HEADER HYDROLASE/HYDROLASE INHIBITOR 06-NOV-14 4WVP
TITLE CRYSTAL STRUCTURE OF AN ACTIVITY-BASED PROBE HNE COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUTROPHIL ELASTASE;
COMPND 3 CHAIN: E;
COMPND 4 SYNONYM: BONE MARROW SERINE PROTEASE,ELASTASE-2,HUMAN LEUKOCYTE
COMPND 5 ELASTASE,HLE,MEDULLASIN,PMN ELASTASE;
COMPND 6 EC: 3.4.21.37;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: BTN-3V3-NLB-OMT-OIC-3V2;
COMPND 9 CHAIN: I;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 MOL_ID: 2;
SOURCE 6 SYNTHETIC: YES;
SOURCE 7 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 8 ORGANISM_TAXID: 32630
KEYWDS NEUTROPHIL ELASTASE, ACITIVITY-BASED PROBE, INHIBITOR, PROTEASE,
KEYWDS 2 COMPLEX, HNE, HYCOSUL, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR B.C.LECHTENBERG,P.KASPERKIEWICZ,H.R.ROBINSON,M.DRAG,S.J.RIEDL
REVDAT 8 15-NOV-23 4WVP 1 LINK ATOM
REVDAT 7 27-SEP-23 4WVP 1 HETSYN LINK
REVDAT 6 29-JUL-20 4WVP 1 COMPND REMARK HETNAM LINK
REVDAT 6 2 1 SITE ATOM
REVDAT 5 22-NOV-17 4WVP 1 REMARK
REVDAT 4 09-SEP-15 4WVP 1 REMARK
REVDAT 3 29-APR-15 4WVP 1 JRNL
REVDAT 2 08-APR-15 4WVP 1 REMARK
REVDAT 1 11-FEB-15 4WVP 0
JRNL AUTH B.C.LECHTENBERG,P.KASPERKIEWICZ,H.ROBINSON,M.DRAG,S.J.RIEDL
JRNL TITL THE ELASTASE-PK101 STRUCTURE: MECHANISM OF AN ULTRASENSITIVE
JRNL TITL 2 ACTIVITY-BASED PROBE REVEALED.
JRNL REF ACS CHEM.BIOL. V. 10 945 2015
JRNL REFN ESSN 1554-8937
JRNL PMID 25581168
JRNL DOI 10.1021/CB500909N
REMARK 2
REMARK 2 RESOLUTION. 1.63 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
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) : 1.63
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 63.32
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 26239
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) : 0.140
REMARK 3 R VALUE (WORKING SET) : 0.138
REMARK 3 FREE R VALUE : 0.169
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1366
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) : 1.63
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.68
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1805
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.90
REMARK 3 BIN R VALUE (WORKING SET) : 0.2060
REMARK 3 BIN FREE R VALUE SET COUNT : 108
REMARK 3 BIN FREE R VALUE : 0.2440
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1712
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 126
REMARK 3 SOLVENT ATOMS : 202
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.13
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.43000
REMARK 3 B22 (A**2) : -0.43000
REMARK 3 B33 (A**2) : 1.38000
REMARK 3 B12 (A**2) : -0.21000
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): 0.081
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.081
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.049
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.605
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.971
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.959
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1887 ; 0.014 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1833 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2567 ; 1.868 ; 2.048
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4150 ; 1.244 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 222 ; 6.969 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 75 ;28.947 ;22.133
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 259 ;11.427 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;16.717 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 310 ; 0.099 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2050 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 450 ; 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): 887 ; 2.218 ; 0.681
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 888 ; 2.216 ; 0.681
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1105 ; 3.348 ; 1.014
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 : 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 : E 16 E 243
REMARK 3 ORIGIN FOR THE GROUP (A): -51.8740 90.6870 0.8240
REMARK 3 T TENSOR
REMARK 3 T11: 0.0537 T22: 0.0609
REMARK 3 T33: 0.0292 T12: -0.0214
REMARK 3 T13: 0.0011 T23: 0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 0.5896 L22: 0.7727
REMARK 3 L33: 1.1116 L12: 0.0845
REMARK 3 L13: -0.0850 L23: -0.0041
REMARK 3 S TENSOR
REMARK 3 S11: -0.0224 S12: 0.0187 S13: -0.0538
REMARK 3 S21: -0.0403 S22: -0.0012 S23: -0.0272
REMARK 3 S31: 0.1068 S32: -0.0627 S33: 0.0236
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.10
REMARK 3 ION PROBE RADIUS : 0.70
REMARK 3 SHRINKAGE RADIUS : 0.70
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 4WVP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JAN-15.
REMARK 100 THE DEPOSITION ID IS D_1000204560.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-APR-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.075
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.2.17
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26261
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.630
REMARK 200 RESOLUTION RANGE LOW (A) : 69.450
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 10.70
REMARK 200 R MERGE (I) : 0.09700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.63
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.20
REMARK 200 R MERGE FOR SHELL (I) : 0.62600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.6
REMARK 200 STARTING MODEL: 1PPG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS PH8, 0.8M AMMONIUM SULFATE,
REMARK 280 PH 8.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 34.72550
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 34.72550
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 34.72550
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, I, A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 19880 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -81.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, I, A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -0.500000 -0.866025 0.000000 36.56000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 189.97133
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 -146.24000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 126.64756
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 S SO4 I 201 LIES ON A SPECIAL POSITION.
REMARK 375 O3 SO4 I 201 LIES ON A SPECIAL POSITION.
REMARK 375 HOH I 308 LIES ON A SPECIAL POSITION.
REMARK 400
REMARK 400 COMPOUND
REMARK 400
REMARK 400 THE 6-MER PEPTIDE BTN-PE5-NLB-OMT-OIC-AXY IS PEPTIDE-LIKE, A MEMBER
REMARK 400 OF INHIBITOR CLASS.
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: 6-MER PEPTIDE BTN-PE5-NLB-OMT-OIC-AXY
REMARK 400 CHAIN: I
REMARK 400 COMPONENT_1: PEPTIDE LIKE POLYMER
REMARK 400 DESCRIPTION: NULL
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 HOH E 656 O HOH E 657 1.89
REMARK 500 O HOH E 508 O HOH E 578 1.92
REMARK 500 O HOH E 501 O HOH E 665 2.07
REMARK 500 ND2 ASN E 202 O HOH E 501 2.14
REMARK 500 O HOH E 669 O HOH E 680 2.16
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 O HOH E 559 O HOH E 571 4584 1.84
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 MET E 53 CG - SD - CE ANGL. DEV. = 11.8 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 ARG E 36 42.45 36.88
REMARK 500 ASN E 61 14.88 54.00
REMARK 500 HIS E 71 -61.49 -132.13
REMARK 500 ASN E 92 49.88 -142.62
REMARK 500 LEU E 223 -57.24 -127.69
REMARK 500
REMARK 500 REMARK: NULL
DBREF 4WVP E 16 243 UNP P08246 ELNE_HUMAN 30 247
DBREF 4WVP I 101 106 PDB 4WVP 4WVP 101 106
SEQRES 1 E 218 ILE VAL GLY GLY ARG ARG ALA ARG PRO HIS ALA TRP PRO
SEQRES 2 E 218 PHE MET VAL SER LEU GLN LEU ARG GLY GLY HIS PHE CYS
SEQRES 3 E 218 GLY ALA THR LEU ILE ALA PRO ASN PHE VAL MET SER ALA
SEQRES 4 E 218 ALA HIS CYS VAL ALA ASN VAL ASN VAL ARG ALA VAL ARG
SEQRES 5 E 218 VAL VAL LEU GLY ALA HIS ASN LEU SER ARG ARG GLU PRO
SEQRES 6 E 218 THR ARG GLN VAL PHE ALA VAL GLN ARG ILE PHE GLU ASN
SEQRES 7 E 218 GLY TYR ASP PRO VAL ASN LEU LEU ASN ASP ILE VAL ILE
SEQRES 8 E 218 LEU GLN LEU ASN GLY SER ALA THR ILE ASN ALA ASN VAL
SEQRES 9 E 218 GLN VAL ALA GLN LEU PRO ALA GLN GLY ARG ARG LEU GLY
SEQRES 10 E 218 ASN GLY VAL GLN CYS LEU ALA MET GLY TRP GLY LEU LEU
SEQRES 11 E 218 GLY ARG ASN ARG GLY ILE ALA SER VAL LEU GLN GLU LEU
SEQRES 12 E 218 ASN VAL THR VAL VAL THR SER LEU CYS ARG ARG SER ASN
SEQRES 13 E 218 VAL CYS THR LEU VAL ARG GLY ARG GLN ALA GLY VAL CYS
SEQRES 14 E 218 PHE GLY ASP SER GLY SER PRO LEU VAL CYS ASN GLY LEU
SEQRES 15 E 218 ILE HIS GLY ILE ALA SER PHE VAL ARG GLY GLY CYS ALA
SEQRES 16 E 218 SER GLY LEU TYR PRO ASP ALA PHE ALA PRO VAL ALA GLN
SEQRES 17 E 218 PHE VAL ASN TRP ILE ASP SER ILE ILE GLN
SEQRES 1 I 6 BTN 3V3 NLB OMT OIC 3V2
HET BTN I 101 15
HET 3V3 I 102 17
HET NLB I 103 16
HET OMT I 104 10
HET OIC I 105 11
HET 3V2 I 106 7
HET NAG A 1 14
HET NAG A 2 14
HET BMA A 3 11
HET FUC A 4 10
HET NAG B 1 14
HET NAG B 2 14
HET FUC B 3 10
HET SO4 E 408 5
HET SO4 E 409 5
HET EDO E 410 4
HET EDO E 411 4
HET EDO E 412 4
HET EDO E 413 4
HET EDO E 414 4
HET EDO E 415 4
HET SO4 I 201 5
HETNAM BTN BIOTIN
HETNAM 3V3 1-AMINO-3,6,9,12-TETRAOXAPENTADECAN-15-OIC ACID
HETNAM NLB 6-(BENZYLOXY)-L-NORLEUCINE
HETNAM OMT S-DIOXYMETHIONINE
HETNAM OIC OCTAHYDROINDOLE-2-CARBOXYLIC ACID
HETNAM 3V2 [(1R)-1-AMINOPROPYL]PHOSPHONIC ACID
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETNAM SO4 SULFATE ION
HETNAM EDO 1,2-ETHANEDIOL
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 BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L-
HETSYN 2 FUC FUCOSE; FUCOSE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 BTN C10 H16 N2 O3 S
FORMUL 2 3V3 C11 H23 N O6
FORMUL 2 NLB C13 H19 N O3
FORMUL 2 OMT C5 H11 N O4 S
FORMUL 2 OIC C9 H15 N O2
FORMUL 2 3V2 C3 H10 N O3 P
FORMUL 3 NAG 4(C8 H15 N O6)
FORMUL 3 BMA C6 H12 O6
FORMUL 3 FUC 2(C6 H12 O5)
FORMUL 5 SO4 3(O4 S 2-)
FORMUL 7 EDO 6(C2 H6 O2)
FORMUL 14 HOH *202(H2 O)
HELIX 1 AA1 ALA E 55 VAL E 59 5 5
HELIX 2 AA2 ASN E 63 ARG E 63B 5 3
HELIX 3 AA3 PHE E 234 GLN E 243 1 10
SHEET 1 AA1 6 ARG E 20 ARG E 21 0
SHEET 2 AA1 6 GLN E 156 VAL E 163 -1 O GLU E 157 N ARG E 20
SHEET 3 AA1 6 GLN E 135 GLY E 140 -1 N ALA E 138 O LEU E 158
SHEET 4 AA1 6 PRO E 198 CYS E 201 -1 O VAL E 200 N LEU E 137
SHEET 5 AA1 6 LEU E 208 VAL E 216 -1 O LEU E 208 N CYS E 201
SHEET 6 AA1 6 OMT I 104 OIC I 105 -1 O OMT I 104 N VAL E 216
SHEET 1 AA2 6 ARG E 20 ARG E 21 0
SHEET 2 AA2 6 GLN E 156 VAL E 163 -1 O GLU E 157 N ARG E 20
SHEET 3 AA2 6 VAL E 181 LEU E 184 -1 O CYS E 182 N VAL E 163
SHEET 4 AA2 6 ASP E 226 PRO E 230 -1 O PHE E 228 N VAL E 181
SHEET 5 AA2 6 LEU E 208 VAL E 216 -1 N ILE E 212 O ALA E 229
SHEET 6 AA2 6 OMT I 104 OIC I 105 -1 O OMT I 104 N VAL E 216
SHEET 1 AA3 7 MET E 30 LEU E 35 0
SHEET 2 AA3 7 GLY E 39 ALA E 48 -1 O CYS E 42 N LEU E 33
SHEET 3 AA3 7 PHE E 51 SER E 54 -1 O MET E 53 N THR E 45
SHEET 4 AA3 7 VAL E 104 LEU E 108 -1 O LEU E 106 N VAL E 52
SHEET 5 AA3 7 GLN E 81 GLU E 90 -1 N ARG E 87 O GLN E 107
SHEET 6 AA3 7 VAL E 64 LEU E 68 -1 N VAL E 66 O PHE E 83
SHEET 7 AA3 7 MET E 30 LEU E 35 -1 N SER E 32 O VAL E 67
SSBOND 1 CYS E 42 CYS E 58 1555 1555 2.10
SSBOND 2 CYS E 136 CYS E 201 1555 1555 2.10
SSBOND 3 CYS E 168 CYS E 182 1555 1555 2.11
SSBOND 4 CYS E 191 CYS E 220 1555 1555 2.14
LINK ND2 ASN E 109 C1 NAG B 1 1555 1555 1.46
LINK ND2 ASN E 159 C1 NAG A 1 1555 1555 1.44
LINK OG SER E 195 P1 3V2 I 106 1555 1555 1.62
LINK C11 BTN I 101 N 3V3 I 102 1555 1555 1.35
LINK C 3V3 I 102 N NLB I 103 1555 1555 1.32
LINK C NLB I 103 N OMT I 104 1555 1555 1.33
LINK C OMT I 104 N OIC I 105 1555 1555 1.35
LINK C OIC I 105 N 3V2 I 106 1555 1555 1.42
LINK O4 NAG A 1 C1 NAG A 2 1555 1555 1.44
LINK O6 NAG A 1 C1 FUC A 4 1555 1555 1.41
LINK O4 NAG A 2 C1 BMA A 3 1555 1555 1.45
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.44
LINK O6 NAG B 1 C1 FUC B 3 1555 1555 1.44
CRYST1 73.120 73.120 69.451 90.00 90.00 120.00 P 63 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 0.013676 0.007896 0.000000 0.00000
SCALE2 0.000000 0.015792 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014399 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
