 A 696 TYR GLY GLY ILE GLY MET VAL ILE GLY HIS GLU ILE THR
SEQRES 42 A 696 HIS GLY PHE ASP ASP ASN GLY ARG ASN PHE ASN LYS ASP
SEQRES 43 A 696 GLY ASP LEU VAL ASP TRP TRP THR GLN GLN SER ALA SER
SEQRES 44 A 696 ASN PHE LYS GLU GLN SER GLN CYS MET VAL TYR GLN TYR
SEQRES 45 A 696 GLY ASN PHE SER TRP ASP LEU ALA GLY GLY GLN HIS LEU
SEQRES 46 A 696 ASN GLY ILE ASN THR LEU GLY GLU ASN ILE ALA ASP ASN
SEQRES 47 A 696 GLY GLY LEU GLY GLN ALA TYR ARG ALA TYR GLN ASN TYR
SEQRES 48 A 696 ILE LYS LYS ASN GLY GLU GLU LYS LEU LEU PRO GLY LEU
SEQRES 49 A 696 ASP LEU ASN HIS LYS GLN LEU PHE PHE LEU ASN PHE ALA
SEQRES 50 A 696 GLN VAL TRP CYS GLY THR TYR ARG PRO GLU TYR ALA VAL
SEQRES 51 A 696 ASN SER ILE LYS THR ASP VAL HIS SER PRO GLY ASN PHE
SEQRES 52 A 696 ARG ILE ILE GLY THR LEU GLN ASN SER ALA GLU PHE SER
SEQRES 53 A 696 GLU ALA PHE HIS CYS ARG LYS ASN SER TYR MET ASN PRO
SEQRES 54 A 696 GLU LYS LYS CYS ARG VAL TRP
MODRES 1Y8J ASN A 144 ASN GLYCOSYLATION SITE
MODRES 1Y8J ASN A 324 ASN GLYCOSYLATION SITE
MODRES 1Y8J ASN A 627 ASN GLYCOSYLATION SITE
HET NAG A 752 14
HET NAG A 753 14
HET NAG A 754 14
HET ZN A 800 1
HET ACT A 801 4
HET STS A 900 19
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM ZN ZINC ION
HETNAM ACT ACETATE ION
HETNAM STS 2-[(1S)-1-BENZYL-2-SULFANYLETHYL]-1H-IMIDAZO[4,5-
HETNAM 2 STS C]PYRIDIN-5-IUM
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
FORMUL 2 NAG 3(C8 H15 N O6)
FORMUL 5 ZN ZN 2+
FORMUL 6 ACT C2 H3 O2 1-
FORMUL 7 STS C15 H16 N3 S 1+
FORMUL 8 HOH *212(H2 O)
HELIX 1 1 SER A 58 MET A 72 1 15
HELIX 2 2 ASP A 81 ASN A 94 1 14
HELIX 3 3 ASN A 105 GLN A 122 1 18
HELIX 4 4 ILE A 129 ASN A 144 1 16
HELIX 5 5 ASN A 144 ARG A 151 1 8
HELIX 6 6 GLY A 153 LYS A 158 1 6
HELIX 7 7 LEU A 159 TYR A 164 5 6
HELIX 8 8 TRP A 166 THR A 170 5 5
HELIX 9 9 ASN A 172 TYR A 177 1 6
HELIX 10 10 THR A 182 TYR A 194 1 13
HELIX 11 11 SER A 227 CYS A 233 5 7
HELIX 12 12 THR A 234 ILE A 236 5 3
HELIX 13 13 TYR A 237 GLU A 259 1 23
HELIX 14 14 ASP A 264 THR A 286 1 23
HELIX 15 15 LYS A 288 ARG A 292 5 5
HELIX 16 16 ASP A 294 TYR A 299 1 6
HELIX 17 17 LEU A 304 PHE A 311 1 8
HELIX 18 18 SER A 321 SER A 331 1 11
HELIX 19 19 THR A 332 ASN A 334 5 3
HELIX 20 20 ALA A 347 THR A 359 1 13
HELIX 21 21 SER A 362 MET A 376 1 15
HELIX 22 22 ASP A 377 LEU A 382 5 6
HELIX 23 23 SER A 383 SER A 389 1 7
HELIX 24 24 ARG A 390 GLY A 399 1 10
HELIX 25 25 ALA A 405 MET A 418 1 14
HELIX 26 26 MET A 418 PHE A 431 1 14
HELIX 27 27 GLU A 434 LEU A 454 1 21
HELIX 28 28 ASP A 461 ALA A 474 1 14
HELIX 29 29 ASP A 483 ASN A 488 1 6
HELIX 30 30 ASN A 488 TYR A 496 1 9
HELIX 31 31 GLU A 505 LYS A 523 1 19
HELIX 32 32 GLY A 557 LEU A 559 5 3
HELIX 33 33 SER A 569 HIS A 587 1 19
HELIX 34 34 GLY A 588 ASP A 590 5 3
HELIX 35 35 ASN A 592 PHE A 596 5 5
HELIX 36 36 THR A 607 ASN A 627 1 21
HELIX 37 37 TRP A 630 GLY A 634 5 5
HELIX 38 38 THR A 643 GLY A 669 1 27
HELIX 39 39 ASN A 680 VAL A 692 1 13
HELIX 40 40 ARG A 698 ASP A 709 1 12
HELIX 41 41 PRO A 713 ASN A 724 1 12
HELIX 42 42 SER A 725 PHE A 732 1 8
SHEET 1 A 2 ARG A 102 GLY A 104 0
SHEET 2 A 2 GLY A 695 TYR A 697 -1 O THR A 696 N TYR A 103
SHEET 1 B 4 ASN A 201 ASP A 207 0
SHEET 2 B 4 ASN A 210 ASP A 219 -1 O VAL A 215 N GLY A 205
SHEET 3 B 4 ASP A 342 VAL A 345 1 O VAL A 344 N ILE A 216
SHEET 4 B 4 ASN A 300 THR A 303 -1 N MET A 302 O VAL A 343
SHEET 1 C 3 LYS A 476 GLY A 480 0
SHEET 2 C 3 GLN A 551 PRO A 555 1 O PHE A 554 N GLY A 480
SHEET 3 C 3 PHE A 544 SER A 546 -1 N SER A 546 O GLN A 551
SSBOND 1 CYS A 56 CYS A 61 1555 1555 2.04
SSBOND 2 CYS A 79 CYS A 734 1555 1555 2.03
SSBOND 3 CYS A 87 CYS A 694 1555 1555 2.03
SSBOND 4 CYS A 142 CYS A 410 1555 1555 2.02
SSBOND 5 CYS A 233 CYS A 241 1555 1555 2.04
SSBOND 6 CYS A 620 CYS A 746 1555 1555 2.04
LINK ND2 ASN A 144 C1 NAG A 752 1555 1555 1.44
LINK ND2 ASN A 324 C1 NAG A 753 1555 1555 1.44
LINK ND2 ASN A 627 C1 NAG A 754 1555 1555 1.44
LINK NE2 HIS A 583 ZN ZN A 800 1555 1555 1.90
LINK NE2 HIS A 587 ZN ZN A 800 1555 1555 2.05
LINK OE1 GLU A 646 ZN ZN A 800 1555 1555 2.08
LINK ZN ZN A 800 S10 STS A 900 1555 1555 2.20
CISPEP 1 LYS A 318 PRO A 319 0 -3.79
CISPEP 2 PRO A 561 PRO A 562 0 5.40
CRYST1 107.355 107.356 112.466 90.00 90.00 120.00 P 32 2 1 6
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.009315 0.005378 0.000000 0.00000
SCALE2 0.000000 0.010756 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008892 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
