HEADER HYDROLASE/HYDROLASE INHIBITOR 26-JUN-96 1CGH
TITLE HUMAN CATHEPSIN G
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATHEPSIN G;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.4.21.20
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS INFLAMMATION, SPECIFICITY, SERINE PROTEASE, HYDROLASE-HYDROLASE
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR P.HOF,W.BODE
REVDAT 4 03-APR-24 1CGH 1 REMARK LINK
REVDAT 3 13-JUL-11 1CGH 1 VERSN
REVDAT 2 24-FEB-09 1CGH 1 VERSN
REVDAT 1 07-JUL-97 1CGH 0
JRNL AUTH P.HOF,I.MAYR,R.HUBER,E.KORZUS,J.POTEMPA,J.TRAVIS,J.C.POWERS,
JRNL AUTH 2 W.BODE
JRNL TITL THE 1.8 A CRYSTAL STRUCTURE OF HUMAN CATHEPSIN G IN COMPLEX
JRNL TITL 2 WITH SUC-VAL-PRO-PHEP-(OPH)2: A JANUS-FACED PROTEINASE WITH
JRNL TITL 3 TWO OPPOSITE SPECIFICITIES.
JRNL REF EMBO J. V. 15 5481 1996
JRNL REFN ISSN 0261-4189
JRNL PMID 8896442
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.2
REMARK 3 NUMBER OF REFLECTIONS : 18433
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1786
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 33
REMARK 3 SOLVENT ATOMS : 145
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.43
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.013
REMARK 3 BOND ANGLES (DEGREES) : 1.765
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.050 ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 RESIDUES SER A 36A AND PRO A 36B ARE NOT DEFINED IN
REMARK 3 ELECTRON DENSITY AND THUS NOT WEIGHTED IN THE REFINEMENT.
REMARK 3
REMARK 3 RESIDUES SER A 36A AND PRO A 36B ARE NOT DEFINED IN
REMARK 3 ELECTRON DENSITY AND THUS NOT WEIGHTED IN THE REFINEMENT.
REMARK 4
REMARK 4 1CGH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000172306.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-SEP-95
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM, ROTAVATA, AGROVATA
REMARK 200 DATA SCALING SOFTWARE : CCP4 (AGROVATA, ROTAVATA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18433
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.1
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.05700
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) : 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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: BOVINE BETA TRYPSIN (W.BODE)
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-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 SMTRY1 2 -1.000000 0.000000 0.000000 20.02000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 39.86000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.80500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 39.86000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.02000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.80500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 GLN A 36
REMARK 475 SER A 36A
REMARK 475 PRO A 36B
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ALA A 37 N CA C O CB
REMARK 480 GLY A 38 N CA C O
REMARK 480 GLN A 39 CB CG CD OE1 NE2
REMARK 480 ARG A 41 CD NE CZ NH1 NH2
REMARK 480 ARG A 76 CG CD NE CZ NH1 NH2
REMARK 480 ARG A 111 CZ NH1 NH2
REMARK 480 ARG A 116 CB CG CD NE CZ NH1 NH2
REMARK 480 GLN A 127 CB CG CD OE1 NE2
REMARK 480 ARG A 131 CB CG CD NE CZ NH1 NH2
REMARK 480 ARG A 164 CZ NH1 NH2
REMARK 480 ARG A 166 CB CG CD NE CZ NH1 NH2
REMARK 480 ARG A 170 CB CG CD NE CZ NH1 NH2
REMARK 480 ARG A 186 CB CG CD NE CZ NH1 NH2
REMARK 480 ARG A 188A CB CG CD NE CZ NH1 NH2
REMARK 480 ARG A 239 CG CD NE CZ NH1 NH2
REMARK 480 SER A 244 OG
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 HE ARG A 87 H1 HOH A 317 1.25
REMARK 500 HH22 ARG A 90 H2 HOH A 367 1.26
REMARK 500 HH22 ARG A 230 H1 HOH A 286 1.29
REMARK 500 O HOH A 261 H2 HOH A 358 1.54
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 HH22 ARG A 125 H2 HOH A 352 1655 1.30
REMARK 500 O HOH A 270 H1 HOH A 374 4555 1.57
REMARK 500 O HOH A 319 H2 HOH A 382 4555 1.57
REMARK 500 O HOH A 304 H2 HOH A 385 4565 1.59
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 LEU A 130 CA - CB - CG ANGL. DEV. = 13.8 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 GLN A 36 155.16 63.14
REMARK 500 ALA A 37 86.19 -59.83
REMARK 500 SER A 40 147.85 -178.00
REMARK 500 HIS A 71 -63.91 -121.22
REMARK 500
REMARK 500 REMARK: NULL
REMARK 630
REMARK 630 MOLECULE TYPE: PEPTIDE-LIKE INHIBITOR
REMARK 630 MOLECULE NAME: N-(3-CARBOXYPROPANOYL)-L-VALYL-N-{(1R)-1-[(S)-
REMARK 630 HYDROXY(OXIDO)PHOSPHANYL]-2-PHENYLETHYL}-L-PROLINAMIDE
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 1ZG A 1
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP: SIN VAL PRO PPH
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 1ZG A 1
DBREF 1CGH A 16 244 UNP P08311 CATG_HUMAN 21 244
SEQRES 1 A 224 ILE ILE GLY GLY ARG GLU SER ARG PRO HIS SER ARG PRO
SEQRES 2 A 224 TYR MET ALA TYR LEU GLN ILE GLN SER PRO ALA GLY GLN
SEQRES 3 A 224 SER ARG CYS GLY GLY PHE LEU VAL ARG GLU ASP PHE VAL
SEQRES 4 A 224 LEU THR ALA ALA HIS CYS TRP GLY SER ASN ILE ASN VAL
SEQRES 5 A 224 THR LEU GLY ALA HIS ASN ILE GLN ARG ARG GLU ASN THR
SEQRES 6 A 224 GLN GLN HIS ILE THR ALA ARG ARG ALA ILE ARG HIS PRO
SEQRES 7 A 224 GLN TYR ASN GLN ARG THR ILE GLN ASN ASP ILE MET LEU
SEQRES 8 A 224 LEU GLN LEU SER ARG ARG VAL ARG ARG ASN ARG ASN VAL
SEQRES 9 A 224 ASN PRO VAL ALA LEU PRO ARG ALA GLN GLU GLY LEU ARG
SEQRES 10 A 224 PRO GLY THR LEU CYS THR VAL ALA GLY TRP GLY ARG VAL
SEQRES 11 A 224 SER MET ARG ARG GLY THR ASP THR LEU ARG GLU VAL GLN
SEQRES 12 A 224 LEU ARG VAL GLN ARG ASP ARG GLN CYS LEU ARG ILE PHE
SEQRES 13 A 224 GLY SER TYR ASP PRO ARG ARG GLN ILE CYS VAL GLY ASP
SEQRES 14 A 224 ARG ARG GLU ARG LYS ALA ALA PHE LYS GLY ASP SER GLY
SEQRES 15 A 224 GLY PRO LEU LEU CYS ASN ASN VAL ALA HIS GLY ILE VAL
SEQRES 16 A 224 SER TYR GLY LYS SER SER GLY VAL PRO PRO GLU VAL PHE
SEQRES 17 A 224 THR ARG VAL SER SER PHE LEU PRO TRP ILE ARG THR THR
SEQRES 18 A 224 MET ARG SER
HET 1ZG A 1 39
HETNAM 1ZG N-(3-CARBOXYPROPANOYL)-L-VALYL-N-{(1R)-1-[(S)-
HETNAM 2 1ZG HYDROXY(OXIDO)PHOSPHANYL]-2-PHENYLETHYL}-L-PROLINAMIDE
FORMUL 2 1ZG C22 H32 N3 O8 P
FORMUL 3 HOH *145(H2 O)
HELIX 1 1 ALA A 56 CYS A 58 5 3
HELIX 2 2 ASP A 165 ILE A 171 1 7
HELIX 3 3 VAL A 231 SER A 233 5 3
HELIX 4 4 LEU A 235 ARG A 243 1 9
SHEET 1 A 7 GLN A 81 THR A 84 0
SHEET 2 A 7 ILE A 64 LEU A 68 -1 N LEU A 68 O GLN A 81
SHEET 3 A 7 MET A 30 ILE A 35 -1 N GLN A 34 O ASN A 65
SHEET 4 A 7 ARG A 41 ARG A 48 -1 N GLY A 44 O ALA A 31
SHEET 5 A 7 PHE A 51 THR A 54 -1 N LEU A 53 O PHE A 45
SHEET 6 A 7 MET A 104 LEU A 108 -1 N LEU A 106 O VAL A 52
SHEET 7 A 7 ALA A 85 ARG A 90 -1 N ILE A 89 O LEU A 105
SHEET 1 B 2 LEU A 135 GLY A 140 0
SHEET 2 B 2 ARG A 156 ARG A 161 -1 N LEU A 160 O CYS A 136
SHEET 1 C 4 GLN A 180 VAL A 183 0
SHEET 2 C 4 GLU A 226 ARG A 230 -1 N PHE A 228 O ILE A 181
SHEET 3 C 4 VAL A 204 TYR A 215 -1 N TYR A 215 O VAL A 227
SHEET 4 C 4 PRO A 198 CYS A 201 -1 N CYS A 201 O VAL A 204
SSBOND 1 CYS A 42 CYS A 58 1555 1555 2.03
SSBOND 2 CYS A 136 CYS A 201 1555 1555 2.01
SSBOND 3 CYS A 168 CYS A 182 1555 1555 2.03
LINK P 1ZG A 1 OG SER A 195 1555 1555 1.59
CISPEP 1 SER A 36A PRO A 36B 0 -0.18
CISPEP 2 PRO A 224 PRO A 225 0 -0.07
SITE 1 AC1 18 HIS A 57 PRO A 177 ARG A 178 ALA A 190
SITE 2 AC1 18 PHE A 191 LYS A 192 GLY A 193 ASP A 194
SITE 3 AC1 18 SER A 195 SER A 214 TYR A 215 GLY A 216
SITE 4 AC1 18 LYS A 217 GLU A 226 HOH A 324 HOH A 379
SITE 5 AC1 18 HOH A 388 HOH A 389
CRYST1 40.040 63.610 79.720 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.024975 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015721 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012544 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
