HEADER ASPARTYL PROTEASE 16-SEP-97 1AVF
TITLE ACTIVATION INTERMEDIATE 2 OF HUMAN GASTRICSIN FROM HUMAN STOMACH
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GASTRICSIN;
COMPND 3 CHAIN: P, Q;
COMPND 4 SYNONYM: PEPSINOGEN C;
COMPND 5 EC: 3.4.23.3;
COMPND 6 OTHER_DETAILS: ASPARTIC PROTEINASE ACTIVATION INTERMEDIATE;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: GASTRICSIN;
COMPND 9 CHAIN: A, J;
COMPND 10 SYNONYM: PEPSINOGEN C;
COMPND 11 EC: 3.4.23.3;
COMPND 12 OTHER_DETAILS: ASPARTIC PROTEINASE ACTIVATION INTERMEDIATE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 ORGAN: STOMACH;
SOURCE 6 TISSUE: GASTRIC MUCOSA;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 ORGAN: STOMACH;
SOURCE 12 TISSUE: GASTRIC MUCOSA
KEYWDS ASPARTYL PROTEASE, GASTRICSIN, ASPARTIC PROTEINASE, INTERMEDIATE,
KEYWDS 2 ACTIVATION, ACID
EXPDTA X-RAY DIFFRACTION
AUTHOR A.R.KHAN,M.M.CHERNEY,N.I.TARASOVA,M.N.G.JAMES
REVDAT 3 02-AUG-23 1AVF 1 REMARK LINK
REVDAT 2 24-FEB-09 1AVF 1 VERSN
REVDAT 1 25-FEB-98 1AVF 0
JRNL AUTH A.R.KHAN,M.M.CHERNEY,N.I.TARASOVA,M.N.JAMES
JRNL TITL STRUCTURAL CHARACTERIZATION OF ACTIVATION 'INTERMEDIATE 2'
JRNL TITL 2 ON THE PATHWAY TO HUMAN GASTRICSIN.
JRNL REF NAT.STRUCT.BIOL. V. 4 1010 1997
JRNL REFN ISSN 1072-8368
JRNL PMID 9406551
JRNL DOI 10.1038/NSB1297-1010
REMARK 2
REMARK 2 RESOLUTION. 2.36 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.36
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.3
REMARK 3 NUMBER OF REFLECTIONS : 34523
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : R-FREE
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.227
REMARK 3 FREE R VALUE : 0.282
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3407
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) : 2.36
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.39
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 80.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 813
REMARK 3 BIN R VALUE (WORKING SET) : 0.3240
REMARK 3 BIN FREE R VALUE : 0.3340
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 90
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 : 5218
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 467
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.54
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) : 0.30
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) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.800
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.690
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) : NULL ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; 2.500
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; 10.0
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; 1.0
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1AVF 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_1000171305.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : SEP-96
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
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) : 1.0
REMARK 200 MONOCHROMATOR : GOBEL MIRRORS
REMARK 200 OPTICS : MIRROR
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 : 34523
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.360
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.06600
REMARK 200 R SYM (I) : 0.11700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.36
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.04500
REMARK 200 R SYM FOR SHELL (I) : 0.30300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: PDB ENTRY 1HTR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED IN 4M NA
REMARK 280 FORMATE, 100 MM BIS-TRIS-PROPANE, PH 7.8.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 78.13000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.20500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 78.13000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 25.20500
REMARK 290 SMTRY3 4 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: P, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: Q, J
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 LEU P 22
REMARK 465 LEU P 23
REMARK 465 GLY P 24
REMARK 465 GLU P 25
REMARK 465 PHE P 26
REMARK 465 SER A 1
REMARK 465 GLY A 76
REMARK 465 GLN A 158
REMARK 465 GLN A 159
REMARK 465 GLY A 160
REMARK 465 SER A 161
REMARK 465 SER A 162
REMARK 465 LEU Q 23
REMARK 465 GLY Q 24
REMARK 465 GLU Q 25
REMARK 465 PHE Q 26
REMARK 465 SER J 1
REMARK 465 GLN J 158
REMARK 465 GLN J 159
REMARK 465 GLY J 160
REMARK 465 SER J 161
REMARK 465 SER J 162
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 VAL A 2 CG1 CG2
REMARK 470 THR A 3 OG1 CG2
REMARK 470 TYR A 75 CA C O CB CG CD1 CD2
REMARK 470 TYR A 75 CE1 CE2 CZ OH
REMARK 470 SER A 79 OG
REMARK 470 ASN A 157 CA C O CB CG OD1 ND2
REMARK 470 ASN A 281 CG OD1 ND2
REMARK 470 VAL J 2 CG1 CG2
REMARK 470 THR J 3 OG1 CG2
REMARK 470 GLN J 74 CG CD OE1 NE2
REMARK 470 ASN J 157 CA C O CB CG OD1 ND2
REMARK 470 ASN J 281 CG OD1 ND2
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 475 O HOH A 485 2556 0.11
REMARK 500 O HOH A 341 O HOH A 457 2556 0.46
REMARK 500 O HOH J 475 O HOH J 519 4445 0.47
REMARK 500 C LEU J 257 O HOH J 530 4455 0.72
REMARK 500 O HOH A 444 O HOH A 538 2556 0.75
REMARK 500 O ASP A 242 O HOH A 539 4556 0.76
REMARK 500 CA LEU J 257 O HOH J 530 4455 0.80
REMARK 500 N GLN A 142 O HOH A 529 2556 0.87
REMARK 500 C ASP A 242 O HOH A 539 4556 0.93
REMARK 500 CB THR A 177 O HOH A 545 4546 1.35
REMARK 500 CA GLN A 255 O HOH A 544 4546 1.36
REMARK 500 CA GLN A 142 O HOH A 529 2556 1.38
REMARK 500 CD1 TYR J 44 O HOH A 516 1545 1.42
REMARK 500 O ASP J 242 O HOH J 524 4445 1.42
REMARK 500 N GLU A 243 O HOH A 539 4556 1.51
REMARK 500 C VAL A 141 O HOH A 529 2556 1.53
REMARK 500 N GLY J 144 O HOH A 524 2556 1.66
REMARK 500 O LEU J 257 O HOH J 530 4455 1.67
REMARK 500 N ASN A 256 O HOH A 530 4546 1.69
REMARK 500 N PRO J 258 O HOH J 530 4455 1.82
REMARK 500 O HOH A 550 O HOH Q 89 2556 1.82
REMARK 500 O GLN J 142 O HOH A 524 2556 1.82
REMARK 500 N LEU J 257 O HOH J 530 4455 1.84
REMARK 500 O HOH A 459 O HOH A 555 4546 1.88
REMARK 500 O ASN J 256 O HOH J 502 4455 1.89
REMARK 500 N GLN A 255 O HOH A 530 4546 1.90
REMARK 500 C GLN J 142 O HOH A 524 2556 1.92
REMARK 500 CB LEU J 257 O HOH J 530 4455 1.93
REMARK 500 CA GLU A 243 O HOH A 539 4556 1.97
REMARK 500 O HOH A 350 O HOH A 509 4546 1.98
REMARK 500 C GLU J 143 O HOH A 524 2556 2.01
REMARK 500 N GLN A 255 O HOH A 544 4546 2.03
REMARK 500 O HOH A 451 O HOH A 530 4546 2.08
REMARK 500 O SER A 253 O HOH A 530 4546 2.08
REMARK 500 N ASP J 242 O HOH J 524 4445 2.09
REMARK 500 CG2 THR A 177 O HOH A 545 4546 2.09
REMARK 500 CB GLN A 255 O HOH A 510 4546 2.10
REMARK 500 O HOH J 392 O HOH J 525 4445 2.13
REMARK 500 CE1 TYR J 44 O HOH A 516 1545 2.14
REMARK 500 O HOH A 350 O HOH A 555 4546 2.15
REMARK 500 CA THR A 177 O HOH A 545 4546 2.16
REMARK 500 O VAL A 141 O HOH A 529 2556 2.17
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 PRO J 6 C - N - CA ANGL. DEV. = 9.3 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 THR A 3 21.91 -145.45
REMARK 500 THR A 51 -18.12 -48.31
REMARK 500 GLN A 92 -126.98 53.46
REMARK 500 LEU A 189 -80.32 -147.66
REMARK 500 ILE A 254 -59.37 -28.22
REMARK 500 ASN A 281 103.51 168.68
REMARK 500 THR J 3 16.19 -148.37
REMARK 500 ALA J 13 -13.37 -142.25
REMARK 500 THR J 51 -26.43 -39.59
REMARK 500 THR J 66 145.07 -176.54
REMARK 500 GLN J 74 -127.13 60.73
REMARK 500 TYR J 75 147.02 -23.09
REMARK 500 SER J 77 33.60 74.96
REMARK 500 GLN J 92 -125.19 52.30
REMARK 500 ASP J 131 19.33 53.21
REMARK 500 GLU J 188 91.83 -69.06
REMARK 500 LEU J 189 -75.93 -153.01
REMARK 500 ASN J 281 104.81 81.97
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 NA A 330 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 275 OG
REMARK 620 2 SER A 311 OG 71.2
REMARK 620 3 HOH A 332 O 93.0 157.9
REMARK 620 4 HOH A 335 O 155.5 93.6 95.6
REMARK 620 5 HOH A 342 O 106.6 88.4 111.3 91.5
REMARK 620 6 HOH A 471 O 81.4 77.9 84.7 76.6 161.1
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 330
DBREF 1AVF P 1 26 UNP P20142 PEPC_HUMAN 17 42
DBREF 1AVF A 1 329 UNP P20142 PEPC_HUMAN 60 388
DBREF 1AVF Q 1 26 UNP P20142 PEPC_HUMAN 17 42
DBREF 1AVF J 1 329 UNP P20142 PEPC_HUMAN 60 388
SEQRES 1 P 26 ALA VAL VAL LYS VAL PRO LEU LYS LYS PHE LYS SER ILE
SEQRES 2 P 26 ARG GLU THR MET LYS GLU LYS GLY LEU LEU GLY GLU PHE
SEQRES 1 A 329 SER VAL THR TYR GLU PRO MET ALA TYR MET ASP ALA ALA
SEQRES 2 A 329 TYR PHE GLY GLU ILE SER ILE GLY THR PRO PRO GLN ASN
SEQRES 3 A 329 PHE LEU VAL LEU PHE ASP THR GLY SER SER ASN LEU TRP
SEQRES 4 A 329 VAL PRO SER VAL TYR CYS GLN SER GLN ALA CYS THR SER
SEQRES 5 A 329 HIS SER ARG PHE ASN PRO SER GLU SER SER THR TYR SER
SEQRES 6 A 329 THR ASN GLY GLN THR PHE SER LEU GLN TYR GLY SER GLY
SEQRES 7 A 329 SER LEU THR GLY PHE PHE GLY TYR ASP THR LEU THR VAL
SEQRES 8 A 329 GLN SER ILE GLN VAL PRO ASN GLN GLU PHE GLY LEU SER
SEQRES 9 A 329 GLU ASN GLU PRO GLY THR ASN PHE VAL TYR ALA GLN PHE
SEQRES 10 A 329 ASP GLY ILE MET GLY LEU ALA TYR PRO ALA LEU SER VAL
SEQRES 11 A 329 ASP GLU ALA THR THR ALA MET GLN GLY MET VAL GLN GLU
SEQRES 12 A 329 GLY ALA LEU THR SER PRO VAL PHE SER VAL TYR LEU SER
SEQRES 13 A 329 ASN GLN GLN GLY SER SER GLY GLY ALA VAL VAL PHE GLY
SEQRES 14 A 329 GLY VAL ASP SER SER LEU TYR THR GLY GLN ILE TYR TRP
SEQRES 15 A 329 ALA PRO VAL THR GLN GLU LEU TYR TRP GLN ILE GLY ILE
SEQRES 16 A 329 GLU GLU PHE LEU ILE GLY GLY GLN ALA SER GLY TRP CYS
SEQRES 17 A 329 SER GLU GLY CYS GLN ALA ILE VAL ASP THR GLY THR SER
SEQRES 18 A 329 LEU LEU THR VAL PRO GLN GLN TYR MET SER ALA LEU LEU
SEQRES 19 A 329 GLN ALA THR GLY ALA GLN GLU ASP GLU TYR GLY GLN PHE
SEQRES 20 A 329 LEU VAL ASN CYS ASN SER ILE GLN ASN LEU PRO SER LEU
SEQRES 21 A 329 THR PHE ILE ILE ASN GLY VAL GLU PHE PRO LEU PRO PRO
SEQRES 22 A 329 SER SER TYR ILE LEU SER ASN ASN GLY TYR CYS THR VAL
SEQRES 23 A 329 GLY VAL GLU PRO THR TYR LEU SER SER GLN ASN GLY GLN
SEQRES 24 A 329 PRO LEU TRP ILE LEU GLY ASP VAL PHE LEU ARG SER TYR
SEQRES 25 A 329 TYR SER VAL TYR ASP LEU GLY ASN ASN ARG VAL GLY PHE
SEQRES 26 A 329 ALA THR ALA ALA
SEQRES 1 Q 26 ALA VAL VAL LYS VAL PRO LEU LYS LYS PHE LYS SER ILE
SEQRES 2 Q 26 ARG GLU THR MET LYS GLU LYS GLY LEU LEU GLY GLU PHE
SEQRES 1 J 329 SER VAL THR TYR GLU PRO MET ALA TYR MET ASP ALA ALA
SEQRES 2 J 329 TYR PHE GLY GLU ILE SER ILE GLY THR PRO PRO GLN ASN
SEQRES 3 J 329 PHE LEU VAL LEU PHE ASP THR GLY SER SER ASN LEU TRP
SEQRES 4 J 329 VAL PRO SER VAL TYR CYS GLN SER GLN ALA CYS THR SER
SEQRES 5 J 329 HIS SER ARG PHE ASN PRO SER GLU SER SER THR TYR SER
SEQRES 6 J 329 THR ASN GLY GLN THR PHE SER LEU GLN TYR GLY SER GLY
SEQRES 7 J 329 SER LEU THR GLY PHE PHE GLY TYR ASP THR LEU THR VAL
SEQRES 8 J 329 GLN SER ILE GLN VAL PRO ASN GLN GLU PHE GLY LEU SER
SEQRES 9 J 329 GLU ASN GLU PRO GLY THR ASN PHE VAL TYR ALA GLN PHE
SEQRES 10 J 329 ASP GLY ILE MET GLY LEU ALA TYR PRO ALA LEU SER VAL
SEQRES 11 J 329 ASP GLU ALA THR THR ALA MET GLN GLY MET VAL GLN GLU
SEQRES 12 J 329 GLY ALA LEU THR SER PRO VAL PHE SER VAL TYR LEU SER
SEQRES 13 J 329 ASN GLN GLN GLY SER SER GLY GLY ALA VAL VAL PHE GLY
SEQRES 14 J 329 GLY VAL ASP SER SER LEU TYR THR GLY GLN ILE TYR TRP
SEQRES 15 J 329 ALA PRO VAL THR GLN GLU LEU TYR TRP GLN ILE GLY ILE
SEQRES 16 J 329 GLU GLU PHE LEU ILE GLY GLY GLN ALA SER GLY TRP CYS
SEQRES 17 J 329 SER GLU GLY CYS GLN ALA ILE VAL ASP THR GLY THR SER
SEQRES 18 J 329 LEU LEU THR VAL PRO GLN GLN TYR MET SER ALA LEU LEU
SEQRES 19 J 329 GLN ALA THR GLY ALA GLN GLU ASP GLU TYR GLY GLN PHE
SEQRES 20 J 329 LEU VAL ASN CYS ASN SER ILE GLN ASN LEU PRO SER LEU
SEQRES 21 J 329 THR PHE ILE ILE ASN GLY VAL GLU PHE PRO LEU PRO PRO
SEQRES 22 J 329 SER SER TYR ILE LEU SER ASN ASN GLY TYR CYS THR VAL
SEQRES 23 J 329 GLY VAL GLU PRO THR TYR LEU SER SER GLN ASN GLY GLN
SEQRES 24 J 329 PRO LEU TRP ILE LEU GLY ASP VAL PHE LEU ARG SER TYR
SEQRES 25 J 329 TYR SER VAL TYR ASP LEU GLY ASN ASN ARG VAL GLY PHE
SEQRES 26 J 329 ALA THR ALA ALA
HET NA A 330 1
HETNAM NA SODIUM ION
FORMUL 5 NA NA 1+
FORMUL 6 HOH *467(H2 O)
HELIX 1 1 ILE P 13 GLU P 19 1 7
HELIX 2 2 GLN A 48 THR A 51 1 4
HELIX 3 3 PRO A 58 GLU A 60 5 3
HELIX 4 4 THR A 110 TYR A 114 5 5
HELIX 5 5 PRO A 126 LEU A 128 5 3
HELIX 6 6 VAL A 130 GLU A 132 5 3
HELIX 7 7 ALA A 136 GLU A 143 1 8
HELIX 8 8 GLN A 227 ALA A 236 5 10
HELIX 9 9 ILE A 254 ASN A 256 5 3
HELIX 10 10 PRO A 273 TYR A 276 1 4
HELIX 11 11 ASP A 306 LEU A 309 1 4
HELIX 12 12 ILE Q 13 LYS Q 20 1 8
HELIX 13 13 GLN J 48 THR J 51 1 4
HELIX 14 14 PRO J 58 GLU J 60 5 3
HELIX 15 15 THR J 110 TYR J 114 5 5
HELIX 16 16 PRO J 126 LEU J 128 5 3
HELIX 17 17 VAL J 130 GLU J 132 5 3
HELIX 18 18 ALA J 136 GLN J 142 1 7
HELIX 19 19 SER J 173 LEU J 175 5 3
HELIX 20 20 GLN J 227 THR J 237 5 11
HELIX 21 21 CYS J 251 ASN J 256 5 6
HELIX 22 22 PRO J 273 TYR J 276 1 4
HELIX 23 23 ASP J 306 LEU J 309 1 4
SHEET 1 A 3 PHE A 15 ILE A 20 0
SHEET 2 A 3 GLN A 25 ASP A 32 -1 N VAL A 29 O GLY A 16
SHEET 3 A 3 GLY A 119 GLY A 122 1 N GLY A 119 O LEU A 30
SHEET 1 B 4 TRP A 39 PRO A 41 0
SHEET 2 B 4 GLN A 99 SER A 104 1 N GLY A 102 O VAL A 40
SHEET 3 B 4 LEU A 80 ASP A 87 -1 N ASP A 87 O GLN A 99
SHEET 4 B 4 THR A 70 LEU A 73 -1 N LEU A 73 O LEU A 80
SHEET 1 C 2 LEU A 89 VAL A 91 0
SHEET 2 C 2 ILE A 94 VAL A 96 -1 N VAL A 96 O LEU A 89
SHEET 1 D 5 ALA A 165 PHE A 168 0
SHEET 2 D 5 VAL A 150 TYR A 154 -1 N TYR A 154 O ALA A 165
SHEET 3 D 5 TYR A 312 ASP A 317 -1 N TYR A 316 O PHE A 151
SHEET 4 D 5 ARG A 322 THR A 327 -1 N ALA A 326 O TYR A 313
SHEET 5 D 5 TYR A 181 PRO A 184 -1 N ALA A 183 O VAL A 323
SHEET 1 E 3 GLN A 192 ILE A 195 0
SHEET 2 E 3 CYS A 212 VAL A 216 -1 N ALA A 214 O ILE A 193
SHEET 3 E 3 LEU A 301 LEU A 304 1 N TRP A 302 O GLN A 213
SHEET 1 F 3 GLU A 197 ILE A 200 0
SHEET 2 F 3 LEU A 260 ILE A 264 -1 N ILE A 263 O GLU A 197
SHEET 3 F 3 VAL A 267 PHE A 269 -1 N PHE A 269 O PHE A 262
SHEET 1 G 2 LEU A 223 PRO A 226 0
SHEET 2 G 2 VAL A 288 THR A 291 1 N GLU A 289 O LEU A 223
SHEET 1 H 2 ILE A 277 SER A 279 0
SHEET 2 H 2 CYS A 284 VAL A 286 -1 N THR A 285 O LEU A 278
SHEET 1 I 3 GLY J 16 ILE J 20 0
SHEET 2 I 3 GLN J 25 ASP J 32 -1 N VAL J 29 O GLY J 16
SHEET 3 I 3 GLY J 119 GLY J 122 1 N GLY J 119 O LEU J 30
SHEET 1 J 4 TRP J 39 PRO J 41 0
SHEET 2 J 4 GLN J 99 SER J 104 1 N GLY J 102 O VAL J 40
SHEET 3 J 4 THR J 81 ASP J 87 -1 N ASP J 87 O GLN J 99
SHEET 4 J 4 THR J 70 SER J 72 -1 N PHE J 71 O GLY J 82
SHEET 1 K 2 LEU J 89 VAL J 91 0
SHEET 2 K 2 ILE J 94 VAL J 96 -1 N VAL J 96 O LEU J 89
SHEET 1 L 5 ALA J 165 PHE J 168 0
SHEET 2 L 5 VAL J 150 TYR J 154 -1 N TYR J 154 O ALA J 165
SHEET 3 L 5 TYR J 312 ASP J 317 -1 N TYR J 316 O PHE J 151
SHEET 4 L 5 ARG J 322 THR J 327 -1 N ALA J 326 O TYR J 313
SHEET 5 L 5 TYR J 181 PRO J 184 -1 N ALA J 183 O VAL J 323
SHEET 1 M 3 GLN J 192 ILE J 195 0
SHEET 2 M 3 CYS J 212 VAL J 216 -1 N ALA J 214 O ILE J 193
SHEET 3 M 3 PRO J 300 LEU J 304 1 N PRO J 300 O GLN J 213
SHEET 1 N 3 GLU J 197 ILE J 200 0
SHEET 2 N 3 LEU J 260 ILE J 264 -1 N ILE J 263 O GLU J 197
SHEET 3 N 3 VAL J 267 LEU J 271 -1 N LEU J 271 O LEU J 260
SHEET 1 O 2 LEU J 223 PRO J 226 0
SHEET 2 O 2 VAL J 288 THR J 291 1 N GLU J 289 O LEU J 223
SHEET 1 P 2 ILE J 277 SER J 279 0
SHEET 2 P 2 CYS J 284 VAL J 286 -1 N THR J 285 O LEU J 278
SSBOND 1 CYS A 45 CYS A 50 1555 1555 2.02
SSBOND 2 CYS A 208 CYS A 212 1555 1555 2.03
SSBOND 3 CYS A 251 CYS A 284 1555 1555 2.03
SSBOND 4 CYS J 45 CYS J 50 1555 1555 2.02
SSBOND 5 CYS J 208 CYS J 212 1555 1555 2.03
SSBOND 6 CYS J 251 CYS J 284 1555 1555 2.02
LINK OG SER A 275 NA NA A 330 1555 1555 2.36
LINK OG SER A 311 NA NA A 330 1555 1555 2.52
LINK NA NA A 330 O HOH A 332 1555 1555 2.37
LINK NA NA A 330 O HOH A 335 1555 1555 2.62
LINK NA NA A 330 O HOH A 342 1555 1555 2.27
LINK NA NA A 330 O HOH A 471 1555 1555 2.34
CISPEP 1 THR A 22 PRO A 23 0 -0.11
CISPEP 2 THR J 22 PRO J 23 0 -0.03
SITE 1 AC1 6 SER A 275 SER A 311 HOH A 332 HOH A 335
SITE 2 AC1 6 HOH A 342 HOH A 471
CRYST1 156.260 50.410 125.180 90.00 117.62 90.00 C 1 2 1 8
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 0.006400 0.000000 0.003348 0.00000
SCALE2 0.000000 0.019837 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009016 0.00000
MTRIX1 1 0.199420 0.013420 -0.979820 13.14116 1
MTRIX2 1 0.018600 -0.999780 -0.009910 -14.41568 1
MTRIX3 1 -0.979740 -0.016250 -0.199630 20.86819 1
(ATOM LINES ARE NOT SHOWN.)
END