HEADER HYDROLASE 22-JUL-08 3DWB
TITLE STRUCTURE OF HUMAN ECE-1 COMPLEXED WITH PHOSPHORAMIDON
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDOTHELIN-CONVERTING ENZYME 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ECTO DOMAIN, EXTRACELLULAR DOMAIN;
COMPND 5 SYNONYM: ECE-1;
COMPND 6 EC: 3.4.24.71;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ECE1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA-GAMI(NOVAGEN);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS PROTEIN, DISEASE MUTATION, GLYCOPROTEIN, HIRSCHSPRUNG DISEASE,
KEYWDS 2 HYDROLASE, MEMBRANE, METAL-BINDING, METALLOPROTEASE, PHOSPHOPROTEIN,
KEYWDS 3 PROTEASE, SIGNAL-ANCHOR, TRANSMEMBRANE, MCH_ECE_H_25A1_LT1.PDB
EXPDTA X-RAY DIFFRACTION
AUTHOR C.OEFNER
REVDAT 7 20-MAR-24 3DWB 1 SOURCE
REVDAT 6 01-NOV-23 3DWB 1 REMARK
REVDAT 5 10-NOV-21 3DWB 1 REMARK SEQADV
REVDAT 4 13-JUL-11 3DWB 1 VERSN
REVDAT 3 23-JUN-09 3DWB 1 ATOM
REVDAT 2 13-JAN-09 3DWB 1 JRNL VERSN
REVDAT 1 25-NOV-08 3DWB 0
JRNL AUTH H.SCHULZ,G.E.DALE,Y.KARIMI-NEJAD,C.OEFNER
JRNL TITL STRUCTURE OF HUMAN ENDOTHELIN-CONVERTING ENZYME I COMPLEXED
JRNL TITL 2 WITH PHOSPHORAMIDON
JRNL REF J.MOL.BIOL. V. 385 178 2009
JRNL REFN ISSN 0022-2836
JRNL PMID 18992253
JRNL DOI 10.1016/J.JMB.2008.10.052
REMARK 2
REMARK 2 RESOLUTION. 2.38 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 2.38
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 31886
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) : 0.266
REMARK 3 R VALUE (WORKING SET) : 0.262
REMARK 3 FREE R VALUE : 0.345
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1705
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) : 2.38
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.51
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4430
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.97
REMARK 3 BIN R VALUE (WORKING SET) : 0.3240
REMARK 3 BIN FREE R VALUE SET COUNT : 263
REMARK 3 BIN FREE R VALUE : 0.4350
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5305
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 52
REMARK 3 SOLVENT ATOMS : 223
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.69
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.91000
REMARK 3 B22 (A**2) : 0.91000
REMARK 3 B33 (A**2) : -1.36000
REMARK 3 B12 (A**2) : 0.45000
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): 0.486
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.351
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.318
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.548
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.917
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.852
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5501 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 4774 ; 0.004 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7473 ; 1.525 ; 1.950
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11164 ; 0.893 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 658 ; 6.797 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 272 ;35.778 ;24.559
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 904 ;19.287 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 29 ;16.460 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 794 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6112 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1125 ; 0.003 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1550 ; 0.220 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 5213 ; 0.183 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2667 ; 0.191 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 3129 ; 0.088 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 215 ; 0.190 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): 2 ; 0.116 ; 0.200
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 1 ; 0.272 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 33 ; 0.195 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 82 ; 0.195 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 12 ; 0.374 ; 0.200
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): 4259 ; 0.893 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1322 ; 0.126 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5356 ; 1.048 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2629 ; 1.435 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2117 ; 2.151 ; 4.500
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 187 A 548
REMARK 3 ORIGIN FOR THE GROUP (A): 86.2534 14.4075 48.4450
REMARK 3 T TENSOR
REMARK 3 T11: 0.1090 T22: 0.0126
REMARK 3 T33: -0.0269 T12: -0.2447
REMARK 3 T13: -0.0847 T23: 0.0853
REMARK 3 L TENSOR
REMARK 3 L11: 1.3830 L22: 2.0287
REMARK 3 L33: 1.3239 L12: -1.2468
REMARK 3 L13: 0.2235 L23: -1.2476
REMARK 3 S TENSOR
REMARK 3 S11: -0.1498 S12: -0.0894 S13: -0.0496
REMARK 3 S21: 0.5203 S22: -0.1395 S23: -0.2795
REMARK 3 S31: -0.4185 S32: 0.6163 S33: 0.2894
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 : 1.20
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
REMARK 4
REMARK 4 3DWB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-JUL-08.
REMARK 100 THE DEPOSITION ID IS D_1000048569.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-JUL-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
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) : 1.5418
REMARK 200 MONOCHROMATOR : OSMIC MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33656
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.380
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 13.70
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07000
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <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: SHARP
REMARK 200 STARTING MODEL: PDB ENTRY 1DMT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% JEFFAMINE D2001, 0.1M BIS TRIS, PH
REMARK 280 6.0, VAPOR DIFFUSION, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 64.11533
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 128.23067
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 96.17300
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 160.28833
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 32.05767
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 64.11533
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 128.23067
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 160.28833
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 96.17300
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 32.05767
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 TYR A 422
REMARK 465 GLY A 423
REMARK 465 THR A 424
REMARK 465 LYS A 425
REMARK 465 LYS A 426
REMARK 465 THR A 427
REMARK 465 SER A 428
REMARK 465 LEU A 429
REMARK 465 PRO A 430
REMARK 465 ARG A 431
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 OE2 GLU A 458 OH TYR A 506 2.09
REMARK 500 O THR A 729 O HOH A 929 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 O HOH A 887 O HOH A 887 12555 1.84
REMARK 500 O HOH A 821 O HOH A 987 7655 1.97
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 188 CG GLU A 188 CD 0.142
REMARK 500 GLU A 188 CD GLU A 188 OE2 0.365
REMARK 500 GLU A 275 CD GLU A 275 OE1 0.099
REMARK 500 GLU A 275 CD GLU A 275 OE2 0.131
REMARK 500 ASP A 412 CG ASP A 412 OD1 0.252
REMARK 500 GLU A 419 CD GLU A 419 OE1 0.111
REMARK 500 GLU A 458 CD GLU A 458 OE1 0.097
REMARK 500 GLU A 458 CD GLU A 458 OE2 0.069
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 GLU A 188 OE1 - CD - OE2 ANGL. DEV. = 15.8 DEGREES
REMARK 500 GLU A 188 CG - CD - OE2 ANGL. DEV. = -23.8 DEGREES
REMARK 500 ASP A 412 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 ARG A 754 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 PRO A 757 C - N - CA ANGL. DEV. = 10.3 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 PRO A 140 -178.30 -60.96
REMARK 500 ARG A 145 119.10 -169.00
REMARK 500 SER A 170 48.25 -103.48
REMARK 500 ARG A 195 -145.68 53.04
REMARK 500 ALA A 216 96.36 -162.59
REMARK 500 ASP A 218 59.79 -91.39
REMARK 500 PHE A 236 -47.87 76.50
REMARK 500 ASN A 247 73.21 -163.52
REMARK 500 SER A 258 -173.89 -177.43
REMARK 500 GLU A 275 133.45 67.61
REMARK 500 LEU A 406 -158.34 -95.26
REMARK 500 PHE A 434 -62.67 -7.63
REMARK 500 VAL A 565 74.87 -100.49
REMARK 500 ASN A 566 -178.75 -171.48
REMARK 500 LEU A 583 45.51 -79.92
REMARK 500 ARG A 627 131.25 179.99
REMARK 500 PRO A 696 -61.44 -93.47
REMARK 500 LEU A 727 -5.44 -50.73
REMARK 500 PRO A 757 -24.75 -33.44
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 771 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 607 NE2
REMARK 620 2 HIS A 611 NE2 100.1
REMARK 620 3 RDF A 817 O1P 103.7 150.2
REMARK 620 N 1 2
REMARK 630
REMARK 630 MOLECULE TYPE: GLYCOPEPTIDE ENZYME INHIBITOR
REMARK 630 MOLECULE NAME: N-ALPHA-L-RHAMNOPYRANOSYLOXY(HYDROXYPHOSPHINYL)-L-
REMARK 630 LEUCYL-L-TRYPTOPHAN
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 630 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 630
REMARK 630 M RES C SSSEQI
REMARK 630 RDF A 817
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP: RHA LEU TRP
REMARK 630 DETAILS: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 771
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5HD A 816
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RDF A 817
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DMT RELATED DB: PDB
DBREF 3DWB A 101 770 UNP P42892 ECE1_HUMAN 101 770
SEQADV 3DWB SER A 428 UNP P42892 CYS 428 ENGINEERED MUTATION
SEQRES 1 A 670 SER GLU ALA CYS VAL SER VAL THR SER SER ILE LEU SER
SEQRES 2 A 670 SER MET ASP PRO THR VAL ASP PRO CYS HIS ASP PHE PHE
SEQRES 3 A 670 SER TYR ALA CYS GLY GLY TRP ILE LYS ALA ASN PRO VAL
SEQRES 4 A 670 PRO ASP GLY HIS SER ARG TRP GLY THR PHE SER ASN LEU
SEQRES 5 A 670 TRP GLU HIS ASN GLN ALA ILE ILE LYS HIS LEU LEU GLU
SEQRES 6 A 670 ASN SER THR ALA SER VAL SER GLU ALA GLU ARG LYS ALA
SEQRES 7 A 670 GLN VAL TYR TYR ARG ALA CYS MET ASN GLU THR ARG ILE
SEQRES 8 A 670 GLU GLU LEU ARG ALA LYS PRO LEU MET GLU LEU ILE GLU
SEQRES 9 A 670 ARG LEU GLY GLY TRP ASN ILE THR GLY PRO TRP ALA LYS
SEQRES 10 A 670 ASP ASN PHE GLN ASP THR LEU GLN VAL VAL THR ALA HIS
SEQRES 11 A 670 TYR ARG THR SER PRO PHE PHE SER VAL TYR VAL SER ALA
SEQRES 12 A 670 ASP SER LYS ASN SER ASN SER ASN VAL ILE GLN VAL ASP
SEQRES 13 A 670 GLN SER GLY LEU GLY LEU PRO SER ARG ASP TYR TYR LEU
SEQRES 14 A 670 ASN LYS THR GLU ASN GLU LYS VAL LEU THR GLY TYR LEU
SEQRES 15 A 670 ASN TYR MET VAL GLN LEU GLY LYS LEU LEU GLY GLY GLY
SEQRES 16 A 670 ASP GLU GLU ALA ILE ARG PRO GLN MET GLN GLN ILE LEU
SEQRES 17 A 670 ASP PHE GLU THR ALA LEU ALA ASN ILE THR ILE PRO GLN
SEQRES 18 A 670 GLU LYS ARG ARG ASP GLU GLU LEU ILE TYR HIS LYS VAL
SEQRES 19 A 670 THR ALA ALA GLU LEU GLN THR LEU ALA PRO ALA ILE ASN
SEQRES 20 A 670 TRP LEU PRO PHE LEU ASN THR ILE PHE TYR PRO VAL GLU
SEQRES 21 A 670 ILE ASN GLU SER GLU PRO ILE VAL VAL TYR ASP LYS GLU
SEQRES 22 A 670 TYR LEU GLU GLN ILE SER THR LEU ILE ASN THR THR ASP
SEQRES 23 A 670 ARG CYS LEU LEU ASN ASN TYR MET ILE TRP ASN LEU VAL
SEQRES 24 A 670 ARG LYS THR SER SER PHE LEU ASP GLN ARG PHE GLN ASP
SEQRES 25 A 670 ALA ASP GLU LYS PHE MET GLU VAL MET TYR GLY THR LYS
SEQRES 26 A 670 LYS THR SER LEU PRO ARG TRP LYS PHE CYS VAL SER ASP
SEQRES 27 A 670 THR GLU ASN ASN LEU GLY PHE ALA LEU GLY PRO MET PHE
SEQRES 28 A 670 VAL LYS ALA THR PHE ALA GLU ASP SER LYS SER ILE ALA
SEQRES 29 A 670 THR GLU ILE ILE LEU GLU ILE LYS LYS ALA PHE GLU GLU
SEQRES 30 A 670 SER LEU SER THR LEU LYS TRP MET ASP GLU GLU THR ARG
SEQRES 31 A 670 LYS SER ALA LYS GLU LYS ALA ASP ALA ILE TYR ASN MET
SEQRES 32 A 670 ILE GLY TYR PRO ASN PHE ILE MET ASP PRO LYS GLU LEU
SEQRES 33 A 670 ASP LYS VAL PHE ASN ASP TYR THR ALA VAL PRO ASP LEU
SEQRES 34 A 670 TYR PHE GLU ASN ALA MET ARG PHE PHE ASN PHE SER TRP
SEQRES 35 A 670 ARG VAL THR ALA ASP GLN LEU ARG LYS ALA PRO ASN ARG
SEQRES 36 A 670 ASP GLN TRP SER MET THR PRO PRO MET VAL ASN ALA TYR
SEQRES 37 A 670 TYR SER PRO THR LYS ASN GLU ILE VAL PHE PRO ALA GLY
SEQRES 38 A 670 ILE LEU GLN ALA PRO PHE TYR THR ARG SER SER PRO LYS
SEQRES 39 A 670 ALA LEU ASN PHE GLY GLY ILE GLY VAL VAL VAL GLY HIS
SEQRES 40 A 670 GLU LEU THR HIS ALA PHE ASP ASP GLN GLY ARG GLU TYR
SEQRES 41 A 670 ASP LYS ASP GLY ASN LEU ARG PRO TRP TRP LYS ASN SER
SEQRES 42 A 670 SER VAL GLU ALA PHE LYS ARG GLN THR GLU CYS MET VAL
SEQRES 43 A 670 GLU GLN TYR SER ASN TYR SER VAL ASN GLY GLU PRO VAL
SEQRES 44 A 670 ASN GLY ARG HIS THR LEU GLY GLU ASN ILE ALA ASP ASN
SEQRES 45 A 670 GLY GLY LEU LYS ALA ALA TYR ARG ALA TYR GLN ASN TRP
SEQRES 46 A 670 VAL LYS LYS ASN GLY ALA GLU HIS SER LEU PRO THR LEU
SEQRES 47 A 670 GLY LEU THR ASN ASN GLN LEU PHE PHE LEU GLY PHE ALA
SEQRES 48 A 670 GLN VAL TRP CYS SER VAL ARG THR PRO GLU SER SER HIS
SEQRES 49 A 670 GLU GLY LEU ILE THR ASP PRO HIS SER PRO SER ARG PHE
SEQRES 50 A 670 ARG VAL ILE GLY SER LEU SER ASN SER LYS GLU PHE SER
SEQRES 51 A 670 GLU HIS PHE ARG CYS PRO PRO GLY SER PRO MET ASN PRO
SEQRES 52 A 670 PRO HIS LYS CYS GLU VAL TRP
HET ZN A 771 1
HET 5HD A 816 14
HET RDF A 817 37
HETNAM ZN ZINC ION
HETNAM 5HD 5-(2-HYDROXYETHYL)NONANE-1,9-DIOL
HETNAM RDF N-ALPHA-L-RHAMNOPYRANOSYLOXY(HYDROXYPHOSPHINYL)-L-
HETNAM 2 RDF LEUCYL-L-TRYPTOPHAN
HETSYN RDF PHOSPHORAMIDON
FORMUL 2 ZN ZN 2+
FORMUL 3 5HD C11 H24 O3
FORMUL 4 RDF C23 H34 N3 O10 P
FORMUL 5 HOH *223(H2 O)
HELIX 1 1 SER A 101 MET A 115 1 15
HELIX 2 2 ASP A 124 ASN A 137 1 14
HELIX 3 3 THR A 148 GLU A 165 1 18
HELIX 4 4 SER A 172 ASN A 187 1 16
HELIX 5 5 GLU A 188 ARG A 195 1 8
HELIX 6 6 ALA A 196 LEU A 206 1 11
HELIX 7 7 ASN A 219 HIS A 230 1 12
HELIX 8 8 ARG A 265 ASN A 270 1 6
HELIX 9 9 LYS A 276 LEU A 292 1 17
HELIX 10 10 ASP A 296 THR A 318 1 23
HELIX 11 11 PRO A 320 ARG A 325 5 6
HELIX 12 12 ASP A 326 TYR A 331 1 6
HELIX 13 13 ALA A 336 ALA A 343 1 8
HELIX 14 14 ASN A 347 PHE A 356 1 10
HELIX 15 15 ASP A 371 THR A 385 1 15
HELIX 16 16 ASP A 386 SER A 403 1 18
HELIX 17 17 SER A 404 LEU A 406 5 3
HELIX 18 18 ASP A 407 GLU A 419 1 13
HELIX 19 19 LYS A 433 PHE A 456 1 24
HELIX 20 20 ALA A 457 SER A 480 1 24
HELIX 21 21 ASP A 486 ILE A 500 1 15
HELIX 22 22 PRO A 507 MET A 511 5 5
HELIX 23 23 ASP A 512 ASN A 521 1 10
HELIX 24 24 LEU A 529 ASP A 547 1 19
HELIX 25 25 GLY A 581 LEU A 583 5 3
HELIX 26 26 PRO A 593 GLY A 600 1 8
HELIX 27 27 GLY A 600 ALA A 612 1 13
HELIX 28 28 GLN A 616 TYR A 620 5 5
HELIX 29 29 LYS A 631 SER A 650 1 20
HELIX 30 30 THR A 664 GLY A 690 1 27
HELIX 31 31 THR A 701 TRP A 714 1 14
HELIX 32 32 THR A 719 ASP A 730 1 12
HELIX 33 33 PRO A 734 ASN A 745 1 12
HELIX 34 34 SER A 746 ARG A 754 1 9
SHEET 1 A 2 ARG A 145 GLY A 147 0
SHEET 2 A 2 SER A 716 ARG A 718 -1 O VAL A 717 N TRP A 146
SHEET 1 B 4 SER A 238 ASP A 244 0
SHEET 2 B 4 ASN A 247 ASP A 256 -1 O SER A 250 N ASP A 244
SHEET 3 B 4 PRO A 366 VAL A 369 1 O VAL A 368 N ILE A 253
SHEET 4 B 4 HIS A 332 THR A 335 -1 N HIS A 332 O VAL A 369
SHEET 1 C 3 TYR A 501 GLY A 505 0
SHEET 2 C 3 GLU A 575 PRO A 579 1 O PHE A 578 N GLY A 505
SHEET 3 C 3 TYR A 568 SER A 570 -1 N SER A 570 O GLU A 575
SSBOND 1 CYS A 122 CYS A 755 1555 1555 2.06
SSBOND 2 CYS A 130 CYS A 715 1555 1555 2.02
SSBOND 3 CYS A 185 CYS A 435 1555 1555 2.05
SSBOND 4 CYS A 644 CYS A 767 1555 1555 2.00
LINK NE2 HIS A 607 ZN ZN A 771 1555 1555 2.25
LINK NE2 HIS A 611 ZN ZN A 771 1555 1555 2.13
LINK ZN ZN A 771 O1P RDF A 817 1555 1555 2.07
CISPEP 1 THR A 212 GLY A 213 0 -28.51
CISPEP 2 TYR A 357 PRO A 358 0 7.09
CISPEP 3 ALA A 585 PRO A 586 0 11.34
SITE 1 AC1 3 HIS A 607 HIS A 611 GLU A 667
SITE 1 AC2 1 GLN A 557
SITE 1 AC3 12 PHE A 149 ASN A 566 ALA A 567 ILE A 582
SITE 2 AC3 12 HIS A 607 GLU A 608 HIS A 611 GLU A 667
SITE 3 AC3 12 PRO A 731 HIS A 732 ARG A 738 HOH A 917
CRYST1 120.880 120.880 192.346 90.00 90.00 120.00 P 61 2 2 12
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 0.008273 0.004776 0.000000 0.00000
SCALE2 0.000000 0.009552 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005199 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
