HEADER SIGNALING PROTEIN 14-MAR-05 1Z3U
TITLE STRUCTURE OF THE ANGIOPOIETIN-2 RECPTOR BINDING DOMAIN AND
TITLE 2 IDENTIFICATION OF SURFACES INVOLVED IN TIE2 RECOGNITION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANGIOPOIETIN-2;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: RECEPTOR BINDING DOMAIN (RESIDUES 281-496);
COMPND 5 SYNONYM: ANG-2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TIE2 BINDING, ANGIOGENESIS, EXTRACELLULAR LIGAND, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR W.A.BARTON,D.TZVETKOVA,D.B.NIKOLOV
REVDAT 3 20-OCT-21 1Z3U 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1Z3U 1 VERSN
REVDAT 1 12-JUL-05 1Z3U 0
JRNL AUTH W.A.BARTON,D.TZVETKOVA,D.B.NIKOLOV
JRNL TITL STRUCTURE OF THE ANGIOPOIETIN-2 RECEPTOR BINDING DOMAIN AND
JRNL TITL 2 IDENTIFICATION OF SURFACES INVOLVED IN TIE2 RECOGNITION.
JRNL REF STRUCTURE V. 13 825 2005
JRNL REFN ISSN 0969-2126
JRNL PMID 15893672
JRNL DOI 10.1016/J.STR.2005.03.009
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
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) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 50119
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.246
REMARK 3 FREE R VALUE : 0.278
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2513
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 : 6876
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 379
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
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) : NULL ; 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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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: NULL
REMARK 4
REMARK 4 1Z3U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032263.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-FEB-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X9A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
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 : 50119
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
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) : 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: AMORE
REMARK 200 STARTING MODEL: NULL
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: AMMONIUM SULFATE AND PEG-4000, PH 5.2,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 70.10900
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.23400
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 70.10900
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 47.23400
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, 3, 4
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 PHE A 496
REMARK 465 PHE B 496
REMARK 465 PHE C 496
REMARK 465 PHE D 496
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 GLY A 331 N - CA - C ANGL. DEV. = -18.0 DEGREES
REMARK 500 PRO A 419 C - N - CA ANGL. DEV. = -10.4 DEGREES
REMARK 500 ALA A 449 N - CA - C ANGL. DEV. = -21.5 DEGREES
REMARK 500 GLY B 331 N - CA - C ANGL. DEV. = -15.7 DEGREES
REMARK 500 PRO B 419 C - N - CD ANGL. DEV. = -12.9 DEGREES
REMARK 500 ALA B 449 N - CA - C ANGL. DEV. = -18.2 DEGREES
REMARK 500 GLY C 331 N - CA - C ANGL. DEV. = -15.7 DEGREES
REMARK 500 PRO C 419 C - N - CD ANGL. DEV. = -12.8 DEGREES
REMARK 500 ALA C 449 N - CA - C ANGL. DEV. = -18.6 DEGREES
REMARK 500 GLY D 331 N - CA - C ANGL. DEV. = -18.7 DEGREES
REMARK 500 PRO D 419 C - N - CA ANGL. DEV. = -9.0 DEGREES
REMARK 500 ALA D 449 N - CA - C ANGL. DEV. = -16.6 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 303 -107.22 -19.45
REMARK 500 GLN A 326 148.85 -172.25
REMARK 500 GLU A 329 -34.39 -149.29
REMARK 500 ASP A 330 98.61 104.13
REMARK 500 SER A 332 104.26 19.24
REMARK 500 ASP A 334 111.31 71.58
REMARK 500 SER A 417 122.62 -35.65
REMARK 500 GLN A 418 -175.71 -59.95
REMARK 500 THR A 442 139.24 78.57
REMARK 500 ASP A 448 -102.12 -98.94
REMARK 500 ALA A 449 47.81 -107.19
REMARK 500 CYS A 450 -63.25 90.84
REMARK 500 ASN A 454 93.96 179.01
REMARK 500 GLN A 464 14.39 -150.18
REMARK 500 TRP A 477 -60.67 -93.20
REMARK 500 PRO A 493 -168.79 -79.60
REMARK 500 LYS B 289 1.12 -60.85
REMARK 500 PRO B 303 -100.38 -13.99
REMARK 500 ASN B 304 42.17 -98.53
REMARK 500 GLU B 316 45.56 -107.13
REMARK 500 GLU B 329 -22.40 -167.17
REMARK 500 ASP B 330 120.86 102.02
REMARK 500 SER B 332 101.02 29.29
REMARK 500 ASP B 334 102.15 55.44
REMARK 500 SER B 417 124.98 -35.83
REMARK 500 THR B 442 139.13 68.81
REMARK 500 ASP B 448 -108.09 -109.34
REMARK 500 ALA B 449 47.80 -98.19
REMARK 500 CYS B 450 -72.88 90.94
REMARK 500 ASN B 454 92.84 177.36
REMARK 500 GLN B 464 1.13 -161.47
REMARK 500 TRP B 474 71.97 -152.41
REMARK 500 PRO C 303 -90.61 -18.61
REMARK 500 ASN C 304 43.12 -103.95
REMARK 500 GLU C 329 -16.75 -171.38
REMARK 500 ASP C 330 111.32 97.62
REMARK 500 SER C 332 98.95 40.26
REMARK 500 ASP C 334 104.87 63.67
REMARK 500 THR C 364 -4.64 -58.95
REMARK 500 SER C 417 120.14 -35.14
REMARK 500 GLN C 418 174.13 -58.94
REMARK 500 THR C 442 147.15 73.49
REMARK 500 ASP C 448 -102.21 -113.31
REMARK 500 ALA C 449 47.71 -105.41
REMARK 500 CYS C 450 -41.55 89.60
REMARK 500 ASN C 454 91.37 177.03
REMARK 500 GLN C 464 4.99 -157.71
REMARK 500 PRO D 303 -65.12 -16.12
REMARK 500 GLU D 329 -18.46 -160.86
REMARK 500 ASP D 330 117.39 93.86
REMARK 500
REMARK 500 THIS ENTRY HAS 61 RAMACHANDRAN OUTLIERS.
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 CA A 497 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 429 OD1
REMARK 620 2 ASP A 429 OD2 55.0
REMARK 620 3 ASP A 431 OD1 83.3 129.0
REMARK 620 4 ASP A 431 OD2 66.6 90.3 42.6
REMARK 620 5 CYS A 433 O 150.4 151.2 78.5 111.6
REMARK 620 6 CYS A 435 O 126.6 89.4 95.1 76.6 78.5
REMARK 620 7 HOH A 529 O 68.2 105.0 80.8 108.9 85.8 164.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 497 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 429 OD2
REMARK 620 2 ASP B 429 OD1 48.6
REMARK 620 3 ASP B 431 OD1 123.8 79.0
REMARK 620 4 CYS B 433 O 147.8 154.8 88.3
REMARK 620 5 CYS B 435 O 91.6 120.6 101.0 82.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 497 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 429 OD2
REMARK 620 2 ASP C 429 OD1 50.9
REMARK 620 3 ASP C 431 OD1 100.9 111.0
REMARK 620 4 CYS C 433 O 155.4 149.5 83.6
REMARK 620 5 CYS C 435 O 81.7 131.6 83.5 74.8
REMARK 620 6 HOH C 557 O 117.8 66.9 99.7 84.7 158.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 497 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 429 OD1
REMARK 620 2 ASP D 429 OD2 51.0
REMARK 620 3 ASP D 431 OD1 84.9 121.7
REMARK 620 4 ASP D 431 OD2 64.0 82.4 40.9
REMARK 620 5 CYS D 433 O 151.3 155.5 79.8 114.8
REMARK 620 6 CYS D 435 O 121.6 82.7 94.6 78.2 83.9
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 CA A 497
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 497
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 497
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 497
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1Z3S RELATED DB: PDB
DBREF 1Z3U A 281 496 UNP O15123 AGP2_HUMAN 281 496
DBREF 1Z3U B 281 496 UNP O15123 AGP2_HUMAN 281 496
DBREF 1Z3U C 281 496 UNP O15123 AGP2_HUMAN 281 496
DBREF 1Z3U D 281 496 UNP O15123 AGP2_HUMAN 281 496
SEQADV 1Z3U SER A 280 UNP O15123 CLONING ARTIFACT
SEQADV 1Z3U ALA A 469 UNP O15123 PHE 469 ENGINEERED MUTATION
SEQADV 1Z3U ALA A 475 UNP O15123 TYR 475 ENGINEERED MUTATION
SEQADV 1Z3U ALA A 476 UNP O15123 TYR 476 ENGINEERED MUTATION
SEQADV 1Z3U SER B 280 UNP O15123 CLONING ARTIFACT
SEQADV 1Z3U ALA B 469 UNP O15123 PHE 469 ENGINEERED MUTATION
SEQADV 1Z3U ALA B 475 UNP O15123 TYR 475 ENGINEERED MUTATION
SEQADV 1Z3U ALA B 476 UNP O15123 TYR 476 ENGINEERED MUTATION
SEQADV 1Z3U SER C 280 UNP O15123 CLONING ARTIFACT
SEQADV 1Z3U ALA C 469 UNP O15123 PHE 469 ENGINEERED MUTATION
SEQADV 1Z3U ALA C 475 UNP O15123 TYR 475 ENGINEERED MUTATION
SEQADV 1Z3U ALA C 476 UNP O15123 TYR 476 ENGINEERED MUTATION
SEQADV 1Z3U SER D 280 UNP O15123 CLONING ARTIFACT
SEQADV 1Z3U ALA D 469 UNP O15123 PHE 469 ENGINEERED MUTATION
SEQADV 1Z3U ALA D 475 UNP O15123 TYR 475 ENGINEERED MUTATION
SEQADV 1Z3U ALA D 476 UNP O15123 TYR 476 ENGINEERED MUTATION
SEQRES 1 A 217 SER PHE ARG ASP CYS ALA GLU VAL PHE LYS SER GLY HIS
SEQRES 2 A 217 THR THR ASN GLY ILE TYR THR LEU THR PHE PRO ASN SER
SEQRES 3 A 217 THR GLU GLU ILE LYS ALA TYR CYS ASP MET GLU ALA GLY
SEQRES 4 A 217 GLY GLY GLY TRP THR ILE ILE GLN ARG ARG GLU ASP GLY
SEQRES 5 A 217 SER VAL ASP PHE GLN ARG THR TRP LYS GLU TYR LYS VAL
SEQRES 6 A 217 GLY PHE GLY ASN PRO SER GLY GLU TYR TRP LEU GLY ASN
SEQRES 7 A 217 GLU PHE VAL SER GLN LEU THR ASN GLN GLN ARG TYR VAL
SEQRES 8 A 217 LEU LYS ILE HIS LEU LYS ASP TRP GLU GLY ASN GLU ALA
SEQRES 9 A 217 TYR SER LEU TYR GLU HIS PHE TYR LEU SER SER GLU GLU
SEQRES 10 A 217 LEU ASN TYR ARG ILE HIS LEU LYS GLY LEU THR GLY THR
SEQRES 11 A 217 ALA GLY LYS ILE SER SER ILE SER GLN PRO GLY ASN ASP
SEQRES 12 A 217 PHE SER THR LYS ASP GLY ASP ASN ASP LYS CYS ILE CYS
SEQRES 13 A 217 LYS CYS SER GLN MET LEU THR GLY GLY TRP TRP PHE ASP
SEQRES 14 A 217 ALA CYS GLY PRO SER ASN LEU ASN GLY MET TYR TYR PRO
SEQRES 15 A 217 GLN ARG GLN ASN THR ASN LYS ALA ASN GLY ILE LYS TRP
SEQRES 16 A 217 ALA ALA TRP LYS GLY SER GLY TYR SER LEU LYS ALA THR
SEQRES 17 A 217 THR MET MET ILE ARG PRO ALA ASP PHE
SEQRES 1 B 217 SER PHE ARG ASP CYS ALA GLU VAL PHE LYS SER GLY HIS
SEQRES 2 B 217 THR THR ASN GLY ILE TYR THR LEU THR PHE PRO ASN SER
SEQRES 3 B 217 THR GLU GLU ILE LYS ALA TYR CYS ASP MET GLU ALA GLY
SEQRES 4 B 217 GLY GLY GLY TRP THR ILE ILE GLN ARG ARG GLU ASP GLY
SEQRES 5 B 217 SER VAL ASP PHE GLN ARG THR TRP LYS GLU TYR LYS VAL
SEQRES 6 B 217 GLY PHE GLY ASN PRO SER GLY GLU TYR TRP LEU GLY ASN
SEQRES 7 B 217 GLU PHE VAL SER GLN LEU THR ASN GLN GLN ARG TYR VAL
SEQRES 8 B 217 LEU LYS ILE HIS LEU LYS ASP TRP GLU GLY ASN GLU ALA
SEQRES 9 B 217 TYR SER LEU TYR GLU HIS PHE TYR LEU SER SER GLU GLU
SEQRES 10 B 217 LEU ASN TYR ARG ILE HIS LEU LYS GLY LEU THR GLY THR
SEQRES 11 B 217 ALA GLY LYS ILE SER SER ILE SER GLN PRO GLY ASN ASP
SEQRES 12 B 217 PHE SER THR LYS ASP GLY ASP ASN ASP LYS CYS ILE CYS
SEQRES 13 B 217 LYS CYS SER GLN MET LEU THR GLY GLY TRP TRP PHE ASP
SEQRES 14 B 217 ALA CYS GLY PRO SER ASN LEU ASN GLY MET TYR TYR PRO
SEQRES 15 B 217 GLN ARG GLN ASN THR ASN LYS ALA ASN GLY ILE LYS TRP
SEQRES 16 B 217 ALA ALA TRP LYS GLY SER GLY TYR SER LEU LYS ALA THR
SEQRES 17 B 217 THR MET MET ILE ARG PRO ALA ASP PHE
SEQRES 1 C 217 SER PHE ARG ASP CYS ALA GLU VAL PHE LYS SER GLY HIS
SEQRES 2 C 217 THR THR ASN GLY ILE TYR THR LEU THR PHE PRO ASN SER
SEQRES 3 C 217 THR GLU GLU ILE LYS ALA TYR CYS ASP MET GLU ALA GLY
SEQRES 4 C 217 GLY GLY GLY TRP THR ILE ILE GLN ARG ARG GLU ASP GLY
SEQRES 5 C 217 SER VAL ASP PHE GLN ARG THR TRP LYS GLU TYR LYS VAL
SEQRES 6 C 217 GLY PHE GLY ASN PRO SER GLY GLU TYR TRP LEU GLY ASN
SEQRES 7 C 217 GLU PHE VAL SER GLN LEU THR ASN GLN GLN ARG TYR VAL
SEQRES 8 C 217 LEU LYS ILE HIS LEU LYS ASP TRP GLU GLY ASN GLU ALA
SEQRES 9 C 217 TYR SER LEU TYR GLU HIS PHE TYR LEU SER SER GLU GLU
SEQRES 10 C 217 LEU ASN TYR ARG ILE HIS LEU LYS GLY LEU THR GLY THR
SEQRES 11 C 217 ALA GLY LYS ILE SER SER ILE SER GLN PRO GLY ASN ASP
SEQRES 12 C 217 PHE SER THR LYS ASP GLY ASP ASN ASP LYS CYS ILE CYS
SEQRES 13 C 217 LYS CYS SER GLN MET LEU THR GLY GLY TRP TRP PHE ASP
SEQRES 14 C 217 ALA CYS GLY PRO SER ASN LEU ASN GLY MET TYR TYR PRO
SEQRES 15 C 217 GLN ARG GLN ASN THR ASN LYS ALA ASN GLY ILE LYS TRP
SEQRES 16 C 217 ALA ALA TRP LYS GLY SER GLY TYR SER LEU LYS ALA THR
SEQRES 17 C 217 THR MET MET ILE ARG PRO ALA ASP PHE
SEQRES 1 D 217 SER PHE ARG ASP CYS ALA GLU VAL PHE LYS SER GLY HIS
SEQRES 2 D 217 THR THR ASN GLY ILE TYR THR LEU THR PHE PRO ASN SER
SEQRES 3 D 217 THR GLU GLU ILE LYS ALA TYR CYS ASP MET GLU ALA GLY
SEQRES 4 D 217 GLY GLY GLY TRP THR ILE ILE GLN ARG ARG GLU ASP GLY
SEQRES 5 D 217 SER VAL ASP PHE GLN ARG THR TRP LYS GLU TYR LYS VAL
SEQRES 6 D 217 GLY PHE GLY ASN PRO SER GLY GLU TYR TRP LEU GLY ASN
SEQRES 7 D 217 GLU PHE VAL SER GLN LEU THR ASN GLN GLN ARG TYR VAL
SEQRES 8 D 217 LEU LYS ILE HIS LEU LYS ASP TRP GLU GLY ASN GLU ALA
SEQRES 9 D 217 TYR SER LEU TYR GLU HIS PHE TYR LEU SER SER GLU GLU
SEQRES 10 D 217 LEU ASN TYR ARG ILE HIS LEU LYS GLY LEU THR GLY THR
SEQRES 11 D 217 ALA GLY LYS ILE SER SER ILE SER GLN PRO GLY ASN ASP
SEQRES 12 D 217 PHE SER THR LYS ASP GLY ASP ASN ASP LYS CYS ILE CYS
SEQRES 13 D 217 LYS CYS SER GLN MET LEU THR GLY GLY TRP TRP PHE ASP
SEQRES 14 D 217 ALA CYS GLY PRO SER ASN LEU ASN GLY MET TYR TYR PRO
SEQRES 15 D 217 GLN ARG GLN ASN THR ASN LYS ALA ASN GLY ILE LYS TRP
SEQRES 16 D 217 ALA ALA TRP LYS GLY SER GLY TYR SER LEU LYS ALA THR
SEQRES 17 D 217 THR MET MET ILE ARG PRO ALA ASP PHE
HET CA A 497 1
HET CA B 497 1
HET CA C 497 1
HET CA D 497 1
HETNAM CA CALCIUM ION
FORMUL 5 CA 4(CA 2+)
FORMUL 9 HOH *379(H2 O)
HELIX 1 1 ASP A 283 LYS A 289 1 7
HELIX 2 2 THR A 338 GLY A 345 1 8
HELIX 3 3 GLY A 356 GLN A 367 1 12
HELIX 4 4 SER A 394 ASN A 398 5 5
HELIX 5 5 LYS A 436 THR A 442 1 7
HELIX 6 6 ALA A 475 GLY A 479 1 5
HELIX 7 7 ASP B 283 LYS B 289 1 7
HELIX 8 8 THR B 338 GLY B 345 1 8
HELIX 9 9 GLY B 356 GLN B 367 1 12
HELIX 10 10 SER B 394 ASN B 398 5 5
HELIX 11 11 LYS B 436 THR B 442 1 7
HELIX 12 12 ALA B 475 GLY B 479 1 5
HELIX 13 13 ASP C 283 SER C 290 1 8
HELIX 14 14 THR C 338 GLY C 345 1 8
HELIX 15 15 GLY C 356 ASN C 365 1 10
HELIX 16 16 SER C 394 ASN C 398 5 5
HELIX 17 17 LYS C 436 THR C 442 1 7
HELIX 18 18 ALA C 475 GLY C 479 1 5
HELIX 19 19 ASP D 283 SER D 290 1 8
HELIX 20 20 THR D 338 GLY D 345 1 8
HELIX 21 21 GLY D 356 ASN D 365 1 10
HELIX 22 22 SER D 394 ASN D 398 5 5
HELIX 23 23 LYS D 436 THR D 442 1 7
HELIX 24 24 ALA D 475 GLY D 479 1 5
SHEET 1 A 5 GLY A 296 THR A 301 0
SHEET 2 A 5 GLU A 308 ASP A 314 -1 O ILE A 309 N LEU A 300
SHEET 3 A 5 TRP A 322 ARG A 328 -1 O TRP A 322 N ASP A 314
SHEET 4 A 5 TYR A 353 TRP A 354 -1 O TYR A 353 N ARG A 327
SHEET 5 A 5 PHE A 346 GLY A 347 -1 N PHE A 346 O TRP A 354
SHEET 1 B 7 GLY A 296 THR A 301 0
SHEET 2 B 7 GLU A 308 ASP A 314 -1 O ILE A 309 N LEU A 300
SHEET 3 B 7 TRP A 322 ARG A 328 -1 O TRP A 322 N ASP A 314
SHEET 4 B 7 ALA A 486 PRO A 493 -1 O MET A 489 N ILE A 325
SHEET 5 B 7 TYR A 369 LYS A 376 -1 N VAL A 370 O ARG A 492
SHEET 6 B 7 GLU A 382 LEU A 392 -1 O SER A 385 N ILE A 373
SHEET 7 B 7 ILE A 401 GLY A 408 -1 O LYS A 404 N HIS A 389
SHEET 1 C 2 SER A 453 ASN A 454 0
SHEET 2 C 2 LYS A 473 TRP A 474 -1 O LYS A 473 N ASN A 454
SHEET 1 D 5 GLY B 296 THR B 301 0
SHEET 2 D 5 GLU B 308 ASP B 314 -1 O ILE B 309 N LEU B 300
SHEET 3 D 5 TRP B 322 ARG B 328 -1 O TRP B 322 N ASP B 314
SHEET 4 D 5 TYR B 353 TRP B 354 -1 O TYR B 353 N ARG B 327
SHEET 5 D 5 PHE B 346 GLY B 347 -1 N PHE B 346 O TRP B 354
SHEET 1 E 7 GLY B 296 THR B 301 0
SHEET 2 E 7 GLU B 308 ASP B 314 -1 O ILE B 309 N LEU B 300
SHEET 3 E 7 TRP B 322 ARG B 328 -1 O TRP B 322 N ASP B 314
SHEET 4 E 7 ALA B 486 PRO B 493 -1 O MET B 489 N ILE B 325
SHEET 5 E 7 TYR B 369 LYS B 376 -1 N LYS B 372 O MET B 490
SHEET 6 E 7 GLU B 382 LEU B 392 -1 O SER B 385 N ILE B 373
SHEET 7 E 7 ILE B 401 GLY B 408 -1 O LYS B 404 N HIS B 389
SHEET 1 F 2 SER B 453 ASN B 454 0
SHEET 2 F 2 LYS B 473 TRP B 474 -1 O LYS B 473 N ASN B 454
SHEET 1 G 5 GLY C 296 THR C 301 0
SHEET 2 G 5 GLU C 308 ASP C 314 -1 O CYS C 313 N GLY C 296
SHEET 3 G 5 TRP C 322 ARG C 328 -1 O ILE C 324 N TYR C 312
SHEET 4 G 5 TYR C 353 TRP C 354 -1 O TYR C 353 N ARG C 327
SHEET 5 G 5 PHE C 346 GLY C 347 -1 N PHE C 346 O TRP C 354
SHEET 1 H 7 GLY C 296 THR C 301 0
SHEET 2 H 7 GLU C 308 ASP C 314 -1 O CYS C 313 N GLY C 296
SHEET 3 H 7 TRP C 322 ARG C 328 -1 O ILE C 324 N TYR C 312
SHEET 4 H 7 ALA C 486 PRO C 493 -1 O MET C 489 N ILE C 325
SHEET 5 H 7 TYR C 369 LYS C 376 -1 N LYS C 372 O MET C 490
SHEET 6 H 7 GLU C 382 LEU C 392 -1 O ALA C 383 N LEU C 375
SHEET 7 H 7 ILE C 401 GLY C 408 -1 O LYS C 404 N HIS C 389
SHEET 1 I 2 SER C 453 ASN C 454 0
SHEET 2 I 2 LYS C 473 TRP C 474 -1 O LYS C 473 N ASN C 454
SHEET 1 J 5 GLY D 296 THR D 301 0
SHEET 2 J 5 GLU D 308 ASP D 314 -1 O ILE D 309 N LEU D 300
SHEET 3 J 5 TRP D 322 ARG D 328 -1 O TRP D 322 N ASP D 314
SHEET 4 J 5 TYR D 353 TRP D 354 -1 O TYR D 353 N ARG D 327
SHEET 5 J 5 PHE D 346 GLY D 347 -1 N PHE D 346 O TRP D 354
SHEET 1 K 7 GLY D 296 THR D 301 0
SHEET 2 K 7 GLU D 308 ASP D 314 -1 O ILE D 309 N LEU D 300
SHEET 3 K 7 TRP D 322 ARG D 328 -1 O TRP D 322 N ASP D 314
SHEET 4 K 7 ALA D 486 PRO D 493 -1 O MET D 489 N ILE D 325
SHEET 5 K 7 TYR D 369 LYS D 376 -1 N LYS D 372 O MET D 490
SHEET 6 K 7 GLU D 382 LEU D 392 -1 O ALA D 383 N LEU D 375
SHEET 7 K 7 ILE D 401 GLY D 408 -1 O GLY D 405 N GLU D 388
SHEET 1 L 2 SER D 453 ASN D 454 0
SHEET 2 L 2 LYS D 473 TRP D 474 -1 O LYS D 473 N ASN D 454
SSBOND 1 CYS A 284 CYS A 313 1555 1555 2.03
SSBOND 2 CYS A 433 CYS A 435 1555 1555 2.04
SSBOND 3 CYS A 437 CYS A 450 1555 1555 2.04
SSBOND 4 CYS B 284 CYS B 313 1555 1555 2.03
SSBOND 5 CYS B 433 CYS B 435 1555 1555 2.04
SSBOND 6 CYS B 437 CYS B 450 1555 1555 2.04
SSBOND 7 CYS C 284 CYS C 313 1555 1555 2.01
SSBOND 8 CYS C 433 CYS C 435 1555 1555 2.04
SSBOND 9 CYS C 437 CYS C 450 1555 1555 2.04
SSBOND 10 CYS D 284 CYS D 313 1555 1555 2.04
SSBOND 11 CYS D 433 CYS D 435 1555 1555 2.03
SSBOND 12 CYS D 437 CYS D 450 1555 1555 2.04
LINK OD1 ASP A 429 CA CA A 497 1555 1555 2.47
LINK OD2 ASP A 429 CA CA A 497 1555 1555 2.26
LINK OD1 ASP A 431 CA CA A 497 1555 1555 2.41
LINK OD2 ASP A 431 CA CA A 497 1555 1555 3.25
LINK O CYS A 433 CA CA A 497 1555 1555 2.48
LINK O CYS A 435 CA CA A 497 1555 1555 2.32
LINK CA CA A 497 O HOH A 529 1555 1555 2.58
LINK OD2 ASP B 429 CA CA B 497 1555 1555 2.75
LINK OD1 ASP B 429 CA CA B 497 1555 1555 2.56
LINK OD1 ASP B 431 CA CA B 497 1555 1555 2.41
LINK O CYS B 433 CA CA B 497 1555 1555 2.54
LINK O CYS B 435 CA CA B 497 1555 1555 2.21
LINK OD2 ASP C 429 CA CA C 497 1555 1555 2.52
LINK OD1 ASP C 429 CA CA C 497 1555 1555 2.58
LINK OD1 ASP C 431 CA CA C 497 1555 1555 2.39
LINK O CYS C 433 CA CA C 497 1555 1555 2.53
LINK O CYS C 435 CA CA C 497 1555 1555 2.58
LINK CA CA C 497 O HOH C 557 1555 1555 2.35
LINK OD1 ASP D 429 CA CA D 497 1555 1555 2.43
LINK OD2 ASP D 429 CA CA D 497 1555 1555 2.65
LINK OD1 ASP D 431 CA CA D 497 1555 1555 2.46
LINK OD2 ASP D 431 CA CA D 497 1555 1555 3.37
LINK O CYS D 433 CA CA D 497 1555 1555 2.91
LINK O CYS D 435 CA CA D 497 1555 1555 2.29
SITE 1 AC1 5 ASP A 429 ASP A 431 CYS A 433 CYS A 435
SITE 2 AC1 5 HOH A 529
SITE 1 AC2 4 ASP B 429 ASP B 431 CYS B 433 CYS B 435
SITE 1 AC3 5 ASP C 429 ASP C 431 CYS C 433 CYS C 435
SITE 2 AC3 5 HOH C 557
SITE 1 AC4 4 ASP D 429 ASP D 431 CYS D 433 CYS D 435
CRYST1 140.218 94.468 84.673 90.00 94.47 90.00 C 1 2 1 16
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 0.007132 0.000000 0.000558 0.00000
SCALE2 0.000000 0.010586 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011846 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
